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Gene Information
Gene symbol: SOD1
Gene name: superoxide dismutase 1, soluble
HGNC ID: 11179
Synonyms: IPOA
Related Genes
Related Sentences
| # | PMID | Sentence |
| 1 | 1336731 | The rate of superoxide anion production was measured spectrophotometrically by superoxide dismutase-inhibitable cytochrome c reduction. |
| 2 | 1392495 | The result showed: (1) The MDA product of both pancreas and liver homogenate in Coptis group was significantly less than that in control and alloxan group (P < 0.01, P < 0.05). (2) Superoxide dismutases (SODs) in erythrocytes activity was the same for all groups (P > 0.50). (3) The blood catalase (CAT) activity in alloxan group markedly decreased compared with control group (P < 0.05), but no significant change between Coptis and alloxan group (P > 0.05). (4) The value of serum glucose in alloxan group was significantly increased in comparing with control group (P < 0.05). |
| 3 | 1406292 | Decreases in the activities of Cu, Zn-superoxide dismutase (Cu,Zn-SOD) (62.7 +/- 11.0 U/mg protein v 172.9 +/- 20.2 U/mg protein), catalase (7.6 +/- 2.1 U/mg protein v 12.3 +/- 3.2 U/mg protein), and GSH peroxidase (134.0 +/- 27.0 mU/mg protein v 179.1 +/- 26.2 mU/mg protein) were observed. |
| 4 | 1455447 | Although alloxan decreased insulin secretion to 35% of the control, SOD increased this level to 73% of the control values. |
| 5 | 1455447 | The increased insulin secretion from islets treated with SOD and alloxan reinforces the free radical hypothesis of alloxan toxicity. |
| 6 | 1455447 | Although alloxan decreased insulin secretion to 35% of the control, SOD increased this level to 73% of the control values. |
| 7 | 1455447 | The increased insulin secretion from islets treated with SOD and alloxan reinforces the free radical hypothesis of alloxan toxicity. |
| 8 | 1483970 | To test whether oxidative stress has an effect on delaying cell replication time in hyperglycemic conditions, human endothelial cells cultured from umbilical veins were incubated in 5 or 20 mM glucose, either alone or in the presence of one of three different antioxidants: superoxide dismutase (SOD), catalase and glutathione (GSH). |
| 9 | 1509740 | This study reports on the effect of streptozotocin (STZ) induced diabetes on water soluble-SH and -SS, as well as on hepatic glutathione peroxidase (GSH-Px), catalase and superoxide dismutase (SOD) activity and on malondialdehyde (MDA) content. |
| 10 | 1510128 | Impairment of endothelium-dependent relaxation to acetylcholine caused by exposure to elevated glucose was prevented by superoxide dismutase, catalase, deferoxamine, or allopurinol and did not occur in aortas from probucol-fed rabbits. |
| 11 | 1512041 | Antioxidant enzymes superoxide dismutase and catalase decreased in all tissues (P less than 0.01) while the activity of glutathione s-transferase increased in heart, but no change in other tissues. |
| 12 | 1521861 | Changes in levels of lipid peroxides and activity of superoxide dismutase and catalase in diabetes associated with myocardial infarction. |
| 13 | 1521861 | The activity of superoxide dismutase and catalase showed a decrease in both the groups. |
| 14 | 1521861 | Changes in levels of lipid peroxides and activity of superoxide dismutase and catalase in diabetes associated with myocardial infarction. |
| 15 | 1521861 | The activity of superoxide dismutase and catalase showed a decrease in both the groups. |
| 16 | 1592880 | Increased glycated Cu,Zn-superoxide dismutase levels in erythrocytes of patients with insulin-dependent diabetis mellitus. |
| 17 | 1632872 | In SA, the erythrocytes expressed a diminished activity of superoxide dismutase (SOD) (SA: 435.59 +/- 76.02, control: 651.69 +/- 145.90, P less than 0.001) and normal activities of catalase and glutathione peroxidase, whereas in UA it showed enhanced activities of both SOD (UA: 735.72 +/- 145.67, P less than 0.01) and catalase (UA: 21.94 +/- 6.26, control: 18.69 +/- 6.37, P less than 0.01). |
| 18 | 1636763 | In the present study, we investigated spontaneous EDRF release in diabetic rat aorta that is unmasked by the addition of superoxide dismutase (SOD). |
| 19 | 1636763 | Measurement of antioxidant enzymes revealed an elevation in catalase in diabetic aorta, with no difference in the SOD or glutathione peroxidase activity. |
| 20 | 1636763 | Pretreatment of rings with the catalase inhibitor, 3-amino-1,2,4-triazole, attenuated the SOD-induced relaxation in diabetic aortic rings but had no effect in control aortic rings. |
| 21 | 1636763 | In the present study, we investigated spontaneous EDRF release in diabetic rat aorta that is unmasked by the addition of superoxide dismutase (SOD). |
| 22 | 1636763 | Measurement of antioxidant enzymes revealed an elevation in catalase in diabetic aorta, with no difference in the SOD or glutathione peroxidase activity. |
| 23 | 1636763 | Pretreatment of rings with the catalase inhibitor, 3-amino-1,2,4-triazole, attenuated the SOD-induced relaxation in diabetic aortic rings but had no effect in control aortic rings. |
| 24 | 1636763 | In the present study, we investigated spontaneous EDRF release in diabetic rat aorta that is unmasked by the addition of superoxide dismutase (SOD). |
| 25 | 1636763 | Measurement of antioxidant enzymes revealed an elevation in catalase in diabetic aorta, with no difference in the SOD or glutathione peroxidase activity. |
| 26 | 1636763 | Pretreatment of rings with the catalase inhibitor, 3-amino-1,2,4-triazole, attenuated the SOD-induced relaxation in diabetic aortic rings but had no effect in control aortic rings. |
| 27 | 1647454 | We have also reported about the research results on ROS, which can be classified as following below; 1) chemical reactivities of O2-., 2) formation and toxicity of 1O2, 3) chemical reactivities of .OH, 4) enzyme mechanism of xanthine oxidase, 5) development of the compounds which induce the formation of O2-. and H2O2 in living cells and 6) development of superoxide dismutase mimics. |
| 28 | 1673279 | Two forms of superoxide dismutase, CuZn-SOD and MnSOD, have been investigated in the kidneys of streptozotocin-induced diabetic rats using both radio-immunoassay and immunoenzyme staining. |
| 29 | 1722548 | The authors have developed methods for measurements of catalase, superoxide dismutase, and lipid peroxidation products. |
| 30 | 1722548 | They introduce a new factor 'F' that is supposed to characterize the blood antioxidant system; this factor is based on the values of catalase and superoxide dismutase activities and the intensity of lipid peroxidation. |
| 31 | 1722548 | In case of an abdominal tumor whole blood catalase level is elevated and superoxide dismutase activity significantly reduced. |
| 32 | 1722548 | The authors have developed methods for measurements of catalase, superoxide dismutase, and lipid peroxidation products. |
| 33 | 1722548 | They introduce a new factor 'F' that is supposed to characterize the blood antioxidant system; this factor is based on the values of catalase and superoxide dismutase activities and the intensity of lipid peroxidation. |
| 34 | 1722548 | In case of an abdominal tumor whole blood catalase level is elevated and superoxide dismutase activity significantly reduced. |
| 35 | 1722548 | The authors have developed methods for measurements of catalase, superoxide dismutase, and lipid peroxidation products. |
| 36 | 1722548 | They introduce a new factor 'F' that is supposed to characterize the blood antioxidant system; this factor is based on the values of catalase and superoxide dismutase activities and the intensity of lipid peroxidation. |
| 37 | 1722548 | In case of an abdominal tumor whole blood catalase level is elevated and superoxide dismutase activity significantly reduced. |
| 38 | 1752151 | Lipid peroxide (LPO) values in blood plasma, along with the glutathione peroxidase (GSH-PX) activity in whole blood and superoxide dismutase (SOD) activity in erythrocytes were determined in 50 patients with non-insulin-dependent diabetes mellitus (NIDDM) and in 33 control subjects. |
| 39 | 1837513 | The oxidative effects of free radicals as total diene conjugates and lipid peroxides were measured, together with redox status extracellularly as plasma albumin-thiols and intracellularly as erythrocyte superoxide dismutase activity. |
| 40 | 1837513 | There were also significant reductions in redox status both extracellularly as plasma albumin thiols (408 (383-473) vs 490 (456-517) mumol l-1, p less than 0.001) and intracellularly as erythrocyte superoxide dismutase activity (34 (27-41) vs 44 (36-51) g l-1, p less than 0.05) between patients with retinopathy and control subjects. |
| 41 | 1837513 | The oxidative effects of free radicals as total diene conjugates and lipid peroxides were measured, together with redox status extracellularly as plasma albumin-thiols and intracellularly as erythrocyte superoxide dismutase activity. |
| 42 | 1837513 | There were also significant reductions in redox status both extracellularly as plasma albumin thiols (408 (383-473) vs 490 (456-517) mumol l-1, p less than 0.001) and intracellularly as erythrocyte superoxide dismutase activity (34 (27-41) vs 44 (36-51) g l-1, p less than 0.05) between patients with retinopathy and control subjects. |
| 43 | 1900813 | Aldolase, glucose-6-phosphate dehydrogenase, superoxide dismutase and aldose reductase activity in the lenses of diabetic rats. |
| 44 | 1915599 | ALS and ALR mice were developed as mouse models of alloxan-induced diabetes. |
| 45 | 1946299 | A study was made of changes in the activity of erythrocyte antioxidant enzymes (superoxide dismutase and catalase) with regard to the blood level of glucose in children with insulin dependent diabetes mellitus and in vitro. |
| 46 | 1946299 | Catalase activity did not change whereas superoxide dismutase activity in decompensation of disease was significantly lower than that in its compensation. |
| 47 | 1946299 | A study was made of changes in the activity of erythrocyte antioxidant enzymes (superoxide dismutase and catalase) with regard to the blood level of glucose in children with insulin dependent diabetes mellitus and in vitro. |
| 48 | 1946299 | Catalase activity did not change whereas superoxide dismutase activity in decompensation of disease was significantly lower than that in its compensation. |
| 49 | 2035280 | The influence of a 4 week course of balneotherapeutic treatment in Bad Hall on different blood parameters and on the activity of the antioxidative enzymes glutathione peroxidase (GSH-Px), catalase and superoxide dismutase (SOD) was examined in diabetics. |
| 50 | 2086281 | Superoxide dismutase, glutathione peroxidase and glutathione reductase activities were measured in erythrocytes of 214 young patients with insulin-dependent diabetes and 37 healthy subjects with similar age and sex distribution. |
| 51 | 2086281 | Results showed that superoxide dismutase, glutathione peroxidase and glutathione reductase activities in young diabetic patients were similar to those in controls, except for patients with retinopathy, whose glutathione peroxidase activity was decreased. |
| 52 | 2086281 | Superoxide dismutase, glutathione peroxidase and glutathione reductase activities were measured in erythrocytes of 214 young patients with insulin-dependent diabetes and 37 healthy subjects with similar age and sex distribution. |
| 53 | 2086281 | Results showed that superoxide dismutase, glutathione peroxidase and glutathione reductase activities in young diabetic patients were similar to those in controls, except for patients with retinopathy, whose glutathione peroxidase activity was decreased. |
| 54 | 2087929 | The activities of enzymes involved in cellular defence mechanisms such as superoxide dismutase, catalase, glutathione peroxidase and glutathione level have been found to be altered in experimental diabetes. |
| 55 | 2087929 | Decreased activities of glutathione peroxidase, catalase, superoxide dismutase and glutathione content found in diabetic rats were corrected to near normal. |
| 56 | 2087929 | The activities of enzymes involved in cellular defence mechanisms such as superoxide dismutase, catalase, glutathione peroxidase and glutathione level have been found to be altered in experimental diabetes. |
| 57 | 2087929 | Decreased activities of glutathione peroxidase, catalase, superoxide dismutase and glutathione content found in diabetic rats were corrected to near normal. |
| 58 | 2109941 | The arachidonic acid-induced postischemic dysfunction was significantly attenuated by coadministration of the oxygen free radical scavengers, superoxide dismutase plus catalase, but not by indomethacin. |
| 59 | 2166735 | Superoxide anion (O2-.) generation during basal conditions and after stimulation with phorbol myristate acetate (PMA) was measured as superoxide dismutase-inhibitable cytochrome c reduction. |
| 60 | 2171534 | Allopurinol and SOD inhibited cytochrome c reduction in a hypoxanthine-xanthine oxidase superoxide generating system, whereas bepridil was ineffective. |
| 61 | 2343573 | Alterations in superoxide dismutase activity, observed in erythrocytes of children with insulin-dependent form of diabetes mellitus, depended on the age of patients, severity and degree of the disease compensation. |
| 62 | 2361527 | To elucidate the genetic background of the two inbred strains, i. e., alloxan-induced diabetes-susceptible (ALS) strain and alloxan-induced diabetes-resistant (ALR) strain, their biochemical genetic markers and immunogenetic markers were examined. 1) For both strains, investigation of biochemical genetic markers at 19 loci and immunogenetic markers at 11 loci revealed no variation in any gene within the same strain, showing to be homogeneous, thus indicating establishment of the inbred strains. 2) The two strains differed from each other at 2 loci of biochemical genetic markers and at 5 loci of immunogenetic markers. 3) The ALS and ALR strains can be regarded as new inbred strains derived from ICR mice. 4) The results show that the marker genes of the two strains are different at 7 loci, but it remains unclear whether or not these genes are involved in the difference between the two strains in susceptibility to alloxan. |
| 63 | 2470263 | Ilo significantly decreased postischemic recovery in CH (from 67 +/- 11 to 15 +/- 4%), which was partially blocked by the coadministration of the calcium-entry blocker diltiazem or almost completely reversed by the free radical scavengers superoxide dismutase plus catalase (100 U/ml). |
| 64 | 2521747 | Retinyl palmitate in vitro did not affect insulin secretion or islet superoxide dismutase. |
| 65 | 2542156 | We reported here that in vivo treatment of spontaneously diabetic NOD mice with the enzyme superoxide dismutase (2000 U for seven injections) and catalase (40,000 U for seven injections) protects islet tissue from disease recurrence following transplantation into spontaneously diabetic mice. |
| 66 | 2561353 | The changes in copper-zinc superoxide dismutase and catalase in diabetic rats were similar to those in starved rats. |
| 67 | 2561353 | In both groups, copper-zinc superoxide dismutase was decreased in liver, while catalase activity was decreased in liver and kidney, and increased in heart. |
| 68 | 2561353 | The changes in copper-zinc superoxide dismutase and catalase in diabetic rats were similar to those in starved rats. |
| 69 | 2561353 | In both groups, copper-zinc superoxide dismutase was decreased in liver, while catalase activity was decreased in liver and kidney, and increased in heart. |
| 70 | 3046720 | Streptozotocin treatment resulted in a significant decrease in plasma insulin and ceruloplasmin, and pancreatic Cu, protein, and Cu-Zn superoxide dismutase activity. |
| 71 | 3214126 | Superoxide dismutase (SOD), glutathione peroxidase (GPX) and catalase were assayed in the erythrocytes of a diabetic population on various treatment regimens (diet, oral therapy, and insulin), to investigate any relationships between their activities and diabetes markers (serum glucose, lipids, and fructosamine, as well as glycated haemoglobin). |
| 72 | 3215628 | Catalase and superoxide dismutase activities in the kidney were not altered. |
| 73 | 3256431 | Superoxide dismutase plus catalase improves post-ischaemic recovery in the diabetic heart. |
| 74 | 3256431 | Streptozotocin induced diabetic rat hearts were perfused under constant flow conditions with or without 1 x 10(5) U.litre-1 each of superoxide dismutase and catalase (SOD + CAT). |
| 75 | 3256431 | SOD + CAT improved isovolumic LV developed pressure to 67(8)% of baseline during early reperfusion of diabetic hearts but did not affect non-diabetic hearts. |
| 76 | 3256431 | SOD + CAT also increased the adenylate energy charge potential in post-ischaemic diabetic hearts to 0.826(0.011) v 0.781(0.012) in diabetic controls, and reduced the incidence and duration of reperfusion induced VF in diabetic hearts. |
| 77 | 3256431 | The beneficial effects of SOD + CAT appear to be mediated mainly by an increase in prostacyclin production during early reperfusion. |
| 78 | 3256431 | Superoxide dismutase plus catalase improves post-ischaemic recovery in the diabetic heart. |
| 79 | 3256431 | Streptozotocin induced diabetic rat hearts were perfused under constant flow conditions with or without 1 x 10(5) U.litre-1 each of superoxide dismutase and catalase (SOD + CAT). |
| 80 | 3256431 | SOD + CAT improved isovolumic LV developed pressure to 67(8)% of baseline during early reperfusion of diabetic hearts but did not affect non-diabetic hearts. |
| 81 | 3256431 | SOD + CAT also increased the adenylate energy charge potential in post-ischaemic diabetic hearts to 0.826(0.011) v 0.781(0.012) in diabetic controls, and reduced the incidence and duration of reperfusion induced VF in diabetic hearts. |
| 82 | 3256431 | The beneficial effects of SOD + CAT appear to be mediated mainly by an increase in prostacyclin production during early reperfusion. |
| 83 | 3256431 | Superoxide dismutase plus catalase improves post-ischaemic recovery in the diabetic heart. |
| 84 | 3256431 | Streptozotocin induced diabetic rat hearts were perfused under constant flow conditions with or without 1 x 10(5) U.litre-1 each of superoxide dismutase and catalase (SOD + CAT). |
| 85 | 3256431 | SOD + CAT improved isovolumic LV developed pressure to 67(8)% of baseline during early reperfusion of diabetic hearts but did not affect non-diabetic hearts. |
| 86 | 3256431 | SOD + CAT also increased the adenylate energy charge potential in post-ischaemic diabetic hearts to 0.826(0.011) v 0.781(0.012) in diabetic controls, and reduced the incidence and duration of reperfusion induced VF in diabetic hearts. |
| 87 | 3256431 | The beneficial effects of SOD + CAT appear to be mediated mainly by an increase in prostacyclin production during early reperfusion. |
| 88 | 3256431 | Superoxide dismutase plus catalase improves post-ischaemic recovery in the diabetic heart. |
| 89 | 3256431 | Streptozotocin induced diabetic rat hearts were perfused under constant flow conditions with or without 1 x 10(5) U.litre-1 each of superoxide dismutase and catalase (SOD + CAT). |
| 90 | 3256431 | SOD + CAT improved isovolumic LV developed pressure to 67(8)% of baseline during early reperfusion of diabetic hearts but did not affect non-diabetic hearts. |
| 91 | 3256431 | SOD + CAT also increased the adenylate energy charge potential in post-ischaemic diabetic hearts to 0.826(0.011) v 0.781(0.012) in diabetic controls, and reduced the incidence and duration of reperfusion induced VF in diabetic hearts. |
| 92 | 3256431 | The beneficial effects of SOD + CAT appear to be mediated mainly by an increase in prostacyclin production during early reperfusion. |
| 93 | 3256431 | Superoxide dismutase plus catalase improves post-ischaemic recovery in the diabetic heart. |
| 94 | 3256431 | Streptozotocin induced diabetic rat hearts were perfused under constant flow conditions with or without 1 x 10(5) U.litre-1 each of superoxide dismutase and catalase (SOD + CAT). |
| 95 | 3256431 | SOD + CAT improved isovolumic LV developed pressure to 67(8)% of baseline during early reperfusion of diabetic hearts but did not affect non-diabetic hearts. |
| 96 | 3256431 | SOD + CAT also increased the adenylate energy charge potential in post-ischaemic diabetic hearts to 0.826(0.011) v 0.781(0.012) in diabetic controls, and reduced the incidence and duration of reperfusion induced VF in diabetic hearts. |
| 97 | 3256431 | The beneficial effects of SOD + CAT appear to be mediated mainly by an increase in prostacyclin production during early reperfusion. |
| 98 | 3301471 | Diabetes was associated with significantly increased activities of catalase (CAT), glutathione reductase (GSSG-RD), and CuZn-superoxide dismutase (SOD) in the pancreas and of CAT and GSSG-RD in the heart. |
| 99 | 3301471 | On the other hand, the liver of diabetic rats showed a generalized decrease in CAT, glutathione peroxidase (GSH-PX), and SOD as well as in the levels of reduced glutathione (GSH). |
| 100 | 3301471 | Diabetic kidney also showed decreases in CAT and SOD, but the activities of GSH-PX were increased. |
| 101 | 3301471 | Diabetes was associated with significantly increased activities of catalase (CAT), glutathione reductase (GSSG-RD), and CuZn-superoxide dismutase (SOD) in the pancreas and of CAT and GSSG-RD in the heart. |
| 102 | 3301471 | On the other hand, the liver of diabetic rats showed a generalized decrease in CAT, glutathione peroxidase (GSH-PX), and SOD as well as in the levels of reduced glutathione (GSH). |
| 103 | 3301471 | Diabetic kidney also showed decreases in CAT and SOD, but the activities of GSH-PX were increased. |
| 104 | 3301471 | Diabetes was associated with significantly increased activities of catalase (CAT), glutathione reductase (GSSG-RD), and CuZn-superoxide dismutase (SOD) in the pancreas and of CAT and GSSG-RD in the heart. |
| 105 | 3301471 | On the other hand, the liver of diabetic rats showed a generalized decrease in CAT, glutathione peroxidase (GSH-PX), and SOD as well as in the levels of reduced glutathione (GSH). |
| 106 | 3301471 | Diabetic kidney also showed decreases in CAT and SOD, but the activities of GSH-PX were increased. |
| 107 | 3329563 | Pancreatic activities of CuZn-superoxide dismutase and glutathione reductase (GSSG-RD) were higher in ISDBB rats, while catalase (CAT) activities were elevated in both ISDBB and their NDLM compared with control animals. |
| 108 | 3332532 | Determination of glucose, insulin and superoxide dismutase in blood and pancreas of rats]. |
| 109 | 3423018 | These rats developed severe nephrotoxic injury as manifested by a marked increase of lipid peroxidation evident by an increase of malondialdehyde from a control level of 0.48 +/- 0.02 to 1.72 +/- 0.12 nmole/mg protein, a shift from unsaturated to saturated fatty acids esterified in renal cortical phospholipids, depression of superoxide dismutase and catalase, and a shift from reduced to oxidized glutathione. |
| 110 | 3512330 | Superoxide dismutase and catalase but not scavengers of hydroxyl radicals protected against the increase in dye uptake. |
| 111 | 3514329 | Effect of insulin and oral glutathione on glutathione levels and superoxide dismutase activities in organs of rats with streptozocin-induced diabetes. |
| 112 | 3514329 | The effect of insulin or glutathione treatment on glutathione content of liver and jejunal mucosa and on superoxide dismutase (SOD) activity of liver, kidney, and erythrocytes was investigated in pair-fed animals with streptozocin (STZ)-induced diabetes. |
| 113 | 3514329 | Treatment of diabetic rats with oral glutathione or intramuscular insulin increased cytosolic SOD activity of renal cortex and liver (but not erythrocytes) to control levels. |
| 114 | 3514329 | Effect of insulin and oral glutathione on glutathione levels and superoxide dismutase activities in organs of rats with streptozocin-induced diabetes. |
| 115 | 3514329 | The effect of insulin or glutathione treatment on glutathione content of liver and jejunal mucosa and on superoxide dismutase (SOD) activity of liver, kidney, and erythrocytes was investigated in pair-fed animals with streptozocin (STZ)-induced diabetes. |
| 116 | 3514329 | Treatment of diabetic rats with oral glutathione or intramuscular insulin increased cytosolic SOD activity of renal cortex and liver (but not erythrocytes) to control levels. |
| 117 | 3514329 | Effect of insulin and oral glutathione on glutathione levels and superoxide dismutase activities in organs of rats with streptozocin-induced diabetes. |
| 118 | 3514329 | The effect of insulin or glutathione treatment on glutathione content of liver and jejunal mucosa and on superoxide dismutase (SOD) activity of liver, kidney, and erythrocytes was investigated in pair-fed animals with streptozocin (STZ)-induced diabetes. |
| 119 | 3514329 | Treatment of diabetic rats with oral glutathione or intramuscular insulin increased cytosolic SOD activity of renal cortex and liver (but not erythrocytes) to control levels. |
| 120 | 3623415 | In a group of normal controls and in a group of diabetics subdivided for type we evaluated the following red blood cell parameters: superoxide dismutase (SOD), glutathione peroxidase (GSH.Px), catalase (C-ase), glutathione content (GSH) and membrane-protein-sulphydryl groups (P-SH). |
| 121 | 3623415 | There was no difference in the enzymatic activities of superoxide dismutase, glutathione peroxidase and catalase in normals and in the diabetics. |
| 122 | 3623415 | In a group of normal controls and in a group of diabetics subdivided for type we evaluated the following red blood cell parameters: superoxide dismutase (SOD), glutathione peroxidase (GSH.Px), catalase (C-ase), glutathione content (GSH) and membrane-protein-sulphydryl groups (P-SH). |
| 123 | 3623415 | There was no difference in the enzymatic activities of superoxide dismutase, glutathione peroxidase and catalase in normals and in the diabetics. |
| 124 | 3663400 | Reference intervals were established in an urban population in the Far East for SOD activity in erythrocytes using the pyrogallol method, and for glutathione peroxidase (GSH-Px) (EC 1.11.1.9) activity in erythrocytes using a standard glutathione reductase-linked method. |
| 125 | 3753756 | To investigate whether the development of the lung antioxidant enzyme system would be similarly delayed, and thus compromise their tolerance to high O2 exposure, we did the following: 1) produced the diabetic state in rats with streptozotocin injection 24 h after the onset of pregnancy; 2) examined fetal animals from streptozotocin and control rats at gestational days 19, 20, and 21, and newborn animals at day 22 for whole lung disaturated phosphatidylcholine and total phospholipid and for the three antioxidant enzymes: superoxide dismutase, catalase, glutathione peroxidase; and 3) exposed newborn offspring from streptozotocin-treated and control rats to greater than 95% O2 for several days and their survival, changes in antioxidant enzymes and disaturated phosphatidylcholine and light microscopic findings in response to hyperoxic challenge were compared. |
| 126 | 3780310 | Enzyme activities of erythrocyte superoxide dismutase (SOD), peroxidase and catalase in groups of diabetic children, the duration of the disease and control qualities were compared with respective values obtained for healthy children. |
| 127 | 3780310 | Generally the disease duration was clearly found to affect SOD activity, and catalase activity only a little. |
| 128 | 3780310 | SOD activity was diminished in diabetics when compared with control subjects, and in turn peroxidase and catalase activities were generally elevated. |
| 129 | 3780310 | Enzyme activities of erythrocyte superoxide dismutase (SOD), peroxidase and catalase in groups of diabetic children, the duration of the disease and control qualities were compared with respective values obtained for healthy children. |
| 130 | 3780310 | Generally the disease duration was clearly found to affect SOD activity, and catalase activity only a little. |
| 131 | 3780310 | SOD activity was diminished in diabetics when compared with control subjects, and in turn peroxidase and catalase activities were generally elevated. |
| 132 | 3780310 | Enzyme activities of erythrocyte superoxide dismutase (SOD), peroxidase and catalase in groups of diabetic children, the duration of the disease and control qualities were compared with respective values obtained for healthy children. |
| 133 | 3780310 | Generally the disease duration was clearly found to affect SOD activity, and catalase activity only a little. |
| 134 | 3780310 | SOD activity was diminished in diabetics when compared with control subjects, and in turn peroxidase and catalase activities were generally elevated. |
| 135 | 3803731 | The activities of catalase (CAT), superoxide dismutase (SOD), glutathione peroxidase (GSH-PX), and glutathione (GSSG) reductase as well as levels of reduced glutathione (GSH) were examined in several tissues and in erythrocytes. |
| 136 | 3828510 | [Quantitative changes in Cu, Zn-superoxide dismutase and catalase isolated from the liver of alloxan diabetic rats]. |
| 137 | 3828510 | The contents of Cu, Zn-superoxide dismutase and catalase isolated and purified from the rat liver at the terminal stages of alloxan diabetes were decreased by 40% and 15%, respectively, as compared to the control. |
| 138 | 3828510 | It can be concluded that the decrease in superoxide dismutase and catalase activity in experimental alloxan diabetes is mainly connected with the decline in the content of these proteins at the terminal stages of the disease, this, probably, being the result of DNA degradation and RNA transport disturbances under the effect of oxygen active forms. |
| 139 | 3828510 | [Quantitative changes in Cu, Zn-superoxide dismutase and catalase isolated from the liver of alloxan diabetic rats]. |
| 140 | 3828510 | The contents of Cu, Zn-superoxide dismutase and catalase isolated and purified from the rat liver at the terminal stages of alloxan diabetes were decreased by 40% and 15%, respectively, as compared to the control. |
| 141 | 3828510 | It can be concluded that the decrease in superoxide dismutase and catalase activity in experimental alloxan diabetes is mainly connected with the decline in the content of these proteins at the terminal stages of the disease, this, probably, being the result of DNA degradation and RNA transport disturbances under the effect of oxygen active forms. |
| 142 | 3828510 | [Quantitative changes in Cu, Zn-superoxide dismutase and catalase isolated from the liver of alloxan diabetic rats]. |
| 143 | 3828510 | The contents of Cu, Zn-superoxide dismutase and catalase isolated and purified from the rat liver at the terminal stages of alloxan diabetes were decreased by 40% and 15%, respectively, as compared to the control. |
| 144 | 3828510 | It can be concluded that the decrease in superoxide dismutase and catalase activity in experimental alloxan diabetes is mainly connected with the decline in the content of these proteins at the terminal stages of the disease, this, probably, being the result of DNA degradation and RNA transport disturbances under the effect of oxygen active forms. |
| 145 | 3905479 | Exogenous copper-zinc superoxide dismutase reproducibly protected the morphological features of pancreatic beta cells against damage by alloxan as determined by light microscopic immunostaining for insulin and by ultrastructural examination. |
| 146 | 4046501 | The lipoperoxide values and glutathione peroxidase activity in blood plasma, along with the glutathione peroxidase, catalase and cupro-zinc superoxide dismutase activities in erythrocytes were investigated in 60 women with Type 2 (non-insulin-dependent) diabetes mellitus and in 71 healthy women. |
| 147 | 4046501 | In contrast to the findings of other authors on the activities of the protective enzymes in erythrocytes against oxidative damage, there were no significant differences of erythrocytes glutathione peroxidase, catalase and superoxide dismutase activities between diabetic and control women. |
| 148 | 4046501 | The lipoperoxide values and glutathione peroxidase activity in blood plasma, along with the glutathione peroxidase, catalase and cupro-zinc superoxide dismutase activities in erythrocytes were investigated in 60 women with Type 2 (non-insulin-dependent) diabetes mellitus and in 71 healthy women. |
| 149 | 4046501 | In contrast to the findings of other authors on the activities of the protective enzymes in erythrocytes against oxidative damage, there were no significant differences of erythrocytes glutathione peroxidase, catalase and superoxide dismutase activities between diabetic and control women. |
| 150 | 6213639 | When islets were protected from alloxan toxicity by including 28 mM glucose with alloxan, the insulin secretory response and SOD specific activity remained identical to controls. |
| 151 | 6213639 | To test the effectiveness of SOD against streptozotocin in vitro, canine islets were incubated 10 min with or without streptozotocin (0.1 mg/ml) with 4 mM glucose; their functional integrity was tested subsequently as the insulin secretory response to 28 mM glucose. |
| 152 | 6213639 | When islets were protected from alloxan toxicity by including 28 mM glucose with alloxan, the insulin secretory response and SOD specific activity remained identical to controls. |
| 153 | 6213639 | To test the effectiveness of SOD against streptozotocin in vitro, canine islets were incubated 10 min with or without streptozotocin (0.1 mg/ml) with 4 mM glucose; their functional integrity was tested subsequently as the insulin secretory response to 28 mM glucose. |
| 154 | 6229439 | The presence of superoxide dismutase (1000 U/ml) and/or catalase (100 U/ml) markedly suppressed alloxan-induced chemiluminescence. |
| 155 | 6281256 | Protection by superoxide dismutase, catalase, and poly(ADP-ribose) synthetase inhibitors against alloxan- and streptozotocin-induced islet DNA strand breaks and against the inhibition of proinsulin synthesis. |
| 156 | 6281256 | We have shown previously that alloxan and streptozotocin, two major diabetogenic agents, cause DNA strand breaks in rat pancreatic islets and stimulate nuclear poly(ADP-ribose) synthetase, thereby depleting intracellular NAD level and inhibiting proinsulin synthesis (Okamoto, H. (1981) Mol. |
| 157 | 6281256 | In the present study, superoxide dismutase and catalase, scavengers of radical oxygens, were found to protect against islet DNA strand breaks and inhibition of proinsulin synthesis induced by alloxan. |
| 158 | 6281256 | On the other hand, compounds that inhibit islet nuclear poly(ADP-ribose) synthetase were found to protect against alloxan- as well as streptozotocin-induced inhibition of proinsulin synthesis. |
| 159 | 6281256 | Protection by superoxide dismutase, catalase, and poly(ADP-ribose) synthetase inhibitors against alloxan- and streptozotocin-induced islet DNA strand breaks and against the inhibition of proinsulin synthesis. |
| 160 | 6281256 | We have shown previously that alloxan and streptozotocin, two major diabetogenic agents, cause DNA strand breaks in rat pancreatic islets and stimulate nuclear poly(ADP-ribose) synthetase, thereby depleting intracellular NAD level and inhibiting proinsulin synthesis (Okamoto, H. (1981) Mol. |
| 161 | 6281256 | In the present study, superoxide dismutase and catalase, scavengers of radical oxygens, were found to protect against islet DNA strand breaks and inhibition of proinsulin synthesis induced by alloxan. |
| 162 | 6281256 | On the other hand, compounds that inhibit islet nuclear poly(ADP-ribose) synthetase were found to protect against alloxan- as well as streptozotocin-induced inhibition of proinsulin synthesis. |
| 163 | 6324223 | The ability of cardiac and skeletal muscles from diabetic rats to metabolize superoxide and hydrogen peroxide was determined by the activities of superoxide dismutase (SOD) and catalase, respectively. |
| 164 | 6327438 | PMNL obtained from insulin-treated diabetic patients showed considerable alleviation of SOD levels. |
| 165 | 6338671 | CuZn superoxide dismutase, Mn superoxide dismutase, catalase and glutathione peroxidase in lymphocytes and erythrocytes in insulin-dependent diabetic children. |
| 166 | 6338671 | CuZn superoxide dismutase, Mn superoxide dismutase, catalase and glutathione peroxidase activities in lymphocytes and erythrocytes were studied in 9 children with insulin-dependent diabetes mellitus (IDDM) as well as in 21 healthy children. |
| 167 | 6338671 | The mean erythrocyte CuZn superoxide dismutase and glutathione peroxidase were statistically significantly lower in the IDDM group compared with the controls although almost all IDDM results fell within the mean +/- 2 SD limits of the controls. |
| 168 | 6338671 | Erythrocyte catalase as well as lymphocyte CuZn superoxide dismutase and Mn superoxide dismutase did not differ from the controls. |
| 169 | 6444904 | A dose of 45 mg/kg streptozotocin alone produced marked glucose intolerance and a decrease in pancreatic insulin content to less than 10% of control; both of these effects were abolished by prior administration of 105 mu/g of superoxide dismutase. |
| 170 | 6444904 | The fall in pancreatic insulin content seen with streptozotocin alone was, however, partially reversed by superoxide dismutase. |
| 171 | 6444904 | A dose of 45 mg/kg streptozotocin alone produced marked glucose intolerance and a decrease in pancreatic insulin content to less than 10% of control; both of these effects were abolished by prior administration of 105 mu/g of superoxide dismutase. |
| 172 | 6444904 | The fall in pancreatic insulin content seen with streptozotocin alone was, however, partially reversed by superoxide dismutase. |
| 173 | 6454601 | Moreover, a loss in pancreatic insulin content and a tripling of pancreatic glucagon content occurred in all mice treated with low dosages of Sz, irrespective of whether or not either SOD or a long-acting derivative of SOD was administered. |
| 174 | 6488563 | Plasma EC-superoxide dismutase activity in insulin-dependent diabetic children. |
| 175 | 6488563 | Toxic oxygen-centered radicals have been linked to beta-cell damage brought about by some chemicals and might conceivably also be of importance in the pathogenesis of spontaneous insulin-dependent diabetes mellitus (IDDM). |
| 176 | 6991324 | Inhibition of alloxan action in isolated pancreatic islets by superoxide dismutase, catalase, and a metal chelator. |
| 177 | 6991324 | The presence of superoxide dismutase (1000 U/ml), catalase (50 microgram/ml), or a metal chelator diethylenetriaminepentacetic acid (1 mM) markedly attenuated this effect of alloxan. |
| 178 | 6991324 | Inhibition of alloxan action in isolated pancreatic islets by superoxide dismutase, catalase, and a metal chelator. |
| 179 | 6991324 | The presence of superoxide dismutase (1000 U/ml), catalase (50 microgram/ml), or a metal chelator diethylenetriaminepentacetic acid (1 mM) markedly attenuated this effect of alloxan. |
| 180 | 7049672 | The current study was undertaken to determine if superoxide dismutase (SOD), the enzyme that converts superoxide to hydrogen peroxide, is altered in the mucosa of the alimentary tract and renal cortex of the diabetic rat, and if so, whether SOD responds to insulin treatment. |
| 181 | 7049672 | Total SOD and cyanide-insensitive [manganese-containing SOD (Mn SOD)] SOD were measured by the nitroblue tetrazolium inhibition assay. |
| 182 | 7049672 | The level of Mn-SOD was not affected by diabetes or insulin treatment, but the cyanide-sensitive [copper- and zinc containing SOD (Cu-Zn SOD] SOD was depressed in the small intestine and colon of diabetic rats. |
| 183 | 7049672 | Insulin treatment restored total and Cu-Zn SOD activity in the small intestine to normal and increased Cu-Zn SOD activity in the colon to normal. |
| 184 | 7049672 | In renal cortex, diabetes did not alter total SOD, but increased Mn SOD and decreased Cu-Zn SOD. |
| 185 | 7049672 | The mucosa of the small intestine and colon show decreased Cu-Zn SOD, the SOD of the cecum is unaffected, and the kidney shows increased Mn SOD and decreased Cu-Zn SOD. |
| 186 | 7049672 | The SOD responses of diabetics are reversed by insulin treatment. |
| 187 | 7049672 | The current study was undertaken to determine if superoxide dismutase (SOD), the enzyme that converts superoxide to hydrogen peroxide, is altered in the mucosa of the alimentary tract and renal cortex of the diabetic rat, and if so, whether SOD responds to insulin treatment. |
| 188 | 7049672 | Total SOD and cyanide-insensitive [manganese-containing SOD (Mn SOD)] SOD were measured by the nitroblue tetrazolium inhibition assay. |
| 189 | 7049672 | The level of Mn-SOD was not affected by diabetes or insulin treatment, but the cyanide-sensitive [copper- and zinc containing SOD (Cu-Zn SOD] SOD was depressed in the small intestine and colon of diabetic rats. |
| 190 | 7049672 | Insulin treatment restored total and Cu-Zn SOD activity in the small intestine to normal and increased Cu-Zn SOD activity in the colon to normal. |
| 191 | 7049672 | In renal cortex, diabetes did not alter total SOD, but increased Mn SOD and decreased Cu-Zn SOD. |
| 192 | 7049672 | The mucosa of the small intestine and colon show decreased Cu-Zn SOD, the SOD of the cecum is unaffected, and the kidney shows increased Mn SOD and decreased Cu-Zn SOD. |
| 193 | 7049672 | The SOD responses of diabetics are reversed by insulin treatment. |
| 194 | 7049672 | The current study was undertaken to determine if superoxide dismutase (SOD), the enzyme that converts superoxide to hydrogen peroxide, is altered in the mucosa of the alimentary tract and renal cortex of the diabetic rat, and if so, whether SOD responds to insulin treatment. |
| 195 | 7049672 | Total SOD and cyanide-insensitive [manganese-containing SOD (Mn SOD)] SOD were measured by the nitroblue tetrazolium inhibition assay. |
| 196 | 7049672 | The level of Mn-SOD was not affected by diabetes or insulin treatment, but the cyanide-sensitive [copper- and zinc containing SOD (Cu-Zn SOD] SOD was depressed in the small intestine and colon of diabetic rats. |
| 197 | 7049672 | Insulin treatment restored total and Cu-Zn SOD activity in the small intestine to normal and increased Cu-Zn SOD activity in the colon to normal. |
| 198 | 7049672 | In renal cortex, diabetes did not alter total SOD, but increased Mn SOD and decreased Cu-Zn SOD. |
| 199 | 7049672 | The mucosa of the small intestine and colon show decreased Cu-Zn SOD, the SOD of the cecum is unaffected, and the kidney shows increased Mn SOD and decreased Cu-Zn SOD. |
| 200 | 7049672 | The SOD responses of diabetics are reversed by insulin treatment. |
| 201 | 7049672 | The current study was undertaken to determine if superoxide dismutase (SOD), the enzyme that converts superoxide to hydrogen peroxide, is altered in the mucosa of the alimentary tract and renal cortex of the diabetic rat, and if so, whether SOD responds to insulin treatment. |
| 202 | 7049672 | Total SOD and cyanide-insensitive [manganese-containing SOD (Mn SOD)] SOD were measured by the nitroblue tetrazolium inhibition assay. |
| 203 | 7049672 | The level of Mn-SOD was not affected by diabetes or insulin treatment, but the cyanide-sensitive [copper- and zinc containing SOD (Cu-Zn SOD] SOD was depressed in the small intestine and colon of diabetic rats. |
| 204 | 7049672 | Insulin treatment restored total and Cu-Zn SOD activity in the small intestine to normal and increased Cu-Zn SOD activity in the colon to normal. |
| 205 | 7049672 | In renal cortex, diabetes did not alter total SOD, but increased Mn SOD and decreased Cu-Zn SOD. |
| 206 | 7049672 | The mucosa of the small intestine and colon show decreased Cu-Zn SOD, the SOD of the cecum is unaffected, and the kidney shows increased Mn SOD and decreased Cu-Zn SOD. |
| 207 | 7049672 | The SOD responses of diabetics are reversed by insulin treatment. |
| 208 | 7049672 | The current study was undertaken to determine if superoxide dismutase (SOD), the enzyme that converts superoxide to hydrogen peroxide, is altered in the mucosa of the alimentary tract and renal cortex of the diabetic rat, and if so, whether SOD responds to insulin treatment. |
| 209 | 7049672 | Total SOD and cyanide-insensitive [manganese-containing SOD (Mn SOD)] SOD were measured by the nitroblue tetrazolium inhibition assay. |
| 210 | 7049672 | The level of Mn-SOD was not affected by diabetes or insulin treatment, but the cyanide-sensitive [copper- and zinc containing SOD (Cu-Zn SOD] SOD was depressed in the small intestine and colon of diabetic rats. |
| 211 | 7049672 | Insulin treatment restored total and Cu-Zn SOD activity in the small intestine to normal and increased Cu-Zn SOD activity in the colon to normal. |
| 212 | 7049672 | In renal cortex, diabetes did not alter total SOD, but increased Mn SOD and decreased Cu-Zn SOD. |
| 213 | 7049672 | The mucosa of the small intestine and colon show decreased Cu-Zn SOD, the SOD of the cecum is unaffected, and the kidney shows increased Mn SOD and decreased Cu-Zn SOD. |
| 214 | 7049672 | The SOD responses of diabetics are reversed by insulin treatment. |
| 215 | 7049672 | The current study was undertaken to determine if superoxide dismutase (SOD), the enzyme that converts superoxide to hydrogen peroxide, is altered in the mucosa of the alimentary tract and renal cortex of the diabetic rat, and if so, whether SOD responds to insulin treatment. |
| 216 | 7049672 | Total SOD and cyanide-insensitive [manganese-containing SOD (Mn SOD)] SOD were measured by the nitroblue tetrazolium inhibition assay. |
| 217 | 7049672 | The level of Mn-SOD was not affected by diabetes or insulin treatment, but the cyanide-sensitive [copper- and zinc containing SOD (Cu-Zn SOD] SOD was depressed in the small intestine and colon of diabetic rats. |
| 218 | 7049672 | Insulin treatment restored total and Cu-Zn SOD activity in the small intestine to normal and increased Cu-Zn SOD activity in the colon to normal. |
| 219 | 7049672 | In renal cortex, diabetes did not alter total SOD, but increased Mn SOD and decreased Cu-Zn SOD. |
| 220 | 7049672 | The mucosa of the small intestine and colon show decreased Cu-Zn SOD, the SOD of the cecum is unaffected, and the kidney shows increased Mn SOD and decreased Cu-Zn SOD. |
| 221 | 7049672 | The SOD responses of diabetics are reversed by insulin treatment. |
| 222 | 7049672 | The current study was undertaken to determine if superoxide dismutase (SOD), the enzyme that converts superoxide to hydrogen peroxide, is altered in the mucosa of the alimentary tract and renal cortex of the diabetic rat, and if so, whether SOD responds to insulin treatment. |
| 223 | 7049672 | Total SOD and cyanide-insensitive [manganese-containing SOD (Mn SOD)] SOD were measured by the nitroblue tetrazolium inhibition assay. |
| 224 | 7049672 | The level of Mn-SOD was not affected by diabetes or insulin treatment, but the cyanide-sensitive [copper- and zinc containing SOD (Cu-Zn SOD] SOD was depressed in the small intestine and colon of diabetic rats. |
| 225 | 7049672 | Insulin treatment restored total and Cu-Zn SOD activity in the small intestine to normal and increased Cu-Zn SOD activity in the colon to normal. |
| 226 | 7049672 | In renal cortex, diabetes did not alter total SOD, but increased Mn SOD and decreased Cu-Zn SOD. |
| 227 | 7049672 | The mucosa of the small intestine and colon show decreased Cu-Zn SOD, the SOD of the cecum is unaffected, and the kidney shows increased Mn SOD and decreased Cu-Zn SOD. |
| 228 | 7049672 | The SOD responses of diabetics are reversed by insulin treatment. |
| 229 | 7068100 | The lipid peroxidation and (of the peroxide metabolism enzymes) the catalase, superoxide dismutase and glutathione peroxidase activities were determined in red blood cell haemolysates from 20-35-year-old human diabetics of both sexes. |
| 230 | 7619452 | Humans are well endowed with antioxidant defences against AOS; these antioxidants, or free radical scavengers, include ascorbic acid (vitamin C), alpha-tocopherol (vitamin E), beta-carotene, coenzyme Q10, enzymes such as catalase and superoxide dismutase, and trace elements including selenium and zinc. |
| 231 | 7621992 | Three key endogenous antioxidant enzymes (e.g., superoxide dismutase, catalase, and glutathione peroxidase) were measured. |
| 232 | 7628782 | We already reported about the allelic distribution, changes of plaque formation and body weight, biochemical nature, toxic activity, vascular permeability factor and bradykinin inactivating factor of the plaque, histological and immunological studies, the pH in the periodontal pocket, amount of saliva, IgA in the saliva, salivary kallikrein, the relationship between sialic acid in the saliva and the serum, leukocyte functions (chemotaxis and superoxide anion) in ODUS/Odu, histamine, mast cell, free radicals, superoxide dismutase activities in gingiva and gingival nerve fibers with substance P or calcitonin gene-related peptide, and effect of diabetes. |
| 233 | 7742795 | Effect of ferritin on lambda DNA strand breaks in the reaction system of alloxan plus NADPH-cytochrome P450 reductase: ferritin's role in diabetogenic action of alloxan. |
| 234 | 7742795 | The incubation of lambda DNA in the reaction system of alloxan plus NADPH-cytochrome P450 reductase (fp2) in the presence of ferritin caused strand breaks after a lag time of about 5 min. |
| 235 | 7742795 | Catalase, scavengers of hydroxyl radicals (HO.) and iron-chelators almost completely inhibited the DNA strand breaks, but superoxide dismutase (SOD) did not, suggesting that the strand breaks are induced by the generation of HO. via the reaction of H2O2 and Fe(II), namely, the Fenton reaction. |
| 236 | 7756973 | Glucose-induced insulin secretion is inhibited by the cytokines interleukin-1 beta (IL-1 beta), interleukin-6 and tumour necrosis factor alpha (TNF) when combined with IL-1 beta in cultured rat islets, by IL-1 beta, TNF and interferon gamma in mouse islets, and by combined treatment of IL-1 beta, TNF and interferon gamma in human islets. |
| 237 | 7756973 | A key factor in the inhibitory effect of IL-1 beta and TNF in rat islets is the generation of nitric oxide which inactivates enzymes such as aconitase and ribonucleotide reductase by formation of iron-nitrosyl complexes. |
| 238 | 7756973 | Potentially important defence and repair responses induced by IL-1 beta treatment of rat islets are formation of heat shock protein, haem oxygenase, and superoxide dismutase. |
| 239 | 7790873 | The specific activities of superoxide dismutase, catalase, and glutathione S-transferase (mu subtype) were significantly lower in the brains of mice with type II diabetes than in the brains of control mice. |
| 240 | 7851943 | Superoxide dismutase was found to be the most effective in inhibiting lysosomal release as compared to catalase and peroxidase. |
| 241 | 7859891 | These effects of hyperglycaemia are reversed by a number of antioxidants, including superoxide dismutase, catalase and glutathione. |
| 242 | 7898413 | Free radicals are normally neutralized by efficient systems in the body that include the antioxidant enzymes (superoxide dismutase, catalase, and glutathione peroxidase) and the nutrient-derived antioxidant small molecules (vitamin E, vitamin C, carotenes, flavonoids, glutathione, uric acid, and taurine). |
| 243 | 7899460 | Rats with a PBLC > 4,200 mm3 have a much lower incidence of insulin-dependent diabetes mellitus (IDDM) and are designated "nonlymphopenic" or BBNL. |
| 244 | 7899460 | In separate cohorts of normoglycemic (prediabetic) BBL rats (high risk for developing diabetes) and BBNL rats (low risk for developing diabetes), the activities of pancreatic cytosolic antioxidant enzymes, copper-zinc superoxide dismutase (CuZnSOD), catalase (CAT), and glutathione peroxidase (GPX) were determined. |
| 245 | 7899450 | Activities of superoxide dismutase and glutathione peroxidase were measured in 60 children aged 5 to 15 with insulin-dependent diabetes of various degrees of compensation and duration. |
| 246 | 7938051 | Pancreatic superoxide dismutase (SOD) and glutathione peroxidase (GSHPx) activities were measured during the development of diabetes in diabetes-prone BB rats (BBdp) prior to insulin dependence. |
| 247 | 7938051 | These changes in CuZnSOD and MnSOD activity resulted in BBdp rats having twice the pancreatic total SOD activity compared with BBc rats (P < 0.0001). |
| 248 | 7938051 | Pancreatic superoxide dismutase (SOD) and glutathione peroxidase (GSHPx) activities were measured during the development of diabetes in diabetes-prone BB rats (BBdp) prior to insulin dependence. |
| 249 | 7938051 | These changes in CuZnSOD and MnSOD activity resulted in BBdp rats having twice the pancreatic total SOD activity compared with BBc rats (P < 0.0001). |
| 250 | 7945563 | Insulin and IGF-I at 10(-7) M caused a 33% and 48% increase in TBARS production, respectively. |
| 251 | 7945563 | Proinsulin and IGF-II at 10(-6) M had no effect. |
| 252 | 7945563 | Insulin-stimulated LDL oxidation was inhibited by superoxide dismutase (SOD), but insulin had no effect on MC superoxide production. |
| 253 | 7945563 | Our in vitro experiments suggest that high levels of insulin and IGF-I stimulate MC-mediated oxidation of LDL, an effect that is potentially atherogenic. |
| 254 | 7964275 | Superoxide dismutase, catalase and glutathione peroxidase activities in the lymphoid organs of diabetic rats. |
| 255 | 7964275 | The effect of alloxan-induced diabetes on CuZn- and Mn-superoxide dismutase (SOD), catalase and glutathione peroxidase (GPX) activities, as well as the content of thiobarbituric acid reactive substances (TBARs) were examined in rat lymphoid organs (mesenteric lymph nodes (MLN), thymus and spleen) and, for comparison, red and white muscle fibres. |
| 256 | 7964275 | The capacity for generation of reduced equivalents was also evaluated by measuring the activities of glucose-6-phosphate dehydrogenase (pentose-phosphate pathway-cytosol) and citrate synthase (Krebs cycle-mitochondria). |
| 257 | 7964275 | In relation to the lymphoid organs, the spleen showed a decrease in the antioxidant enzyme activities (except for glutathione peroxidase), whereas the thymus showed an increased level (except for Mn-SOD), and the MLN presented a reduction in Mn-SOD and catalase activities and an increase in GPX activity caused by diabetes. |
| 258 | 7964275 | Superoxide dismutase, catalase and glutathione peroxidase activities in the lymphoid organs of diabetic rats. |
| 259 | 7964275 | The effect of alloxan-induced diabetes on CuZn- and Mn-superoxide dismutase (SOD), catalase and glutathione peroxidase (GPX) activities, as well as the content of thiobarbituric acid reactive substances (TBARs) were examined in rat lymphoid organs (mesenteric lymph nodes (MLN), thymus and spleen) and, for comparison, red and white muscle fibres. |
| 260 | 7964275 | The capacity for generation of reduced equivalents was also evaluated by measuring the activities of glucose-6-phosphate dehydrogenase (pentose-phosphate pathway-cytosol) and citrate synthase (Krebs cycle-mitochondria). |
| 261 | 7964275 | In relation to the lymphoid organs, the spleen showed a decrease in the antioxidant enzyme activities (except for glutathione peroxidase), whereas the thymus showed an increased level (except for Mn-SOD), and the MLN presented a reduction in Mn-SOD and catalase activities and an increase in GPX activity caused by diabetes. |
| 262 | 7987655 | Two groups of patients with insulin-dependent diabetes mellitus of > 10 years duration and either persistent normoalbuminuria (group 1, n = 49; albumin excretion < 30 mg/day) or microalbuminuria (group 2, n = 33; albumin excretion 30-300 mg/day) were investigated for evidence of free oxygen radical activity (erythrocytic superoxide dismutase and glutathione peroxidase) and oxidant injury (serum malondialdehyde). |
| 263 | 7988042 | Extracellular-superoxide dismutase (EC-SOD) is a secretory glycoprotein that is the major SOD isozyme in extracellular fluids. |
| 264 | 7988055 | Early changes of serum N-acetyl-beta-glucosaminidase, tissue plasminogen activator and erythrocyte superoxide dismutase in relation to retinopathy in type 1 diabetes mellitus. |
| 265 | 7988055 | We investigated activities of serum N-acetyl-beta-glucosaminidase (NAG), tissue plasminogen activator and erythrocyte superoxide dismutase in well defined groups of type 1 diabetic patients. |
| 266 | 7988055 | Early changes of serum N-acetyl-beta-glucosaminidase, tissue plasminogen activator and erythrocyte superoxide dismutase in relation to retinopathy in type 1 diabetes mellitus. |
| 267 | 7988055 | We investigated activities of serum N-acetyl-beta-glucosaminidase (NAG), tissue plasminogen activator and erythrocyte superoxide dismutase in well defined groups of type 1 diabetic patients. |
| 268 | 8063201 | This impairment is restored towards normal by prostaglandin (PG) H2/thromboxane A2 receptor blockade or superoxide dismutase, indicating that the PGH2 and/or superoxide anion (O2-.) generated contributes to the abnormality. |
| 269 | 8067247 | Similar changes were found in catalase activity, while the activity changes of superoxide dismutase (SOD) were identical in tendency to the above ones; in fact, it hardly showed any alterations. |
| 270 | 8118109 | Maternal and fetal tissues were assessed for copper concentrations, the activities of the cuproenzymes copper, zinc superoxide dismutase and ceruloplasmin, and the copper binding protein metallothionein. |
| 271 | 8118109 | Dams fed the low copper diet had low tissue copper concentrations, and low plasma ceruloplasmin and erythrocyte superoxide dismutase activities compared to copper-adequate dams. |
| 272 | 8118109 | Maternal and fetal tissues were assessed for copper concentrations, the activities of the cuproenzymes copper, zinc superoxide dismutase and ceruloplasmin, and the copper binding protein metallothionein. |
| 273 | 8118109 | Dams fed the low copper diet had low tissue copper concentrations, and low plasma ceruloplasmin and erythrocyte superoxide dismutase activities compared to copper-adequate dams. |
| 274 | 8119455 | To add new insights to the question, changes in lipid peroxidation products and activities of three antioxidant enzymes: catalase (CAT), glutathione peroxidase (GPX) and superoxide dismutase (SOD) in maternal red blood cells haemolysates were evaluated in pregnant women with insulin-dependent diabetes mellitus (IDDM-PW) and in healthy pregnant women (HPW). |
| 275 | 8119455 | Pregnancy provoked an increase of lipoperoxidation products and an high SOD activity since early pregnancy, while CAT and GPX activities did not change during gestation. |
| 276 | 8119455 | IDDM-PW showed higher content of lipoperoxidation breakdown products and lower SOD activity at each trimester, if compared with HPW; moreover, a slight increase of CAT and SOD activity is reported during late diabetic pregnancy. |
| 277 | 8119455 | To add new insights to the question, changes in lipid peroxidation products and activities of three antioxidant enzymes: catalase (CAT), glutathione peroxidase (GPX) and superoxide dismutase (SOD) in maternal red blood cells haemolysates were evaluated in pregnant women with insulin-dependent diabetes mellitus (IDDM-PW) and in healthy pregnant women (HPW). |
| 278 | 8119455 | Pregnancy provoked an increase of lipoperoxidation products and an high SOD activity since early pregnancy, while CAT and GPX activities did not change during gestation. |
| 279 | 8119455 | IDDM-PW showed higher content of lipoperoxidation breakdown products and lower SOD activity at each trimester, if compared with HPW; moreover, a slight increase of CAT and SOD activity is reported during late diabetic pregnancy. |
| 280 | 8119455 | To add new insights to the question, changes in lipid peroxidation products and activities of three antioxidant enzymes: catalase (CAT), glutathione peroxidase (GPX) and superoxide dismutase (SOD) in maternal red blood cells haemolysates were evaluated in pregnant women with insulin-dependent diabetes mellitus (IDDM-PW) and in healthy pregnant women (HPW). |
| 281 | 8119455 | Pregnancy provoked an increase of lipoperoxidation products and an high SOD activity since early pregnancy, while CAT and GPX activities did not change during gestation. |
| 282 | 8119455 | IDDM-PW showed higher content of lipoperoxidation breakdown products and lower SOD activity at each trimester, if compared with HPW; moreover, a slight increase of CAT and SOD activity is reported during late diabetic pregnancy. |
| 283 | 8150225 | Bovine superoxide dismutase and catalase were each coupled to polyethylene glycol. |
| 284 | 8150417 | All these results were consistent with the in vivo studies that Cu,Zn-superoxide dismutase activity in erythrocytes of non-insulin dependent diabetic patients was inversely correlated with their plasma glucose. |
| 285 | 8168209 | The hemolysis, hemoglobin oxidation and lipid peroxidation of erythrocytes induced by hydrogen peroxide and Fe(++)-induced MDA formation of liver microsomes were inhibited by AH-9, and the activity of SOD and catalase were shown to be increased in normal and alloxan-diabetic mice after treatment with AH-9. |
| 286 | 8231839 | On the other hand, activities of the antioxidative enzymes catalase and superoxide dismutase (SOD) were decreased. |
| 287 | 8232245 | The loss of relaxation to acetylcholine in diabetic aorta was prevented or attenuated by pretreatment with catalase, dimethylthiourea or desferrioxamine, but not by mannitol or superoxide dismutase. |
| 288 | 8252716 | Although superoxide dismutase (SOD; EC 1.15.1.1) and catalase (EC 1.11.1.6) decreased the yield of the product, monoformazan dye (MF+), the yield of MF+ was slightly greater under anaerobic than aerobic conditions, excluding a role for superoxide as an intermediate in the reduction of NBT during the fructosamine assay. |
| 289 | 8252716 | The inhibitory effects of SOD and catalase are most likely the result of oxygen regeneration in the assay mixture. |
| 290 | 8252716 | Although superoxide dismutase (SOD; EC 1.15.1.1) and catalase (EC 1.11.1.6) decreased the yield of the product, monoformazan dye (MF+), the yield of MF+ was slightly greater under anaerobic than aerobic conditions, excluding a role for superoxide as an intermediate in the reduction of NBT during the fructosamine assay. |
| 291 | 8252716 | The inhibitory effects of SOD and catalase are most likely the result of oxygen regeneration in the assay mixture. |
| 292 | 8280723 | Considerably increased levels of malondialdehyde (MDA), as well as of superoxide dismutase (SOD) and catalase (CAT) activity were found in the myocardium of diabetic animals. |
| 293 | 8280723 | The reduced glutathione (GSH) level as well as the activity of glutathione S-transferase (GST) were significantly lower. |
| 294 | 8280723 | CAT and SOD activity values were unchanged. |
| 295 | 8280723 | Considerably increased levels of malondialdehyde (MDA), as well as of superoxide dismutase (SOD) and catalase (CAT) activity were found in the myocardium of diabetic animals. |
| 296 | 8280723 | The reduced glutathione (GSH) level as well as the activity of glutathione S-transferase (GST) were significantly lower. |
| 297 | 8280723 | CAT and SOD activity values were unchanged. |
| 298 | 8287643 | Forty normotensive patients with insulin-dependent diabetes mellitus of between 10 and 20 years duration with persistent normoalbuminuria (albumin excretion < 30 mg/day) and normal renal function were investigated for markers of endothelial dysfunction (plasma von Willebrand factor, soluble thrombomodulin and angiotensin-converting enzyme activity), free oxygen radical generation (erythrocytic superoxide dismutase and glutathione peroxidase) and oxidant injury (serum malondialdehyde). |
| 299 | 8287643 | Group 1 comprised 21 patients with elevated markers of endothelial dysfunction, and group 2 comprised 19 patients with normal levels of plasma von Willebrand factor, soluble thrombomodulin and angiotensin-converting enzyme activity. |
| 300 | 8296227 | The parameters of the antioxidant defense enzymes changed on the treatment week 12: catalase activity rose by 41%, that of superoxide dismutase and glutathione peroxidase lowered by 35 and 65%, respectively. |
| 301 | 8312692 | The purpose of this study was to verify the effect of Jin-Qi-Jiang-Tang-Pian (JQJTP) on fasting blood glucose (FBG), postcibal blood glucose (PBG), total cholesterol (TC), triglycerides (TG), acetylcholine esterase (AchE), insulin, RBC-superoxide dismutase (RBC-SOD) and malondialdehyde (MDA). |
| 302 | 8342636 | Pretreatment with superoxide dismutase, catalase, indomethacin, or meclofenamic acid preserved EDRF-mediated vasodilation during exposure to a D-glucose concentration of 500 mg/100 ml at almost all the ACh dosages tested. |
| 303 | 8348756 | Scavenging of extracellular oxygen radicals by superoxide dismutase and catalase did not improve islet cell survival. |
| 304 | 8351410 | Lithium therapy effectively normalized the decreased activities of catalase (CAT) and glutathione peroxidase (GSH-PX) but could not restore the lowered superoxide dismutase (SOD) in the liver of diabetic rats; while in kidney, the treatment proved to be ineffective. |
| 305 | 8351410 | Inclusion of vanadate produced synergistic effect and caused partial restoration of the altered CAT, GSH-PX and CuZn-SOD levels in diabetic kidney and the depressed SOD activity in diabetic liver. |
| 306 | 8351410 | Lithium therapy effectively normalized the decreased activities of catalase (CAT) and glutathione peroxidase (GSH-PX) but could not restore the lowered superoxide dismutase (SOD) in the liver of diabetic rats; while in kidney, the treatment proved to be ineffective. |
| 307 | 8351410 | Inclusion of vanadate produced synergistic effect and caused partial restoration of the altered CAT, GSH-PX and CuZn-SOD levels in diabetic kidney and the depressed SOD activity in diabetic liver. |
| 308 | 8371013 | In mammalian tissues three superoxide dismutases (SODs) designated Cu,Zn-SOD, Mn-SOD and extracellular SOD exist. |
| 309 | 8454224 | Activities of the antioxidant enzymes, glutathione reductase, glutathione peroxidase, and superoxide dismutase, were lower in liver mitochondria from diabetic compared to normal rats. |
| 310 | 8468025 | To test the feasibility of this idea, we have compared the activities of superoxide dismutase, catalase, glutathione peroxidase, and glutathione reductase in isolated islets, pancreas, and other tissues of age- and sex-matched NOD, BALB/c, C57BL/10, and B10.GD mice. |
| 311 | 8485869 | We studied the acute influence of improved glycemic control on the concentrations of plasma lipid peroxidation intermediates [malondialdehydes (MDA), organic hydroperoxides (OHP)] in ketotic insulin-dependent diabetic patients, as well as the interplay of enzymes such as glutathione peroxidase (GPX) and CuZn superoxide dismutase (CuZn-SOD), and trace elements (Zn, Se, Cu) postulated to be involved in free radical protection. |
| 312 | 8569756 | We therefore investigated the levels of lipid peroxidation by measuring thiobarbituric acid reactive substances (TBARS) and activity of antioxidant enzymes [superoxide dismutase (SOD), glutathione peroxidase (GSH-Px) and catalase (CAT)] in tissues and blood of streptozotocin (STZ)-induced diabetic rats. |
| 313 | 8577802 | Significant changes also occurred in glutathione levels (increased in heart and decreased in liver) and in the activities of catalase (reduced in liver and kidney), glutathione reductase (elevated in heart and liver), and glutathione peroxidase (decreased in liver and lung), but not Cu,Zn-superoxide dismutase. |
| 314 | 8603769 | The activity and the mRNA expression of the antioxidant enzymes CuZn-superoxide-dismutase, Mn-superoxide-dismutase, catalase, and glutathione peroxidase were evaluated after 2, 7, and 14 days of culture. |
| 315 | 8603769 | High glucose at days 7 and 14 induced an overexpression of CuZn-superoxide-dismutase, catalase, and glutathione peroxidase in both human endothelial cells from umbilical vein and immortalized human endothelial cells, while in transfected cells it did not. |
| 316 | 8649761 | No alteration was observed in the superoxide dismutase activity of treated animals, but catalase activity was weaker (p < 0.05). |
| 317 | 8720919 | Using a sensitive Northern blot hybridization technique, gene expression of superoxide dismutase (SOD), catalase, and glutathione peroxidase was studied in pancreatic islets and for comparison in various other mouse tissues (liver, kidney, brain, lung, skeletal muscle, heart muscle, adrenal gland, and pituitary gland). |
| 318 | 8720919 | The levels of the cytoplasmic Cu/Zn SOD and the mitochondrial Mn SOD gene expression were in the range of 30-40% of those in the liver. |
| 319 | 8720919 | Using a sensitive Northern blot hybridization technique, gene expression of superoxide dismutase (SOD), catalase, and glutathione peroxidase was studied in pancreatic islets and for comparison in various other mouse tissues (liver, kidney, brain, lung, skeletal muscle, heart muscle, adrenal gland, and pituitary gland). |
| 320 | 8720919 | The levels of the cytoplasmic Cu/Zn SOD and the mitochondrial Mn SOD gene expression were in the range of 30-40% of those in the liver. |
| 321 | 8748220 | Probucol treatment caused a small but significant improvement in serum insulin and decrease in glucose levels as well as increased myocardial SOD, GSHPx, and catalase activities with a concomitant decrease in TBARS in the diabetic animals. |
| 322 | 8770936 | It has also been shown that diabetes-induced inactivation of NO can be rescued with administration of insulin as well as with free radical scavengers such as superoxide dismutase (SOD). |
| 323 | 8770936 | Lastly, we report the localization of endothelial nitric oxide synthase, inducible NOS, Cu/Zn SOD, and the LH receptor to the same population of endothelial cells surrounding the preovulatory follicle, supporting our hypothesis that the signaling of ovarian NO within the ovarian microvasculature at the time of ovulation may be compromised in these diabetic mice as a consequence of the loss of the protective activity of Cu/Zn SOD. |
| 324 | 8770936 | It has also been shown that diabetes-induced inactivation of NO can be rescued with administration of insulin as well as with free radical scavengers such as superoxide dismutase (SOD). |
| 325 | 8770936 | Lastly, we report the localization of endothelial nitric oxide synthase, inducible NOS, Cu/Zn SOD, and the LH receptor to the same population of endothelial cells surrounding the preovulatory follicle, supporting our hypothesis that the signaling of ovarian NO within the ovarian microvasculature at the time of ovulation may be compromised in these diabetic mice as a consequence of the loss of the protective activity of Cu/Zn SOD. |
| 326 | 8772524 | Neutrophils and monocytes adhere to the vascular endothelium and release mediators, such as tumor necrosis factor-alpha (TNF-alpha), interleukin (IL)-1 beta, and reactive oxygen species. |
| 327 | 8772524 | TNF-alpha, IL-1 beta, and antioxidants (superoxide dismutase; catalase; and dimethyl sulfoxide) all induced RBC adhesion to BPAEC. |
| 328 | 8777831 | Lipid peroxidation products in plasma and erythrocytes were assayed as thiobarbituric acid reactive substances, along with the erythrocyte antioxidant enzymes, namely superoxide dismutase, catalase and glutathione peroxidase. |
| 329 | 8777831 | Lipid peroxidation was significantly raised within the first 2 years of diagnosis, and superoxide dismutase, catalase, reduced glutathione and vitamins C and E were significantly lowered. 3. |
| 330 | 8777831 | Lipid peroxidation products in plasma and erythrocytes were assayed as thiobarbituric acid reactive substances, along with the erythrocyte antioxidant enzymes, namely superoxide dismutase, catalase and glutathione peroxidase. |
| 331 | 8777831 | Lipid peroxidation was significantly raised within the first 2 years of diagnosis, and superoxide dismutase, catalase, reduced glutathione and vitamins C and E were significantly lowered. 3. |
| 332 | 8804988 | The aim of the present study was to investigate if maternal diabetes in vivo, or high glucose in vitro alters the expression of the free oxygen radical scavenging enzymes superoxide dismutase (CuZnSOD and MnSOD), catalase and glutathione peroxidase in rat embryos during late organogenesis. |
| 333 | 8804988 | The CuZnSOD and MnSOD enzymes were expressed on gestational day 11 and both CuZnSOD, MnSOD and catalase were expressed on day 12 with increased concentrations of MnSOD transcripts when challenged by a diabetic milieu. |
| 334 | 8804988 | Maternal diabetes in vivo and high glucose concentration in vitro induced increased MnSOD expression, concomitant with increased total SOD activity, and a tentative decrease in catalase expression and activity in the embryos. |
| 335 | 8804988 | The aim of the present study was to investigate if maternal diabetes in vivo, or high glucose in vitro alters the expression of the free oxygen radical scavenging enzymes superoxide dismutase (CuZnSOD and MnSOD), catalase and glutathione peroxidase in rat embryos during late organogenesis. |
| 336 | 8804988 | The CuZnSOD and MnSOD enzymes were expressed on gestational day 11 and both CuZnSOD, MnSOD and catalase were expressed on day 12 with increased concentrations of MnSOD transcripts when challenged by a diabetic milieu. |
| 337 | 8804988 | Maternal diabetes in vivo and high glucose concentration in vitro induced increased MnSOD expression, concomitant with increased total SOD activity, and a tentative decrease in catalase expression and activity in the embryos. |
| 338 | 8810235 | Copper, zinc-superoxide dismutase (Cu, Zn-SOD), a scavenger of superoxide radicals, whose function is complementary to manganese-SOD (Mn-SOD), is inactivated during glycation. |
| 339 | 8811335 | This increased resistance to injury is associated with higher expression of heat shock protein 70, catalase and superoxide dismutase. |
| 340 | 8844116 | Superoxide dismutase-like activity (SOD-like), isoenzyme lactate dehydrogenase-C4 (LDH-C4) and NADH-diaphorase activities in spermatozoa have been investigated from 58 normozoospermic and 27 oligozoospermic men. |
| 341 | 8844116 | Significantly higher SOD-like, LDH-C4 and diaphorase activities (P < 0.01, P < 0.005 and P < 0.0001, respectively) were detected in spermatozoa from oligozoospermic men, compared to the activities found in normozoospermic samples. |
| 342 | 8844116 | There was a close correlation between the SOD-like activity and biochemical indicators of the presence of residual cytoplasm i.e. isoenzyme LDH-C4 and NADH-diaphorase (r = 0.53 and r = 0.66 in normozoospermic and r = 0.63 and r = 0.54 in oligozoospermic men, respectively). |
| 343 | 8844116 | Superoxide dismutase-like activity (SOD-like), isoenzyme lactate dehydrogenase-C4 (LDH-C4) and NADH-diaphorase activities in spermatozoa have been investigated from 58 normozoospermic and 27 oligozoospermic men. |
| 344 | 8844116 | Significantly higher SOD-like, LDH-C4 and diaphorase activities (P < 0.01, P < 0.005 and P < 0.0001, respectively) were detected in spermatozoa from oligozoospermic men, compared to the activities found in normozoospermic samples. |
| 345 | 8844116 | There was a close correlation between the SOD-like activity and biochemical indicators of the presence of residual cytoplasm i.e. isoenzyme LDH-C4 and NADH-diaphorase (r = 0.53 and r = 0.66 in normozoospermic and r = 0.63 and r = 0.54 in oligozoospermic men, respectively). |
| 346 | 8844116 | Superoxide dismutase-like activity (SOD-like), isoenzyme lactate dehydrogenase-C4 (LDH-C4) and NADH-diaphorase activities in spermatozoa have been investigated from 58 normozoospermic and 27 oligozoospermic men. |
| 347 | 8844116 | Significantly higher SOD-like, LDH-C4 and diaphorase activities (P < 0.01, P < 0.005 and P < 0.0001, respectively) were detected in spermatozoa from oligozoospermic men, compared to the activities found in normozoospermic samples. |
| 348 | 8844116 | There was a close correlation between the SOD-like activity and biochemical indicators of the presence of residual cytoplasm i.e. isoenzyme LDH-C4 and NADH-diaphorase (r = 0.53 and r = 0.66 in normozoospermic and r = 0.63 and r = 0.54 in oligozoospermic men, respectively). |
| 349 | 8849337 | Hormonal regulation of superoxide dismutase, catalase, and glutathione peroxidase activities in rat macrophages. |
| 350 | 8849337 | This study examined the effects of glycocorticoids, insulin, thyroxine, and epinephrine upon the activities of CuZn- and Mn-superoxide dismutases (SOD), catalase, and glutathione peroxidase (GPX) and upon hydrogen peroxide production in rat macrophages obtained from the intraperitoneal cavity. |
| 351 | 8849337 | Insulin increased the activities of CuZn-SOD, catalase, and GPX and reduced that of Mn-SOD. |
| 352 | 8849337 | Hormonal regulation of superoxide dismutase, catalase, and glutathione peroxidase activities in rat macrophages. |
| 353 | 8849337 | This study examined the effects of glycocorticoids, insulin, thyroxine, and epinephrine upon the activities of CuZn- and Mn-superoxide dismutases (SOD), catalase, and glutathione peroxidase (GPX) and upon hydrogen peroxide production in rat macrophages obtained from the intraperitoneal cavity. |
| 354 | 8849337 | Insulin increased the activities of CuZn-SOD, catalase, and GPX and reduced that of Mn-SOD. |
| 355 | 8852273 | Free radicals are eliminated by cellular enzymes such as superoxide dismutase, catalase and glutathione peroxidase. |
| 356 | 8862945 | Antioxidant enzymes superoxide dismutase and catalase were significantly lower in red blood cells obtained from IGT and early hyperglycaemic groups. |
| 357 | 8891455 | This study attempted to verify the existence of a relationship between oxidative stress documented by malondialdehyde (MDA) and superoxide dismutase (SOD) and fibrinolysis analysed by tissue plasminogen activator (tPA) and its inhibitor (PAI-1) in diabetes mellitus. |
| 358 | 8891455 | The following were analysed: plasma MDA concentration, SOD activity in erythrocytes, tPA activity and antigen, PAI-1 activity and antigen, fasting blood glucose, fructosamine, glycated haemoglobin (HbAlc), and urine albumin. |
| 359 | 8891455 | This contrasted with an increased plasma MDA concentration especially in Type 2 diabetes as compared with Type 1 or healthy persons (p < 0.001). tPA activity was increased in both groups of patients with diabetes as compared to healthy persons (p < 0.001), PAI-1 activity was higher in Type 2 diabetes with vascular changes than in the remaining subgroups (p < 0.001). |
| 360 | 8891455 | Multivariate analysis revealed a significant positive relationship between plasma MDA concentrations and PAI-1 antigen (r = 0.53, p < 0.001) and a negative relationship between SOD and tPA activities (r = -0.53, p < 0.01). |
| 361 | 8891455 | This study attempted to verify the existence of a relationship between oxidative stress documented by malondialdehyde (MDA) and superoxide dismutase (SOD) and fibrinolysis analysed by tissue plasminogen activator (tPA) and its inhibitor (PAI-1) in diabetes mellitus. |
| 362 | 8891455 | The following were analysed: plasma MDA concentration, SOD activity in erythrocytes, tPA activity and antigen, PAI-1 activity and antigen, fasting blood glucose, fructosamine, glycated haemoglobin (HbAlc), and urine albumin. |
| 363 | 8891455 | This contrasted with an increased plasma MDA concentration especially in Type 2 diabetes as compared with Type 1 or healthy persons (p < 0.001). tPA activity was increased in both groups of patients with diabetes as compared to healthy persons (p < 0.001), PAI-1 activity was higher in Type 2 diabetes with vascular changes than in the remaining subgroups (p < 0.001). |
| 364 | 8891455 | Multivariate analysis revealed a significant positive relationship between plasma MDA concentrations and PAI-1 antigen (r = 0.53, p < 0.001) and a negative relationship between SOD and tPA activities (r = -0.53, p < 0.01). |
| 365 | 8891455 | This study attempted to verify the existence of a relationship between oxidative stress documented by malondialdehyde (MDA) and superoxide dismutase (SOD) and fibrinolysis analysed by tissue plasminogen activator (tPA) and its inhibitor (PAI-1) in diabetes mellitus. |
| 366 | 8891455 | The following were analysed: plasma MDA concentration, SOD activity in erythrocytes, tPA activity and antigen, PAI-1 activity and antigen, fasting blood glucose, fructosamine, glycated haemoglobin (HbAlc), and urine albumin. |
| 367 | 8891455 | This contrasted with an increased plasma MDA concentration especially in Type 2 diabetes as compared with Type 1 or healthy persons (p < 0.001). tPA activity was increased in both groups of patients with diabetes as compared to healthy persons (p < 0.001), PAI-1 activity was higher in Type 2 diabetes with vascular changes than in the remaining subgroups (p < 0.001). |
| 368 | 8891455 | Multivariate analysis revealed a significant positive relationship between plasma MDA concentrations and PAI-1 antigen (r = 0.53, p < 0.001) and a negative relationship between SOD and tPA activities (r = -0.53, p < 0.01). |
| 369 | 8894182 | Preincubation of aortic strips with superoxide dismutase (SOD, 60 u ml-1) normalized the recovery phase of the relaxation of diabetic aorta after single administration of ACh, whereas catalase (150 u ml-1) or indomethacin (10(-5) M) had no effects on the relaxation. 4. |
| 370 | 8901484 | This was also accompanied by an improvement in SOD and GSHPx activities and there was further increase in the catalase activity. |
| 371 | 8902197 | Superoxide dismutase, catalase, Trolox, and diethylenetriamine pentaacetic acid inhibited the signals while EDTA enhanced them. |
| 372 | 8978321 | p22phox mRNA expression and NADPH oxidase activity are increased in aortas from hypertensive rats. |
| 373 | 8978321 | To investigate the mechanism responsible for this increased oxidase activity, we examined p22phox mRNA expression in rats made hypertensive by implanting an osmotic minipump that delivered Ang II (0.7 mg/kg per day). |
| 374 | 8978321 | Furthermore, infusion of recombinant heparin-binding superoxide dismutase decreased both blood pressure and p22phox mRNA expression. |
| 375 | 8978321 | These findings suggest that Ang II-induced hypertension activates the NADPH/NADH oxidase system by upregulating mRNA levels of one or several components of this oxidase system, including the p22phox, and that the NADPH/NADH oxidase system is associated with the pathology of hypertension in vivo. |
| 376 | 8983869 | In the present study, we investigated the lipid peroxide level [thiobarbituric acid-reactive substances (TBARS)] and activities of antioxidant enzymes (superoxide dismutase, catalase and glutathione peroxidase) in aorta, heart and blood of control and streptozotocin-induced diabetic rats at various stages of development of diabetes (0 to 6 weeks). 2. |
| 377 | 8983869 | There were no significant changes in the activities of superoxide dismutase, catalase and glutathione peroxidase in the aorta, heart and blood of control rats at all time intervals. |
| 378 | 8983869 | In the diabetic group, there was a significant (P < 0.05) increase in the activity of superoxide dismutase and glutathione peroxidase in aorta from the fourth week onwards while the activity of catalase increased at all time intervals. |
| 379 | 8983869 | In the blood, the activity of superoxide dismutase and glutathione peroxidase increased from the third week while catalase activity increased from the fourth week. 4. |
| 380 | 8983869 | In the present study, we investigated the lipid peroxide level [thiobarbituric acid-reactive substances (TBARS)] and activities of antioxidant enzymes (superoxide dismutase, catalase and glutathione peroxidase) in aorta, heart and blood of control and streptozotocin-induced diabetic rats at various stages of development of diabetes (0 to 6 weeks). 2. |
| 381 | 8983869 | There were no significant changes in the activities of superoxide dismutase, catalase and glutathione peroxidase in the aorta, heart and blood of control rats at all time intervals. |
| 382 | 8983869 | In the diabetic group, there was a significant (P < 0.05) increase in the activity of superoxide dismutase and glutathione peroxidase in aorta from the fourth week onwards while the activity of catalase increased at all time intervals. |
| 383 | 8983869 | In the blood, the activity of superoxide dismutase and glutathione peroxidase increased from the third week while catalase activity increased from the fourth week. 4. |
| 384 | 8983869 | In the present study, we investigated the lipid peroxide level [thiobarbituric acid-reactive substances (TBARS)] and activities of antioxidant enzymes (superoxide dismutase, catalase and glutathione peroxidase) in aorta, heart and blood of control and streptozotocin-induced diabetic rats at various stages of development of diabetes (0 to 6 weeks). 2. |
| 385 | 8983869 | There were no significant changes in the activities of superoxide dismutase, catalase and glutathione peroxidase in the aorta, heart and blood of control rats at all time intervals. |
| 386 | 8983869 | In the diabetic group, there was a significant (P < 0.05) increase in the activity of superoxide dismutase and glutathione peroxidase in aorta from the fourth week onwards while the activity of catalase increased at all time intervals. |
| 387 | 8983869 | In the blood, the activity of superoxide dismutase and glutathione peroxidase increased from the third week while catalase activity increased from the fourth week. 4. |
| 388 | 8983869 | In the present study, we investigated the lipid peroxide level [thiobarbituric acid-reactive substances (TBARS)] and activities of antioxidant enzymes (superoxide dismutase, catalase and glutathione peroxidase) in aorta, heart and blood of control and streptozotocin-induced diabetic rats at various stages of development of diabetes (0 to 6 weeks). 2. |
| 389 | 8983869 | There were no significant changes in the activities of superoxide dismutase, catalase and glutathione peroxidase in the aorta, heart and blood of control rats at all time intervals. |
| 390 | 8983869 | In the diabetic group, there was a significant (P < 0.05) increase in the activity of superoxide dismutase and glutathione peroxidase in aorta from the fourth week onwards while the activity of catalase increased at all time intervals. |
| 391 | 8983869 | In the blood, the activity of superoxide dismutase and glutathione peroxidase increased from the third week while catalase activity increased from the fourth week. 4. |
| 392 | 9005653 | Activity of the antioxidant enzymes (superoxide dismutase, catalase) has reduced and the amount of the final product of lipid peroxidation, MDA has increased. |
| 393 | 9013090 | Plasma superoxide dismutase was significantly reduced in diabetes (P < 0.01); smaller decreases in plasma catalase and glutathione levels were observed. |
| 394 | 9013090 | In nervous tissue, diabetes caused increased catalase activity, uninfluenced by insulin (P < 0.05). |
| 395 | 9013121 | Diabetes or experimental galactosemia of 2 months duration significantly decreased the activities of glutathione reductase and glutathione peroxidase in the retina while having no effect on the glutathione synthesizing enzymes glutathione synthetase and gamma-glutamyl cysteine synthetase. |
| 396 | 9013121 | Activities of two other important antioxidant defense enzymes-superoxide dismutase (SOD) and catalase-also were decreased (by more than 25%) in retinas of diabetic rats and galactosemic rats. |
| 397 | 9013121 | In experimentally galactosemic rats, the supplemental antioxidants were not as effective: SOD activity was normalized, but the enzymes of the glutathione redox cycle were only partly restored, and the subnormal catalase activity was unaffected. |
| 398 | 9013121 | Diabetes or experimental galactosemia of 2 months duration significantly decreased the activities of glutathione reductase and glutathione peroxidase in the retina while having no effect on the glutathione synthesizing enzymes glutathione synthetase and gamma-glutamyl cysteine synthetase. |
| 399 | 9013121 | Activities of two other important antioxidant defense enzymes-superoxide dismutase (SOD) and catalase-also were decreased (by more than 25%) in retinas of diabetic rats and galactosemic rats. |
| 400 | 9013121 | In experimentally galactosemic rats, the supplemental antioxidants were not as effective: SOD activity was normalized, but the enzymes of the glutathione redox cycle were only partly restored, and the subnormal catalase activity was unaffected. |
| 401 | 9022079 | The oxidative formation of CML from glycated proteins was reduced by lipoic acid, aminoguanidine, superoxide dismutase, catalase, and particularly vitamin E and desferrioxamine. |
| 402 | 9028714 | To test the hypothesis that this response also occurs in vivo, Cu.Zn-superoxide dismutase (Cu.Zn-SOD) and catalase mRNA levels, were measured in the kidneys of Sprague-Dawley rats 17 days after intravenous injection of streptozotocin (60 mg/kg body weight) and compared with those of control rats. |
| 403 | 9028714 | Renal Cu,Zn-SOD and catalase mRNA levels were significantly greater in untreated diabetic and in low-dose (2 IU/day) insulin-treated rats than in controls. |
| 404 | 9028714 | Treatment with a moderate dose (3-8 IU/day) of insulin normalized catalase but not Cu,Zn-SOD mRNA levels. |
| 405 | 9028714 | The highest insulin regimen (6-10 IU/day), in addition to achieving complete metabolic control as evidenced by normal growth and plasma glucose levels, normalized both catalase and Cu,Zn-SOD mRNA levels. |
| 406 | 9048969 | In the present study, we investigated the lipid peroxide level measured as thiobarbituric acid reactive substances (TBARS) and activities of antioxidant enzymes viz., [superoxide dismutase (SOD), catalase (CAT) and glutathione-peroxidase (GSH-Px)] in the kidney of streptozotocin induced diabetic rats at various stages of development of diabetes. |
| 407 | 9048969 | Total SOD and CuZn-SOD activity increased significantly in diabetic kidney as compared to controls at all time intervals, while Mn-SOD activity showed no change. |
| 408 | 9048969 | In the present study, we investigated the lipid peroxide level measured as thiobarbituric acid reactive substances (TBARS) and activities of antioxidant enzymes viz., [superoxide dismutase (SOD), catalase (CAT) and glutathione-peroxidase (GSH-Px)] in the kidney of streptozotocin induced diabetic rats at various stages of development of diabetes. |
| 409 | 9048969 | Total SOD and CuZn-SOD activity increased significantly in diabetic kidney as compared to controls at all time intervals, while Mn-SOD activity showed no change. |
| 410 | 9184822 | The results of this study demonstrate that the sulfonylurea, glyburide, is capable of exerting direct insulin-like effects on muscle SOD activity in vivo. |
| 411 | 9226234 | Cu/Zn-SOD and Mn-SOD (SOD = superoxide dismutase), glutathione peroxidase, and catalase, activities in diabetic SHR. |
| 412 | 9226234 | Glomerular Cu/Zn-SOD or Mn-SOD, glutathione peroxidase, and catalase activities in nondiabetic SHR were slightly lower than those in nondiabetic WKY rats. |
| 413 | 9237536 | The goal of this study was to test the hypothesis that administration of superoxide dismutase restores nitric oxide synthase-mediated dilatation of the basilar artery during diabetes mellitus. |
| 414 | 9237536 | We measured the diameter of the basilar artery in vivo in nondiabetic and diabetic rats (streptozotocin; 50-60 mg/kg i.p.) in response to nitric oxide synthase-dependent agonists (acetylcholine and bradykinin) and a nitric oxide synthase-independent agonist (nitroglycerin) before and during application of superoxide dismutase. |
| 415 | 9237536 | However, topical application of superoxide dismutase partially restored nitric oxide synthase-dependent dilatation of the basilar artery in diabetic rats towards that observed in nondiabetic rats. |
| 416 | 9237536 | The goal of this study was to test the hypothesis that administration of superoxide dismutase restores nitric oxide synthase-mediated dilatation of the basilar artery during diabetes mellitus. |
| 417 | 9237536 | We measured the diameter of the basilar artery in vivo in nondiabetic and diabetic rats (streptozotocin; 50-60 mg/kg i.p.) in response to nitric oxide synthase-dependent agonists (acetylcholine and bradykinin) and a nitric oxide synthase-independent agonist (nitroglycerin) before and during application of superoxide dismutase. |
| 418 | 9237536 | However, topical application of superoxide dismutase partially restored nitric oxide synthase-dependent dilatation of the basilar artery in diabetic rats towards that observed in nondiabetic rats. |
| 419 | 9237536 | The goal of this study was to test the hypothesis that administration of superoxide dismutase restores nitric oxide synthase-mediated dilatation of the basilar artery during diabetes mellitus. |
| 420 | 9237536 | We measured the diameter of the basilar artery in vivo in nondiabetic and diabetic rats (streptozotocin; 50-60 mg/kg i.p.) in response to nitric oxide synthase-dependent agonists (acetylcholine and bradykinin) and a nitric oxide synthase-independent agonist (nitroglycerin) before and during application of superoxide dismutase. |
| 421 | 9237536 | However, topical application of superoxide dismutase partially restored nitric oxide synthase-dependent dilatation of the basilar artery in diabetic rats towards that observed in nondiabetic rats. |
| 422 | 9240011 | The present study was to investigate the levels of plasma lipid peroxide products including malondialdehyde (MDA) and conjugated dienes (CD), and antioxidants including enzyme superoxide dismutase, glutathione peroxidase, catalase, plasma vitamin E and vitamin C in diabetic patients. |
| 423 | 9242227 | Although catalase and glutathione peroxidase maintained high levels of mRNA expression through d 60, induction of CuZu-superoxide dismutase was transient, with the activity and mRNA levels returning to baseline values by d 40. |
| 424 | 9249512 | Dimethylthiourea and Tiron, intracellular free radical scavengers, normalized the vasodilatory response to diabetic platelets, whereas superoxide dismutase, catalase, and mannitol did not. |
| 425 | 9259354 | The suppressive effect of high glucose on NO production by mesangial cells was not modified by inhibition of protein kinase C (H-7), the addition of antioxidants (vitamin E or superoxide dismutase), or a pan-specific anti-transforming growth factor-beta antibody. |
| 426 | 9263727 | Copper-zinc superoxide dismutase (Cu,Zn-superoxide dismutase) activity was evaluated in lymphocytes and polymorphonuclear cells of insulin-dependent (n = 33) and non-insulin-dependent (n = 34) diabetic patients. |
| 427 | 9263727 | In comparison to healthy control subjects (n = 32), a significantly lower Cu,Zn-superoxide dismutase activity was found in both lymphocytes and polymorphonuclear cells of insulin-dependent (2.08 +/- 0.58 vs. 1.70 +/- 0.46 U/mg protein, p < 0.05, and 1.06 +/- 0.46 vs. 0.64 +/- 0.40 U/mg protein, p < 0.001, respectively) and non-insulin-dependent diabetic patients (2.08 +/- 0.58 vs. 1.61 +/- 0.48 U/mg protein, p < 0.01, and 1.06 +/- 0.46 vs. 0.53 +/- 0.24 U/mg protein, p < 0.001, respectively). |
| 428 | 9263727 | Copper-zinc superoxide dismutase (Cu,Zn-superoxide dismutase) activity was evaluated in lymphocytes and polymorphonuclear cells of insulin-dependent (n = 33) and non-insulin-dependent (n = 34) diabetic patients. |
| 429 | 9263727 | In comparison to healthy control subjects (n = 32), a significantly lower Cu,Zn-superoxide dismutase activity was found in both lymphocytes and polymorphonuclear cells of insulin-dependent (2.08 +/- 0.58 vs. 1.70 +/- 0.46 U/mg protein, p < 0.05, and 1.06 +/- 0.46 vs. 0.64 +/- 0.40 U/mg protein, p < 0.001, respectively) and non-insulin-dependent diabetic patients (2.08 +/- 0.58 vs. 1.61 +/- 0.48 U/mg protein, p < 0.01, and 1.06 +/- 0.46 vs. 0.53 +/- 0.24 U/mg protein, p < 0.001, respectively). |
| 430 | 9315241 | These alterations in SOD were counteracted by insulin as well as with powdered fruit of C. decidua. |
| 431 | 9315241 | Result shows that treatment with C. decidua lowers alloxan induced LPO and alters SOD and CAT enzymes to reduce oxidative stress. |
| 432 | 9315241 | These alterations in SOD were counteracted by insulin as well as with powdered fruit of C. decidua. |
| 433 | 9315241 | Result shows that treatment with C. decidua lowers alloxan induced LPO and alters SOD and CAT enzymes to reduce oxidative stress. |
| 434 | 9356019 | Although superoxide dismutase expression was in the range of 30% of the liver values, the expression of the hydrogen peroxide-inactivating enzymes catalase and glutathione peroxidase was extremely low, in the range of 5% of the liver. |
| 435 | 9356019 | Thus inactivation of hydrogen peroxide through catalase seems to be a step of critical importance for the removal of reactive oxygen species in insulin-producing cells. |
| 436 | 9366962 | Impaired antioxidant defences may predispose to the increased resting and exercise-induced oxidative stress found in patients with insulin-dependent diabetes mellitus (IDDM). |
| 437 | 9366962 | Red cell Cu, Zn-superoxide dismutase and catalase activities were lower in the IDDM group (P = 0.033 and P = 0.023, respectively). |
| 438 | 9366962 | To conclude, lower erythrocyte Cu, Zn-superoxide dismutase and catalase activity in young men with IDDM at rest may contribute to increased oxidative stress. |
| 439 | 9366962 | Impaired antioxidant defences may predispose to the increased resting and exercise-induced oxidative stress found in patients with insulin-dependent diabetes mellitus (IDDM). |
| 440 | 9366962 | Red cell Cu, Zn-superoxide dismutase and catalase activities were lower in the IDDM group (P = 0.033 and P = 0.023, respectively). |
| 441 | 9366962 | To conclude, lower erythrocyte Cu, Zn-superoxide dismutase and catalase activity in young men with IDDM at rest may contribute to increased oxidative stress. |
| 442 | 9371721 | Glycation-induced inactivation and loss of antigenicity of catalase and superoxide dismutase. |
| 443 | 9371721 | Here we investigate the inactivation of catalase and superoxide dismutase, both powerful antioxidant enzymes, by sugars of different glycating abilities, and the loss of antigenicity that was monitored by the loss of activity after immunoprecipitation with monospecific antibodies. |
| 444 | 9371721 | Glycation-induced inactivation and loss of antigenicity of catalase and superoxide dismutase. |
| 445 | 9371721 | Here we investigate the inactivation of catalase and superoxide dismutase, both powerful antioxidant enzymes, by sugars of different glycating abilities, and the loss of antigenicity that was monitored by the loss of activity after immunoprecipitation with monospecific antibodies. |
| 446 | 9485543 | The activity of fetal oxygen-free radical scavenging enzymes, including superoxide dismutase (SOD), glutathione peroxidase (GPX), and catalase (CAT), were determined. |
| 447 | 9485543 | Glutathione peroxidase and catalase activity were significantly reduced in malformed versus normal-formed embryos of nondiabetic mothers (GPX-2.68 +/- 1.15 vs. 4.46 +/- 1.12 mu/mg protein, CAT -1.67 +/- 0.53 vs 2.49 +/- 0.61 u/mg protein respectively; P < 0.01). |
| 448 | 9485543 | Two-way analysis of variance identified fetal malformations as the variance associated with reduced fetal SOD activity, whereas maternal diabetes was associated with the increase in fetal catalase activity. |
| 449 | 9485543 | Defects in embryonic SOD and catalase activity, regardless of maternal diabetic status, may reduce the ability of the fetus to clear free oxygen radicals, thereby exposing it to an increased oxidative load that may cause fetal dysmorphogenesis. |
| 450 | 9485543 | The activity of fetal oxygen-free radical scavenging enzymes, including superoxide dismutase (SOD), glutathione peroxidase (GPX), and catalase (CAT), were determined. |
| 451 | 9485543 | Glutathione peroxidase and catalase activity were significantly reduced in malformed versus normal-formed embryos of nondiabetic mothers (GPX-2.68 +/- 1.15 vs. 4.46 +/- 1.12 mu/mg protein, CAT -1.67 +/- 0.53 vs 2.49 +/- 0.61 u/mg protein respectively; P < 0.01). |
| 452 | 9485543 | Two-way analysis of variance identified fetal malformations as the variance associated with reduced fetal SOD activity, whereas maternal diabetes was associated with the increase in fetal catalase activity. |
| 453 | 9485543 | Defects in embryonic SOD and catalase activity, regardless of maternal diabetic status, may reduce the ability of the fetus to clear free oxygen radicals, thereby exposing it to an increased oxidative load that may cause fetal dysmorphogenesis. |
| 454 | 9485543 | The activity of fetal oxygen-free radical scavenging enzymes, including superoxide dismutase (SOD), glutathione peroxidase (GPX), and catalase (CAT), were determined. |
| 455 | 9485543 | Glutathione peroxidase and catalase activity were significantly reduced in malformed versus normal-formed embryos of nondiabetic mothers (GPX-2.68 +/- 1.15 vs. 4.46 +/- 1.12 mu/mg protein, CAT -1.67 +/- 0.53 vs 2.49 +/- 0.61 u/mg protein respectively; P < 0.01). |
| 456 | 9485543 | Two-way analysis of variance identified fetal malformations as the variance associated with reduced fetal SOD activity, whereas maternal diabetes was associated with the increase in fetal catalase activity. |
| 457 | 9485543 | Defects in embryonic SOD and catalase activity, regardless of maternal diabetic status, may reduce the ability of the fetus to clear free oxygen radicals, thereby exposing it to an increased oxidative load that may cause fetal dysmorphogenesis. |
| 458 | 9522273 | One week after LPS or streptozotocin treatments, oxidative stress was determined by measuring changes in antioxidant activity (glutathione peroxidase, glutathione reductase, superoxide dismutase, catalase, glutathione S-transferase, and gamma-glutamyltranspeptidase) and in concentrations of glutathione, nitrite, and thiobarbituric acid reactants in liver, kidney, intestine, and spleen. |
| 459 | 9530434 | We tested and compared antioxidant enzymes (superoxide dismutase-, glutathione peroxidase- and catalase activities) glutathione reductase activity regenerate reduced glutathione (GSH). |
| 460 | 9568703 | Interestingly, the antioxidants superoxide dismutase (SOD) and N-acetylcysteine (NAC) were each able to diminish the dysmorphogenesis induced by the COX inhibitors, at doses previously shown to diminish glucose-induced embryonic damage in the same in vitro culture system. |
| 461 | 9614361 | The effects of recombinant human IGF-I administration on concentrations of acid labile subunit, IGF binding protein-3, IGF-I, IGF-II and proteolysis of IGF binding protein-3 in adolescents with insulin-dependent diabetes mellitus. |
| 462 | 9614361 | The long term therapeutic potential of recombinant human (rh) IGF-I administration in insulin-dependent diabetes mellitus (IDDM) may be determined by changes in the IGF binding proteins (IGFBPs) and thus the bioavailability of IGF-I. |
| 463 | 9614361 | We have therefore studied the effects of a single subcutaneous dose of rhIGF-I (40 micrograms/kg at 1800 h), when compared with an untreated control night, in 17 subjects with IDDM, on serum concentrations of IGF-I, IGF-II, IGFBP-3, acid labile subunit (ALS), and IGFBP-3 proteolysis. |
| 464 | 9614361 | IGF-I levels increased from 242 +/- 30 ng/ml to 399 +/- 26 ng/ml (P = 0.01) after rhIGF-I whereas IGF-II levels declined from 600 +/- 45 ng/ml to 533 +/- 30 ng/ml. |
| 465 | 9614361 | On the baseline night, IGFBP-3 levels correlated with the sum of IGF-I and IGF-II (r = 0.73, P = 0.02) and with levels of the ALS (r = 0.7, P = 0.002). |
| 466 | 9614361 | However after rhIGF-I, the sum of IGF-I and IGF-II no longer correlated with IGFBP-3, whereas the relationship with ALS was maintained. |
| 467 | 9614361 | In conclusion, despite a slight but significant fall in ALS, IGFBP-3 levels rise after rhIGF-I administration in IDDM. |
| 468 | 9614361 | This cannot be explained by alterations in IGFBP-3 proteolysis, and may relate to the relative stability of ALS/IGFBP-3 when complexed principally with IGF-I rather than IGF-II. |
| 469 | 9614361 | The effects of recombinant human IGF-I administration on concentrations of acid labile subunit, IGF binding protein-3, IGF-I, IGF-II and proteolysis of IGF binding protein-3 in adolescents with insulin-dependent diabetes mellitus. |
| 470 | 9614361 | The long term therapeutic potential of recombinant human (rh) IGF-I administration in insulin-dependent diabetes mellitus (IDDM) may be determined by changes in the IGF binding proteins (IGFBPs) and thus the bioavailability of IGF-I. |
| 471 | 9614361 | We have therefore studied the effects of a single subcutaneous dose of rhIGF-I (40 micrograms/kg at 1800 h), when compared with an untreated control night, in 17 subjects with IDDM, on serum concentrations of IGF-I, IGF-II, IGFBP-3, acid labile subunit (ALS), and IGFBP-3 proteolysis. |
| 472 | 9614361 | IGF-I levels increased from 242 +/- 30 ng/ml to 399 +/- 26 ng/ml (P = 0.01) after rhIGF-I whereas IGF-II levels declined from 600 +/- 45 ng/ml to 533 +/- 30 ng/ml. |
| 473 | 9614361 | On the baseline night, IGFBP-3 levels correlated with the sum of IGF-I and IGF-II (r = 0.73, P = 0.02) and with levels of the ALS (r = 0.7, P = 0.002). |
| 474 | 9614361 | However after rhIGF-I, the sum of IGF-I and IGF-II no longer correlated with IGFBP-3, whereas the relationship with ALS was maintained. |
| 475 | 9614361 | In conclusion, despite a slight but significant fall in ALS, IGFBP-3 levels rise after rhIGF-I administration in IDDM. |
| 476 | 9614361 | This cannot be explained by alterations in IGFBP-3 proteolysis, and may relate to the relative stability of ALS/IGFBP-3 when complexed principally with IGF-I rather than IGF-II. |
| 477 | 9614361 | The effects of recombinant human IGF-I administration on concentrations of acid labile subunit, IGF binding protein-3, IGF-I, IGF-II and proteolysis of IGF binding protein-3 in adolescents with insulin-dependent diabetes mellitus. |
| 478 | 9614361 | The long term therapeutic potential of recombinant human (rh) IGF-I administration in insulin-dependent diabetes mellitus (IDDM) may be determined by changes in the IGF binding proteins (IGFBPs) and thus the bioavailability of IGF-I. |
| 479 | 9614361 | We have therefore studied the effects of a single subcutaneous dose of rhIGF-I (40 micrograms/kg at 1800 h), when compared with an untreated control night, in 17 subjects with IDDM, on serum concentrations of IGF-I, IGF-II, IGFBP-3, acid labile subunit (ALS), and IGFBP-3 proteolysis. |
| 480 | 9614361 | IGF-I levels increased from 242 +/- 30 ng/ml to 399 +/- 26 ng/ml (P = 0.01) after rhIGF-I whereas IGF-II levels declined from 600 +/- 45 ng/ml to 533 +/- 30 ng/ml. |
| 481 | 9614361 | On the baseline night, IGFBP-3 levels correlated with the sum of IGF-I and IGF-II (r = 0.73, P = 0.02) and with levels of the ALS (r = 0.7, P = 0.002). |
| 482 | 9614361 | However after rhIGF-I, the sum of IGF-I and IGF-II no longer correlated with IGFBP-3, whereas the relationship with ALS was maintained. |
| 483 | 9614361 | In conclusion, despite a slight but significant fall in ALS, IGFBP-3 levels rise after rhIGF-I administration in IDDM. |
| 484 | 9614361 | This cannot be explained by alterations in IGFBP-3 proteolysis, and may relate to the relative stability of ALS/IGFBP-3 when complexed principally with IGF-I rather than IGF-II. |
| 485 | 9621289 | To test whether the growth phenotype of cells from patients with diabetic nephropathy was related to a lack of protection from oxidative stress, the effect of reduced glutathione (GSH) on cultured skin fibroblasts from 13 insulin-dependent diabetes mellitus (IDDM) patients with nephropathy (DN), 10 IDDM patients without kidney disease (D), and 10 nondiabetic control subjects (C), in normal (5 mM) glucose (NG) and high (22 mM) glucose (HG) medium was studied. |
| 486 | 9621289 | The treatment of fibroblasts from D and C with the inhibitor of the gamma-glutamylcysteine synthetase activity, L-buthionine-S,R-sulfoximine, resulted in growth impairment, and the addition to the culture medium of another antioxidant, superoxide dismutase, corrected the growth abnormalities in fibroblasts from DN. |
| 487 | 9621289 | The impaired growth of cultured fibroblasts from IDDM patients with nephropathy is prevented by GSH and superoxide dismutase and is independent of prevailing glucose concentrations. |
| 488 | 9621289 | To test whether the growth phenotype of cells from patients with diabetic nephropathy was related to a lack of protection from oxidative stress, the effect of reduced glutathione (GSH) on cultured skin fibroblasts from 13 insulin-dependent diabetes mellitus (IDDM) patients with nephropathy (DN), 10 IDDM patients without kidney disease (D), and 10 nondiabetic control subjects (C), in normal (5 mM) glucose (NG) and high (22 mM) glucose (HG) medium was studied. |
| 489 | 9621289 | The treatment of fibroblasts from D and C with the inhibitor of the gamma-glutamylcysteine synthetase activity, L-buthionine-S,R-sulfoximine, resulted in growth impairment, and the addition to the culture medium of another antioxidant, superoxide dismutase, corrected the growth abnormalities in fibroblasts from DN. |
| 490 | 9621289 | The impaired growth of cultured fibroblasts from IDDM patients with nephropathy is prevented by GSH and superoxide dismutase and is independent of prevailing glucose concentrations. |
| 491 | 9687076 | The decrease in thiobarbituric acid reactive substances (TBARS) and increase in reduced glutathione (GSH), superoxide dismutase (SOD) and catalase (CAT) clearly show the antioxidant property of the JSEt. |
| 492 | 9706303 | The properties and changes of antioxidant enzyme activities (superoxide dismutase, glutathione peroxidase and catalase) as well as lipid peroxidation (LP) have been studied earlier without selecting the different type of human diabetics. |
| 493 | 9706304 | In the hemolysates the antioxidant enzymes namely superoxide dismutase (SOD), glutathione peroxidase (GPx-ase), glutathione reductase (GR-ase) and catalase (C-ase) are also compared. |
| 494 | 9753295 | To determine the importance of different antioxidative enzymes for the defense status of insulin-producing cells, the effects of stable overexpression of glutathione peroxidase (Gpx), catalase (Cat), or Cu/Zn superoxide dismutase (SOD) in insulin-producing RINm5F cells on the cytotoxicity of hydrogen peroxide (H2O2), hypoxanthine/xanthine oxidase (H/XO), and menadione have been investigated. |
| 495 | 9753295 | Thus, overexpression of Cat and Gpx, alone or in combination with SOD, by use of molecular biology techniques can protect insulin-producing cells against oxidative damage. |
| 496 | 9753295 | To determine the importance of different antioxidative enzymes for the defense status of insulin-producing cells, the effects of stable overexpression of glutathione peroxidase (Gpx), catalase (Cat), or Cu/Zn superoxide dismutase (SOD) in insulin-producing RINm5F cells on the cytotoxicity of hydrogen peroxide (H2O2), hypoxanthine/xanthine oxidase (H/XO), and menadione have been investigated. |
| 497 | 9753295 | Thus, overexpression of Cat and Gpx, alone or in combination with SOD, by use of molecular biology techniques can protect insulin-producing cells against oxidative damage. |
| 498 | 9812649 | [Effect of salvia miltiorrhiza composita on superoxide dismutase and malonyldialdehyde in treating patients with non-insulin dependent diabetes mellitus (NIDDM)]. |
| 499 | 9819766 | The glucose levels in blood and urine of all the alloxan-treated ALS mice were markedly elevated while those in alloxan-treated ALR and non-treated ALS and ALR mice were not altered. |
| 500 | 9819766 | The results from using ALS and ALR mice suggest that the vasoreactivities to some vasomodulators are changed especially in the long-term diabetic state and that when diabetes was not induced the dose of alloxan does not have any effect on vascular smooth muscle. |
| 501 | 9819766 | The glucose levels in blood and urine of all the alloxan-treated ALS mice were markedly elevated while those in alloxan-treated ALR and non-treated ALS and ALR mice were not altered. |
| 502 | 9819766 | The results from using ALS and ALR mice suggest that the vasoreactivities to some vasomodulators are changed especially in the long-term diabetic state and that when diabetes was not induced the dose of alloxan does not have any effect on vascular smooth muscle. |
| 503 | 9823540 | On the other hand, in vivo studies have given conflicting results: some studies suggesting that nitric oxide synthase inhibitors do not suppress streptozotocin-induced diabetes in mice, while others revealed that nitric oxide synthase inhibitors can reduce the incidence of insulin-dependent diabetes mellitus in rats. |
| 504 | 9823540 | Alloxan-induced diabetes also induced a fall in the levels of anti-oxidant enzymes such as superoxide dismutase, glutathione reductase, and total glutathione, and antioxidants: vitamin E and ceruloplasmin, and an increase in glutathione peroxidase and glutathione-S-transferase. |
| 505 | 9827694 | This study showed that citiolone (CIT), a free radical scavenger, significantly increased superoxide dismutase (P < 0.001 vs. untreated NOD, NMMA-treated, and silica-treated animals), catalase (P < 0.01 vs. untreated NOD), and glutathione peroxidase (P < 0.001 vs. untreated NOD and C57BL6/J) values. |
| 506 | 9831896 | The planar surface area increase induced by 10 nM GHHb was abolished by superoxide dismutase (SOD; 50 200 u ml(-1)), deferoxamine (100 nM-100 microM), or dimethylthiourea (1 mM), while catalase (50 200 u ml(-1)) or mannitol (1 mM) resulted in a partial inhibition of cell size enhancement. 4. |
| 507 | 9831896 | Indeed, enhancements of cell size were observed, which were inhibited by SOD, deferoxamine, or catalase. 5. |
| 508 | 9831896 | The planar surface area increase induced by 10 nM GHHb was abolished by superoxide dismutase (SOD; 50 200 u ml(-1)), deferoxamine (100 nM-100 microM), or dimethylthiourea (1 mM), while catalase (50 200 u ml(-1)) or mannitol (1 mM) resulted in a partial inhibition of cell size enhancement. 4. |
| 509 | 9831896 | Indeed, enhancements of cell size were observed, which were inhibited by SOD, deferoxamine, or catalase. 5. |
| 510 | 9853804 | The effect of aminoguanidine (AG) on the malondialdehyde (MDA) concentration and activities of superoxide dismutase (SOD), catalase and glutathione peroxidase (GSH-Px) in erythrocytes of rats with streptozotocin-induced diabetes was studied. |
| 511 | 9853804 | Induction of diabetes resulted in an increase of MDA concentration and decreases of SOD and catalase activities after 6 and 12 weeks. |
| 512 | 9853804 | AG administration did not affect body weight, blood glucose level and HbA1c content in diabetic rats but led to a decrease of MDA concentration and SOD and catalase activities after 12 weeks of treatment, with no significant effect after 6 weeks. |
| 513 | 9853804 | The effect of aminoguanidine (AG) on the malondialdehyde (MDA) concentration and activities of superoxide dismutase (SOD), catalase and glutathione peroxidase (GSH-Px) in erythrocytes of rats with streptozotocin-induced diabetes was studied. |
| 514 | 9853804 | Induction of diabetes resulted in an increase of MDA concentration and decreases of SOD and catalase activities after 6 and 12 weeks. |
| 515 | 9853804 | AG administration did not affect body weight, blood glucose level and HbA1c content in diabetic rats but led to a decrease of MDA concentration and SOD and catalase activities after 12 weeks of treatment, with no significant effect after 6 weeks. |
| 516 | 9853804 | The effect of aminoguanidine (AG) on the malondialdehyde (MDA) concentration and activities of superoxide dismutase (SOD), catalase and glutathione peroxidase (GSH-Px) in erythrocytes of rats with streptozotocin-induced diabetes was studied. |
| 517 | 9853804 | Induction of diabetes resulted in an increase of MDA concentration and decreases of SOD and catalase activities after 6 and 12 weeks. |
| 518 | 9853804 | AG administration did not affect body weight, blood glucose level and HbA1c content in diabetic rats but led to a decrease of MDA concentration and SOD and catalase activities after 12 weeks of treatment, with no significant effect after 6 weeks. |
| 519 | 9854460 | We therefore investigated the lipid peroxide level (thiobarbituric acid-reactive substances, TBARS) and activities of antioxidant enzymes [superoxide dismutase (SOD), catalase and glutathione peroxidase] in liver and pancreas of control and streptozotocin-induced diabetic rats at various stages of development of diabetes. 3. |
| 520 | 9854460 | Total SOD and Cu-Zn-SOD activity increased (P < 0.05) with progression of diabetes while Mn-SOD activity showed no significant change in either tissue. |
| 521 | 9854460 | We therefore investigated the lipid peroxide level (thiobarbituric acid-reactive substances, TBARS) and activities of antioxidant enzymes [superoxide dismutase (SOD), catalase and glutathione peroxidase] in liver and pancreas of control and streptozotocin-induced diabetic rats at various stages of development of diabetes. 3. |
| 522 | 9854460 | Total SOD and Cu-Zn-SOD activity increased (P < 0.05) with progression of diabetes while Mn-SOD activity showed no significant change in either tissue. |
| 523 | 9860046 | Glucose-6-phosphate dehydrogenase (G6PDH) is an important lens enzyme diverting about 14% of the tissue glucose to the hexose monophosphate shunt pathway. |
| 524 | 9860046 | This led to a significant loss of its activity, which was prevented by superoxide dismutase, catalase, mannitol and myoinositol. |
| 525 | 9870562 | They showed a significant superoxide dismutase (SOD) inhibitable reduction of cytochrome C by acetoacetate, but not by beta-hydroxybutyrate, suggesting the generation of superoxide anion radicals by acetoacetate. |
| 526 | 9891847 | Hexokinase, glucose-6-phosphate dehydrogenase and antioxidant enzymes in diabetic reticulocytes: effects of insulin and vanadate. |
| 527 | 9891847 | The activities of hexokinase (HK) and glucose-6-phosphate dehydrogenase (G-6PDH) were increased in reticulocyte hemolysate isolated from the diabetic rats and were restored to normal levels by insulin. |
| 528 | 9891847 | The enzymes of glutathione metabolism namely glutathione peroxidase (GPx), glutathione reductase (GR) and glutathione-s-transferase (GST) exhibited increases in their activities with diabetes and were restored to almost control values by insulin treatment. |
| 529 | 9891847 | The level of superoxide dismutase(SOD) decreased in the reticulocytes of diabetic rats and catalase (CAT) was unchanged. |
| 530 | 9891847 | Both CAT and SOD had normal values when the diabetic rats were treated with insulin and vanadate. |
| 531 | 9891847 | Hexokinase, glucose-6-phosphate dehydrogenase and antioxidant enzymes in diabetic reticulocytes: effects of insulin and vanadate. |
| 532 | 9891847 | The activities of hexokinase (HK) and glucose-6-phosphate dehydrogenase (G-6PDH) were increased in reticulocyte hemolysate isolated from the diabetic rats and were restored to normal levels by insulin. |
| 533 | 9891847 | The enzymes of glutathione metabolism namely glutathione peroxidase (GPx), glutathione reductase (GR) and glutathione-s-transferase (GST) exhibited increases in their activities with diabetes and were restored to almost control values by insulin treatment. |
| 534 | 9891847 | The level of superoxide dismutase(SOD) decreased in the reticulocytes of diabetic rats and catalase (CAT) was unchanged. |
| 535 | 9891847 | Both CAT and SOD had normal values when the diabetic rats were treated with insulin and vanadate. |
| 536 | 9951299 | High activity of catalase and superoxide dismutase activity was compensatory. |
| 537 | 10076065 | SOD-1 samples were prepared from erythrocytes by removing hemoglobin using hemoglobind gel followed by ethanol and chloroform extraction. |
| 538 | 10076185 | Moreover it significantly decreased MHC class II expression (but not class I) in vivo by week 10, and significantly enhanced intercellular adhesion molecule-1 (ICAM-1) expression, mainly by week 25, within the pancreas, where 5-bromo-2'-deoxyuridine positive nuclei and insulin positive cells were present, demonstrating that a stimulation of endocrine cell proliferation occurs. (3) In addition, NIC partly counteracted the fall of superoxide dismutase levels, observed in untreated diabetic NOD animals. (4) In vitro studies demonstrated that NIC: (i) was able to significantly reduce nitrite accumulation and to increase NAD+NADH content significantly, and (ii) was able to increase the levels of interleukin-4, a T helper 2 lymphocyte (Th2) protective cytokine, and of interferon-alpha (IFN-alpha), which is known to be able to induce MHC class I and ICAM-1 but not MHC class II expression, as well as IFN-gamma, which is also known to be able to induce MHC class I and ICAM-1 expression. |
| 539 | 10077485 | In the superoxide dismutase-dependent cytochrome c assay, 1 mM Chelex-treated aqueous solutions of monofructose-amino acids 4-6 generated 0.9-3.6 x 10(-10) M s-1 O2*- at pH 7. |
| 540 | 10077544 | A wide array of non-enzymatic and enzymatic antioxidant defenses exists, including superoxide dismutase (SOD), glutathione peroxidase (GPX) and catalase (CAT). |
| 541 | 10078995 | The purpose of the present study was to investigate the time course of changes in plasma low-density lipoprotein (LDL) cholesterol, tissue lipid peroxidation, the expression of hepatic LDL-receptor mRNA and aortic superoxide dismutase, and the relaxation response to acetylcholine in streptozotocin-induced diabetic rats. |
| 542 | 10099840 | Total mRNA of the purified pericytes was isolated for quantitative reverse transcriptase (RT)-PCR assay. mRNA levels of a death protease (CPP32), the major enzyme that initiates the proteolytic cascade leading to cell death, were determined in association with the expression of antioxidative enzymes including glutathione peroxidase (GSH-Px), glutathione reductase, CuZn superoxide dismutase (SOD), MnSOD and catalase genes in pericytes. |
| 543 | 10099840 | In diabetic pericytes, up-regulation of glutathione peroxidase (GSH-Px) (8.2 +/- 0.9 fold increase, p < 0.01, n = 9) and down-regulation of glutathione reductase (Gr) (4.1 +/- 0.4 fold decrease, p < 0.05, n = 9) and CuZnSOD (2.1 +/- 0.7 fold decrease, p < 0.05, n = 9) were observed. mRNA levels of MnSOD and catalase of diabetic pericytes did not differ significantly from those of non-diabetic pericytes. |
| 544 | 10099840 | Overexpression of a member of interleukin-1 beta-converting enzyme (ICE) family, CPP32, indicated that the pericytes from diabetic retinas are in a "pre-PCD" state. |
| 545 | 10230044 | In liver, Glutathione Peroxidase and Superoxide Dismutase decreased and in intestine Glutathione-S-transferase (GST) increased by diabetes. |
| 546 | 10319913 | GLUT-4, tumor necrosis factor, essential fatty acids and daf-genes and their role in insulin resistance and non-insulin dependent diabetes mellitus. |
| 547 | 10319913 | It is now believed that the GLUT-4 receptor, tumor necrosis factor-alpha (TNF-alpha), essential fatty acids (EFAs) and their metabolites and daf-genes have an important role in the development of obesity and non-insulin dependent diabetes mellitus (NIDDM). |
| 548 | 10319913 | The protein encoded by daf-2 is 35% identical to the human insulin receptor, daf-7 codes a transforming growth factor-beta (TGF-beta) type signal and daf-16 can enhance superoxide dismutase (SOD) expression. |
| 549 | 10319913 | EFAs and their metabolites can alter the cell membrane fluidity and enhance the expression of GLUT-4 and insulin receptors. |
| 550 | 10319913 | EFAs can suppress TNF-alpha production and secretion, a mechanism that may have relevance to the role of these fatty acids in the pathogenesis of insulin resistance, obesity and NIDDM. |
| 551 | 10319913 | Melatonin has anti-oxidant actions similar to daf-16, TGF-beta and SOD. |
| 552 | 10319913 | Based on this evidence, it is proposed that GLUT-4, TNF-alpha, EFAs, daf-genes, melatonin and leptin interact with each other in ways which may have relevance to the development or abrogation of insulin resistance, obesity, NIDDM, complications due to NIDDM, longevity and ageing. |
| 553 | 10319913 | GLUT-4, tumor necrosis factor, essential fatty acids and daf-genes and their role in insulin resistance and non-insulin dependent diabetes mellitus. |
| 554 | 10319913 | It is now believed that the GLUT-4 receptor, tumor necrosis factor-alpha (TNF-alpha), essential fatty acids (EFAs) and their metabolites and daf-genes have an important role in the development of obesity and non-insulin dependent diabetes mellitus (NIDDM). |
| 555 | 10319913 | The protein encoded by daf-2 is 35% identical to the human insulin receptor, daf-7 codes a transforming growth factor-beta (TGF-beta) type signal and daf-16 can enhance superoxide dismutase (SOD) expression. |
| 556 | 10319913 | EFAs and their metabolites can alter the cell membrane fluidity and enhance the expression of GLUT-4 and insulin receptors. |
| 557 | 10319913 | EFAs can suppress TNF-alpha production and secretion, a mechanism that may have relevance to the role of these fatty acids in the pathogenesis of insulin resistance, obesity and NIDDM. |
| 558 | 10319913 | Melatonin has anti-oxidant actions similar to daf-16, TGF-beta and SOD. |
| 559 | 10319913 | Based on this evidence, it is proposed that GLUT-4, TNF-alpha, EFAs, daf-genes, melatonin and leptin interact with each other in ways which may have relevance to the development or abrogation of insulin resistance, obesity, NIDDM, complications due to NIDDM, longevity and ageing. |
| 560 | 10322889 | [Study on syndrome-type in TCM and its correlation with superoxide dismutase and malonyldialdehyde in patients with non-insulin dependent diabetes mellitus]. |
| 561 | 10334313 | In the FT rats, insulin resistance, lower red cell CuZn superoxide dismutase activity and lower blood reduced glutathione were observed. |
| 562 | 10334467 | The above mentioned antioxidant systems of erythrocyte were determined after treatment of diabetic rats with superoxide dismutase, trolox, catalase and allopurinol. |
| 563 | 10342823 | Incubation of freshly isolated smooth muscle cells from control subjects with the *O2- -generating system xanthine oxidase/hypoxanthine mimicked the effect of diabetic patients on subcellular Ca2+ distribution in a superoxide dismutase-sensitive manner. |
| 564 | 10343979 | The content of glutathione (GSH) and its synthesizing enzyme gamma-glutamylcystein synthetase and also superoxide dismutase (SOD) and catalase activities (reactive oxygen scavenging enzymes) were significantly decreased from almost all the brain regions studied. |
| 565 | 10343979 | However, glutathione peroxidase (GPx), glutathione reductase (GR), glutathione S-transferase (GST), gamma-glutamyl transpeptidase (gamma-GTP), and glutamine synthetase (GS) activities were increased in the diabetic rat brain. |
| 566 | 10353323 | To evaluate oxidative stress in type I diabetes mellitus, two antioxidant enzymes in erythrocytes, copper-zinc superoxide dismutase (SOD EC 1.15.1.1.) and seleno-dependent glutathione peroxidase (GSH-Px; EC 1.11.19), and two indexes of peroxidation in plasma, thiobarbituric acid reactive substances (TBARS) and organic hydroperoxides (OHP), were measured in 118 patients with insulin-dependent diabetes mellitus (IDDM), classified in accordance with the presence or absence of vascular complications and the degree of metabolic control established by the HbA1c level. |
| 567 | 10381203 | Effect of superoxide dismutase, catalase, chelating agents, and free radical scavengers on the toxicity of alloxan to isolated pancreatic islets in vitro. |
| 568 | 10381203 | The effect of superoxide dismutase, catalase, metal-chelating agents and hydroxyl radical scavengers on the toxicity of alloxan to isolated ob/ob mouse pancreatic islets in vitro has been compared with the reported ability of such substances to protect against alloxan diabetes in vivo. |
| 569 | 10381203 | Superoxide dismutase and catalase protected beta-cells of isolated pancreatic islets against alloxan cytotoxicity, as did the hydroxyl radical scavengers dimethyl sulfoxide (DMSO) and butanol. |
| 570 | 10381203 | Effect of superoxide dismutase, catalase, chelating agents, and free radical scavengers on the toxicity of alloxan to isolated pancreatic islets in vitro. |
| 571 | 10381203 | The effect of superoxide dismutase, catalase, metal-chelating agents and hydroxyl radical scavengers on the toxicity of alloxan to isolated ob/ob mouse pancreatic islets in vitro has been compared with the reported ability of such substances to protect against alloxan diabetes in vivo. |
| 572 | 10381203 | Superoxide dismutase and catalase protected beta-cells of isolated pancreatic islets against alloxan cytotoxicity, as did the hydroxyl radical scavengers dimethyl sulfoxide (DMSO) and butanol. |
| 573 | 10381203 | Effect of superoxide dismutase, catalase, chelating agents, and free radical scavengers on the toxicity of alloxan to isolated pancreatic islets in vitro. |
| 574 | 10381203 | The effect of superoxide dismutase, catalase, metal-chelating agents and hydroxyl radical scavengers on the toxicity of alloxan to isolated ob/ob mouse pancreatic islets in vitro has been compared with the reported ability of such substances to protect against alloxan diabetes in vivo. |
| 575 | 10381203 | Superoxide dismutase and catalase protected beta-cells of isolated pancreatic islets against alloxan cytotoxicity, as did the hydroxyl radical scavengers dimethyl sulfoxide (DMSO) and butanol. |
| 576 | 10381563 | Previous evidence from our laboratory indicated that glycation-induced inactivation and loss of antigenicity of catalase and superoxide dismutase are simultaneous. |
| 577 | 10420119 | Superoxide dismutase, catalase, glutathione peroxidase and xanthine oxidase in diabetic rat lenses. |
| 578 | 10420119 | The activities of the protective enzymes, superoxide dismutase, catalase, glutathione peroxidase and of xanthine oxidase, an enzyme acting as a source of O(-)(2), were measured in the lenses of alloxan-induced diabetic and control rats. |
| 579 | 10420119 | Superoxide dismutase and glutathione peroxidase activities were found to be significantly decreased, while catalase and xanthine oxidase activities were increased. |
| 580 | 10420119 | Superoxide dismutase, catalase, glutathione peroxidase and xanthine oxidase in diabetic rat lenses. |
| 581 | 10420119 | The activities of the protective enzymes, superoxide dismutase, catalase, glutathione peroxidase and of xanthine oxidase, an enzyme acting as a source of O(-)(2), were measured in the lenses of alloxan-induced diabetic and control rats. |
| 582 | 10420119 | Superoxide dismutase and glutathione peroxidase activities were found to be significantly decreased, while catalase and xanthine oxidase activities were increased. |
| 583 | 10420119 | Superoxide dismutase, catalase, glutathione peroxidase and xanthine oxidase in diabetic rat lenses. |
| 584 | 10420119 | The activities of the protective enzymes, superoxide dismutase, catalase, glutathione peroxidase and of xanthine oxidase, an enzyme acting as a source of O(-)(2), were measured in the lenses of alloxan-induced diabetic and control rats. |
| 585 | 10420119 | Superoxide dismutase and glutathione peroxidase activities were found to be significantly decreased, while catalase and xanthine oxidase activities were increased. |
| 586 | 10443915 | Our observations suggest that increased production of oxygen-derived free radicals (OFRs) in diabetic state leads to a decrease in SOD activity resulting an increase in endogenous superoxide anions (O2*-), that is limited cytotoxic actions, and an increase in catalase activity resulting a decrease in both H2O2 concentrations and the production of harmful hydroxyl radical (*OH) in diabetic aorta in long-term. |
| 587 | 10457996 | Activity of antioxidant enzyme superoxide-dismutase was decreased, activity of catalase was increased. |
| 588 | 10468221 | Alloxan-susceptible (ALS/Lt) and AL-resistant (ALR/Lt) are inbred mouse strains derived in Japan by inbreeding CD-1 (ICR) mice with concomitant selection for high or low sensitivity to a relatively low AL dose. |
| 589 | 10468221 | Superoxide dismutase (SOD), catalase (CAT), glutathione reductase (GR), and glutathione peroxidase (GPX) activities were determined in tissues of AL-untreated ALR/Lt and ALS/Lt male mice at 7 weeks of age. |
| 590 | 10468221 | Specific activities of pancreatic SOD1, GR, and GPX were significantly increased in ALR/Lt mice compared with ALS/Lt mice. |
| 591 | 10468221 | Alloxan-susceptible (ALS/Lt) and AL-resistant (ALR/Lt) are inbred mouse strains derived in Japan by inbreeding CD-1 (ICR) mice with concomitant selection for high or low sensitivity to a relatively low AL dose. |
| 592 | 10468221 | Superoxide dismutase (SOD), catalase (CAT), glutathione reductase (GR), and glutathione peroxidase (GPX) activities were determined in tissues of AL-untreated ALR/Lt and ALS/Lt male mice at 7 weeks of age. |
| 593 | 10468221 | Specific activities of pancreatic SOD1, GR, and GPX were significantly increased in ALR/Lt mice compared with ALS/Lt mice. |
| 594 | 10468221 | Alloxan-susceptible (ALS/Lt) and AL-resistant (ALR/Lt) are inbred mouse strains derived in Japan by inbreeding CD-1 (ICR) mice with concomitant selection for high or low sensitivity to a relatively low AL dose. |
| 595 | 10468221 | Superoxide dismutase (SOD), catalase (CAT), glutathione reductase (GR), and glutathione peroxidase (GPX) activities were determined in tissues of AL-untreated ALR/Lt and ALS/Lt male mice at 7 weeks of age. |
| 596 | 10468221 | Specific activities of pancreatic SOD1, GR, and GPX were significantly increased in ALR/Lt mice compared with ALS/Lt mice. |
| 597 | 10509893 | The aim of this study was to analyse the effect of angiotensin convertase inhibitor, enalapril (ENA), and angiotensin AT-1 receptor antagonist, losartan potassium (LP), on lipid peroxidation and activities of Cu,Zn-superoxide dismutase, catalase and glutathione peroxidase in kidneys of streptozotocin (STZ)-induced diabetic rats after 6 and 12 weeks of treatment. |
| 598 | 10509893 | Kidneys of STZ-diabetic rats had increased malondialdehyde content and decreased activities of antioxidant enzymes (Cu,Zn-superoxide dismutase, catalase and glutathione peroxidase). |
| 599 | 10509893 | The aim of this study was to analyse the effect of angiotensin convertase inhibitor, enalapril (ENA), and angiotensin AT-1 receptor antagonist, losartan potassium (LP), on lipid peroxidation and activities of Cu,Zn-superoxide dismutase, catalase and glutathione peroxidase in kidneys of streptozotocin (STZ)-induced diabetic rats after 6 and 12 weeks of treatment. |
| 600 | 10509893 | Kidneys of STZ-diabetic rats had increased malondialdehyde content and decreased activities of antioxidant enzymes (Cu,Zn-superoxide dismutase, catalase and glutathione peroxidase). |
| 601 | 10515583 | Mouse islets were found to contain little EC-SOD, whereas the content of the cytosolic Cu- and Zn-containing SOD was very high. |
| 602 | 10547879 | The catalase, superoxide dismutase, glutathione reductase, and glutathione peroxidase activities of cytosolic fractions from both liver and forebrain were shown to decrease significantly in prediabetic rats, and these alterations were virtually prevented by the course of MK-801 administration. |
| 603 | 10590399 | We found a high rate of congenital anomalies, decreased growth and protein content, and a decrease in the activity of both superoxide dismutase (SOD) and catalase (CAT) under diabetic conditions, as compared with controls. |
| 604 | 10591149 | Both sorbitol accumulation-linked osmotic stress and "pseudohypoxia" [increase in NADH/NAD+, similar to that in hypoxic tissues, and attributed to increased sorbitol dehydrogenase (1-iditol:NAD+ 5-oxidoreductase; EC 1.1.1.14; SDH) activity] have been invoked among the mechanisms underlying oxidative injury in target tissues for diabetic complications. |
| 605 | 10591149 | Superoxide dismutase (superoxide:superoxide oxidoreductase; EC 1.15.1.1), GSSG reductase (NAD[P]H:oxidized-glutathione oxidoreductase; EC 1.6.4.2), GSH transferase (glutathione S-transferase; EC 2.5.1.18), GSH peroxidase (glutathione:hydrogen-peroxide oxidoreductase; EC 1.11.1.9), and cytoplasmic NADH oxidase activities were increased in diabetic rats versus controls, and all the enzymes but GSH peroxidase were up-regulated further by SDI. |
| 606 | 10615956 | Increased mRNA levels of Mn-SOD and catalase in embryos of diabetic rats from a malformation-resistant strain. |
| 607 | 10615956 | We determined the mRNA levels of catalase, glutathione peroxidase, gamma-glutamylcystein-synthetase, glutathione reductase, and superoxide dismutase (CuZn-SOD and Mn-SOD) in day 11 embryos of normal and diabetic H and U rats using semiquantitative reverse transcription-polymerase chain reaction. |
| 608 | 10615956 | The mRNA levels of catalase and Mn-SOD were increased in H embryos as a response to maternal diabetes, and no differences were found for the other genes. |
| 609 | 10617683 | The glutathione level and activities of superoxide dismutase and glutathione reductase in liver and other tissues examined were not affected by HNF-1alpha deficiency. |
| 610 | 10617683 | The loss of hepatic catalase activity in HNF-1alpha-null mice is probably caused by an insufficient heme pool in liver cells, because the mRNA level of ferrochelatase, the enzyme that catalyzes the last step of heme biosynthesis, was significantly reduced in liver, and the daily hemin treatment restored partial catalase activity in liver of HNF-1alpha-null mice. |
| 611 | 10619578 | ROS was monitored with the dye, dihydrorhodamine-123 (DHR; 1 micromol/L) in the presence or absence of superoxide dismutase (superoxide scavenger), sodium azide (singlet oxygen/hydrogen peroxide scavenger), genistein (tyrosine kinase inhibitor), or bisindolylmaleimide (protein kinase C inhibitor). |
| 612 | 10619578 | The fMLP-induced ROS increase was significantly reduced in the presence of sodium azide in all groups (P<.01) but was largely unaffected in the presence of SOD. |
| 613 | 10619578 | ROS was monitored with the dye, dihydrorhodamine-123 (DHR; 1 micromol/L) in the presence or absence of superoxide dismutase (superoxide scavenger), sodium azide (singlet oxygen/hydrogen peroxide scavenger), genistein (tyrosine kinase inhibitor), or bisindolylmaleimide (protein kinase C inhibitor). |
| 614 | 10619578 | The fMLP-induced ROS increase was significantly reduced in the presence of sodium azide in all groups (P<.01) but was largely unaffected in the presence of SOD. |
| 615 | 10625575 | Role of endothelin and free radicals was examined using ET-A or ET-B receptor antagonists (BQ-123 or BQ-788) and superoxide anions or hydroxyl radicals scavengers (superoxide dismutase (SOD) or N-acetyl cysteine (NAC)). |
| 616 | 10625575 | BQ-123 and BQ-788 were equally potent normalizing the PE responses to SP whereas SOD and NAC had no effect. |
| 617 | 10625575 | Role of endothelin and free radicals was examined using ET-A or ET-B receptor antagonists (BQ-123 or BQ-788) and superoxide anions or hydroxyl radicals scavengers (superoxide dismutase (SOD) or N-acetyl cysteine (NAC)). |
| 618 | 10625575 | BQ-123 and BQ-788 were equally potent normalizing the PE responses to SP whereas SOD and NAC had no effect. |
| 619 | 10641141 | Superoxide dismutase, catalase and glutathione peroxidase activities in the brain of streptozotocin induced diabetic rats. |
| 620 | 10641141 | Brain antioxidant enzymes, superoxide dismutase (SOD), catalase (CAT) and glutathione peroxidase (GPX) levels were studied in the brains of early diabetic (72 hr) and long term diabetic (one month) rats. |
| 621 | 10641141 | On the contrary, increased CAT decreased GPX activities with no alteration in the SOD activity, was noted in the long-term Diabetic rats. |
| 622 | 10641141 | Superoxide dismutase, catalase and glutathione peroxidase activities in the brain of streptozotocin induced diabetic rats. |
| 623 | 10641141 | Brain antioxidant enzymes, superoxide dismutase (SOD), catalase (CAT) and glutathione peroxidase (GPX) levels were studied in the brains of early diabetic (72 hr) and long term diabetic (one month) rats. |
| 624 | 10641141 | On the contrary, increased CAT decreased GPX activities with no alteration in the SOD activity, was noted in the long-term Diabetic rats. |
| 625 | 10641141 | Superoxide dismutase, catalase and glutathione peroxidase activities in the brain of streptozotocin induced diabetic rats. |
| 626 | 10641141 | Brain antioxidant enzymes, superoxide dismutase (SOD), catalase (CAT) and glutathione peroxidase (GPX) levels were studied in the brains of early diabetic (72 hr) and long term diabetic (one month) rats. |
| 627 | 10641141 | On the contrary, increased CAT decreased GPX activities with no alteration in the SOD activity, was noted in the long-term Diabetic rats. |
| 628 | 10657585 | In parallel experiments, the keto acid was replaced by catalase, superoxide dismutase (SOD), or diethylene triaminepentaacetic acid (DTPA). |
| 629 | 10657585 | Catalase, SOD, and DTPA were also effective. |
| 630 | 10657585 | In parallel experiments, the keto acid was replaced by catalase, superoxide dismutase (SOD), or diethylene triaminepentaacetic acid (DTPA). |
| 631 | 10657585 | Catalase, SOD, and DTPA were also effective. |
| 632 | 10661714 | Alloxan elicited significant inhibition of antioxidants including superoxide dismutase, catalase and glutathione reductase activities and decreased glutathione content in testis. |
| 633 | 10662734 | Experiments were performed to test the hypothesis that the impact of endogenous nitric oxide (NO) on ANG II-induced renal arteriolar constriction is reduced in rats with insulin-dependent diabetes mellitus (65 mg/kg streptozotocin; STZ). |
| 634 | 10662734 | Superoxide dismutase (150 U/ml) restored the ability of L-NNA to allow exaggerated afferent arteriolar responses to ANG II in kidneys from STZ rats. |
| 635 | 10685115 | The decrease in thiobarbituric acid reactive substances (TBARS) and the increase in reduced glutathione (GSH), glutathione peroxidase (GSH-Px), superoxide dismutase (SOD) and catalase (CAT) clearly shows the antioxidant property of BFEt. |
| 636 | 10693916 | Measurements were taken of hemostatic variables, the oxidative status of the plasma, and the redox status, both extracellularly as plasma albumin-thiols (PSH) and lipid peroxides, and intracellularly as red blood cell superoxide dismutase activity (SOD). |
| 637 | 10720884 | Administration of superoxide dismutase (SOD), which dismutates.O(-)(2) to H(2)O(2), and of catalase which reacts with H(2)O(2) to form H(2)O and molecular oxygen failed to inhibit the increased extravasation of the macromolecular tracer when administered separately. |
| 638 | 10776471 | The activity of antioxidant enzymes such as superoxide dismutase (P < 0.001), catalase (P < 0.001), GSHPxase and GSSGRase was found to be increased in the heart tissue of diabetic animals treated with SOB. |
| 639 | 10778531 | GLUT-4, tumour necrosis factor, essential fatty acids and daf-genes and their role in glucose homeostasis, insulin resistance, non-insulin dependent diabetes mellitus, and longevity. |
| 640 | 10778531 | GLUT-4 receptor, tumor necrosis factor-alpha (TNF-alpha), essential fatty acids (EFAs) and their metabolites and daf-genes seem to play an important and essential role in the maintenance of glucose homeostasis, and in the pathobiology of obesity and non-insulin dependent diabetes mellitus (NIDDM). |
| 641 | 10778531 | Daf-genes encode for proteins which are 35% identical to the human insulin receptor, a transforming growth factor-beta (TGF-beta) type signal and can also enhance the expression of superoxide dismutase (SOD). |
| 642 | 10778531 | On the other hand, EFAs and their metabolites can increase the cell membrane fluidity and thus, enhance the expression of GLUT-4 and insulin receptors. |
| 643 | 10778531 | In addition, EFAs can suppress TNF-alpha production and secretion and thus, are capable of reversing insulin resistance. |
| 644 | 10778531 | Melatonin has anti-oxidant actions similar to daf-16, TGF-beta and SOD. |
| 645 | 10778531 | Hence, it is likely that there is a close interaction between GLUT-4, TNF-alpha, EFAs, daf-genes, melatonin and leptin that may have relevance to the development of insulin resistance, obesity, NIDDM, complications due to NIDDM, longevity and ageing. |
| 646 | 10778531 | GLUT-4, tumour necrosis factor, essential fatty acids and daf-genes and their role in glucose homeostasis, insulin resistance, non-insulin dependent diabetes mellitus, and longevity. |
| 647 | 10778531 | GLUT-4 receptor, tumor necrosis factor-alpha (TNF-alpha), essential fatty acids (EFAs) and their metabolites and daf-genes seem to play an important and essential role in the maintenance of glucose homeostasis, and in the pathobiology of obesity and non-insulin dependent diabetes mellitus (NIDDM). |
| 648 | 10778531 | Daf-genes encode for proteins which are 35% identical to the human insulin receptor, a transforming growth factor-beta (TGF-beta) type signal and can also enhance the expression of superoxide dismutase (SOD). |
| 649 | 10778531 | On the other hand, EFAs and their metabolites can increase the cell membrane fluidity and thus, enhance the expression of GLUT-4 and insulin receptors. |
| 650 | 10778531 | In addition, EFAs can suppress TNF-alpha production and secretion and thus, are capable of reversing insulin resistance. |
| 651 | 10778531 | Melatonin has anti-oxidant actions similar to daf-16, TGF-beta and SOD. |
| 652 | 10778531 | Hence, it is likely that there is a close interaction between GLUT-4, TNF-alpha, EFAs, daf-genes, melatonin and leptin that may have relevance to the development of insulin resistance, obesity, NIDDM, complications due to NIDDM, longevity and ageing. |
| 653 | 10779046 | The basal ET-1 production was markedly attenuated by ROS scavengers including superoxide dismutase, catalase, dimethyl sulfoxide, and deferoxamine in diabetic glomeruli. |
| 654 | 10779046 | Exogenous ROS generated by xanthine/xanthine oxidase significantly enhanced ET-1 generation by both diabetic and normal glomeruli. |
| 655 | 10779046 | A high glucose concentration (500 mg/dL) in vitro increased ET-1 production by normal glomeruli but not diabetic glomeruli, and insulin partly suppressed ET- 1 production by diabetic glomeruli. |
| 656 | 10779046 | The in vivo study demonstrated that when diabetic rats were injected daily with superoxide dismutase or catalase after diabetes was induced, the basal production of ET-1 was markedly attenuated after 1 week and 1 month, respectively. |
| 657 | 10779046 | The effects of ROS on ET-1 production of diabetic glomeruli may be partly caused by the effect of hyperglycemia or insulin deficiency. |
| 658 | 10779046 | The basal ET-1 production was markedly attenuated by ROS scavengers including superoxide dismutase, catalase, dimethyl sulfoxide, and deferoxamine in diabetic glomeruli. |
| 659 | 10779046 | Exogenous ROS generated by xanthine/xanthine oxidase significantly enhanced ET-1 generation by both diabetic and normal glomeruli. |
| 660 | 10779046 | A high glucose concentration (500 mg/dL) in vitro increased ET-1 production by normal glomeruli but not diabetic glomeruli, and insulin partly suppressed ET- 1 production by diabetic glomeruli. |
| 661 | 10779046 | The in vivo study demonstrated that when diabetic rats were injected daily with superoxide dismutase or catalase after diabetes was induced, the basal production of ET-1 was markedly attenuated after 1 week and 1 month, respectively. |
| 662 | 10779046 | The effects of ROS on ET-1 production of diabetic glomeruli may be partly caused by the effect of hyperglycemia or insulin deficiency. |
| 663 | 10780678 | We evaluated the gene expression of glutathione peroxidase, catalase, and superoxide dismutase (cuprozinc and manganese separately) in L4,5 dorsal root ganglion (DRG) and superior cervical ganglion, as well as enzyme activity of glutathione peroxidase in DRG and sciatic nerve in experimental diabetic neuropathy of 3 months and 12 months durations. |
| 664 | 10780678 | Gene expression of glutathione peroxidase, catalase, cuprozinc superoxide dismutase, and manganese superoxide dismutase were not reduced in experimental diabetic neuropathy at either 3 or 12 months. |
| 665 | 10782751 | Other parameters of antioxidant capacity such as blood GSH, catalase and superoxide dismutase activities, as well as in vitro formation of thiobarbituric acid reactive substances (TBARS), were unaffected by either flavonoid or placebo. |
| 666 | 10789496 | Activity levels of superoxide dismutase, catalase, glutathione peroxidase, and glutathione reductase, concentrations of oxidized and reduced glutathione, and lipid peroxidation were used as measures of antioxidant defense in liver, kidney, heart, and brain tissue. |
| 667 | 10804329 | SO(2) exposure, while markedly decreasing Cu, Zn-Superoxide dismutase (Cu, Zn-SOD) activity, significantly increased glutathione peroxidase (GSH-Px), catalase (CAT), glutathione (GSH) and glutathione-s-transferase (GST) activities and TBARS values in CSO(2) and DSO(2) groups compared with their respective control groups. |
| 668 | 10810880 | Incubation of human aortic endothelial cells(HAEC) with glycated LDL had little influence on the expression of antioxidant enzymes such as nitric oxide synthase(NOS), Cu2+Zn(2+)-superoxide dismutase (Cu2+Zn(2+)-SOD), catalase, and p22 phox in the cells. |
| 669 | 10810880 | In contrast, exposure of glycated HDL induced a marked decrease of Cu2+Zn(2+)-SOD, catalase, and endothelial NOS as well as a slight increase of p22 phox in HAEC in term of both protein and mRNA expression, suggesting that increased formation of reactive oxygen species such as O2- and OH radical participate in the deterioration for the function of vascular endothelial cells in diabetic patients. |
| 670 | 10810880 | Incubation of human aortic endothelial cells(HAEC) with glycated LDL had little influence on the expression of antioxidant enzymes such as nitric oxide synthase(NOS), Cu2+Zn(2+)-superoxide dismutase (Cu2+Zn(2+)-SOD), catalase, and p22 phox in the cells. |
| 671 | 10810880 | In contrast, exposure of glycated HDL induced a marked decrease of Cu2+Zn(2+)-SOD, catalase, and endothelial NOS as well as a slight increase of p22 phox in HAEC in term of both protein and mRNA expression, suggesting that increased formation of reactive oxygen species such as O2- and OH radical participate in the deterioration for the function of vascular endothelial cells in diabetic patients. |
| 672 | 10826918 | The purpose of this study was to examine whether the activities of glyceraldehyde-3-phosphate dehydrogenase (GAPDH), catalase and superoxide dismutase (SOD) could be affected by the high levels of fructose prevalent in diabetic lenses. |
| 673 | 10826918 | This was followed by the inactivation of catalase (3-4 days) and SOD (6 days). |
| 674 | 10826918 | The purpose of this study was to examine whether the activities of glyceraldehyde-3-phosphate dehydrogenase (GAPDH), catalase and superoxide dismutase (SOD) could be affected by the high levels of fructose prevalent in diabetic lenses. |
| 675 | 10826918 | This was followed by the inactivation of catalase (3-4 days) and SOD (6 days). |
| 676 | 10831236 | Hepatic superoxide dismutase (SOD), catalase (CAT) and glutathione peroxidase (GSH-Px) activities were significantly lower in vehicle-treated diabetic rats compared with vehicle-treated normal rats. |
| 677 | 10831236 | The extract, as well as metformin, significantly increased the activity of SOD and CAT, but had no significant effect on GSH-Px activity in diabetic rats. |
| 678 | 10831236 | Hepatic superoxide dismutase (SOD), catalase (CAT) and glutathione peroxidase (GSH-Px) activities were significantly lower in vehicle-treated diabetic rats compared with vehicle-treated normal rats. |
| 679 | 10831236 | The extract, as well as metformin, significantly increased the activity of SOD and CAT, but had no significant effect on GSH-Px activity in diabetic rats. |
| 680 | 10856458 | Superoxide dismutase, glutathione peroxidase (GSHPx), glutathione reductase (GSSGRed) and glutathione transferase (GSHTrans) activities were decreased in diabetic rats vs. controls. |
| 681 | 10871429 | The aim of the study was to investigate the effect of 10 ppm sulfur dioxide (SO(2)) exposure on visual evoked potentials (VEPs), thiobarbituric acid reactive substances (TBARS), and the activities of Cu,Zn superoxide dismutase (SOD), glutathione peroxidase (GSH-Px), and catalase (CAT) in diabetes mellitus. |
| 682 | 10909968 | We therefore examined whether overexpression of catalase (Cat), glutathione peroxidase (Gpx), and Cu/Zn superoxide dismutase (SOD) can provide protection for bioengineered RINm5F cells against cytokine-mediated toxicity. |
| 683 | 10909968 | A 72-h exposure of RINm5F control cells to interleukin-1beta (IL-1beta) alone or a combination of IL-1beta, tumor necrosis factor-alpha, and gamma-interferon resulted in a time- and concentration-dependent decrease of cell viability in the 3-[4,5-dimethylthiazol-2-yl]-2,5-diphenyl tetrazolium bromide (MTT) cytotoxicity assay. |
| 684 | 10909968 | Overexpression of Cat, Gpx, and Cu/Zn SOD protected against toxicity of the cytokine mixture but not against that of IL-1beta alone. |
| 685 | 10909968 | We therefore examined whether overexpression of catalase (Cat), glutathione peroxidase (Gpx), and Cu/Zn superoxide dismutase (SOD) can provide protection for bioengineered RINm5F cells against cytokine-mediated toxicity. |
| 686 | 10909968 | A 72-h exposure of RINm5F control cells to interleukin-1beta (IL-1beta) alone or a combination of IL-1beta, tumor necrosis factor-alpha, and gamma-interferon resulted in a time- and concentration-dependent decrease of cell viability in the 3-[4,5-dimethylthiazol-2-yl]-2,5-diphenyl tetrazolium bromide (MTT) cytotoxicity assay. |
| 687 | 10909968 | Overexpression of Cat, Gpx, and Cu/Zn SOD protected against toxicity of the cytokine mixture but not against that of IL-1beta alone. |
| 688 | 10971747 | In aged rats (18 months old), higher levels of skin superoxide dismutase (SOD), glutathione peroxidase (Gpx) and thiobarbituric acid reactive substances (TBARS) and lower levels of catalase and GSH were found as compared to their values in young rats (3-4 months old). |
| 689 | 10971747 | The levels of SOD, GPx, catalase, AA, GSH and vitamin E in 7-d wound tissue of aged rats were significantly lower in comparison to those in young rats. |
| 690 | 10971747 | The non-wounded skin of immunocompromised (athymic) mice showed lower levels of SOD, catalase, and TBARS and higher GSH and GPx levels in comparison to those present in normal mouse skin. |
| 691 | 10971747 | Surprisingly, the analysis of 7-d wound tissue showed higher levels of SOD, catalase, GPx, and GSH and lower TBARS level in athymic mice compared to the wound tissue of normal mice. |
| 692 | 10971747 | In aged rats (18 months old), higher levels of skin superoxide dismutase (SOD), glutathione peroxidase (Gpx) and thiobarbituric acid reactive substances (TBARS) and lower levels of catalase and GSH were found as compared to their values in young rats (3-4 months old). |
| 693 | 10971747 | The levels of SOD, GPx, catalase, AA, GSH and vitamin E in 7-d wound tissue of aged rats were significantly lower in comparison to those in young rats. |
| 694 | 10971747 | The non-wounded skin of immunocompromised (athymic) mice showed lower levels of SOD, catalase, and TBARS and higher GSH and GPx levels in comparison to those present in normal mouse skin. |
| 695 | 10971747 | Surprisingly, the analysis of 7-d wound tissue showed higher levels of SOD, catalase, GPx, and GSH and lower TBARS level in athymic mice compared to the wound tissue of normal mice. |
| 696 | 10971747 | In aged rats (18 months old), higher levels of skin superoxide dismutase (SOD), glutathione peroxidase (Gpx) and thiobarbituric acid reactive substances (TBARS) and lower levels of catalase and GSH were found as compared to their values in young rats (3-4 months old). |
| 697 | 10971747 | The levels of SOD, GPx, catalase, AA, GSH and vitamin E in 7-d wound tissue of aged rats were significantly lower in comparison to those in young rats. |
| 698 | 10971747 | The non-wounded skin of immunocompromised (athymic) mice showed lower levels of SOD, catalase, and TBARS and higher GSH and GPx levels in comparison to those present in normal mouse skin. |
| 699 | 10971747 | Surprisingly, the analysis of 7-d wound tissue showed higher levels of SOD, catalase, GPx, and GSH and lower TBARS level in athymic mice compared to the wound tissue of normal mice. |
| 700 | 10971747 | In aged rats (18 months old), higher levels of skin superoxide dismutase (SOD), glutathione peroxidase (Gpx) and thiobarbituric acid reactive substances (TBARS) and lower levels of catalase and GSH were found as compared to their values in young rats (3-4 months old). |
| 701 | 10971747 | The levels of SOD, GPx, catalase, AA, GSH and vitamin E in 7-d wound tissue of aged rats were significantly lower in comparison to those in young rats. |
| 702 | 10971747 | The non-wounded skin of immunocompromised (athymic) mice showed lower levels of SOD, catalase, and TBARS and higher GSH and GPx levels in comparison to those present in normal mouse skin. |
| 703 | 10971747 | Surprisingly, the analysis of 7-d wound tissue showed higher levels of SOD, catalase, GPx, and GSH and lower TBARS level in athymic mice compared to the wound tissue of normal mice. |
| 704 | 10976754 | Xanthine/xanthine oxidase, which produces superoxide anion, lowered the creatine kinase activity in the same manner whose effect was protected by superoxide dismutase. |
| 705 | 10979539 | Plasma lipids and apolipoprotein B levels were determined as well as two antioxidants: alpha-tocopherol level and superoxide dismutase activity. |
| 706 | 10984609 | In addition, the lipid peroxidation caused by Amadori-PE was effectively inhibited by superoxide dismutase, mannitol, catalase and metal chelator. |
| 707 | 10995033 | Effects of the angiotensin convertase inhibitors captopril (CAP) and enalapril (ENA) on the malondialdehyde (MDA) content and the activities of superoxide dismutase (SOD) and catalase in the kidneys of rats with streptozotocin-induced diabetes were studied. |
| 708 | 10995033 | Induction of diabetes resulted in an increase of MDA concentration and progressive decreases of SOD and catalase activities after 6 and 12 weeks. |
| 709 | 10995033 | CAP and ENA administration did not affect body weight changes or blood glucose and HbA1c contents in diabetic rats but decreased albuminuria and kidney weight increase, attenuated lipid peroxidation, and prevented the decreases in SOD and catalase activities. |
| 710 | 10995033 | Effects of the angiotensin convertase inhibitors captopril (CAP) and enalapril (ENA) on the malondialdehyde (MDA) content and the activities of superoxide dismutase (SOD) and catalase in the kidneys of rats with streptozotocin-induced diabetes were studied. |
| 711 | 10995033 | Induction of diabetes resulted in an increase of MDA concentration and progressive decreases of SOD and catalase activities after 6 and 12 weeks. |
| 712 | 10995033 | CAP and ENA administration did not affect body weight changes or blood glucose and HbA1c contents in diabetic rats but decreased albuminuria and kidney weight increase, attenuated lipid peroxidation, and prevented the decreases in SOD and catalase activities. |
| 713 | 10995033 | Effects of the angiotensin convertase inhibitors captopril (CAP) and enalapril (ENA) on the malondialdehyde (MDA) content and the activities of superoxide dismutase (SOD) and catalase in the kidneys of rats with streptozotocin-induced diabetes were studied. |
| 714 | 10995033 | Induction of diabetes resulted in an increase of MDA concentration and progressive decreases of SOD and catalase activities after 6 and 12 weeks. |
| 715 | 10995033 | CAP and ENA administration did not affect body weight changes or blood glucose and HbA1c contents in diabetic rats but decreased albuminuria and kidney weight increase, attenuated lipid peroxidation, and prevented the decreases in SOD and catalase activities. |
| 716 | 11050665 | Removal of oxygen species by incubating pancreatic tissues in the presence of polyethylene glycol-conjugated superoxide dismutase (PEG-SOD) (1 U/ml) produced a decrease in nitrite levels (42%) and NO synthase (NOS) activity (50%) in diabetic but not in control samples. |
| 717 | 11050665 | Moreover, inhibition of NOS activity produces an increase in SOD activity and a decrease in lipoperoxidation in diabetic pancreatic tissues. |
| 718 | 11050665 | Removal of oxygen species by incubating pancreatic tissues in the presence of polyethylene glycol-conjugated superoxide dismutase (PEG-SOD) (1 U/ml) produced a decrease in nitrite levels (42%) and NO synthase (NOS) activity (50%) in diabetic but not in control samples. |
| 719 | 11050665 | Moreover, inhibition of NOS activity produces an increase in SOD activity and a decrease in lipoperoxidation in diabetic pancreatic tissues. |
| 720 | 11064109 | The enzymes tested were dipeptidyl-peptidase I (DPP-I), cathepsin B and D, NADPH oxidase and superoxide dismutase (oxidative burst) and collagenase. |
| 721 | 11064109 | Enzyme activity of cathepsin B and D in all cell subsets, oxidative burst in PMN cells, and DPP-I in lymphocytes and monocytes from patients, was higher than those from healthy females (P<0.05). |
| 722 | 11083086 | Liver, kidney, brain, and heart were assayed for degree of lipid peroxidation, reduced and oxidized glutathione (GSH and GSSG, respectively) content, and activities of the free-radical detoxifying enzymes catalase, superoxide dismutase, glutathione peroxidase, and glutathione reductase. |
| 723 | 11083086 | Treatment with piperine reversed the diabetic effects on GSSG concentration in brain, on renal glutathione peroxidase and superoxide dismutase activities, and on cardiac glutathione reductase activity and lipid peroxidation. |
| 724 | 11083086 | Piperine treatment did not reverse the effects of diabetes on hepatic GSH concentrations, lipid peroxidation, or glutathione peroxidase or catalase activities; on renal superoxide dismutase activity; or on cardiac glutathione peroxidase or catalase activities. |
| 725 | 11083086 | Liver, kidney, brain, and heart were assayed for degree of lipid peroxidation, reduced and oxidized glutathione (GSH and GSSG, respectively) content, and activities of the free-radical detoxifying enzymes catalase, superoxide dismutase, glutathione peroxidase, and glutathione reductase. |
| 726 | 11083086 | Treatment with piperine reversed the diabetic effects on GSSG concentration in brain, on renal glutathione peroxidase and superoxide dismutase activities, and on cardiac glutathione reductase activity and lipid peroxidation. |
| 727 | 11083086 | Piperine treatment did not reverse the effects of diabetes on hepatic GSH concentrations, lipid peroxidation, or glutathione peroxidase or catalase activities; on renal superoxide dismutase activity; or on cardiac glutathione peroxidase or catalase activities. |
| 728 | 11083086 | Liver, kidney, brain, and heart were assayed for degree of lipid peroxidation, reduced and oxidized glutathione (GSH and GSSG, respectively) content, and activities of the free-radical detoxifying enzymes catalase, superoxide dismutase, glutathione peroxidase, and glutathione reductase. |
| 729 | 11083086 | Treatment with piperine reversed the diabetic effects on GSSG concentration in brain, on renal glutathione peroxidase and superoxide dismutase activities, and on cardiac glutathione reductase activity and lipid peroxidation. |
| 730 | 11083086 | Piperine treatment did not reverse the effects of diabetes on hepatic GSH concentrations, lipid peroxidation, or glutathione peroxidase or catalase activities; on renal superoxide dismutase activity; or on cardiac glutathione peroxidase or catalase activities. |
| 731 | 11095103 | Certain cytokines (interleukin-1beta, tumor necrosis factor-alpha and interferon-gamma) either alone or in combination, are able to activate signal transduction pathways in beta-cells leading to transcription factor activation and de novo gene expression. |
| 732 | 11095103 | However, other induced proteins SUCH AS heat shock protein 70 and superoxide dismutase may reflect a defense reaction elicited in the beta-cells by the cytokines. |
| 733 | 11106836 | We determined: (1) plasma carbonyl (PCO), plasma total thiol (T-SH), and nitrotyrosine (NT) levels as markers of oxidative protein damage; (2) plasma lipid hydroperoxide (LHP), and nitric oxide (NO) levels as markers of oxidative stress; (3) plasma total antioxidant capacity (TAO), ceruloplasmin (Cp), transferrin (TRF), unsaturated iron binding capacity (UIBC), erythrocyte glutathione (GSH), and erythrocyte superoxide dismutase (SOD) as markers of free radical scavengers. |
| 734 | 11119018 | All the diabetic patients had higher concentrations of glycated hemoglobin (HbA1) compared to controls (10.51 +/- 2.42% vs 6.31 +/- 0.85% P <0.001). |
| 735 | 11119018 | Erythrocyte catalase (CAT) activity was increased and Glutathione peroxidase (GPx) activity was decreased in diabetic patients compared to controls, but no significant change in Superoxide dismutase (SOD) activity was observed in diabetic patients (CAT: 104.94 +/- 37.1 KU/g Hb vs 85.8 +/- 23.6 KU/g Hb, P <0.01; GPx: 30 +/- 9.7 U/g Hb/min vs 40.84 +/- 12.3 U/g Hb/min, P <0. 001; SOD: 2.4 +/- 1.2 U/mg Hb/min vs 2.55 +/- 0.84 U/mg Hb/min, P=NS). |
| 736 | 11119018 | In comparison with the diabetic group without MVC, the diabetic group with MVC had decreased GPx and SOD activities, while no difference was observed between these two groups regarding CAT activity (GPx: 25.32 +/- 8.4 U/g Hb/min vs 34.5 +/- 8.8 U/g Hb/min, P <0.001; SOD: 1.83 +/- 0.53 U/mg Hb/min vs 2.84 +/- 1.4 U/mg Hb/min, P<0.001; CAT: 106.3 +/- 39.9 KU/g Hb vs 103 +/- 34.9 KU/g Hb, P =NS). |
| 737 | 11119018 | All the diabetic patients had higher concentrations of glycated hemoglobin (HbA1) compared to controls (10.51 +/- 2.42% vs 6.31 +/- 0.85% P <0.001). |
| 738 | 11119018 | Erythrocyte catalase (CAT) activity was increased and Glutathione peroxidase (GPx) activity was decreased in diabetic patients compared to controls, but no significant change in Superoxide dismutase (SOD) activity was observed in diabetic patients (CAT: 104.94 +/- 37.1 KU/g Hb vs 85.8 +/- 23.6 KU/g Hb, P <0.01; GPx: 30 +/- 9.7 U/g Hb/min vs 40.84 +/- 12.3 U/g Hb/min, P <0. 001; SOD: 2.4 +/- 1.2 U/mg Hb/min vs 2.55 +/- 0.84 U/mg Hb/min, P=NS). |
| 739 | 11119018 | In comparison with the diabetic group without MVC, the diabetic group with MVC had decreased GPx and SOD activities, while no difference was observed between these two groups regarding CAT activity (GPx: 25.32 +/- 8.4 U/g Hb/min vs 34.5 +/- 8.8 U/g Hb/min, P <0.001; SOD: 1.83 +/- 0.53 U/mg Hb/min vs 2.84 +/- 1.4 U/mg Hb/min, P<0.001; CAT: 106.3 +/- 39.9 KU/g Hb vs 103 +/- 34.9 KU/g Hb, P =NS). |
| 740 | 11125843 | Superoxide dismutase (SOD), glutathione peroxidase and glutathione reductase activities were unaltered in the brain of diabetic rats. |
| 741 | 11165687 | The activity of superoxide dismutase, catalase and glutathione peroxidase and the level of insulin were decreased by 46% (from 1367+/-73 to 737+/-59 U/g Hb, P<0.001), 36% (from 2.3+/-0.3 to 1.4+/-0.1 U Bergmayera/g Hb, P<0.001), 31% (from 236+/-19 to 163+/-24 U/g Hb, P<0.001) and 91% (from 47.5+/-1.7 to 2.4+/-0.5 mU/l, P<0.001) respectively in rats treated with streptozotocin. |
| 742 | 11165687 | The administration of bradykinin caused the decrease in glucose, hydrogen peroxide and malondi-aldehyde levels by 38% (from 21.4+/-1.3 to 13.3+/-1.0 mmol/l, P<0.001), 37% (from 5.6+/-0.3 to 4.3+/-0.2 mmol H2O2/ml, P<0.001), 39% (from 4.9+/-0.2 to 3.0+/-0.2 nmol/l, P<0.001) respectively and the increase in insulin level and superoxide dismutase, catalase and glutathione peroxidase activity by 62% (from 2.4+/-0.5 to 4.0+/-0.4 mU/l, P<0.001), 23% (from 736.8+/-58.5 to 906.7+/-47.8 U/g Hb, P<0.001), 23% (from 1.4+/-0.1 to 1.9+/-0.1 U Bergmayera/g Hb, P<0.01) and 19% (from 163.1+/-23.6 to 202.3+/-11.7 U/g Hb, P<0.001) respectively in rats with hyperglycaemia. |
| 743 | 11165687 | The activity of superoxide dismutase, catalase and glutathione peroxidase and the level of insulin were decreased by 46% (from 1367+/-73 to 737+/-59 U/g Hb, P<0.001), 36% (from 2.3+/-0.3 to 1.4+/-0.1 U Bergmayera/g Hb, P<0.001), 31% (from 236+/-19 to 163+/-24 U/g Hb, P<0.001) and 91% (from 47.5+/-1.7 to 2.4+/-0.5 mU/l, P<0.001) respectively in rats treated with streptozotocin. |
| 744 | 11165687 | The administration of bradykinin caused the decrease in glucose, hydrogen peroxide and malondi-aldehyde levels by 38% (from 21.4+/-1.3 to 13.3+/-1.0 mmol/l, P<0.001), 37% (from 5.6+/-0.3 to 4.3+/-0.2 mmol H2O2/ml, P<0.001), 39% (from 4.9+/-0.2 to 3.0+/-0.2 nmol/l, P<0.001) respectively and the increase in insulin level and superoxide dismutase, catalase and glutathione peroxidase activity by 62% (from 2.4+/-0.5 to 4.0+/-0.4 mU/l, P<0.001), 23% (from 736.8+/-58.5 to 906.7+/-47.8 U/g Hb, P<0.001), 23% (from 1.4+/-0.1 to 1.9+/-0.1 U Bergmayera/g Hb, P<0.01) and 19% (from 163.1+/-23.6 to 202.3+/-11.7 U/g Hb, P<0.001) respectively in rats with hyperglycaemia. |
| 745 | 11170314 | Liver, kidney, brain, and heart were assayed for degree of lipid peroxidation, reduced and oxidized glutathione contents, and activities of catalase, superoxide dismutase, glutathione peroxidase, and glutathione reductase. |
| 746 | 11170314 | Treatment with the lipophilic compound coenzyme Q10 reversed diabetic effects on hepatic glutathione peroxidase activity, on renal superoxide dismutase activity, on cardiac lipid peroxidation, and on oxidized glutathione concentration in brain. |
| 747 | 11170314 | However, treatment with coenzyme Q10 also exacerbated the increase in cardiac catalase activity, which was already elevated by diabetes, further decreased hepatic glutathione reductase activity, augmented the increase in hepatic lipid peroxidation, and further increased glutathione peroxidase activity in the heart and brain of diabetic animals. |
| 748 | 11170314 | Liver, kidney, brain, and heart were assayed for degree of lipid peroxidation, reduced and oxidized glutathione contents, and activities of catalase, superoxide dismutase, glutathione peroxidase, and glutathione reductase. |
| 749 | 11170314 | Treatment with the lipophilic compound coenzyme Q10 reversed diabetic effects on hepatic glutathione peroxidase activity, on renal superoxide dismutase activity, on cardiac lipid peroxidation, and on oxidized glutathione concentration in brain. |
| 750 | 11170314 | However, treatment with coenzyme Q10 also exacerbated the increase in cardiac catalase activity, which was already elevated by diabetes, further decreased hepatic glutathione reductase activity, augmented the increase in hepatic lipid peroxidation, and further increased glutathione peroxidase activity in the heart and brain of diabetic animals. |
| 751 | 11225659 | We studied the effect of metformin treatment on the activities of Cu, Zn-superoxide dismutase (EC 1. 15. 1. 1.), catalase (EC 1. 11. 1. 6.) and glutathione peroxidase (EC 1. 11. 1. 9.) in relation to lipid peroxidation products and reduced glutathione level in plasma and erythrocytes. |
| 752 | 11225659 | Although metformin monotherapy ameliorated the imbalance between free radical-induced increase in lipid peroxidation (by reducing the MDA level in both erythrocytes and plasma) and decreased plasma and cellular antioxidant defences (by increasing the erythrocyte activities of Cu, Zn, SOD, catalase and GSH level) and decreased erythrocyte susceptibility to oxidative stress, it had negligible effect to scavenge Fe ion-induced free radical generation in a phospholipid-liposome system. |
| 753 | 11225659 | We studied the effect of metformin treatment on the activities of Cu, Zn-superoxide dismutase (EC 1. 15. 1. 1.), catalase (EC 1. 11. 1. 6.) and glutathione peroxidase (EC 1. 11. 1. 9.) in relation to lipid peroxidation products and reduced glutathione level in plasma and erythrocytes. |
| 754 | 11225659 | Although metformin monotherapy ameliorated the imbalance between free radical-induced increase in lipid peroxidation (by reducing the MDA level in both erythrocytes and plasma) and decreased plasma and cellular antioxidant defences (by increasing the erythrocyte activities of Cu, Zn, SOD, catalase and GSH level) and decreased erythrocyte susceptibility to oxidative stress, it had negligible effect to scavenge Fe ion-induced free radical generation in a phospholipid-liposome system. |
| 755 | 11228749 | For this, oxidant stress was generated by preincubation of rat aortic rings (RARs) in either 25 mM glucose (mimicking hyperglycemic stress) or 0.5 mM pyrogallol (a superoxide generator) and the effects of the superoxide dismutase (SOD)-mimetic compound 4-hydroxy-2,2,6,6-tetramethylpiperidinyloxy free radical (TEMPOL) on the vasorelaxant and cGMP-producing effects of acetylcholine (ACh) and glyceryl trinitrate (GTN) in control RARs and RARs exposed to oxidant stress were examined. |
| 756 | 11232755 | Although the superoxide dismutase (SOD) activity in aortic homogenates was not changed by diabetes or antioxidant treatment, catalase or glutathione peroxidase (GPx) activity significantly increased in untreated diabetic rats. |
| 757 | 11256783 | Superoxide dismutase activity was also significantly decreased (p<0.001) in smokers with coronary artery disease as compared to hypertensives and non-insulin dependent diabetes mellitus. |
| 758 | 11264900 | There was a decrease in the activity of Mn-superoxide dismutase (SOD), suggesting abnormal mitochondrial metabolism of reactive oxygen species. |
| 759 | 11264900 | The expression of transforming growth factor-beta1 (TGF-beta1), known as a growth factor and a suppressor of GSH synthesis, elevated in DM rat hearts. |
| 760 | 11264900 | Collectively, it was suggested a linkage between mitochondrial damage to generate reactive oxygen species and inactivation of Mn-SOD and elevation of the expression of TGF-beta1 to lead suppression of GSH synthesis and induction of fibrous change for the consequent cardiac dysfunction in DM. |
| 761 | 11277310 | Activities of superoxide dismutase and catalase were markedly elevated in the diabetic myocardium. |
| 762 | 11311962 | The mRNA expression of antioxidant enzymes such as catalase, glutathione peroxidase, and CuZn-superoxide dismutase, was unaltered in glomeruli of diabetic rats and was comparable to control rats. |
| 763 | 11311962 | A treatment with insulin as well as with vitamin E (40 mg/kg body weight every other day, intra-peritoneal injection) normalized the mRNA expression of HO-1 in the glomeruli of diabetic rats. |
| 764 | 11341743 | The mean leukocyte count (p<0.001), polymorphonuclear elastase (p<0.001), erythrocyte malondialdehyde (p<0.001), and glycated haemoglobin (p<0.001) levels, and copper/ zinc ratio (p<0.001) were found to be higher in diabetic patients than in the control group, but serum zinc levels (p<0.001) and erythrocyte superoxide dismutase activities (p<0.001) were lower, and serum copper levels showed no differences. |
| 765 | 11341743 | Closer correlations between the copper/zinc ratio and polymorphonuclear elastase (r=0.82, p<0.01), erythrocyte malondialdehyde (r=0.46, p<0.05) or erythrocyte superoxide dismutase (r= -0.85, p<0.01) were found in patients with vascular complications compared to those without, and all of those showed significant relationships with poor glycaemic metabolic control. |
| 766 | 11341743 | The mean leukocyte count (p<0.001), polymorphonuclear elastase (p<0.001), erythrocyte malondialdehyde (p<0.001), and glycated haemoglobin (p<0.001) levels, and copper/ zinc ratio (p<0.001) were found to be higher in diabetic patients than in the control group, but serum zinc levels (p<0.001) and erythrocyte superoxide dismutase activities (p<0.001) were lower, and serum copper levels showed no differences. |
| 767 | 11341743 | Closer correlations between the copper/zinc ratio and polymorphonuclear elastase (r=0.82, p<0.01), erythrocyte malondialdehyde (r=0.46, p<0.05) or erythrocyte superoxide dismutase (r= -0.85, p<0.01) were found in patients with vascular complications compared to those without, and all of those showed significant relationships with poor glycaemic metabolic control. |
| 768 | 11350569 | Lack of association between polymorphisms of catalase, copper-zinc superoxide dismutase (SOD), extracellular SOD and endothelial nitric oxide synthase genes and macroangiopathy in patients with type 2 diabetes mellitus. |
| 769 | 11351355 | Oral administration of 2.5 g and 5.0 g/kg body weight of the aqueous extract of the roots for 6 weeks resulted in a significant reduction in thiobarbituric acid reactive substances (TBARS) and an increase in reduced glutathione (GSH), catalase (CAT) and superoxide dismutase (SOD) in alloxan diabetic rats. |
| 770 | 11356606 | Our goal was to test whether adenovirus (Ad)-mediated gene transfer of copper/zinc (CuZn) or manganese superoxide dismutase (Mn SOD) improves relaxation of diabetic vessels. |
| 771 | 11356606 | Control and DM rings were transduced ex vivo with Ad vectors encoding Mn SOD (AdMn SOD), CuZn SOD (AdCuZn SOD), beta-galactosidase (Ad(beta)gal), or diluents. |
| 772 | 11356606 | Gene transfer of CuZn SOD and Mn SOD corrected both of these defects. |
| 773 | 11356606 | Thus Ad-mediated gene transfer CuZn and Mn SOD to the diabetic aorta improves endothelium-dependent relaxation. |
| 774 | 11356606 | Our goal was to test whether adenovirus (Ad)-mediated gene transfer of copper/zinc (CuZn) or manganese superoxide dismutase (Mn SOD) improves relaxation of diabetic vessels. |
| 775 | 11356606 | Control and DM rings were transduced ex vivo with Ad vectors encoding Mn SOD (AdMn SOD), CuZn SOD (AdCuZn SOD), beta-galactosidase (Ad(beta)gal), or diluents. |
| 776 | 11356606 | Gene transfer of CuZn SOD and Mn SOD corrected both of these defects. |
| 777 | 11356606 | Thus Ad-mediated gene transfer CuZn and Mn SOD to the diabetic aorta improves endothelium-dependent relaxation. |
| 778 | 11356606 | Our goal was to test whether adenovirus (Ad)-mediated gene transfer of copper/zinc (CuZn) or manganese superoxide dismutase (Mn SOD) improves relaxation of diabetic vessels. |
| 779 | 11356606 | Control and DM rings were transduced ex vivo with Ad vectors encoding Mn SOD (AdMn SOD), CuZn SOD (AdCuZn SOD), beta-galactosidase (Ad(beta)gal), or diluents. |
| 780 | 11356606 | Gene transfer of CuZn SOD and Mn SOD corrected both of these defects. |
| 781 | 11356606 | Thus Ad-mediated gene transfer CuZn and Mn SOD to the diabetic aorta improves endothelium-dependent relaxation. |
| 782 | 11356606 | Our goal was to test whether adenovirus (Ad)-mediated gene transfer of copper/zinc (CuZn) or manganese superoxide dismutase (Mn SOD) improves relaxation of diabetic vessels. |
| 783 | 11356606 | Control and DM rings were transduced ex vivo with Ad vectors encoding Mn SOD (AdMn SOD), CuZn SOD (AdCuZn SOD), beta-galactosidase (Ad(beta)gal), or diluents. |
| 784 | 11356606 | Gene transfer of CuZn SOD and Mn SOD corrected both of these defects. |
| 785 | 11356606 | Thus Ad-mediated gene transfer CuZn and Mn SOD to the diabetic aorta improves endothelium-dependent relaxation. |
| 786 | 11375352 | Hyperglycemia potentiated both platelet aggregation and the subsequent release of platelet-derived growth factor AB induced by a nonaggregating subthreshold concentration of collagen, which were also completely inhibited by TTFA or CCCP. |
| 787 | 11375352 | Furthermore, hyperglycemia was found to inhibit protein tyrosine phosphatase (PTP) activity and increase phosphorylation of the tyrosine kinase Syk in platelets exposed to collagen. |
| 788 | 11375352 | Hyperglycemia-induced PTP inhibition and Syk phosphorylation were found to be completely prevented by TTFA, CCCP, or Mn(III)tetrakis (4-benzoic acid) porphyrin, a stable cell-permeable superoxide dismutase mimetic. |
| 789 | 11378211 | The relationship between serum lipids, lipoproteins, lipid peroxides [thiobarbituric acid reactive substances (TBARS)] and erythrocyte antioxidant enzymes [catalase (CAT), glutathione peroxidase (GPx) and superoxide dismutase (SOD)] was investigated in non-insulin-dependent diabetic patients with and without coronary heart disease (CHD), and a comparison was made for all the above parameters with non-diabetic patients with CHD. |
| 790 | 11389877 | Quinone formation was not affected by co-incubation with catalase or sodium azide and was partially inhibited (25%) by superoxide dismutase (SOD). |
| 791 | 11389877 | CYP3A isoforms were characterized as the primary enzymes involved in quinone formation by several lines of evidence including: (a) troleandomycin and ketoconazole almost completely inhibited microsomal quinone formation when SOD was present, whereas other CYP inhibitors had minimal effects (<20%); (b) TGZ quinone formation was highly correlated with regard to both contents (r(2): 0.9374) and activities (r(2): 0.7951) of CYP3A4 in human liver microsomes (HLM); (c) baculovirus insect cell-expressed human CYP3A4 was able to catalyze TGZ quinone formation at a higher capacity (V(max)/K(m)) than other human CYPs with the relative contribution of CYP3A4 in HLM estimated to be 20-fold higher than that of other CYPs; (d) TGZ quinone formation was increased by 350% in liver microsomes from rats pretreated with dexamethasone (DEX); and (e) plasma concentrations of TGZ quinone were increased by 260-680% in rats pretreated with DEX. |
| 792 | 11389877 | Quinone formation was not affected by co-incubation with catalase or sodium azide and was partially inhibited (25%) by superoxide dismutase (SOD). |
| 793 | 11389877 | CYP3A isoforms were characterized as the primary enzymes involved in quinone formation by several lines of evidence including: (a) troleandomycin and ketoconazole almost completely inhibited microsomal quinone formation when SOD was present, whereas other CYP inhibitors had minimal effects (<20%); (b) TGZ quinone formation was highly correlated with regard to both contents (r(2): 0.9374) and activities (r(2): 0.7951) of CYP3A4 in human liver microsomes (HLM); (c) baculovirus insect cell-expressed human CYP3A4 was able to catalyze TGZ quinone formation at a higher capacity (V(max)/K(m)) than other human CYPs with the relative contribution of CYP3A4 in HLM estimated to be 20-fold higher than that of other CYPs; (d) TGZ quinone formation was increased by 350% in liver microsomes from rats pretreated with dexamethasone (DEX); and (e) plasma concentrations of TGZ quinone were increased by 260-680% in rats pretreated with DEX. |
| 794 | 11398514 | GPx-EIA) and plasma superoxide dismutase activity (colorimetric method based on cytochrome c reduction). |
| 795 | 11420306 | Gelatin zymography and Western blot analysis revealed that the activity and expression of 92-kDa (MMP-9) gelatinase, but not of 72 kDa (MMP-2) gelatinase, were significantly increased in vascular tissue and plasma of two distinct rodent models of DM. |
| 796 | 11420306 | Enhanced MMP-9 activity was significantly reduced by treatment with the antioxidants polyethylene glycol-superoxide dismutase and N-acetyl-L-cysteine but not by inhibitors of protein kinase C. |
| 797 | 11424224 | Quercetin, 2-(3,4-dihydroxyphenyl)-3,5,7-trihydroxy-4H-1-benzopyran-4-one, was administered at a dose of 10mg/kg/day, ip for 14 days, after which liver, kidney, brain, and heart were assayed for degree of lipid peroxidation, reduced and oxidized glutathione content, and activities of the free-radical detoxifying enzymes catalase, superoxide dismutase, glutathione peroxidase, and glutathione reductase. |
| 798 | 11424226 | Liver, kidney, brain, and heart were assayed for degree of lipid peroxidation, reduced and oxidized glutathione content, and activities of the free radical-detoxifying enzymes catalase, superoxide dismutase, glutathione peroxidase, and glutathione reductase. |
| 799 | 11424226 | Some effects of isoeugenol treatment, such as decreased activity of hepatic superoxide dismutase and glutathione reductase in diabetic rats, were unrelated to the oxidative effects of diabetes. |
| 800 | 11424226 | Liver, kidney, brain, and heart were assayed for degree of lipid peroxidation, reduced and oxidized glutathione content, and activities of the free radical-detoxifying enzymes catalase, superoxide dismutase, glutathione peroxidase, and glutathione reductase. |
| 801 | 11424226 | Some effects of isoeugenol treatment, such as decreased activity of hepatic superoxide dismutase and glutathione reductase in diabetic rats, were unrelated to the oxidative effects of diabetes. |
| 802 | 11440784 | Catalase/superoxide dismutase (SOD) and catalase/paraoxonase (PON) ratios may implicate poor glycemic control. |
| 803 | 11451017 | The addition of xanthine/xanthine oxidase or hydrogen peroxide to placental incubates enhanced MMP-9 activity, while the addition of superoxide dismutase (SOD) diminished it. |
| 804 | 11451017 | In placental tissue from patients with PDM, concentrations of nitrates/nitrites and thiobarbituric acid-reactive substances (TBARS) were enhanced, whereas SOD activity was decreased, suggesting that elevated concentrations of NO and ROS may be related to the enhanced MMP-9 concentrations found in these tissues. |
| 805 | 11451017 | The activity of MMP-9 in placental tissue from patients with GDM was stimulated by ROS donor systems and was inhibited by the addition of SOD; however, TBARS and SOD concentrations were unchanged in these tissues compared with controls. |
| 806 | 11451017 | The addition of xanthine/xanthine oxidase or hydrogen peroxide to placental incubates enhanced MMP-9 activity, while the addition of superoxide dismutase (SOD) diminished it. |
| 807 | 11451017 | In placental tissue from patients with PDM, concentrations of nitrates/nitrites and thiobarbituric acid-reactive substances (TBARS) were enhanced, whereas SOD activity was decreased, suggesting that elevated concentrations of NO and ROS may be related to the enhanced MMP-9 concentrations found in these tissues. |
| 808 | 11451017 | The activity of MMP-9 in placental tissue from patients with GDM was stimulated by ROS donor systems and was inhibited by the addition of SOD; however, TBARS and SOD concentrations were unchanged in these tissues compared with controls. |
| 809 | 11451017 | The addition of xanthine/xanthine oxidase or hydrogen peroxide to placental incubates enhanced MMP-9 activity, while the addition of superoxide dismutase (SOD) diminished it. |
| 810 | 11451017 | In placental tissue from patients with PDM, concentrations of nitrates/nitrites and thiobarbituric acid-reactive substances (TBARS) were enhanced, whereas SOD activity was decreased, suggesting that elevated concentrations of NO and ROS may be related to the enhanced MMP-9 concentrations found in these tissues. |
| 811 | 11451017 | The activity of MMP-9 in placental tissue from patients with GDM was stimulated by ROS donor systems and was inhibited by the addition of SOD; however, TBARS and SOD concentrations were unchanged in these tissues compared with controls. |
| 812 | 11514301 | Treatment of cremaster muscles of OZR with the superoxide scavengers polyethylene glycol-superoxide dismutase and catalase improved arteriolar dilation to acetylcholine and sodium nitroprusside and restored flow-induced dilation and microvascular ability to regulate wall shear rate. |
| 813 | 11522108 | The aim of the present study was to investigate the effect of the oxidative stress on the activities of blood superoxide dismutase (SOD), catalase (CAT), glutathione peroxidase (GSH-Px), glutathione reductase (GSSG-R) and aldose reductase, the levels of reduced glutathione (GSH), lipid peroxidation (thiobarbituric acid reactive substances; TBARS) and plasma levels of insulin-like growth factor-1 (IGF-1), follicle-stimulating hormone (FSH), luteinizing hormone (LH) and testosterone in type 2 (non-insulin-dependent diabetes) patients and in healthy controls. |
| 814 | 11522108 | Blood SOD, CAT, GSH-Px and GSSG-R were lower in type 2 diabetic patients compared with the the control group. |
| 815 | 11522108 | The aim of the present study was to investigate the effect of the oxidative stress on the activities of blood superoxide dismutase (SOD), catalase (CAT), glutathione peroxidase (GSH-Px), glutathione reductase (GSSG-R) and aldose reductase, the levels of reduced glutathione (GSH), lipid peroxidation (thiobarbituric acid reactive substances; TBARS) and plasma levels of insulin-like growth factor-1 (IGF-1), follicle-stimulating hormone (FSH), luteinizing hormone (LH) and testosterone in type 2 (non-insulin-dependent diabetes) patients and in healthy controls. |
| 816 | 11522108 | Blood SOD, CAT, GSH-Px and GSSG-R were lower in type 2 diabetic patients compared with the the control group. |
| 817 | 11522679 | In both SOD and D-SOD mice, renal cortical SOD-1 activity was twofold higher than values in the WT mice; blood glucose and glycosylated hemoglobin (GHb) levels did not differ in the two diabetic groups. |
| 818 | 11522679 | Urinary albumin excretion, fractional albumin clearance, urinary transforming growth factor-beta (TGF-beta) excretion, glomerular volume, glomerular content of immunoreactive TGF-beta, and collagen alpha1 (IV) and renal cortical malondialdehyde (MDA) levels were significantly higher in D-WT mice compared with corresponding values in D-SOD mice. |
| 819 | 11522679 | Glomerular volume, glomerular content of TGF-beta and collagen IV, renal cortical MDA, and urinary excretion of TGF-beta in D-SOD mice did not differ significantly from corresponding values in either the nondiabetic SOD or WT mice. |
| 820 | 11522679 | In vitro infection of mesangial cells (MC) with a recombinant adenovirus encoding human SOD-1 increased SOD-1 activity threefold over control cells and prevented the reduction of aconitase activity, an index of cellular superoxide, and the increase in collagen synthesis that otherwise occurred in control MC in response to culture with 300 or 500 mg/dl glucose. |
| 821 | 11522679 | In both SOD and D-SOD mice, renal cortical SOD-1 activity was twofold higher than values in the WT mice; blood glucose and glycosylated hemoglobin (GHb) levels did not differ in the two diabetic groups. |
| 822 | 11522679 | Urinary albumin excretion, fractional albumin clearance, urinary transforming growth factor-beta (TGF-beta) excretion, glomerular volume, glomerular content of immunoreactive TGF-beta, and collagen alpha1 (IV) and renal cortical malondialdehyde (MDA) levels were significantly higher in D-WT mice compared with corresponding values in D-SOD mice. |
| 823 | 11522679 | Glomerular volume, glomerular content of TGF-beta and collagen IV, renal cortical MDA, and urinary excretion of TGF-beta in D-SOD mice did not differ significantly from corresponding values in either the nondiabetic SOD or WT mice. |
| 824 | 11522679 | In vitro infection of mesangial cells (MC) with a recombinant adenovirus encoding human SOD-1 increased SOD-1 activity threefold over control cells and prevented the reduction of aconitase activity, an index of cellular superoxide, and the increase in collagen synthesis that otherwise occurred in control MC in response to culture with 300 or 500 mg/dl glucose. |
| 825 | 11522679 | In both SOD and D-SOD mice, renal cortical SOD-1 activity was twofold higher than values in the WT mice; blood glucose and glycosylated hemoglobin (GHb) levels did not differ in the two diabetic groups. |
| 826 | 11522679 | Urinary albumin excretion, fractional albumin clearance, urinary transforming growth factor-beta (TGF-beta) excretion, glomerular volume, glomerular content of immunoreactive TGF-beta, and collagen alpha1 (IV) and renal cortical malondialdehyde (MDA) levels were significantly higher in D-WT mice compared with corresponding values in D-SOD mice. |
| 827 | 11522679 | Glomerular volume, glomerular content of TGF-beta and collagen IV, renal cortical MDA, and urinary excretion of TGF-beta in D-SOD mice did not differ significantly from corresponding values in either the nondiabetic SOD or WT mice. |
| 828 | 11522679 | In vitro infection of mesangial cells (MC) with a recombinant adenovirus encoding human SOD-1 increased SOD-1 activity threefold over control cells and prevented the reduction of aconitase activity, an index of cellular superoxide, and the increase in collagen synthesis that otherwise occurred in control MC in response to culture with 300 or 500 mg/dl glucose. |
| 829 | 11542339 | During oxidation of hemoglobin to methemoglobin superoxide radical anion (O2-) is formed: HbFe2+ + O2 --> MetHbFe3+ + O2- (1) Ferrous and ferric ions present in the cytoplasm of red blood cells may be catalysts of the Fenton reaction leading to the production of the hydroxyl radical: O2- + Fe3+ --> O2- + Fe2+ (2) Fe2+ + H2O2 --> Fe3+ + OH + HO- (3) OH shows a tremendous reactivity. |
| 830 | 11542339 | The most important antioxidative enzymes of the red blood cells are superoxide dismutase (Cu,Zn-SOD, EC 1.15.1.1) catalase (CAT, EC 1.11.1.6) and glutathione peroxidase (GSH-Px, EC 1.11.1.9). |
| 831 | 11553023 | Enalapril enhanced the activity of catalase in the renal cortex of OLETF rats, but had no effect on the activity of either superoxide dismutase or glutathione peroxidase. 4. |
| 832 | 11568480 | Antioxidant enzymes such as superoxide dismutase and catalase remain unaffected after this treatment. |
| 833 | 11584100 | Increased life span was partially associated with decreased body weight, blunting renal proinflammatory cytokine (interferon-gamma, interleukins-10 and -12 and tumor necrosis factor-alpha) levels and lower nuclear factor-kappaB (NF-kappaB). |
| 834 | 11584100 | Reductions in NF-kappaB were preceded by enhanced superoxide dismutase, catalase and glutathione peroxidase activities. |
| 835 | 11812741 | We found that the SOD mimic significantly inhibited antigen-presenting cell-dependent T-cell proliferation and IFN-gamma production in vitro. |
| 836 | 11812741 | In addition, pretreatment of lipopolysaccharide (LPS)-stimulated peritoneal macrophages with SOD mimic inhibited the LPS-dependent increase in TNF-alpha as well as the NADPH oxidase-dependent release of superoxide. |
| 837 | 11812741 | We found that the SOD mimic significantly inhibited antigen-presenting cell-dependent T-cell proliferation and IFN-gamma production in vitro. |
| 838 | 11812741 | In addition, pretreatment of lipopolysaccharide (LPS)-stimulated peritoneal macrophages with SOD mimic inhibited the LPS-dependent increase in TNF-alpha as well as the NADPH oxidase-dependent release of superoxide. |
| 839 | 11812749 | A variety of protective genes were upregulated, with markedly increased expression of the antioxidant genes heme oxygenase-1 and glutathione peroxidase and the antiapoptotic gene A20. |
| 840 | 11812749 | Cu/Zn-superoxide dismutase (SOD) and Mn-SOD were modestly induced, and Bcl-2 was modestly reduced; however, several other stress genes (catalase, heat shock protein 70, and p53) were unaltered. |
| 841 | 11836018 | This study examined whether oxidative stress was induced in adipocytes and liver that were exposed to TCDD. 3T3-F442A adipocyte cultures were treated with TCDD (5-200 nM) for up to 72 h, and the activity and mRNA levels of superoxide dismutase (SOD), catalase, and glutathione peroxidase (GSH-Px) in adipocyte cell lysates were measured. |
| 842 | 11836018 | In contrast, TCDD had no significant effect on the activity of catalase or GSH-Px in the adipocytes, and the increase in SOD activity was not accompanied by a change in SOD mRNA levels. |
| 843 | 11836018 | SOD, catalase, and GSH-Px activities were measured in the liver and adipose tissue of these rats. |
| 844 | 11836018 | This study examined whether oxidative stress was induced in adipocytes and liver that were exposed to TCDD. 3T3-F442A adipocyte cultures were treated with TCDD (5-200 nM) for up to 72 h, and the activity and mRNA levels of superoxide dismutase (SOD), catalase, and glutathione peroxidase (GSH-Px) in adipocyte cell lysates were measured. |
| 845 | 11836018 | In contrast, TCDD had no significant effect on the activity of catalase or GSH-Px in the adipocytes, and the increase in SOD activity was not accompanied by a change in SOD mRNA levels. |
| 846 | 11836018 | SOD, catalase, and GSH-Px activities were measured in the liver and adipose tissue of these rats. |
| 847 | 11836018 | This study examined whether oxidative stress was induced in adipocytes and liver that were exposed to TCDD. 3T3-F442A adipocyte cultures were treated with TCDD (5-200 nM) for up to 72 h, and the activity and mRNA levels of superoxide dismutase (SOD), catalase, and glutathione peroxidase (GSH-Px) in adipocyte cell lysates were measured. |
| 848 | 11836018 | In contrast, TCDD had no significant effect on the activity of catalase or GSH-Px in the adipocytes, and the increase in SOD activity was not accompanied by a change in SOD mRNA levels. |
| 849 | 11836018 | SOD, catalase, and GSH-Px activities were measured in the liver and adipose tissue of these rats. |
| 850 | 11884287 | Plasma superoxide dismutase, catalase, and vitamin E levels were comparable between the groups. |
| 851 | 11937081 | Lens superoxide dismutase and catalase activities in diabetic cataract. |
| 852 | 11937300 | F1 progeny from reciprocal outcrosses between ALR and ALS mice exhibited an intermediate burst level, higher than ALR but significantly lower than ALS. |
| 853 | 11985536 | In order to assess the redox status of various organs in the diabetic and control rats, thiobarbituric acid-reactive substances (TBARS) and glutathione (GSH) levels, as well as superoxide dismutase (SOD), glutathione peroxidase (G-Px) and glutathione reductase (G-Red) activities were determined in the liver, pancreas and kidney. 3. |
| 854 | 12002418 | In the renal cortex of rats with streptozotocin-induced diabetes, the activity of superoxide dismutase (SOD) isoenzymes, glutathione peroxidase (GSH-Pox). glutathione S-transferase (GST) and glutathione reductase (GSH-RED) was measured in the 5th, 10th and 15th weeks of diabetes. |
| 855 | 12007704 | In an experimental animal model, chronic Swarnabhasma-treated animals showed significantly increased superoxide dismutase and catalase activity, two enzymes that reduce free radical concentrations in the body. |
| 856 | 12007924 | In diabetic but not in control aorta, the noradrenaline-induced contraction was significantly enhanced by catalase and significantly inhibited by polyethylene-glycolated superoxide dismutase. |
| 857 | 12007924 | Adding catalase to the superoxide dismutase prevented the latter's attenuation of the contraction. |
| 858 | 12007924 | In the latter, the noradrenaline-induced nitrite and nitrate level was significantly enhanced by incubation with superoxide dismutase but not by incubation with catalase plus superoxide dismutase. |
| 859 | 12007924 | In diabetic but not in control aorta, the noradrenaline-induced contraction was significantly enhanced by catalase and significantly inhibited by polyethylene-glycolated superoxide dismutase. |
| 860 | 12007924 | Adding catalase to the superoxide dismutase prevented the latter's attenuation of the contraction. |
| 861 | 12007924 | In the latter, the noradrenaline-induced nitrite and nitrate level was significantly enhanced by incubation with superoxide dismutase but not by incubation with catalase plus superoxide dismutase. |
| 862 | 12007924 | In diabetic but not in control aorta, the noradrenaline-induced contraction was significantly enhanced by catalase and significantly inhibited by polyethylene-glycolated superoxide dismutase. |
| 863 | 12007924 | Adding catalase to the superoxide dismutase prevented the latter's attenuation of the contraction. |
| 864 | 12007924 | In the latter, the noradrenaline-induced nitrite and nitrate level was significantly enhanced by incubation with superoxide dismutase but not by incubation with catalase plus superoxide dismutase. |
| 865 | 12010774 | BH(4) and superoxide dismutase (SOD, 150 u ml(-1)), either alone or in combination, had no effect on either ACh or SNP-induced relaxation in SMA from eNOS -/- mice. 7. |
| 866 | 12010774 | Incubation of SMA with SOD (150 iu ml(-1)), catalase (200 iu ml(-1)) and L-arginine (1 mM) had no effect on ACh-induced relaxation of SMA. |
| 867 | 12010774 | BH(4) and superoxide dismutase (SOD, 150 u ml(-1)), either alone or in combination, had no effect on either ACh or SNP-induced relaxation in SMA from eNOS -/- mice. 7. |
| 868 | 12010774 | Incubation of SMA with SOD (150 iu ml(-1)), catalase (200 iu ml(-1)) and L-arginine (1 mM) had no effect on ACh-induced relaxation of SMA. |
| 869 | 12080716 | To study the relationship between nitric oxide(NO) and oxygen free radicals in rat kidney of diabetes mellitus(DM), the authors examined the changes of renal tissue NO level and nitric oxide synthase(NOS) activity, lipid peroxidation(LPO) level and superoxide dismutase(SOD), peroxidase(POD) and catalase (CAT) activities in streptozotocin(STZ)-induced diabetic rats and normal controls(NC) at the 2nd, 8th- and 16th-week. |
| 870 | 12105098 | The energy deficits in the central nervous system can lead to the generation of reactive oxygen and nitrogen species as indicated by increased activity of the free radical scavenging enzymes like catalase and superoxide dismutase. |
| 871 | 12123763 | Particularly, a major form of SOD in the vessel wall is the extracellular SOD (ecSOD). |
| 872 | 12127321 | Over the past 8 years, we diagnosed 132 cases (55 kinds) of variant proteins including hemoglobin (Hb), transthyretin (TTR), and Cu/Zn-superoxide dismutase (SOD-1), using MS as the leading technology. |
| 873 | 12190123 | With the premise that oxygen free radicals may be responsible for the severity and complications of diabetes, the level of antioxidant enzymes catalase (CAT), superoxide dismutase (SOD) and glutathione peroxidase (GPx) as well as the oxidative damage were examined in the tissues of control, diabetic and treated rats. |
| 874 | 12230234 | The extract also causes a significant increase in reduced glutathione, superoxide dismutase, catalase, glutathione peroxidase and glutathione-S-transferase in the liver and kidneys of rats with streptozotocin-induced diabetes. |
| 875 | 12242690 | In this experiment, amounts of lipid peroxidation, glutathione, and glutathione disulfide, and activity levels of catalase, glutathione peroxidase, glutathione reductase, superoxide dismutase, and gamma-glutamyl transpeptidase were measured in the liver, kidney, and heart of Sprague-Dawley rats with streptozotocin-induced diabetes, and after treatment with 10 mg/kg/day of beta-carotene for 14 days. |
| 876 | 12242689 | Effects of combined quercetin and coenzyme Q(10) treatment on oxidative stress in normal and diabetic rats. |
| 877 | 12242689 | Our objective was to determine if subacute treatment with combined antioxidants quercetin and coenzyme Q(10) (10 mg/kg/day ip for 14 days) affects the activities of antioxidant enzymes in normal and 30-day streptozotocin-induced diabetic Sprague-Dawley rats. |
| 878 | 12242689 | Quercetin treatment raised blood glucose concentrations in normal and diabetic rats, whereas treatment with coenzyme Q(10) did not. |
| 879 | 12242689 | Liver, kidney, heart, and brain tissues were excised and the activities of catalase, glutathione reductase, glutathione peroxidase, superoxide dismutase, and concentrations of oxidized and reduced glutathione were determined. |
| 880 | 12242689 | In heart, catalase activity was increased in diabetic animals and restored to normal levels after combined treatment with quercetin and coenzyme Q(10). |
| 881 | 12242689 | Cardiac superoxide dismutase was lower than normal in quercetin- and quercetin + coenzyme Q(10)-treated diabetic rats. |
| 882 | 12242689 | There were no adverse effects on oxidative stress markers after treatment with quercetin or coenzyme Q(10) singly or in combination. |
| 883 | 12242689 | In spite of the elevation of glucose, quercetin may be effective in reversing some effects of diabetes, but the combination of quercetin + coenzyme Q(10) did not increase effectiveness in reversing effects of diabetes. |
| 884 | 12242689 | Effects of combined quercetin and coenzyme Q(10) treatment on oxidative stress in normal and diabetic rats. |
| 885 | 12242689 | Our objective was to determine if subacute treatment with combined antioxidants quercetin and coenzyme Q(10) (10 mg/kg/day ip for 14 days) affects the activities of antioxidant enzymes in normal and 30-day streptozotocin-induced diabetic Sprague-Dawley rats. |
| 886 | 12242689 | Quercetin treatment raised blood glucose concentrations in normal and diabetic rats, whereas treatment with coenzyme Q(10) did not. |
| 887 | 12242689 | Liver, kidney, heart, and brain tissues were excised and the activities of catalase, glutathione reductase, glutathione peroxidase, superoxide dismutase, and concentrations of oxidized and reduced glutathione were determined. |
| 888 | 12242689 | In heart, catalase activity was increased in diabetic animals and restored to normal levels after combined treatment with quercetin and coenzyme Q(10). |
| 889 | 12242689 | Cardiac superoxide dismutase was lower than normal in quercetin- and quercetin + coenzyme Q(10)-treated diabetic rats. |
| 890 | 12242689 | There were no adverse effects on oxidative stress markers after treatment with quercetin or coenzyme Q(10) singly or in combination. |
| 891 | 12242689 | In spite of the elevation of glucose, quercetin may be effective in reversing some effects of diabetes, but the combination of quercetin + coenzyme Q(10) did not increase effectiveness in reversing effects of diabetes. |
| 892 | 12357295 | We measured plasma TBARS levels, superoxide dismutase (SOD) and catalase (CAT) activities and compared their relation to the metabolic control of diabetes and diabetic microangiopathy. |
| 893 | 12361782 | Antioxidants (e.g., glutathione, arginine, citrulline, taurine, creatine, selenium, zinc, vitamin E, vitamin C, vitamin A, and tea polyphenols) and antioxidant enzymes (e.g., superoxide dismutase, catalase, glutathione reductase, and glutathione peroxidases) exert synergistic actions in scavenging free radicals. |
| 894 | 12369709 | The rats were maintained on these regimens for 30 days, at which point the activities of catalase, glutathione peroxidase, glutathione reductase, and superoxide dismutase, as well as levels of lipid peroxidation and reduced and oxidized glutathione were determined in heart, liver, and kidney. |
| 895 | 12369709 | In addition, several effects of diabetes (increased hepatic glutathione peroxidase activity, increased superoxide dismutase activity in kidney and heart, decreased renal and increased cardiac catalase activity) were not mimicked in galactosemic rats, and glutathione concentration in both liver and heart was affected in opposite ways in diabetic rats and galactose-fed rats. |
| 896 | 12369709 | Insulin treatment reversed/prevented the activity changes in renal and cardiac superoxide dismutase, renal and cardiac catalase, and hepatic glutathione peroxidase as well as the hepatic changes in lipid peroxidation and reduced and oxidized glutathione, and the increase in cardiac glutathione. |
| 897 | 12369709 | The rats were maintained on these regimens for 30 days, at which point the activities of catalase, glutathione peroxidase, glutathione reductase, and superoxide dismutase, as well as levels of lipid peroxidation and reduced and oxidized glutathione were determined in heart, liver, and kidney. |
| 898 | 12369709 | In addition, several effects of diabetes (increased hepatic glutathione peroxidase activity, increased superoxide dismutase activity in kidney and heart, decreased renal and increased cardiac catalase activity) were not mimicked in galactosemic rats, and glutathione concentration in both liver and heart was affected in opposite ways in diabetic rats and galactose-fed rats. |
| 899 | 12369709 | Insulin treatment reversed/prevented the activity changes in renal and cardiac superoxide dismutase, renal and cardiac catalase, and hepatic glutathione peroxidase as well as the hepatic changes in lipid peroxidation and reduced and oxidized glutathione, and the increase in cardiac glutathione. |
| 900 | 12369709 | The rats were maintained on these regimens for 30 days, at which point the activities of catalase, glutathione peroxidase, glutathione reductase, and superoxide dismutase, as well as levels of lipid peroxidation and reduced and oxidized glutathione were determined in heart, liver, and kidney. |
| 901 | 12369709 | In addition, several effects of diabetes (increased hepatic glutathione peroxidase activity, increased superoxide dismutase activity in kidney and heart, decreased renal and increased cardiac catalase activity) were not mimicked in galactosemic rats, and glutathione concentration in both liver and heart was affected in opposite ways in diabetic rats and galactose-fed rats. |
| 902 | 12369709 | Insulin treatment reversed/prevented the activity changes in renal and cardiac superoxide dismutase, renal and cardiac catalase, and hepatic glutathione peroxidase as well as the hepatic changes in lipid peroxidation and reduced and oxidized glutathione, and the increase in cardiac glutathione. |
| 903 | 12370847 | This present study applied quantitative competitive polymerase chain reaction (QC-PCR) in the analyses of mRNA expression of the endogenous antioxidative enzymes CuZn superoxide dismutase (SOD), MnSOD, catalase, and glutathione peroxidase in tissue samples from the retina and kidney cortex of diabetic rats. |
| 904 | 12370847 | In the kidney cortex, the relative glutathione peroxidase mRNA level was 10 to 15 times higher, and catalase mRNA level about half of those of CuZnSOD and MnSOD. |
| 905 | 12458659 | Plasma total cholesterol, high-density lipoprotein (HDL) cholesterol, triglyceride, superoxide dismutase, nitric oxide, nitric oxide synthase, insulin, and glucose were quantitated at monthly or bimonthly intervals. |
| 906 | 12469627 | [Associative analysis of the connection between mutation C1167T in the catalase gene and polymorphic marker D6S392 nearby the Mn-dependent superoxide dismutase gene with diabetic microangiopathies]. |
| 907 | 12492633 | Blood samples were taken at 0, 5 and 10 days after the wounds were created for the determination of malondialdehyde levels and red cell superoxide dismutase, catalase and glutathione peroxidase activities. |
| 908 | 12521600 | Superoxide dismutase, glutathione peroxidase, glutathione reductase, glutathione transferase, and NADH oxidase, but not catalase, were upregulated in diabetic rats vs. controls, and these activities, except glutathione peroxidase, were decreased by DL-alpha-lipoic acid. |
| 909 | 12524661 | In addition, stimulation of HAECs with gly-ox-HDL for 48 hours elicited a marked downregulation of catalase and Cu(2+), Zn(2+)-superoxide dismutase (CuZn-SOD), suggesting H(2)O(2) formation by gly-ox-HDL to be due to a disturbance involving oxidant and antioxidant enzymes in the cells. |
| 910 | 12524661 | Treatment of HAECs with gly-ox-HDL attenuated the expression of endothelial nitric oxide synthase (eNOS), but not inducible nitric oxide synthase (iNOS), and this was followed by decreased production of nitric oxide (NO) by the cells. |
| 911 | 12535867 | Because the cerebral microcirculation is much less affected in diabetes, our objectives are to compare: (1) glutathione peroxidase activity, (2) superoxide dismutase levels, (3) superoxide production, and (4) junctional protein (ZO-1) levels between retinal and brain-derived endothelial cells. |
| 912 | 12535867 | The results demonstrate that, compared to brain-derived endothelial cells, retinal endothelial cells release high levels of superoxide, have less glutathione peroxidase activity and lower levels of superoxide dismutase, and ZO-1. |
| 913 | 12535867 | Because the cerebral microcirculation is much less affected in diabetes, our objectives are to compare: (1) glutathione peroxidase activity, (2) superoxide dismutase levels, (3) superoxide production, and (4) junctional protein (ZO-1) levels between retinal and brain-derived endothelial cells. |
| 914 | 12535867 | The results demonstrate that, compared to brain-derived endothelial cells, retinal endothelial cells release high levels of superoxide, have less glutathione peroxidase activity and lower levels of superoxide dismutase, and ZO-1. |
| 915 | 12546278 | Activity of superoxide dismutase (SOD) and catalase-like enzymes and levels of ascorbic acid (AA), uric acid (UA), and dehydroascorbic acid (DHAA) were measured in embryonic homogenates. |
| 916 | 12546278 | Activity of SOD and catalase was not different in embryos of CDs and CDr rats fed RD. |
| 917 | 12546278 | Activity of superoxide dismutase (SOD) and catalase-like enzymes and levels of ascorbic acid (AA), uric acid (UA), and dehydroascorbic acid (DHAA) were measured in embryonic homogenates. |
| 918 | 12546278 | Activity of SOD and catalase was not different in embryos of CDs and CDr rats fed RD. |
| 919 | 12579518 | At the end of the experiment, all animals were sacrificed by decapitation, heart and aorta samples were removed for determination of thiobarbituric acid reactive substance (TBARS) level and superoxide dismutase (SOD), catalase (CAT) and glutathione peroxidase (GSH-Px) activities. |
| 920 | 12606529 | The expression of catalase (CAT), CuZn superoxide-dismutase (CuZnSOD), glutathione peroxidase (GPX), and Mn superoxide-dismutase (MnSOD) mRNA was quantified in peripheral blood mononuclear cells-obtained from 26 patients with type 1 diabetes and nephropathy, 15 with no microvascular complications after 20 years' duration of diabetes, and 10 normal healthy control subjects-that were exposed in vitro to hyperglycemia (HG) (31 mmol/l D-glucose). |
| 921 | 12606529 | Under HG, there was a twofold increase in the expression of CAT, CuZnSOD, and GPX mRNA in the patients without complications and the control subjects versus patients with nephropathy (P < 0.0001), and MnSOD did not change in any of the groups. |
| 922 | 12606529 | The aldose reductase inhibitor zopolrestat partially restored the levels of CAT, CuZnSOD, and GPX mRNA in the patients with nephropathy (P < 0.05). |
| 923 | 12606529 | There was a highly significant correlation between increased aldose reductase (ALR2) expression, CAT, CuZnSOD, and GPX mRNA levels under HG conditions and polymorphisms of ALR2 in the patients with nephropathy (P < 0.00001). |
| 924 | 12616644 | Changes in oxidative stress biomarkers, including superoxide dismutase, catalase, glutathione reductase, glutathione peroxidase, glutathione levels, vitamins, lipid peroxidation, nitrite concentration, nonenzymatic glycosylated proteins, and hyperglycemia in diabetes, and their consequences, are discussed in this review. |
| 925 | 12619885 | Significant increase in the activities of superoxide dismutase, catalase, glutathione peroxidase, glutathione-S-transferase and reduced glutathione were observed in brain on treatment with Cassia auriculata flower extract (CFEt) and glibenclamide. |
| 926 | 12619900 | The expression of catalase, superoxide dismutase and glutathione peroxidase, the three primary scavenger enzymes involved in detoxifying reactive oxygen species has been evaluated in the renal cortex of rats after 6 weeks of streptozotocin-induced diabetes. |
| 927 | 12619900 | The enzyme assays showed significant and varied alterations in catalase, superoxide dismutase and glutathione peroxidase activities. |
| 928 | 12619900 | While an increase in glutathione peroxidase and Cu-Zn superoxide dismutase mRNA parallels the increase in the activities of the enzymes, an increase in catalase gene expression in contrast to a decrease in enzyme activity suggests a role for post-translational modification in altering the activity of this enzyme. |
| 929 | 12619900 | The expression of catalase, superoxide dismutase and glutathione peroxidase, the three primary scavenger enzymes involved in detoxifying reactive oxygen species has been evaluated in the renal cortex of rats after 6 weeks of streptozotocin-induced diabetes. |
| 930 | 12619900 | The enzyme assays showed significant and varied alterations in catalase, superoxide dismutase and glutathione peroxidase activities. |
| 931 | 12619900 | While an increase in glutathione peroxidase and Cu-Zn superoxide dismutase mRNA parallels the increase in the activities of the enzymes, an increase in catalase gene expression in contrast to a decrease in enzyme activity suggests a role for post-translational modification in altering the activity of this enzyme. |
| 932 | 12619900 | The expression of catalase, superoxide dismutase and glutathione peroxidase, the three primary scavenger enzymes involved in detoxifying reactive oxygen species has been evaluated in the renal cortex of rats after 6 weeks of streptozotocin-induced diabetes. |
| 933 | 12619900 | The enzyme assays showed significant and varied alterations in catalase, superoxide dismutase and glutathione peroxidase activities. |
| 934 | 12619900 | While an increase in glutathione peroxidase and Cu-Zn superoxide dismutase mRNA parallels the increase in the activities of the enzymes, an increase in catalase gene expression in contrast to a decrease in enzyme activity suggests a role for post-translational modification in altering the activity of this enzyme. |
| 935 | 12621526 | Incubation with D-glucose activated protein kinase C (PKC), endothelial NO synthase (eNOS), p42 and p44 mitogen-activated protein kinases (p42/44(mapk)), but inhibited superoxide dismutase (SOD). |
| 936 | 12621526 | The effect of D-glucose was blocked by the PKC inhibitor calphostin C, the MAP kinase kinase 1/2 (MEK1/2) inhibitor PD-98059, the eNOS inhibitor L-NAME, the protein kinase G (PKG) inhibitor KT-5823 and the protein kinase A (PKA) inhibitor KT-5720. |
| 937 | 12621526 | D-Glucose-dependent inhibition of thymidine incorporation and cell proliferation is associated with increased PKC, eNOS, and MEK1/2, but decreased SOD activity, and higher intracellular levels of cGMP, cAMP and Ca2+ in HUVECs. |
| 938 | 12621526 | Incubation with D-glucose activated protein kinase C (PKC), endothelial NO synthase (eNOS), p42 and p44 mitogen-activated protein kinases (p42/44(mapk)), but inhibited superoxide dismutase (SOD). |
| 939 | 12621526 | The effect of D-glucose was blocked by the PKC inhibitor calphostin C, the MAP kinase kinase 1/2 (MEK1/2) inhibitor PD-98059, the eNOS inhibitor L-NAME, the protein kinase G (PKG) inhibitor KT-5823 and the protein kinase A (PKA) inhibitor KT-5720. |
| 940 | 12621526 | D-Glucose-dependent inhibition of thymidine incorporation and cell proliferation is associated with increased PKC, eNOS, and MEK1/2, but decreased SOD activity, and higher intracellular levels of cGMP, cAMP and Ca2+ in HUVECs. |
| 941 | 12633745 | Sequential inactivation of reactive oxygen species by combined overexpression of SOD isoforms and catalase in insulin-producing cells. |
| 942 | 12633745 | Insulin-producing cells show very low activity levels of the cytoprotective enzymes catalase, glutathione peroxidase, and superoxide dismutase. |
| 943 | 12633745 | Catalase alone was able to increase the resistance of transfected RINm5F insulin-producing tissue culture cells against H(2)O(2) and HX/XO, but no protection was seen in the case of menadione. |
| 944 | 12633745 | In combination with an increase of the MnSOD or Cu,ZnSOD expression, the protective action of catalase overexpression could be further increased and extended to the toxicity of menadione. |
| 945 | 12633745 | Sequential inactivation of reactive oxygen species by combined overexpression of SOD isoforms and catalase in insulin-producing cells. |
| 946 | 12633745 | Insulin-producing cells show very low activity levels of the cytoprotective enzymes catalase, glutathione peroxidase, and superoxide dismutase. |
| 947 | 12633745 | Catalase alone was able to increase the resistance of transfected RINm5F insulin-producing tissue culture cells against H(2)O(2) and HX/XO, but no protection was seen in the case of menadione. |
| 948 | 12633745 | In combination with an increase of the MnSOD or Cu,ZnSOD expression, the protective action of catalase overexpression could be further increased and extended to the toxicity of menadione. |
| 949 | 12640491 | In contrast, the overall infection rate was higher (P<0.05) in the diabetic rats (SO-D and PE-D subgroups, but not in the NO-D subgroup). |
| 950 | 12640491 | Considering that the overall infection rate was similar in the SO-D and PE-D subgroups, we suggest that surgery but not pneumonectomy was related to the higher prevalence of infection in diabetic rats. |
| 951 | 12640491 | In contrast, the overall infection rate was higher (P<0.05) in the diabetic rats (SO-D and PE-D subgroups, but not in the NO-D subgroup). |
| 952 | 12640491 | Considering that the overall infection rate was similar in the SO-D and PE-D subgroups, we suggest that surgery but not pneumonectomy was related to the higher prevalence of infection in diabetic rats. |
| 953 | 12644725 | Furthermore, depletion of BH(4) by 2,4-diamino-6-hydroxypyrimidine (DAHP) in control arterioles also resulted in reduced flow-dependent dilations, which were restored by intraluminal sepiapterin [but not with superoxide dismutase (SOD) plus catalase (CAT) (SOD+CAT)] and then could be inhibited by L-NAME. |
| 954 | 12644725 | Dilations induced by the NO donor sodium nitroprusside (SNP) were unaffected by L-NAME in diabetes mellitus arterioles or when eNOS was activated by intraluminal flow in DAHP-treated arterioles (with or without SOD+CAT). |
| 955 | 12644725 | In contrast, pyrogallol (known to produce reactive oxygen species) substantially reduced acetylcholine- and SNP-induced dilation in a SOD+CAT-reversible manner. |
| 956 | 12644725 | Furthermore, depletion of BH(4) by 2,4-diamino-6-hydroxypyrimidine (DAHP) in control arterioles also resulted in reduced flow-dependent dilations, which were restored by intraluminal sepiapterin [but not with superoxide dismutase (SOD) plus catalase (CAT) (SOD+CAT)] and then could be inhibited by L-NAME. |
| 957 | 12644725 | Dilations induced by the NO donor sodium nitroprusside (SNP) were unaffected by L-NAME in diabetes mellitus arterioles or when eNOS was activated by intraluminal flow in DAHP-treated arterioles (with or without SOD+CAT). |
| 958 | 12644725 | In contrast, pyrogallol (known to produce reactive oxygen species) substantially reduced acetylcholine- and SNP-induced dilation in a SOD+CAT-reversible manner. |
| 959 | 12644725 | Furthermore, depletion of BH(4) by 2,4-diamino-6-hydroxypyrimidine (DAHP) in control arterioles also resulted in reduced flow-dependent dilations, which were restored by intraluminal sepiapterin [but not with superoxide dismutase (SOD) plus catalase (CAT) (SOD+CAT)] and then could be inhibited by L-NAME. |
| 960 | 12644725 | Dilations induced by the NO donor sodium nitroprusside (SNP) were unaffected by L-NAME in diabetes mellitus arterioles or when eNOS was activated by intraluminal flow in DAHP-treated arterioles (with or without SOD+CAT). |
| 961 | 12644725 | In contrast, pyrogallol (known to produce reactive oxygen species) substantially reduced acetylcholine- and SNP-induced dilation in a SOD+CAT-reversible manner. |
| 962 | 12648810 | The extract also causes a significant increase in reduced glutathione, superoxide dismutase, catalase, glutathione peroxidase and glutathione-S-transferase in liver and kidney of streptozotocin diabetic rats, which clearly shows the antioxidant property of CLEt. |
| 963 | 12648817 | Oral administration of an aqueous Jamun seed extract (JSEt) for 6 weeks caused a significant decrease in lipids, thiobarbituric acid reactive substances (TBARS) and an increase in catalase and superoxide dismutase in the brain of alloxan induced diabetic rats. |
| 964 | 12666831 | Cobalt therapy effectively decreased the increased activities of catalase (CAT), superoxide dismutase (SOD), and thiobarbituric acid reactant substances (TBARS) but could not restore the increased glutathione peroxidase (GSH-Px) in the liver of diabetic rats. |
| 965 | 12678688 | The current review summarizes results from knockout mice with the target disruption of genes involved in the development of DA neurons (engrailed 1 and 2, lmx1b, and Nurr1), in maintaining DA neurotransmission (tyrosine hydroxylase, vesicular monoamine transporter, DA transporter, DA D2 and D3 receptors) and important for DA neuron survival (alpha-synuclein, glia cell line-derived neurotrophic factor and superoxide dismutase). |
| 966 | 12688636 | RT-PCR studies were employed to investigate the effects of the toxins on the expression of antioxidative enzymes, superoxide dismutase (SOD), glutathionine peroxidase (GPX) and catalase (CAT). |
| 967 | 12688636 | RT-PCR showed that 90 minutes exposure of BRIN-BD11 cells or RINm5F cells to 5 mM ninhydrin down regulates SOD, GPX and CAT antioxidative enzymes. |
| 968 | 12688636 | RT-PCR studies were employed to investigate the effects of the toxins on the expression of antioxidative enzymes, superoxide dismutase (SOD), glutathionine peroxidase (GPX) and catalase (CAT). |
| 969 | 12688636 | RT-PCR showed that 90 minutes exposure of BRIN-BD11 cells or RINm5F cells to 5 mM ninhydrin down regulates SOD, GPX and CAT antioxidative enzymes. |
| 970 | 12712694 | Plasma nitric oxide(P-NO), vitamin C(P-VC), vitamin E(P-VE), beta-carotene (P-beta-CAR), lipoperoxides (P-LPO) contents, the activities of erythrocyte superoxide dismutase(E-SOD), catalase(E-CAT), glutathione peroxidase (E-GSH-Px) and lipoperoxides (E-LPO) in 114 diabetic patients and 100 healthy subjects were measured. |
| 971 | 12716823 | Poly(ADP-ribose) polymerase activation in turn depletes the intracellular concentration of its substrate NAD(+), slowing the rate of glycolysis, electron transport, and ATP formation, and produces an ADP-ribosylation of the GAPDH. |
| 972 | 12716823 | New low-molecular mass compounds that act as SOD or catalase mimetics or L-propionyl-carnitine and lipoic acid, which work as intracellular superoxide scavengers, improving mitochondrial function and reducing DNA damage, may be good candidates for such a strategy, and preliminary studies support this hypothesis. |
| 973 | 12751697 | Serum antioxidants and intracellular enzymatic antioxidants composed mainly of glutathione peroxidase (GSH-Px), catalase (CAT), superoxide dismutase (SOD) and glutathione reductase counterbalance oxidative stress. |
| 974 | 12751697 | The aim of this study was to assess the activity of CAT, GSH-Px, SOD and glutathione reductase in children with a family history of premature CHD who did not present any other major risk factors of CHD (diabetes, obesity, dyslipidaemia or hypertension). |
| 975 | 12751697 | The erythrocyte activity of CAT, GSH-Px, SOD and glutathione reductase was assessed. |
| 976 | 12751697 | There were no statistically significant differences in the activity of SOD and glutathione reductase. |
| 977 | 12751697 | Serum antioxidants and intracellular enzymatic antioxidants composed mainly of glutathione peroxidase (GSH-Px), catalase (CAT), superoxide dismutase (SOD) and glutathione reductase counterbalance oxidative stress. |
| 978 | 12751697 | The aim of this study was to assess the activity of CAT, GSH-Px, SOD and glutathione reductase in children with a family history of premature CHD who did not present any other major risk factors of CHD (diabetes, obesity, dyslipidaemia or hypertension). |
| 979 | 12751697 | The erythrocyte activity of CAT, GSH-Px, SOD and glutathione reductase was assessed. |
| 980 | 12751697 | There were no statistically significant differences in the activity of SOD and glutathione reductase. |
| 981 | 12751697 | Serum antioxidants and intracellular enzymatic antioxidants composed mainly of glutathione peroxidase (GSH-Px), catalase (CAT), superoxide dismutase (SOD) and glutathione reductase counterbalance oxidative stress. |
| 982 | 12751697 | The aim of this study was to assess the activity of CAT, GSH-Px, SOD and glutathione reductase in children with a family history of premature CHD who did not present any other major risk factors of CHD (diabetes, obesity, dyslipidaemia or hypertension). |
| 983 | 12751697 | The erythrocyte activity of CAT, GSH-Px, SOD and glutathione reductase was assessed. |
| 984 | 12751697 | There were no statistically significant differences in the activity of SOD and glutathione reductase. |
| 985 | 12751697 | Serum antioxidants and intracellular enzymatic antioxidants composed mainly of glutathione peroxidase (GSH-Px), catalase (CAT), superoxide dismutase (SOD) and glutathione reductase counterbalance oxidative stress. |
| 986 | 12751697 | The aim of this study was to assess the activity of CAT, GSH-Px, SOD and glutathione reductase in children with a family history of premature CHD who did not present any other major risk factors of CHD (diabetes, obesity, dyslipidaemia or hypertension). |
| 987 | 12751697 | The erythrocyte activity of CAT, GSH-Px, SOD and glutathione reductase was assessed. |
| 988 | 12751697 | There were no statistically significant differences in the activity of SOD and glutathione reductase. |
| 989 | 12787913 | Significant correlations were determined between strand breakage and HbA(1c) (r = 0.37, P<0.05); Fpg-sensitive sites and HbA(1c) (r = 0.59, P<0.01); Fpg-sensitive sites and glucose (r = 0.45, P<0.02); Fpg-sensitive sites and SOD (r = -0.48, P<0.02); HbA(1c) and SOD (r = -0.50, P<0.02). |
| 990 | 12813567 | This study determined the effect of melatonin on the antioxidant enzymes: superoxide dismutase (SOD), catalase (CAT) and glutathione peroxidase (GPx), and the level of glutathione (GSH) in human diabetic (C2 line) skin fibroblasts. |
| 991 | 12813567 | Next, the GSH level and SOD, CAT and GPx activities were measured colorimetrically. |
| 992 | 12813567 | This study determined the effect of melatonin on the antioxidant enzymes: superoxide dismutase (SOD), catalase (CAT) and glutathione peroxidase (GPx), and the level of glutathione (GSH) in human diabetic (C2 line) skin fibroblasts. |
| 993 | 12813567 | Next, the GSH level and SOD, CAT and GPx activities were measured colorimetrically. |
| 994 | 12890544 | Concomitantly, significant decreases in the levels of antioxidants ceruloplasmin, albumin and total thiols were found in the plasma of diabetic rats. |
| 995 | 12890544 | In erythrocytes lysate, glutathione S-transferase (GST) activities were increased significantly in rats treated with garlic oil or melatonin, while lipid peroxides decreased significantly and total thiol increased significantly in melatonin or garlic oil treatment, respectively. |
| 996 | 12890544 | In liver homogenates of rats treated with garlic or melatonin, lipid peroxides were decreased significantly, and GST activities increased significantly, while SOD activities were increased significantly in liver and kidney after garlic or melatonin treatment. |
| 997 | 12910484 | In this study, erythrocyte glutathione levels, lipid peroxidation, superoxide dismutase, catalase, and glutathione peroxidase and some extracellular antioxidant protein levels of patients with type II diabetes mellitus and healthy controls were investigated. |
| 998 | 12910484 | Levels of erythrocyte lipid peroxidation, serum ceruloplasmin and glucose levels, HbA1C levels, and erythrocyte catalase activity were significantly increased, whereas serum albumin and transferrin levels, erythrocyte glutathione levels, and glutathione peroxidase activity were significantly decreased compared to those of controls. |
| 999 | 12916162 | Superoxide dismutase and glutathione reductase activities of both brain homogenate and erythrocytes as well as catalase and glutathione peroxidase activities of brain homogenate were shown to decrease significantly in diabetic rats, meanwhile, catalase activity of erythrocytes was increased and glutathione peroxidase unchanged. |
| 1000 | 12967931 | Relationship between peroxisome proliferator-activated receptors (PPAR alpha and PPAR gamma) and endothelium-dependent relaxation in streptozotocin-induced diabetic rats. |
| 1001 | 12967931 | The decreased relaxation in diabetes was improved by the chronic administration of bezafibrate (30 mg kg-1, p.o., 4 weeks). (3) The expressions of the mRNAs for PPARalpha and PPARgamma were significantly decreased in STZ-induced diabetic rats (compared with the controls) and this decrease was restored partially, but not completely, by the chronic administration of bezafibrate. (4) Superoxide dismutase activity in the aorta was not significantly different between diabetic rats and bezafibrate-treated diabetic rats. (5) The expression of the mRNA for the p22phox subunit of NAD(P)H oxidase was significantly higher in diabetics than in controls, but it was lower in bezafibrate-treated diabetic rats than in nontreated diabetic rats. |
| 1002 | 12967931 | Although the expression of the mRNA for prepro ET-1 (ppET-1) was markedly increased in diabetic rats (compared with controls), this increase was prevented to a significant extent by the chronic administration of bezafibrate. (6) These results suggest that downregulations of PPARalpha and PPARgamma may lead to an increased expression of ppET-1 mRNA in diabetic states and this increment may trigger endothelial dysfunction. |
| 1003 | 13677624 | These antioxidants are produced either endogenously or received from exogenous sources and include enzymes like superoxide dismutase, catalase, glutathione peroxidase and glutathione reductase, minerals like Se, Mn, Cu and Zn, and vitamins like vitamin A, C and E. |
| 1004 | 14532905 | Liver, brain, heart, and kidney xanthine oxidase (XO), xanthine dehydrogenase (XDH), antioxidant enzymes (glutathione peroxidase, superoxide dismutase, catalase), and nitrite levels were measured in control and early and late diabetic rat models. |
| 1005 | 14551045 | In aortas of db/db mice, activity of SOD and catalase was reduced, whereas NAD(P)H oxidase activity was enhanced. |
| 1006 | 14551045 | ROSI treatment enhanced catalase and reduced NAD(P)H oxidase activity but did not affect the activity of SOD. |
| 1007 | 14551045 | In aortas of db/db mice, activity of SOD and catalase was reduced, whereas NAD(P)H oxidase activity was enhanced. |
| 1008 | 14551045 | ROSI treatment enhanced catalase and reduced NAD(P)H oxidase activity but did not affect the activity of SOD. |
| 1009 | 14592535 | A distinct elevation in the activities of catalase (123.9%) and superoxide dismutase (71.9%) and a decline in the activity of glutathione peroxidase (67.7%) were also observed. |
| 1010 | 14592535 | In contrast, no changes in the levels of protein and non-protein thiols as well as the activities of glutathione reductase and glutathione-S-transferase were detected. |
| 1011 | 14597598 | Polyethylene glycolated superoxide dismutase (100 U ml-1), the catalase inhibitor 3-amino-1,2,4-triazole (3-AT, 50 mM) and treatment with the copper chelator diethyldithiolcarbamate (3 mM) did not affect relaxations to ACh. 5. |
| 1012 | 14623026 | After 4 weeks of diabetes the superoxide dismutase (Cu,Zn-SOD) activity in the liver was diminished while the catalase (CAT) activity and the level of ascorbic acid (AA) were elevated in comparison with the control group. |
| 1013 | 14659454 | The aim of this study was to analyze the effect of the flavonoid silymarin, a free radical scavenger that prevents lipoperoxidation, on the pancreatic activity of superoxide dismutase (SOD), glutathione peroxidase (GSHPx) and catalase (CAT) in rats with alloxan-induced diabetes mellitus. |
| 1014 | 14680989 | This study compared the activities of superoxide dismutase, catalase, glutathione peroxidase, and glutathione reductase and the concentrations of glutathione, glutathione disulfide, and thiobarbituric acid reactants (as a measure of lipid peroxidation) in liver, kidney, and heart of Sprague-Dawley rats after 60 days of either a 50% galactose diet or insulin deficiency caused by streptozotocin injection. |
| 1015 | 14680989 | Streptozotocin diabetic rats exhibited elevated activities of renal superoxide dismutase, cardiac catalase, and renal and cardiac glutathione peroxidase, as well as elevated hepatic lipid peroxidation. |
| 1016 | 14680989 | This study compared the activities of superoxide dismutase, catalase, glutathione peroxidase, and glutathione reductase and the concentrations of glutathione, glutathione disulfide, and thiobarbituric acid reactants (as a measure of lipid peroxidation) in liver, kidney, and heart of Sprague-Dawley rats after 60 days of either a 50% galactose diet or insulin deficiency caused by streptozotocin injection. |
| 1017 | 14680989 | Streptozotocin diabetic rats exhibited elevated activities of renal superoxide dismutase, cardiac catalase, and renal and cardiac glutathione peroxidase, as well as elevated hepatic lipid peroxidation. |
| 1018 | 14682207 | Plasma lipid profile, activities of antioxidant enzymes: copper/zinc (Cu/ZnSOD) and manganese-containing superoxide dismutase (MnSOD) and glutathione peroxidase (GSH-Px), as well as concentrations of malondialdehyde (MDA)--a product of lipid peroxidation, were examined. |
| 1019 | 14694267 | The aim of this study was to analyze the effect of vitamins C and E on malondialdehyde (MDA) content and activities of key antioxidant enzymes: superoxide dismutase (SOD), catalase (CAT), and glutathione peroxidase (GSH-Px) as well as glomerular basement membrane (GBM) thickness in streptozotocin-induced diabetic kidney in rats. |
| 1020 | 14694267 | After 6 and 12 weeks, MDA content and activities of SOD, CAT and GSH-Px were measured in the kidney homogenate supernatants. |
| 1021 | 14694267 | An increase in the MDA level and decrease in the SOD, CAT and GSH-Px activities in the kidney of diabetic rats were observed after 6 and 12 weeks of experiment. |
| 1022 | 14694267 | The aim of this study was to analyze the effect of vitamins C and E on malondialdehyde (MDA) content and activities of key antioxidant enzymes: superoxide dismutase (SOD), catalase (CAT), and glutathione peroxidase (GSH-Px) as well as glomerular basement membrane (GBM) thickness in streptozotocin-induced diabetic kidney in rats. |
| 1023 | 14694267 | After 6 and 12 weeks, MDA content and activities of SOD, CAT and GSH-Px were measured in the kidney homogenate supernatants. |
| 1024 | 14694267 | An increase in the MDA level and decrease in the SOD, CAT and GSH-Px activities in the kidney of diabetic rats were observed after 6 and 12 weeks of experiment. |
| 1025 | 14694267 | The aim of this study was to analyze the effect of vitamins C and E on malondialdehyde (MDA) content and activities of key antioxidant enzymes: superoxide dismutase (SOD), catalase (CAT), and glutathione peroxidase (GSH-Px) as well as glomerular basement membrane (GBM) thickness in streptozotocin-induced diabetic kidney in rats. |
| 1026 | 14694267 | After 6 and 12 weeks, MDA content and activities of SOD, CAT and GSH-Px were measured in the kidney homogenate supernatants. |
| 1027 | 14694267 | An increase in the MDA level and decrease in the SOD, CAT and GSH-Px activities in the kidney of diabetic rats were observed after 6 and 12 weeks of experiment. |
| 1028 | 14695477 | In addition, it enhanced the activity of catalase (CAT) and superoxide dismutase (SOD) significantly. |
| 1029 | 14703801 | Oxidation of AA to MG, NH4+, and H2O2 has been reported to be catalyzed by a copper-dependent semicarbazide sensitive amine oxidase (SSAO) as well as by copper- and iron ion-catalyzed reactions with oxygen. |
| 1030 | 14703801 | Incubation of apoferritin with AA (2.5-50 mM, after 6 h) changes the apoprotein electrophoretic behavior, suggesting a structural modification of the apoprotein by AA-generated ROS. |
| 1031 | 14703801 | Superoxide dismutase (SOD) was able to partially protect apoferritin from structural modification whereas catalase, ethanol, and mannitol were ineffective in protection. |
| 1032 | 14703801 | The AA promoted damage to apoferritin produced a 40% decrease in apoprotein ferroxidase activity and an 80% decrease in its iron uptake ability. |
| 1033 | 14703974 | The study showed a significant elevation (p < 0.05) of erythrocyte thiobarbituric acid reactive substances (TBARS), an index of lipid peroxidation and significant reduction (p < 0.05) in reduced glutathione (GSH), ascorbic acid (vitamin C), alpha-tocopherol (vitamin E), superoxide dismutase (SOD), catalase (CAT) and glutathione peroxidase (GPx) in the STZ diabetic rats. |
| 1034 | 14746166 | Antioxidant status has been evaluated through the colorimetrically assessed serum activity of key antioxidant enzymes: superoxide dismutase (SOD), catalase, and glutathione peroxidase (GLPX) as well as through total antioxidant status (TAS) determination. |
| 1035 | 14746166 | In PVD+DM- group, as well as PVD-DM+ group, a significantly lower activity of the GLPX, catalase and TAS was found, whereas activity of SOD was significantly higher. |
| 1036 | 14746166 | Antioxidant status has been evaluated through the colorimetrically assessed serum activity of key antioxidant enzymes: superoxide dismutase (SOD), catalase, and glutathione peroxidase (GLPX) as well as through total antioxidant status (TAS) determination. |
| 1037 | 14746166 | In PVD+DM- group, as well as PVD-DM+ group, a significantly lower activity of the GLPX, catalase and TAS was found, whereas activity of SOD was significantly higher. |
| 1038 | 14759628 | The population (n = 122; males = 60; mean age = 72.57 +/- 7.06) consisted of controls (CTR), DAT and VD patients, with (DAT + DIAB, VD + DIAB) and without concomitant DIAB, resulting in six groups where the antioxidant profile was determined: copper-zinc superoxide dismutase (SOD), thiobarbituric acid reactive substances (TBARS), and total antioxidant capacity (TRAP). |
| 1039 | 14759628 | The ANOVAs yielded significant differences between groups for all components of the profile: SOD, p = 0.00000006; TBARS, p = 0.0000012; TRAP, p = 0.0000003. |
| 1040 | 14759628 | The population (n = 122; males = 60; mean age = 72.57 +/- 7.06) consisted of controls (CTR), DAT and VD patients, with (DAT + DIAB, VD + DIAB) and without concomitant DIAB, resulting in six groups where the antioxidant profile was determined: copper-zinc superoxide dismutase (SOD), thiobarbituric acid reactive substances (TBARS), and total antioxidant capacity (TRAP). |
| 1041 | 14759628 | The ANOVAs yielded significant differences between groups for all components of the profile: SOD, p = 0.00000006; TBARS, p = 0.0000012; TRAP, p = 0.0000003. |
| 1042 | 14768769 | In the present study, kidney superoxide dismutase (SOD), glutathione peroxidase (GSH-Px), catalase (CAT) activities, vitamin C and lipid peroxidation levels were investigated in diabetic rats. |
| 1043 | 14977448 | Significant increases in the activities of insulin, superoxide dismutase, catalase, glutathione peroxidase, glutathione-S-transferase, reduced glutathione, vitamin C, and vitamin E were observed in liver, kidney, and brain on treatment with SPEt. |
| 1044 | 14995150 | No significant difference was found in the antioxidant enzyme (superoxide dismutase, glutathione peroxidase, catalase) activities during supplementations. |
| 1045 | 15000296 | Dysregulation of hepatic superoxide dismutase, catalase and glutathione peroxidase in diabetes: response to insulin and antioxidant therapies. |
| 1046 | 15000296 | The main antioxidant enzymes include superoxide dismutase (SOD), catalase (CAT) and glutathione peroxidase (GPX). |
| 1047 | 15000296 | Diabetic animals showed marked weight loss, decreased activities of Cu Zn SOD and CAT and normal GPX activity. |
| 1048 | 15000296 | Dysregulation of hepatic superoxide dismutase, catalase and glutathione peroxidase in diabetes: response to insulin and antioxidant therapies. |
| 1049 | 15000296 | The main antioxidant enzymes include superoxide dismutase (SOD), catalase (CAT) and glutathione peroxidase (GPX). |
| 1050 | 15000296 | Diabetic animals showed marked weight loss, decreased activities of Cu Zn SOD and CAT and normal GPX activity. |
| 1051 | 15000296 | Dysregulation of hepatic superoxide dismutase, catalase and glutathione peroxidase in diabetes: response to insulin and antioxidant therapies. |
| 1052 | 15000296 | The main antioxidant enzymes include superoxide dismutase (SOD), catalase (CAT) and glutathione peroxidase (GPX). |
| 1053 | 15000296 | Diabetic animals showed marked weight loss, decreased activities of Cu Zn SOD and CAT and normal GPX activity. |
| 1054 | 15007513 | We have therefore used the spontaneously diabetic BB/S rat model of type 1 diabetes to compare islet catalase and superoxide dismutase activities in diabetes-prone and diabetes-resistant animals. |
| 1055 | 15007513 | There was clear evidence of oxidative damage in freshly isolated rat islets from diabetes-prone animals and significantly lower catalase and superoxide dismutase activities than in islets from age-matched diabetes-resistant BB/S and control Wistar rats. |
| 1056 | 15007513 | The mRNA expression of catalase was lower, whereas MnSOD expression was higher, in diabetes-prone compared to diabetes-resistant BB/S rat islets, suggesting regulation at the level of gene expression as well as of the activities of these enzymes in diabetes. |
| 1057 | 15007513 | The protein expression of catalase, CuZnSOD and MnSOD was assessed by Western blotting and found to be unchanged in DETA-NO treated cells. |
| 1058 | 15007513 | Protein expression of MnSOD was increased by cytokines in RINm5F cells whereas the expression of CuZnSOD was slightly decreased and the level of catalase protein was unchanged. |
| 1059 | 15007513 | We conclude that there are some changes, mostly upregulation, in protein expression but no decreases in the mRNA expression of catalase, CuZnSOD or MnSOD enzymes in beta cells treated with either cytokines or DETA-NO. |
| 1060 | 15007513 | We have therefore used the spontaneously diabetic BB/S rat model of type 1 diabetes to compare islet catalase and superoxide dismutase activities in diabetes-prone and diabetes-resistant animals. |
| 1061 | 15007513 | There was clear evidence of oxidative damage in freshly isolated rat islets from diabetes-prone animals and significantly lower catalase and superoxide dismutase activities than in islets from age-matched diabetes-resistant BB/S and control Wistar rats. |
| 1062 | 15007513 | The mRNA expression of catalase was lower, whereas MnSOD expression was higher, in diabetes-prone compared to diabetes-resistant BB/S rat islets, suggesting regulation at the level of gene expression as well as of the activities of these enzymes in diabetes. |
| 1063 | 15007513 | The protein expression of catalase, CuZnSOD and MnSOD was assessed by Western blotting and found to be unchanged in DETA-NO treated cells. |
| 1064 | 15007513 | Protein expression of MnSOD was increased by cytokines in RINm5F cells whereas the expression of CuZnSOD was slightly decreased and the level of catalase protein was unchanged. |
| 1065 | 15007513 | We conclude that there are some changes, mostly upregulation, in protein expression but no decreases in the mRNA expression of catalase, CuZnSOD or MnSOD enzymes in beta cells treated with either cytokines or DETA-NO. |
| 1066 | 15008960 | The occurrence of OS was determined in liver homogenates by measuring hydroperoxide-initiated chemiluminescence and the activity of anti-oxidant enzymes (superoxide dismutase, catalase and glutathione peroxidase). 3. |
| 1067 | 15013179 | The decrease in activities of superoxide dismutase (SOD) and catalase (CAT) and increase in lipid peroxidation (LPO) of erythrocytes as observed in diabetes was regained after insulin, NSH, and NSK treatments. |
| 1068 | 15013179 | However, there was insignificant improvement in SOD, CAT, and LPO of kidney on NSK and NSH treatment. |
| 1069 | 15013179 | In spite of increased CAT and SOD activities in liver and heart, LPO was also increased in diabetic rats. |
| 1070 | 15013179 | The decrease in activities of superoxide dismutase (SOD) and catalase (CAT) and increase in lipid peroxidation (LPO) of erythrocytes as observed in diabetes was regained after insulin, NSH, and NSK treatments. |
| 1071 | 15013179 | However, there was insignificant improvement in SOD, CAT, and LPO of kidney on NSK and NSH treatment. |
| 1072 | 15013179 | In spite of increased CAT and SOD activities in liver and heart, LPO was also increased in diabetic rats. |
| 1073 | 15013179 | The decrease in activities of superoxide dismutase (SOD) and catalase (CAT) and increase in lipid peroxidation (LPO) of erythrocytes as observed in diabetes was regained after insulin, NSH, and NSK treatments. |
| 1074 | 15013179 | However, there was insignificant improvement in SOD, CAT, and LPO of kidney on NSK and NSH treatment. |
| 1075 | 15013179 | In spite of increased CAT and SOD activities in liver and heart, LPO was also increased in diabetic rats. |
| 1076 | 15022163 | Circulatory lipid peroxidation, vitamin C, vitamin E and enzymic antioxidants such as superoxide dismutase and catalase were analyzed. |
| 1077 | 15022163 | Quercetin also resulted in the activities of superoxide dismutase, catalase coming to near normal, along with the levels of vitamin C and vitamin E. |
| 1078 | 15022163 | Circulatory lipid peroxidation, vitamin C, vitamin E and enzymic antioxidants such as superoxide dismutase and catalase were analyzed. |
| 1079 | 15022163 | Quercetin also resulted in the activities of superoxide dismutase, catalase coming to near normal, along with the levels of vitamin C and vitamin E. |
| 1080 | 15052603 | This was associated with a depression of glutathione (GSH) concentration as well as superoxide dismutase (SOD) and catalase (CAT) activities in the liver and brain. |
| 1081 | 15053821 | The renal oxidative stress marker malonaldehyde, glutathione levels and the anti-oxidant enzymes superoxide dismutase and catalase were measured in kidney homogenate. 3. |
| 1082 | 15070172 | Treatment with B. forficata extract did not interfere in the albumin, total protein and lipid, triglyceride, cholesterol and SOD determinations. |
| 1083 | 15072974 | This effect was accompanied by increased superoxide production by aortic rings and cultured endothelial cells that were coincubated with EMPs and was inhibited by a SOD mimetic and blunted by an endothelial nitric oxide synthase inhibitor. |
| 1084 | 15072974 | In addition, p22(phox) subunit of NADPH-oxidase was detected in EMP. |
| 1085 | 15090261 | PKC, PP2A, COX-2, 5-lipooxygenase, nitric oxide synthase, NADPH-oxidase, superoxide dismutase, phopholipase A2) and modulates the expression of genes that are involved in atherosclerosis (e.g. scavenger receptors, integrins, selectins, cytokines, cyclins). |
| 1086 | 15090267 | The activity of antioxidant enzymes: superoxide dismutase (SOD), catalase (CAT), glutathione peroxidase (GPx) and total glutathione (GSH) was measured spectrophotometrically. |
| 1087 | 15090267 | The presence of AGE-Lys or Ang II induced the increase of SOD activity. |
| 1088 | 15090267 | The activity of antioxidant enzymes: superoxide dismutase (SOD), catalase (CAT), glutathione peroxidase (GPx) and total glutathione (GSH) was measured spectrophotometrically. |
| 1089 | 15090267 | The presence of AGE-Lys or Ang II induced the increase of SOD activity. |
| 1090 | 15111505 | Therefore, we examined whether acute hyperinsulinemia increases the production of free radicals and whether this condition affects proliferative extracellular signal-regulated kinase (ERK-1 and -2) signaling in human fibroblasts in vitro. |
| 1091 | 15111505 | Insulin treatment significantly increased intracellular superoxide anion (O(2)(-)) production, an effect completely abolished by Tiron, a cell-permeable superoxide dismutase (SOD) mimetic and by polyethylene glycol (PEG)-SOD, but not by PEG catalase. |
| 1092 | 15111505 | The insulin-induced free radical production led to membranous translocation of p47phox and markedly enhanced ERK-1 and -2 activation in human fibroblasts. |
| 1093 | 15111506 | Protein kinase C (PKC) activity and production of superoxide anion were increased in the cerebral arteries of ZO rats, and pretreatment with superoxide dismutase restored all examined dilator responses. |
| 1094 | 15117550 | However, KS-III increased Phase II enzyme activities such as SOD, glutathione peroxidase, and catalase, suggesting the activation of free radical-scavenging enzymes. |
| 1095 | 15133294 | The results showed that the radon and thermal therapy enhanced the antioxidation functions, such as the activities of superoxide dismutase (SOD) and catalase, which inhibit lipid peroxidation and total cholesterol produced in the body. |
| 1096 | 15133294 | Moreover the therapy enhanced concanavalin A (ConA)-induced mitogen response and increased the percentage of CD4 positive cells, which is the marker of helper T cells, and decreased the percentage of CD8 positive cells, which is the common marker of killer T cells and suppressor T cells, in the white blood cell differentiation antigen (CD8/CD4) assay. |
| 1097 | 15133294 | Furthermore, the therapy increased the levels of alpha atrial natriuretic polypeptide (alpha ANP), beta endorphin, adrenocorticotropic hormone (ACTH), insulin and glucose-6-phosphate dehydrogenase (G-6-PDH), and it decreased the vasopression level. |
| 1098 | 15162367 | The activities of glutathione peroxidase (GPx), superoxide dismutase (SOD) and catalase (CAT) decreased in the liver. |
| 1099 | 15162367 | FA also resulted in increased activities of SOD, CAT, GPx and expansion of pancreatic islets. |
| 1100 | 15162367 | The activities of glutathione peroxidase (GPx), superoxide dismutase (SOD) and catalase (CAT) decreased in the liver. |
| 1101 | 15162367 | FA also resulted in increased activities of SOD, CAT, GPx and expansion of pancreatic islets. |
| 1102 | 15224410 | To assess changes in the cellular antioxidant defense system, we measured the activities of antioxidant enzymes (such as glutathione peroxidase (GSHPx), superoxide dismutase (SOD), and catalase (CAT)) in pancreatic homogenates. |
| 1103 | 15228097 | Significant decrease in mitochondrial catalase, manganese superoxide-dismutase (Mn-SOD) and reduced glutathione (GSH) content and increase in the lipid peroxidation (LPx) and glutathione peroxidase (GPx) activity was observed under these metabolic stress conditions with more pronounced effects in hypoglycemic group. |
| 1104 | 15240923 | Moreover glutathione peroxidase (GSHPx), superoxide dismutase (SOD) and catalase (CAT) were also measured in pancreatic homogenates. |
| 1105 | 15266913 | Aqueous extract also decreased the formation of lipid peroxides estimated as thiobarbituric acid reactive substance, (TBARS), and increased antioxidants (superoxide dismutase, catalase, glutathione peroxidase and glutathione transferase) in erythrocytes. |
| 1106 | 15266957 | To add new insight to the question, changes in the lipid peroxidation products (MDA) and activities of antioxidant enzymes: superoxide dismutase (SOD) and catalase in red blood cell hemolysates were evaluated in 20 women with gestational diabetes. 20 healthy pregnant women served as the control group. |
| 1107 | 15266957 | Pregnant women with gestational diabetes showed an increase in lipoperoxidation products (P < 0.001) and a decrease in SOD activity (P < 0.01) as compared to normal pregnant women while no significant change was observed in catalase activity. |
| 1108 | 15266957 | To add new insight to the question, changes in the lipid peroxidation products (MDA) and activities of antioxidant enzymes: superoxide dismutase (SOD) and catalase in red blood cell hemolysates were evaluated in 20 women with gestational diabetes. 20 healthy pregnant women served as the control group. |
| 1109 | 15266957 | Pregnant women with gestational diabetes showed an increase in lipoperoxidation products (P < 0.001) and a decrease in SOD activity (P < 0.01) as compared to normal pregnant women while no significant change was observed in catalase activity. |
| 1110 | 15276645 | Altered activities of superoxide dismutase (SOD) and catalase (CAT) were also recorded in diabetics. |
| 1111 | 15289896 | ROS are anihilated by an intracelluar enzymatic system composed mainly of glutathione peroxidase (GPx), superoxide dismutase (SOD) and catalase (CAT). |
| 1112 | 15289896 | Erythrocyte activities of GPx, SOD, CAT and TAS were measured in diabetic patients without retinopathy, with non-proliferative and proliferative retinopathy. |
| 1113 | 15289896 | Only CAT was significantly negatively correlated with the period of insulin treatment. |
| 1114 | 15289896 | ROS are anihilated by an intracelluar enzymatic system composed mainly of glutathione peroxidase (GPx), superoxide dismutase (SOD) and catalase (CAT). |
| 1115 | 15289896 | Erythrocyte activities of GPx, SOD, CAT and TAS were measured in diabetic patients without retinopathy, with non-proliferative and proliferative retinopathy. |
| 1116 | 15289896 | Only CAT was significantly negatively correlated with the period of insulin treatment. |
| 1117 | 15292654 | Biochemical analysis of kidneys revealed a marked increase in oxidative stress demonstrated by increased lipid peroxidation and decreased activities of key antioxidant enzymes, glutathione (GSH), superoxide dismutase (SOD) and catalase in diabetic rats. |
| 1118 | 15298542 | A significant reduction in mRNA levels and the protein content of hepatic Mn-superoxide dismutase (SOD) and glutathione peroxidase (GPx) were observed in non-exercise obese groups, but the mRNA and protein levels of these enzymes were markedly increased after exercise training. |
| 1119 | 15298757 | Sea tangle and sodium alginate did not affect activities of catalase and glutathione peroxidase; however, supplementation of water extract of sea tangle resulted in higher superoxide dismutase activity as compared with the control and sodium alginate groups. |
| 1120 | 15305024 | Administration of seed kernel to diabetic rats significantly decreased the levels of blood glucose, glycosylated hemoglobin and increased body weight gain, plasma insulin and hemoglobin. |
| 1121 | 15305024 | The diabetic rats showed the low activities of superoxide dismutase, catalase, glutathione peroxidase and reduced glutathione content in liver and kidney, which were restored to near normal levels by treatment with the seed kernel extract. |
| 1122 | 15332498 | The depressed activities of superoxide dismutase, catalase and glutathione peroxidase and lowered glutathione content in the heart and pancreas of diabetic rats were found to increase on treatment with AMFEt. |
| 1123 | 15347773 | CuZn superoxide dismutase (SOD), MnSOD, catalase (CAT), and glutathione-peroxidase (GPX) activity and mRNA expression were measured before and after 3 mo of synthetic vitamin E supplementation (600 mg twice daily); on both occasions, IAP was evaluated at different ex vivo glucose concentrations (5 and 22 mM). |
| 1124 | 15347773 | In normal glucose concentrations, CuZnSOD, MnSOD, CAT, and GPX activity and mRNA expression were not different among the groups. |
| 1125 | 15356917 | Treatment with the macrocyclic binuclear oxovanadium complex decreased the lipid peroxides and the antioxidant enzymes such as superoxide dismutase, catalase and glutathione peroxidase to near control levels. |
| 1126 | 15362485 | Our aim is to study the effect of orally administered L-tryptophan (TRP), the melatonin precursor, an endogenous antioxidant, on circulating levels of glycaemia, insulin and melatonin, and on the superoxide dismutase and catalase antioxidant systems in non-diabetic (ND) and type 2 diabetic (n5-STZ) male Wistar rats. |
| 1127 | 15362485 | At the beginning and end of treatment (at 09:00; 21:00; 02:00) plasma insulin and melatonin levels were measured, and (at 09:00) the enzymatic activities of catalase and superoxide dismutase (SOD) in erythrocytes were also measured. |
| 1128 | 15362485 | Our aim is to study the effect of orally administered L-tryptophan (TRP), the melatonin precursor, an endogenous antioxidant, on circulating levels of glycaemia, insulin and melatonin, and on the superoxide dismutase and catalase antioxidant systems in non-diabetic (ND) and type 2 diabetic (n5-STZ) male Wistar rats. |
| 1129 | 15362485 | At the beginning and end of treatment (at 09:00; 21:00; 02:00) plasma insulin and melatonin levels were measured, and (at 09:00) the enzymatic activities of catalase and superoxide dismutase (SOD) in erythrocytes were also measured. |
| 1130 | 15369706 | The levels of lipidperoxides, reduced glutathione and activities of superoxide dismutase, catalase and glutathione peroxidase were assayed in pancreatic tissue of control and experimental groups of rats. |
| 1131 | 15375788 | Ach-evoked relaxation and Ach- and A23187-evoked cGMP formation were significantly impaired in aortae from diabetic rabbits compared to controls, effects that were reversed with superoxide dismutase (SOD) and catalase (CAT). |
| 1132 | 15375788 | This reduction by copper was again reversed by SOD and CAT. |
| 1133 | 15375788 | Ach-evoked relaxation and Ach- and A23187-evoked cGMP formation were significantly impaired in aortae from diabetic rabbits compared to controls, effects that were reversed with superoxide dismutase (SOD) and catalase (CAT). |
| 1134 | 15375788 | This reduction by copper was again reversed by SOD and CAT. |
| 1135 | 15381345 | Whilst plasma levels for malondialdehyde (MDAP) and erythrocyte malondialdehyde (MDAE) were measured as markers of oxidative stress, activity of erythrocyte superoxide dismutase (SOD), glutathion peroxidase (GSH-Px), and catalase (CAT) were taken as markers of oxidative defense system. |
| 1136 | 15381345 | Whilst CAT was elevated in groups 3 and 4 compared to control subjects (P = 0.025 and 0.002, respectively), no difference was found for SOD between the groups. |
| 1137 | 15381345 | Whilst plasma levels for malondialdehyde (MDAP) and erythrocyte malondialdehyde (MDAE) were measured as markers of oxidative stress, activity of erythrocyte superoxide dismutase (SOD), glutathion peroxidase (GSH-Px), and catalase (CAT) were taken as markers of oxidative defense system. |
| 1138 | 15381345 | Whilst CAT was elevated in groups 3 and 4 compared to control subjects (P = 0.025 and 0.002, respectively), no difference was found for SOD between the groups. |
| 1139 | 15383233 | Ethanolic extract of G. montanum leaves was administered orally (50, 100, and 200 mg/kg of body weight) for 3 weeks, and changes in blood glucose, plasma insulin, and lipid peroxidation markers such as thiobarbituric acid-reactive substances (TBARS), hydroperoxides, and levels of antioxidants, namely, superoxide dismutase, catalase, glutathione peroxidase, reduced glutathione, and glutathione-S-transferase, were examined in the brain of alloxan-induced diabetic rats. |
| 1140 | 15448086 | EUK-8 is a member of a new class of synthetic salen-manganese compounds with low toxicity that possess catalytic superoxide dismutase, peroxidase, and catalase activity that can inactivate superoxide and nitrogen oxides (e.g., peroxynitrite and nitrogen dioxide). |
| 1141 | 15452882 | The aim of this study was to examine the effect of caffeic acid phenethyl ester (CAPE) on lipid peroxidation (LPO) and the activities of antioxidant enzymes such as superoxide dismutase (SOD), catalase (CAT), and glutathione peroxidase (GSH-Px) in the liver of streptozotocin (STZ)-induced diabetic rats. |
| 1142 | 15452882 | The liver was excised after 8 weeks of CAPE treatment, the levels of malondialdehyde (MDA) and the activities of SOD, CAT, and GSH-Px in the hepatic tissues of all groups were analyzed. |
| 1143 | 15452882 | The activities of SOD, CAT, and GSH-Px in the untreated diabetic group were higher than that in the control group (p < 0.0001). |
| 1144 | 15452882 | Rats in the CAPE-treated diabetic group had reduced activities of SOD and CAT in comparison with the rats of untreated diabetic group (p < 0.0001). |
| 1145 | 15452882 | The aim of this study was to examine the effect of caffeic acid phenethyl ester (CAPE) on lipid peroxidation (LPO) and the activities of antioxidant enzymes such as superoxide dismutase (SOD), catalase (CAT), and glutathione peroxidase (GSH-Px) in the liver of streptozotocin (STZ)-induced diabetic rats. |
| 1146 | 15452882 | The liver was excised after 8 weeks of CAPE treatment, the levels of malondialdehyde (MDA) and the activities of SOD, CAT, and GSH-Px in the hepatic tissues of all groups were analyzed. |
| 1147 | 15452882 | The activities of SOD, CAT, and GSH-Px in the untreated diabetic group were higher than that in the control group (p < 0.0001). |
| 1148 | 15452882 | Rats in the CAPE-treated diabetic group had reduced activities of SOD and CAT in comparison with the rats of untreated diabetic group (p < 0.0001). |
| 1149 | 15452882 | The aim of this study was to examine the effect of caffeic acid phenethyl ester (CAPE) on lipid peroxidation (LPO) and the activities of antioxidant enzymes such as superoxide dismutase (SOD), catalase (CAT), and glutathione peroxidase (GSH-Px) in the liver of streptozotocin (STZ)-induced diabetic rats. |
| 1150 | 15452882 | The liver was excised after 8 weeks of CAPE treatment, the levels of malondialdehyde (MDA) and the activities of SOD, CAT, and GSH-Px in the hepatic tissues of all groups were analyzed. |
| 1151 | 15452882 | The activities of SOD, CAT, and GSH-Px in the untreated diabetic group were higher than that in the control group (p < 0.0001). |
| 1152 | 15452882 | Rats in the CAPE-treated diabetic group had reduced activities of SOD and CAT in comparison with the rats of untreated diabetic group (p < 0.0001). |
| 1153 | 15452882 | The aim of this study was to examine the effect of caffeic acid phenethyl ester (CAPE) on lipid peroxidation (LPO) and the activities of antioxidant enzymes such as superoxide dismutase (SOD), catalase (CAT), and glutathione peroxidase (GSH-Px) in the liver of streptozotocin (STZ)-induced diabetic rats. |
| 1154 | 15452882 | The liver was excised after 8 weeks of CAPE treatment, the levels of malondialdehyde (MDA) and the activities of SOD, CAT, and GSH-Px in the hepatic tissues of all groups were analyzed. |
| 1155 | 15452882 | The activities of SOD, CAT, and GSH-Px in the untreated diabetic group were higher than that in the control group (p < 0.0001). |
| 1156 | 15452882 | Rats in the CAPE-treated diabetic group had reduced activities of SOD and CAT in comparison with the rats of untreated diabetic group (p < 0.0001). |
| 1157 | 15478189 | Decreased concentration of glutathione (GSH) and decreased activities of superoxide dismutase (SOD), and catalase in liver and kidney of diabetic rats were also noted. |
| 1158 | 15479564 | Effects of PPARgamma ligands and C/EBPbeta enhancer on expression of extracellular-superoxide dismutase. |
| 1159 | 15479564 | Extracellular-superoxide dismutase (EC-SOD) is the major SOD isozyme in the blood vessel walls and may be important for antioxidant capability of the vascular walls. |
| 1160 | 15479564 | Recently, we found that the plasma EC-SOD levels in type 2 diabetic patients were significantly and inversely related to indices of insulin resistance, whereas they were strongly and positively related to adiponectin. |
| 1161 | 15479564 | Administration of pioglitazone significantly increased the plasma level of EC-SOD and adiponectin. |
| 1162 | 15479564 | Transcription factors such as CCAAT/enhancer-binding proteins (C/EBPs) and peroxisome proliferator-activated receptors (PPARs) are known to regulate genes associated with insulin resistance. |
| 1163 | 15479564 | We found that a C/EBPbeta enhancer, prolactin, significantly induced the EC-SOD mRNA and protein levels in cultured fibroblast cell lines, but PPARgamma ligands, pioglitazone and other thiazolidinedione agents did not. |
| 1164 | 15479564 | Deletion analysis of the EC-SOD promoter-luciferase construct showed that an important element responsible for prolactin is located between -242 and -178 in the promoter region of the EC-SOD gene in which a known C/EBPbeta-binding site is located. |
| 1165 | 15479564 | Increasing the EC-SOD expression by treatment with ligands of transcription factors might be one approach to ameliorate the pathological conditions of insulin resistance. |
| 1166 | 15492127 | Prediabetes and diabetes in nonobese diabetic (NOD) mice have been targeted by a variety of immunotherapies, including the use of a soluble form of cytotoxic T lymphocyte antigen 4 (CTLA-4) and interferon (IFN)-gamma. |
| 1167 | 15492127 | The defect is characterized by impaired induction of immunosuppressive tryptophan catabolism, is related to transient blockade of the signal transducer and activator of transcription (STAT)1 pathway of intracellular signaling by IFN-gamma, and is caused by peroxynitrite production. |
| 1168 | 15492127 | Here, we show that soluble CTLA-4 imparts suppressive properties to DCs from early prediabetic NOD female mice through mechanisms that rely on autocrine signaling by IFN-gamma. |
| 1169 | 15492127 | Although phosphorylation of STAT1 in response to IFN-gamma is compromised in those mice, CTLA-4 obviates the defect. |
| 1170 | 15492127 | IFN-gamma-driven expression of tryptophan catabolism by CTLA-4-immunoglobulin is made possible through the concomitant activation of the Forkhead Box class O (FOXO) transcription factor FOXO3a, induction of the superoxide dismutase gene, and prevention of peroxynitrite formation. |
| 1171 | 15492479 | A mutation of the CD36 gene that encodes a fatty acid transporter has been reported to play a role in insulin resistance in spontaneously hypertensive rat (SHR). |
| 1172 | 15492479 | The objective of this study was to determine the role of CD36 and the significance of statin therapy in insulin-resistance syndromes. |
| 1173 | 15492479 | We determined the isometric relaxation induced by acetylcholine or lecithinized superoxide dismutase (SOD) in aortas obtained from Otsuka Long Evans Tokushima Fatty (OLETF) rats, a model of insulin resistance and dyslipidemia, and normal control (Long Evans Tokushima Otsuka; LETO) rats with or without cerivastatin treatment. |
| 1174 | 15492479 | We also determined the effect of cerivastatin on aortic expression of CD36 and PPARgamma. |
| 1175 | 15492479 | Cerivastatin increased the aortic expression of CD36 and PPARgamma mRNA in both LETO and OLETF rats. |
| 1176 | 15492479 | In conclusion, insulin resistance in OLETF rats may be partially due to an altered expression of CD36. |
| 1177 | 15492479 | Increased aortic expression of CD36 in response to cerivastatin could explain the reduction in serum triglyceride concentrations with statin therapy and may have pronounced beneficial effects in insulin-resistance syndromes. |
| 1178 | 15500942 | LH was increased and GSH-Px was decreased, while no alterations were observed in SOD and catalase in serum of DCu-60 animals. |
| 1179 | 15501693 | High glucose concentration augments angiotensin II mediated contraction via AT1 receptors in rat thoracic aorta. |
| 1180 | 15501693 | Ang II induced contraction via AT1 receptor was significantly enhanced (by 60 +/- 2 %) in HG exposed thoracic aortic rings isolated from vehicle treated but not STZ treated rats. |
| 1181 | 15501693 | However, there was no change in the pD2 of Ang II while potassium chloride (KCl) induced contraction was unaltered. |
| 1182 | 15501693 | Ang II induced contractile response was blocked by valsartan (100 microM, selective AT1 receptor antagonist) but not PD 123,319 (100 microM, selective and potent AT2 receptor antagonist). |
| 1183 | 15501693 | Tempol (100 microM, a cell permeable superoxide dismutase mimetic) partially reduced the augmented Ang II response in HG exposed aortic rings, while it did not affect the Ang II responses in normal glucose (NG 5.5 mM) exposed aortic rings isolated from control rats. [3H] Ang II binding at AT1 receptors was unaltered in vascular smooth muscle membranes prepared from thoracic aorta exposed to HG for 2 h compared to NG exposed aortic rings. |
| 1184 | 15501693 | From our results, we conclude that high glucose concentration augments Ang II mediated contraction via AT1 receptors and reactive oxygen species partly contribute to this augmented contraction. |
| 1185 | 15528954 | Cu/Zn superoxide dismutase (SOD) and phosphatidylinositol-3-kinase (PI3K) were also measured. |
| 1186 | 15528954 | Diabetes led to increased activity (45%) and expression (70%) of liver iNOS, an effect that was attenuated by insulin treatment both in vitro and in whole animals. |
| 1187 | 15528954 | Levels of PI3K protein were significantly lower in diabetic rats while insulin treatment markedly increased expression. |
| 1188 | 15528954 | Glycemic control via insulin administration was able to downregulate enhanced hepatic iNOS activity and expression in the liver observed in the diabetic state and improve SOD activity, responses that can potentially reduce the free radical damage associated with diabetes. |
| 1189 | 15528954 | Cu/Zn superoxide dismutase (SOD) and phosphatidylinositol-3-kinase (PI3K) were also measured. |
| 1190 | 15528954 | Diabetes led to increased activity (45%) and expression (70%) of liver iNOS, an effect that was attenuated by insulin treatment both in vitro and in whole animals. |
| 1191 | 15528954 | Levels of PI3K protein were significantly lower in diabetic rats while insulin treatment markedly increased expression. |
| 1192 | 15528954 | Glycemic control via insulin administration was able to downregulate enhanced hepatic iNOS activity and expression in the liver observed in the diabetic state and improve SOD activity, responses that can potentially reduce the free radical damage associated with diabetes. |
| 1193 | 15536073 | ROS levels in 3T3-L1 adipocytes can be reduced significantly with pharmacological agents that lower the mitochondrial membrane potential, or by overexpression of uncoupling protein 1 or superoxide dismutase. |
| 1194 | 15540607 | In comparison to the normoglycaemic group the treatment of rats with a single dose of STZ (65 mg/kg body weight) only revealed a significant increase (P < 0.05) in plasma hydrogen peroxide (H2O2) by 230%, increased the thiobarbituric acid reactive substances (TBARS) as index of the lipid peroxidation level by 69%, while total antioxidant activity was decreased by 36%, with a consistent significant decrease (P < 0.05) in the activity of erythrocytes antioxidative enzymes catalase (CAT), superoxide dismutase (SOD), glutathione peroxidase (GPx), and paraoxonase (PON). |
| 1195 | 15540607 | Exogenous administration of individual gradual doses of naringin to hyperglycaemic rats causes a dose-dependent decrease of the glucose level, an increase of the insulin concentration, a decrease of the H2O2 and TBARS levels, as well as the increase of the total antioxidant status with an increase of antioxidant enzyme activities (CAT, SOD, GPx, and PON). |
| 1196 | 15540607 | In comparison to the normoglycaemic group the treatment of rats with a single dose of STZ (65 mg/kg body weight) only revealed a significant increase (P < 0.05) in plasma hydrogen peroxide (H2O2) by 230%, increased the thiobarbituric acid reactive substances (TBARS) as index of the lipid peroxidation level by 69%, while total antioxidant activity was decreased by 36%, with a consistent significant decrease (P < 0.05) in the activity of erythrocytes antioxidative enzymes catalase (CAT), superoxide dismutase (SOD), glutathione peroxidase (GPx), and paraoxonase (PON). |
| 1197 | 15540607 | Exogenous administration of individual gradual doses of naringin to hyperglycaemic rats causes a dose-dependent decrease of the glucose level, an increase of the insulin concentration, a decrease of the H2O2 and TBARS levels, as well as the increase of the total antioxidant status with an increase of antioxidant enzyme activities (CAT, SOD, GPx, and PON). |
| 1198 | 15549711 | Administration of an aqueous extract of Scoparia dulcis by intragastric intubation (po) at a dose of 200 mg/kg body weight significantly decreased the blood glucose and lipid peroxidative marker thiobarbituric acid reactive substances (TBARS) with significant increase in the activities of plasma insulin, pancreatic superoxide dismutase (SOD), catalase (CAT), and reduced glutathione (GSH) in streptozotocin diabetic rats at the end of 15 days treatment. |
| 1199 | 15559165 | The present study was designed to explore the relationship between lipid peroxidation and antioxidant enzymes in young Malaysian insulin dependant diabetes mellitus (IDDM) patients. |
| 1200 | 15559165 | Antioxidant enzymes namely superoxide dismutase (SOD), catalase (CAT) and glutathione peroxidase (GPx) were significantly decreased while plasma malondialdehyde (MDA), an indicator for lipid peroxidation was significantly increased in IDDM patients compared to control subjects. |
| 1201 | 15563975 | There are many molecules, including Fas ligand (FasL) and cytokines, such as IL-1, TNF-alpha and IFN-gamma that cause release of other cytokine-mediators that have potential to damage the beta cells. |
| 1202 | 15563975 | The beta cell-death appears to ultimately be caused by receptor (Fas/FasL)-mediated mechanisms and/or by secretion of cytotoxic molecules (e.g., granzymes, perforin). |
| 1203 | 15563975 | Transgenic mice with beta cell specific overexpression of copper, zinc superoxide dismutase, or thioredoxin are resistant to autoimmune and STZ-induced diabetes. |
| 1204 | 15575595 | Decreased concentration of glutathione (GSH) and decreased activities of superoxide dismutase (SOD), catalase and glutathione peroxidase (GPx) in heart and brain of diabetic rats were also noted. |
| 1205 | 15601754 | Previous studies have shown the presence of 5-HT2A, 5-HT2B, and 5-HT1B receptors in vascular smooth muscle cells (VSMCs). |
| 1206 | 15601754 | There are currently no data regarding 5-HT2B and 5-HT1B receptor activation of the JAK/STAT pathway in VSMCs and resultant potential alterations in 5-HT signaling in diabetes. |
| 1207 | 15601754 | Therefore, we tested the hypothesis that 5-HT differentially activates the JAK/STAT pathway in VSMCs under conditions of normal (5 mM) and high (25 mM) glucose. |
| 1208 | 15601754 | Treatment of rat VSMCs with 5-HT (10(-6) M) resulted in time-dependent activation ( approximately 2-fold) of JAK2, JAK1, and STAT1, but not STAT3 (maximal at 5 min, returned to baseline by 30 min). |
| 1209 | 15601754 | The 5-HT2B receptor agonist BW723C86 and the 5-HT1B receptor agonist CGS12066A (10(-9)-10(-5) M, 5-min stimulation) did not activate the JAK/STAT pathway. |
| 1210 | 15601754 | Treatment with the 5-HT2A receptor antagonist ketanserin (10 nM) inhibited JAK2 activation by 5-HT. |
| 1211 | 15601754 | Treatment of streptozotocin-induced diabetic rats with ketanserin (5 mg.kg-1.day-1) reduced activation of JAK2 and STAT1 but not STAT3 in endothelium-denuded thoracic aorta in vivo. 5-HT (10(-6) M) treatment resulted in increased cell proliferation and increased DNA synthesis, which were inhibited by the JAK2 inhibitor AG490. |
| 1212 | 15601754 | Further studies with apocynin, diphenyleneiodonium chloride, catalase, and virally transfected superoxide dismutase had no effect at either glucose concentration on activation of the JAK/STAT pathway by 5-HT. |
| 1213 | 15601754 | Therefore, we conclude that 5-HT activates JAK2, JAK1, and STAT1 via the 5-HT2A receptors in a reactive oxygen species-independent manner under both normal and high glucose conditions. |
| 1214 | 15607912 | MG significantly and concentration-dependently increased NO and O2*- generation in A-10 cells, which was significantly inhibited by L-NAME and SOD or DPI, respectively. |
| 1215 | 15607912 | An elevated MG level and the consequential ROS/RNS generation would alter cellular signaling pathways, contributing to the development of different insulin resistance states such as diabetes or hypertension. |
| 1216 | 15621558 | Oxidative stress in diabetic pregnancy: SOD, CAT and GSH-Px activity and lipid peroxidation products. |
| 1217 | 15621558 | Diabetic control was monitored by fasting blood glucose and glycosylated hemoglobin (HbA(1c)) and these values, as well as measured biochemical parameters (urea, creatinine, total cholesterol and uric acid), were appropriate throughout the study. |
| 1218 | 15621558 | The concentration of TBARS, as a measure of lipid peroxidation, and activity of antioxidant enzymes superoxide dismutase (Cu, Zn-SOD), glutathione peroxidase (GSH-Px) and catalase (CAT) were investigated in hemolysate of erythrocytes. |
| 1219 | 15621558 | Oxidative stress in diabetic pregnancy: SOD, CAT and GSH-Px activity and lipid peroxidation products. |
| 1220 | 15621558 | Diabetic control was monitored by fasting blood glucose and glycosylated hemoglobin (HbA(1c)) and these values, as well as measured biochemical parameters (urea, creatinine, total cholesterol and uric acid), were appropriate throughout the study. |
| 1221 | 15621558 | The concentration of TBARS, as a measure of lipid peroxidation, and activity of antioxidant enzymes superoxide dismutase (Cu, Zn-SOD), glutathione peroxidase (GSH-Px) and catalase (CAT) were investigated in hemolysate of erythrocytes. |
| 1222 | 15621935 | Molybdenosis and Mo-induced disturbances of Cu metabolism in moose are characterized by numerous severe lesions caused by reduced activity of Cu-containing enzymes such as ceruloplasmin, superoxide dismutase in blood, and myocardial cytochrome c oxidase. |
| 1223 | 15629256 | In order to determine the changes of cellular antioxidant defense system, antioxidant enzymes such as glutathione peroxidase (GSHPx), superoxide dismutase (SOD) and catalase (CAT) activities were measured in pancreatic homogenates. |
| 1224 | 15629260 | The results show that EEP and WSD led to decreased levels of blood glucose (FBG), fructosamine (FRU), malonaldehyde (MDA), nitric oxide (NO), nitric oxide synthetase (NOS), total cholesterol (TC), triglyceride (TG), low-density lipoprotein cholesterol (LDL-C), very low-density lipoprotein cholesterol (VLDL-C) in serum of fasting rats; and to increased serum levels of high-density lipoprotein cholesterol (HDL-C) and superoxide dismutase (SOD). |
| 1225 | 15652272 | The decreased activities of key antioxidant enzymes such as superoxide dismutase, catalase, glutathione peroxidase, glutathione reductase and glutathione in diabetic rats were brought back to near normal range upon ACF treatment. |
| 1226 | 15652492 | TNF-alpha induces interleukin-8 and endothelin-1 expression in human endothelial cells with different redox pathways. |
| 1227 | 15652492 | We investigated the effect of TNF-alpha on interleukin-8 (IL-8) and endothelin-1 (ET-1) expression, and their different signal transduction pathways. |
| 1228 | 15652492 | By Northern blot analysis, TNF-alpha at 50, 100, 200, and 400 U/ml significantly induced IL-8 mRNA expression by 206%, 252%, 211%, and 158%, respectively, as compared to controls (p < 0.05). |
| 1229 | 15652492 | Overexpression of human superoxide dismutase (SOD) by adenovirus-mediated gene transfer or addition of exogenous hydrogen peroxide (H(2)O(2)) significantly enhanced TNF-alpha-induced IL-8 mRNA expression. |
| 1230 | 15652492 | Furthermore, HMECs treated with TNF-alpha at 50, 100, and 200 U/ml significantly increased ET-1 mRNA expression by 71%, 82%, and 66%, respectively (p < 0.05). |
| 1231 | 15652492 | By contrast, SOD gene transfer and exogenous H(2)O(2) significantly inhibited TNF-alpha-induced ET-1 mRNA expression. |
| 1232 | 15652492 | Thus, TNF-alpha significantly induces both IL-8 and ET-1 gene expression in HMECs possibly through different redox signaling pathways. |
| 1233 | 15652492 | H(2)O(2) enhances TNF-alpha-induced IL-8 expression, but inhibits TNF-alpha-induced ET-1 expression. |
| 1234 | 15652492 | TNF-alpha induces interleukin-8 and endothelin-1 expression in human endothelial cells with different redox pathways. |
| 1235 | 15652492 | We investigated the effect of TNF-alpha on interleukin-8 (IL-8) and endothelin-1 (ET-1) expression, and their different signal transduction pathways. |
| 1236 | 15652492 | By Northern blot analysis, TNF-alpha at 50, 100, 200, and 400 U/ml significantly induced IL-8 mRNA expression by 206%, 252%, 211%, and 158%, respectively, as compared to controls (p < 0.05). |
| 1237 | 15652492 | Overexpression of human superoxide dismutase (SOD) by adenovirus-mediated gene transfer or addition of exogenous hydrogen peroxide (H(2)O(2)) significantly enhanced TNF-alpha-induced IL-8 mRNA expression. |
| 1238 | 15652492 | Furthermore, HMECs treated with TNF-alpha at 50, 100, and 200 U/ml significantly increased ET-1 mRNA expression by 71%, 82%, and 66%, respectively (p < 0.05). |
| 1239 | 15652492 | By contrast, SOD gene transfer and exogenous H(2)O(2) significantly inhibited TNF-alpha-induced ET-1 mRNA expression. |
| 1240 | 15652492 | Thus, TNF-alpha significantly induces both IL-8 and ET-1 gene expression in HMECs possibly through different redox signaling pathways. |
| 1241 | 15652492 | H(2)O(2) enhances TNF-alpha-induced IL-8 expression, but inhibits TNF-alpha-induced ET-1 expression. |
| 1242 | 15674846 | Concentrations of thiobarbituric acid reactive substances, glutathione and glutathione disulfide, and activities of glutathione reductase, glutathione peroxidase, superoxide dismutase, and catalase were measured in liver, kidney, and heart. |
| 1243 | 15674846 | Four types of effects were observed: (1) treatment with beta-carotene alone either reversed (cardiac glutathione disulfide) or elevated (cardiac glutathione, hepatic glutathione peroxidase activity) levels seen in diabetic animals; (2) beta-carotene alone produced no effect, but pycnogenol both alone and in combinations elevated (renal glutathione peroxidase and glutathione reductase activities, hepatic glutathione reductase activity and glutathione disulfide) or depressed (cardiac glutathione disulfide) levels seen in untreated diabetic animals; (3) all treatments with antioxidants, either alone or in combination, either normalized (lipid peroxidation in all tissues), elevated (hepatic GSH, cardiac glutathione peroxidase activity), or had no effect on (activities of hepatic catalase and superoxide dismutase in all tissues) levels seen in diabetic animals; (4) in only one case (cardiac glutathione reductase activity) levels in diabetic animals treated with combinations of antioxidants were normal, but elevated in animals treated with either antioxidant alone. |
| 1244 | 15674846 | Concentrations of thiobarbituric acid reactive substances, glutathione and glutathione disulfide, and activities of glutathione reductase, glutathione peroxidase, superoxide dismutase, and catalase were measured in liver, kidney, and heart. |
| 1245 | 15674846 | Four types of effects were observed: (1) treatment with beta-carotene alone either reversed (cardiac glutathione disulfide) or elevated (cardiac glutathione, hepatic glutathione peroxidase activity) levels seen in diabetic animals; (2) beta-carotene alone produced no effect, but pycnogenol both alone and in combinations elevated (renal glutathione peroxidase and glutathione reductase activities, hepatic glutathione reductase activity and glutathione disulfide) or depressed (cardiac glutathione disulfide) levels seen in untreated diabetic animals; (3) all treatments with antioxidants, either alone or in combination, either normalized (lipid peroxidation in all tissues), elevated (hepatic GSH, cardiac glutathione peroxidase activity), or had no effect on (activities of hepatic catalase and superoxide dismutase in all tissues) levels seen in diabetic animals; (4) in only one case (cardiac glutathione reductase activity) levels in diabetic animals treated with combinations of antioxidants were normal, but elevated in animals treated with either antioxidant alone. |
| 1246 | 15683752 | The aim of this study was to investigate an extensive array of redox status indices: glutathione (GSH), malondialdehyde (MDA), peroxidation potential, superoxide dismutase (SOD), catalase (CAT), total hydroperoxide (TH) and advanced oxidation protein products (AOPP) in relation to blood glucose and glucose indicators control such as glycosylated haemoglobin (HbA1c) and fructosamine by spectophotometric techniques. |
| 1247 | 15683752 | These patients also showed an increase of AOPP and PP levels as well as an increase of both CAT and SOD activity. |
| 1248 | 15683752 | The aim of this study was to investigate an extensive array of redox status indices: glutathione (GSH), malondialdehyde (MDA), peroxidation potential, superoxide dismutase (SOD), catalase (CAT), total hydroperoxide (TH) and advanced oxidation protein products (AOPP) in relation to blood glucose and glucose indicators control such as glycosylated haemoglobin (HbA1c) and fructosamine by spectophotometric techniques. |
| 1249 | 15683752 | These patients also showed an increase of AOPP and PP levels as well as an increase of both CAT and SOD activity. |
| 1250 | 15685205 | Acute incubation of SMA with a combination of polyethylene glycol superoxide dismutase and catalase significantly reduced the enhanced contraction to PE in db/db mice. |
| 1251 | 15718825 | Normal and 30-day streptozotocin-induced diabetic Sprague-Dawley rats received daily intraperitoneal doses (10 mg/kg) of beta-carotene, alpha-lipoic, and Pycnogenol individually or in combinations for 14 days, after which retinae were dissected and fractionated for the assay of activities of glutathione reductase, glutathione peroxidase, gamma-glutamyl transferase, and superoxide dismutase. |
| 1252 | 15720789 | Similarly, the treatment also resulted in a significant reduction in thiobarbituric acid reactive substances, hydroperoxides, superoxide dismutase, catalase and glutathione peroxidase and significant improvement in reduced glutathione in the pancreas of STZ-induced diabetic rats when compared with untreated diabetic rats. |
| 1253 | 15802869 | To investigate the effect of urinary tract infection on oxidative stress in diabetic patients, we measured the activities of antioxidant enzymes such as catalase and superoxide dismutase, and lipid peroxidation levels in urine specimens of type II diabetic patents with urinary tract infection. |
| 1254 | 15802869 | In urine samples of diabetic patients with or without urinary tract infection and in urine samples of non-diabetic patients with urinary tract infection, catalase and superoxide dismutase activities were lower and lipid peroxidation levels were higher than those of the healthy subjects (p < 0.05). |
| 1255 | 15802869 | To investigate the effect of urinary tract infection on oxidative stress in diabetic patients, we measured the activities of antioxidant enzymes such as catalase and superoxide dismutase, and lipid peroxidation levels in urine specimens of type II diabetic patents with urinary tract infection. |
| 1256 | 15802869 | In urine samples of diabetic patients with or without urinary tract infection and in urine samples of non-diabetic patients with urinary tract infection, catalase and superoxide dismutase activities were lower and lipid peroxidation levels were higher than those of the healthy subjects (p < 0.05). |
| 1257 | 15814255 | Antioxidant activities of WGLE supplementation further extend in suppressing activities of antioxidant related enzymes, such as glutathione peroxidase (GSH-Px), catalase (CAT) and superoxide dismutase (SOD), in organs of diabetic rats. |
| 1258 | 15821039 | Antioxidant mechanism of heme oxygenase-1 involves an increase in superoxide dismutase and catalase in experimental diabetes. |
| 1259 | 15821039 | We examined the effect of HO-1 protein and HO activity on extracellular SOD (EC-SOD), catalase, O2-, inducible nitric oxide synthase (iNOS), and endothelial nitric oxide synthase (eNOS) levels and vascular responses to ACh in control and diabetic rats. |
| 1260 | 15821039 | Vascular EC-SOD and plasma catalase activities were significantly reduced in diabetic compared with nondiabetic rats (P < 0.05). |
| 1261 | 15821039 | Upregulation of HO-1 expression by intermittent administration of cobalt protoporphyrin, an inducer of HO-1 protein and activity, resulted in a robust increase in EC-SOD but no significant change in Cu-Zn-SOD. |
| 1262 | 15821039 | Administration of tin mesoporphyrin, an inhibitor of HO-1 activity, decreased EC-SOD protein. |
| 1263 | 15821039 | Increased HO-1 activity in diabetic rats was associated with a decrease in iNOS but increases in eNOS and plasma catalase activity. |
| 1264 | 15821039 | These data demonstrate that an increase in HO-1 protein and activity, i.e., CO and bilirubin production, in diabetic rats brings about a robust increase in EC-SOD, catalase, and eNOS with a concomitant increase in endothelial relaxation and a decrease in O2-. |
| 1265 | 15821039 | These observations in experimental diabetes suggest that the vascular cytoprotective mechanism of HO-1 against oxidative stress requires an increase in EC-SOD and catalase. |
| 1266 | 15821039 | Antioxidant mechanism of heme oxygenase-1 involves an increase in superoxide dismutase and catalase in experimental diabetes. |
| 1267 | 15821039 | We examined the effect of HO-1 protein and HO activity on extracellular SOD (EC-SOD), catalase, O2-, inducible nitric oxide synthase (iNOS), and endothelial nitric oxide synthase (eNOS) levels and vascular responses to ACh in control and diabetic rats. |
| 1268 | 15821039 | Vascular EC-SOD and plasma catalase activities were significantly reduced in diabetic compared with nondiabetic rats (P < 0.05). |
| 1269 | 15821039 | Upregulation of HO-1 expression by intermittent administration of cobalt protoporphyrin, an inducer of HO-1 protein and activity, resulted in a robust increase in EC-SOD but no significant change in Cu-Zn-SOD. |
| 1270 | 15821039 | Administration of tin mesoporphyrin, an inhibitor of HO-1 activity, decreased EC-SOD protein. |
| 1271 | 15821039 | Increased HO-1 activity in diabetic rats was associated with a decrease in iNOS but increases in eNOS and plasma catalase activity. |
| 1272 | 15821039 | These data demonstrate that an increase in HO-1 protein and activity, i.e., CO and bilirubin production, in diabetic rats brings about a robust increase in EC-SOD, catalase, and eNOS with a concomitant increase in endothelial relaxation and a decrease in O2-. |
| 1273 | 15821039 | These observations in experimental diabetes suggest that the vascular cytoprotective mechanism of HO-1 against oxidative stress requires an increase in EC-SOD and catalase. |
| 1274 | 15831211 | The activities of superoxide dismutase and catalase were increased significantly by E. littorale treatment in diabetic rats. |
| 1275 | 15833036 | That ROS-driven thiol cross-linking underlies the CP aggregation was evidenced by the inhibitory effects of added superoxide dismutase, catalase, mannitol, and dithiothreitol. |
| 1276 | 15838275 | The endothelin-1- induced attenuation was very strongly suppressed by co-incubation with J-104132, endothelin receptor A/B antagonist, or polyethylene-glycolated superoxide dismutase, a cell-permeant superoxide anion scavenger or LY294002, phosphoinositide 3-kinase inhibitor. |
| 1277 | 15838275 | These results indicate that endothelin-1 can induce endothelial dysfunction, and that this may be related to superoxide generation and to PI3-kinase activity. |
| 1278 | 15849382 | The extract treatment also resulted in a significant increase in reduced glutathione, superoxide dismutase, catalase, glutathione peroxidase and glutathione-S-transferase in the liver and kidney of diabetic rats. |
| 1279 | 15850715 | GLUT-4 (glucose transporter) receptor, tumor necrosis factor-alpha (TNF-alpha), interleukins-6 (IL-6), daf-genes and PPARs (peroxisomal proliferation activator receptors) play a role in the development of insulin resistance syndrome and associated conditions. |
| 1280 | 15850715 | Long chain polyunsaturated fatty acids (LCPUFAs) increase cell membrane fluidity and enhance the number of insulin receptors and the affinity of insulin to its receptors; suppress TNF-alpha, IL-6, macrophage migration inhibitory factor (MIF) and leptin synthesis; increase the number of GLUT-4 receptors, serve as endogenous ligands of PPARs, modify lipolysis, and regulate the balance between pro- and anti-oxidants, and thus, play a critical role in the pathogenesis of insulin resistance. |
| 1281 | 15850715 | In the nematode, Caenorhabditis elegans, the protein encoded by daf-2 is 35% identical to the human insulin receptor; daf-7 codes a transforming growth factor-beta (TGF-beta) type signal and daf-16 enhances superoxide dismutase (SOD) expression. |
| 1282 | 15850715 | Melatonin has anti-oxidant actions similar to daf-16, TGF-beta and SOD. |
| 1283 | 15850715 | These evidences suggest that the activities of Delta6 and Delta5 enzymes play a critical role in the expression and regulation of GLUT-4, TNF-alpha, IL-6, MIF, daf-genes, melatonin, and leptin by modulating the synthesis and tissue concentrations of LCPUFAs. |
| 1284 | 15850715 | Both insulin and insulin-like growth factor-1 (IGF-1) attenuated this response. |
| 1285 | 15850715 | SIRT1 sequesters the proapoptotic factor Bax, prevents stress-induced apoptosis of cells, and thus, prolongs survival. |
| 1286 | 15850715 | In addition, SIRT1 repressed PPAR-gamma, and overexpression of SIRT1 attenuated adipogenesis, and upregulation of SIRT in differentiated fat cells triggered lipolysis and loss of fat, events that are known to attenuate insulin resistance and prolong life span. |
| 1287 | 15850715 | GLUT-4 (glucose transporter) receptor, tumor necrosis factor-alpha (TNF-alpha), interleukins-6 (IL-6), daf-genes and PPARs (peroxisomal proliferation activator receptors) play a role in the development of insulin resistance syndrome and associated conditions. |
| 1288 | 15850715 | Long chain polyunsaturated fatty acids (LCPUFAs) increase cell membrane fluidity and enhance the number of insulin receptors and the affinity of insulin to its receptors; suppress TNF-alpha, IL-6, macrophage migration inhibitory factor (MIF) and leptin synthesis; increase the number of GLUT-4 receptors, serve as endogenous ligands of PPARs, modify lipolysis, and regulate the balance between pro- and anti-oxidants, and thus, play a critical role in the pathogenesis of insulin resistance. |
| 1289 | 15850715 | In the nematode, Caenorhabditis elegans, the protein encoded by daf-2 is 35% identical to the human insulin receptor; daf-7 codes a transforming growth factor-beta (TGF-beta) type signal and daf-16 enhances superoxide dismutase (SOD) expression. |
| 1290 | 15850715 | Melatonin has anti-oxidant actions similar to daf-16, TGF-beta and SOD. |
| 1291 | 15850715 | These evidences suggest that the activities of Delta6 and Delta5 enzymes play a critical role in the expression and regulation of GLUT-4, TNF-alpha, IL-6, MIF, daf-genes, melatonin, and leptin by modulating the synthesis and tissue concentrations of LCPUFAs. |
| 1292 | 15850715 | Both insulin and insulin-like growth factor-1 (IGF-1) attenuated this response. |
| 1293 | 15850715 | SIRT1 sequesters the proapoptotic factor Bax, prevents stress-induced apoptosis of cells, and thus, prolongs survival. |
| 1294 | 15850715 | In addition, SIRT1 repressed PPAR-gamma, and overexpression of SIRT1 attenuated adipogenesis, and upregulation of SIRT in differentiated fat cells triggered lipolysis and loss of fat, events that are known to attenuate insulin resistance and prolong life span. |
| 1295 | 15900084 | The decrease in thiobarbituric acid reactive substances (TBARS) and hydroperoxides (HPX) and increase in the activities of superoxide dismutase (SOD), catalase (CAT), glutathione peroxidase (GPx), reduced glutathione (GSH) and glutathione-S-transferase (GST) clearly show the antioxidant properties of SPEt in addition to its antidiabetic effect. |
| 1296 | 15902099 | Proteome of H-411E (liver) cells exposed to insulin and tumor necrosis factor-alpha: analysis of proteins involved in insulin resistance. |
| 1297 | 15902099 | Insulin resistance may be modeled in H-411E liver cells in tissue culture with the use of the cytokine tumor necrosis factor-alpha (TNF-alpha) and insulin. |
| 1298 | 15902099 | After incubation of liver cells in tissue culture with INS alone, TNF-alpha alone, and TNF-alpha plus insulin, as well as a control sample, liver-cell extracts were separated on 2D polyacrylamide-gel electrophoresis on the basis of isoelectric point and molecular weight. |
| 1299 | 15902099 | We analyzed the gel images with the use of PD Quest software (Bio-Rad Laboratories, Hercules, Calif) to identify differentially expressed protein spots (ie, up or down with insulin vs down or up with TNF-alpha plus insulin). |
| 1300 | 15902099 | The first series of experiments identified 6 differentially expressed proteins: eukaryotic translation initiation factor-3, subunit 2, regulator of G-protein signaling-5, superoxide dismutase, protein disulfide isomerase A6, proteasome subunit-alpha type 3, and regucalcin. |
| 1301 | 15902099 | A second series of experiments identified 7 additional proteins with significantly altered differential expression: cell-division protein kinase-4, kinogen heavy chain, carbonic anhydrase-7, E 3 ubiquitin protein ligase, URE-B1; Rab GDP dissociation inhibitor-beta, Rab GDP dissociation inhibitor-beta2, and MAWDBP. |
| 1302 | 15902099 | It can be seen that differentially expressed proteins, affected by treatment with insulin or with TNF-alpha plus insulin, include regulators of translation, protein degradation, cellular Ca ++ , G-proteins, and free-radical production. |
| 1303 | 15902099 | Although one cannot detail the mechanism or mechanisms of TNF-alpha induced IR from this data alone, it is easy to relate all of these proteins to a role in insulin signal transduction and, hence, insulin resistance. |
| 1304 | 15927932 | The treatment also resulted in a significant increase in reduced glutathione, superoxide dismutase, catalase, glutathione peroxidase and glutathione-s-transferase in the liver and kidney of diabetic rats. |
| 1305 | 15928880 | The enzymatic activities of glutathione peroxidase (GSH-Px), superoxide dismutase (SOD) and catalase (CAT) were measured as indicators of antioxidation in these tissues. |
| 1306 | 15928880 | The SOD and CAT contents of the heart in Group 2 were significantly increased as compared to Groups 1 and 3 (P<0.05). |
| 1307 | 15928880 | The enzymatic activities of glutathione peroxidase (GSH-Px), superoxide dismutase (SOD) and catalase (CAT) were measured as indicators of antioxidation in these tissues. |
| 1308 | 15928880 | The SOD and CAT contents of the heart in Group 2 were significantly increased as compared to Groups 1 and 3 (P<0.05). |
| 1309 | 15932790 | Blood samples were collected at the beginning and at the end of the study to measure malondialdehyde production, glycated hemoglobin, selenium dependent-glutathione peroxidase, Cu,Zn-superoxide dismutase in erythrocytes and total antioxidant status, glucose, lipid and lipoproteins in serum. |
| 1310 | 15932790 | However, an unexpected increase on cholesterol levels and a reduced erythrocyte-Cu,Zn-superoxide dismutase activity was observed after alpha-tocopherol treatment. alpha-Tocopherol administration did not affect glucose, glycated hemoglobin, triacylglycerides, lipoprotein levels and serum malondialdehyde. |
| 1311 | 15932790 | Blood samples were collected at the beginning and at the end of the study to measure malondialdehyde production, glycated hemoglobin, selenium dependent-glutathione peroxidase, Cu,Zn-superoxide dismutase in erythrocytes and total antioxidant status, glucose, lipid and lipoproteins in serum. |
| 1312 | 15932790 | However, an unexpected increase on cholesterol levels and a reduced erythrocyte-Cu,Zn-superoxide dismutase activity was observed after alpha-tocopherol treatment. alpha-Tocopherol administration did not affect glucose, glycated hemoglobin, triacylglycerides, lipoprotein levels and serum malondialdehyde. |
| 1313 | 15936462 | Impairment of blood antioxidant potential in diabetic patients was reflected by an 81% increase in superoxide dismutase (SOD) activity, a 30% decrease in catalase (CT), 20% decrease in glutathione peroxidase (GPx) and glutathione reductase (GR) activities as well as by lowered total antioxidant status (TAS). |
| 1314 | 15936462 | CD, TBARS and SOD values were positively correlated with plasma glucose concentration and glycated hemoglobin level. |
| 1315 | 15936462 | Impairment of blood antioxidant potential in diabetic patients was reflected by an 81% increase in superoxide dismutase (SOD) activity, a 30% decrease in catalase (CT), 20% decrease in glutathione peroxidase (GPx) and glutathione reductase (GR) activities as well as by lowered total antioxidant status (TAS). |
| 1316 | 15936462 | CD, TBARS and SOD values were positively correlated with plasma glucose concentration and glycated hemoglobin level. |
| 1317 | 15946965 | Relief of stress by the NADPH oxidase inhibitor apocynin or by superoxide dismutase (SOD) but not by catalase reversed the attenuation of K+ currents and reduced DHE fluorescence. |
| 1318 | 15946965 | In cells from diabetic females, neither apocynin nor SOD augmented K+ currents, ANG II was not elevated and DHE fluorescence was significantly weaker than in cells from males. |
| 1319 | 15946965 | Diabetic male rats pretreated with the angiotensin-converting enzyme (ACE) inhibitor quinapril were hyperglycaemic, but their cellular ANG II levels and DHE fluorescence were significantly decreased. |
| 1320 | 15946965 | When ANG II levels are lower, as in diabetic females or following ACE inhibition in males, oxidative stress is reduced, with blunted alterations in K+ currents. |
| 1321 | 15946965 | Relief of stress by the NADPH oxidase inhibitor apocynin or by superoxide dismutase (SOD) but not by catalase reversed the attenuation of K+ currents and reduced DHE fluorescence. |
| 1322 | 15946965 | In cells from diabetic females, neither apocynin nor SOD augmented K+ currents, ANG II was not elevated and DHE fluorescence was significantly weaker than in cells from males. |
| 1323 | 15946965 | Diabetic male rats pretreated with the angiotensin-converting enzyme (ACE) inhibitor quinapril were hyperglycaemic, but their cellular ANG II levels and DHE fluorescence were significantly decreased. |
| 1324 | 15946965 | When ANG II levels are lower, as in diabetic females or following ACE inhibition in males, oxidative stress is reduced, with blunted alterations in K+ currents. |
| 1325 | 15957552 | Biochemical analysis of kidneys revealed a marked increase in oxidative stress demonstrated by increased lipid peroxidation and decreased activities of key antioxidant enzymes, GSH, SOD, and catalase in diabetic rats. |
| 1326 | 15959628 | The study was undertaken to analyze the effect of pioglitazone on superoxide dismutase (Cu, Zn-SOD), catalase (CAT), glutathione peroxidase (GSH-Px), glutathione reductase (GSSG-R), glutathione (GSH), ascorbic acid (AA), lipid peroxidation products (LPO) and protein carbonyl groups (PCG) in the heart of alloxan-induced diabetic rabbits after 4 and 8 weeks of pioglitazone treatment. |
| 1327 | 15983212 | Islets from transgenic mice expressing combinations of human copper/zinc superoxide dismutase (SOD), extracellular SOD, and cellular glutathione peroxidase (Gpx-1) were subjected to oxidative stress in vitro. |
| 1328 | 15983212 | Relative viability after hypoxanthine/xanthine oxidase treatment was as follows: extracellular SOD + Gpx-1 + Cu/Zn SOD > extracellular SOD + Gpx-1 > extracellular SOD > wild type. |
| 1329 | 15983212 | Islets from transgenic mice expressing combinations of human copper/zinc superoxide dismutase (SOD), extracellular SOD, and cellular glutathione peroxidase (Gpx-1) were subjected to oxidative stress in vitro. |
| 1330 | 15983212 | Relative viability after hypoxanthine/xanthine oxidase treatment was as follows: extracellular SOD + Gpx-1 + Cu/Zn SOD > extracellular SOD + Gpx-1 > extracellular SOD > wild type. |
| 1331 | 15993507 | Long-term delivery of superoxide dismutase and catalase entrapped in poly(lactide-co-glycolide) microspheres: in vitro effects on isolated neonatal porcine pancreatic cell clusters. |
| 1332 | 15993507 | Preliminarily, in vitro exposure of isolated NPCCs to slow release microsphere-embedded SOD and CAT could permit or contribute to overcome hurdles associated with scarcity in islet tissue procurement for transplant in T1DM. |
| 1333 | 15993507 | Long-term delivery of superoxide dismutase and catalase entrapped in poly(lactide-co-glycolide) microspheres: in vitro effects on isolated neonatal porcine pancreatic cell clusters. |
| 1334 | 15993507 | Preliminarily, in vitro exposure of isolated NPCCs to slow release microsphere-embedded SOD and CAT could permit or contribute to overcome hurdles associated with scarcity in islet tissue procurement for transplant in T1DM. |
| 1335 | 15997089 | The extract increased the activities of the cellular antioxidant enzymes, superoxide dismutase (SOD) and catalase (CAT). |
| 1336 | 15997089 | The diabetic rats showed low activities of superoxide dismutase and catalase in the liver, and the ethanol extract increased the CAT activity. |
| 1337 | 15997089 | The extract increased the activities of the cellular antioxidant enzymes, superoxide dismutase (SOD) and catalase (CAT). |
| 1338 | 15997089 | The diabetic rats showed low activities of superoxide dismutase and catalase in the liver, and the ethanol extract increased the CAT activity. |
| 1339 | 16004216 | We determined the oxidative status by measuring the level of superoxide dismutase (SOD-Minanui method), catalase (CAT-Aebi method), glutathione peroxidase (GPx-Fukuzawa method) and glutathione (GSH-Ellman method) in 87 type 1 diabetic patients (44 with normal urinary protein excretion-group A and 43 with MA-group B) and 38 nondiabetic matched controls, before and 24 hours after a test effort. |
| 1340 | 16005359 | The mRNA expression of antioxidant enzymes, superoxide dismutase 1 (SOD-1) and glutathione peroxidase 1 (GPx-1) in the kidney and heart were quantified using a real-time polymerase chain reaction. |
| 1341 | 16005359 | Although GPx-1 and SOD-1 showed elevated mRNA expression in the KKAy mice in the kidney and heart, in the STZ mice they did not increase compared to the controls. |
| 1342 | 16005359 | The mRNA expression of antioxidant enzymes, superoxide dismutase 1 (SOD-1) and glutathione peroxidase 1 (GPx-1) in the kidney and heart were quantified using a real-time polymerase chain reaction. |
| 1343 | 16005359 | Although GPx-1 and SOD-1 showed elevated mRNA expression in the KKAy mice in the kidney and heart, in the STZ mice they did not increase compared to the controls. |
| 1344 | 16010244 | The occurrence of OS was determined in liver homogenates by measuring the hydroperoxide-initiated chemiluminescence and the activity of antioxidant enzymes (superoxide dismutase, catalase and glutathione peroxidase). |
| 1345 | 16026269 | New, low molecular mass compounds that act as SOD or catalase mimetics or L-propionyl-carnitine and lipoic acid, that work as intracellular superoxide scavengers, improving mitochondrial function and reducing DNA damage, may be good candidates for such strategy, and preliminary studies support this hypothesis. |
| 1346 | 16037248 | In addition, the Amadori-PE-induced lipid peroxidation was effectively inhibited by superoxide dismutase, mannitol, catalase, and EDTA. |
| 1347 | 16037268 | The results showed that: (1) fructoselysine was observed in the hepatic portal veins, arteries, and femoral veins of rats fed with glycated proteins after 2 h of feeding; (2) blood sugar of glycated protein-fed rats was lower than that of diabetic rats fed with intact protein, while HbA1C in blood and glucose in urine of both groups were similar; (3) lipid peroxidation status in serum, liver, and kidney of both groups was similar; (4) superoxide dismutase (SOD) and glutathione-S-transferase (GST) enzymatic activity in serum and liver of both groups were also similar; (5) there were no differences in degree of cataract formation and concentration of glucose, fructose, sorbitol, and lipid peroxide in the lenses of both groups. |
| 1348 | 16054794 | DL also produced an increase in the hepatic levels of the endogenous antioxidants, namely superoxide dismutase (SOD), catalase and glutathione, while it brought down the levels of thiobarbituric acid-reactive substances (TBARS) in alloxan-induced diabetic rats. |
| 1349 | 16080381 | Leukocyte lipid peroxidation, superoxide dismutase and catalase activities of type 2 diabetic patients with retinopathy. |
| 1350 | 16080381 | The present study has been undertaken to investigate whether there is any relationship between retinopathy degree and leukocyte superoxide dismutase (SOD) and catalase (CAT) activities and lipid peroxidation (LPO) in diabetic individuals with type 2 diabetic retinopathy. |
| 1351 | 16080381 | Leukocyte lipid peroxidation, superoxide dismutase and catalase activities of type 2 diabetic patients with retinopathy. |
| 1352 | 16080381 | The present study has been undertaken to investigate whether there is any relationship between retinopathy degree and leukocyte superoxide dismutase (SOD) and catalase (CAT) activities and lipid peroxidation (LPO) in diabetic individuals with type 2 diabetic retinopathy. |
| 1353 | 16082415 | The effect of leptin on renal Na(+),K(+)-ATPase and urinary H(2)O(2) was augmented by a superoxide dismutase mimetic, tempol, and was abolished by catalase. |
| 1354 | 16082415 | Inhibitors of extracellular signal regulated kinases (ERKs), PD98059 or U0126, prevented Na(+),K(+)-ATPase stimulation by leptin and H(2)O(2). |
| 1355 | 16082415 | These data indicate that leptin, by acting directly within the kidney, has a delayed stimulatory effect on Na(+),K(+)-ATPase, mediated by JAKs, H(2)O(2) and ERKs. |
| 1356 | 16117620 | Circulatory lipid peroxidation, vitamin C, vitamin E, and enzymic antioxidants such as superoxide dismutase and catalase were analyzed. |
| 1357 | 16125723 | Higher levels of myocardial 8-isoprostane (8-iso PGF(2alpha)), oxidized glutathione (GSSG), as well as greater upregulation of superoxide dismutase (SOD) and catalase (CAT) protein expression paralleled by increases in enzymatic activity was observed in the diabetic MI animals, indicating higher oxidative stress. |
| 1358 | 16132687 | Oral administration of C. gynandra leaf extract significantly increased the levels of lipid peroxides and activities of catalase, glutathione peroxidase and decreased the levels of reduced glutathione and superoxide dismutase activity in arthritis induced rats. |
| 1359 | 16136216 | Oral administration of C. fenestratum stem extract in graded doses caused a significant increase in enzymatic antioxidants such as catalase, superoxide dismutase, glutathione synthetase, peroxidase, and glutathione peroxidase and in the nonenzymatic antioxidants ascorbic acid, ceruloplasmin and tocopherol. |
| 1360 | 16136216 | Effects of alcoholic extract on glycolytic enzymes such as glucose-6-phosphate dehydrogenase, lactate dehydrogenase and hexokinase showed a significant increase in their levels, whereas a significant decrease was observed in the levels of gluconeogenic enzyme, glucose-6-phosphatase and alanine aminotransferase in treated diabetic rats. |
| 1361 | 16137706 | The activities of superoxide dismutase (Cu,Zn-SOD), catalase (CAT), glutathione peroxidase (GSH-Px), glutathione reductase (GSSG-R), glutathione (GSH), ascorbic acid (AA), products of lipid peroxidation (LPO) and protein carbonyl groups (PCG) were estimated after 4 and 8 weeks of repaglinide treatment (1 mg daily). |
| 1362 | 16168716 | Lipid peroxidation, superoxide dismutase, catalase, and reduced glutathione were estimated in liver, kidney, and aorta. |
| 1363 | 16176151 | The antioxidant effect was evaluated by estimating thiobarbituric acid-reactive substances and reduced glutathione and measuring the activities of catalase and superoxide dismutase in liver, heart, and kidney in diabetic rats. |
| 1364 | 16177186 | Quercetin decreases oxidative stress, NF-kappaB activation, and iNOS overexpression in liver of streptozotocin-induced diabetic rats. |
| 1365 | 16177186 | Eight weeks later we measured TBARS and hydroperoxide-initiated chemiluminescence (QL) in liver as markers of oxidative stress, and activities of the antioxidant enzymes catalase, superoxide dismutase (SOD), and glutathione peroxidase, NF-kappaB activation by an electrophoretic mobility shift assay and expression of IkappaB kinases (IKKalpha and IKKbeta), the inhibitor IkappaB (IkappaBalpha and IkappaBbeta), and iNOS by Western blot. |
| 1366 | 16177186 | Streptozotocin administration induced significant increases in hepatic TBARS concentration, QL, and SOD and catalase activities that were prevented by quercetin. |
| 1367 | 16177186 | Activation of NF-kappaB, induction of IKKalpha and iNOS protein levels, and increased degradation of IkappaBalpha were also observed in streptozotocin-treated rats. |
| 1368 | 16177186 | Quercetin decreases oxidative stress, NF-kappaB activation, and iNOS overexpression in liver of streptozotocin-induced diabetic rats. |
| 1369 | 16177186 | Eight weeks later we measured TBARS and hydroperoxide-initiated chemiluminescence (QL) in liver as markers of oxidative stress, and activities of the antioxidant enzymes catalase, superoxide dismutase (SOD), and glutathione peroxidase, NF-kappaB activation by an electrophoretic mobility shift assay and expression of IkappaB kinases (IKKalpha and IKKbeta), the inhibitor IkappaB (IkappaBalpha and IkappaBbeta), and iNOS by Western blot. |
| 1370 | 16177186 | Streptozotocin administration induced significant increases in hepatic TBARS concentration, QL, and SOD and catalase activities that were prevented by quercetin. |
| 1371 | 16177186 | Activation of NF-kappaB, induction of IKKalpha and iNOS protein levels, and increased degradation of IkappaBalpha were also observed in streptozotocin-treated rats. |
| 1372 | 16184010 | Blood glucose levels, activity of superoxide dismutase (SOD), catalase (CAT), glutathione peroxidase (GPx), Na+/K+ ATPase, membrane lipid peroxidation and fluidity were determined in different fractions of whole brain after 21 days of treatment. |
| 1373 | 16184010 | Diabetic rats showed high blood glucose (P less than 0.001), decreased activities of SOD, catalase and Na+/K+ ATPase (P less than 0.01, P less than 0.001 and P less than 0.01), increased levels of GPx and MDA (P less than 0.01 and P less than 0.001) and decreased membrane fluidity (P less than 0.01). |
| 1374 | 16184010 | Blood glucose levels, activity of superoxide dismutase (SOD), catalase (CAT), glutathione peroxidase (GPx), Na+/K+ ATPase, membrane lipid peroxidation and fluidity were determined in different fractions of whole brain after 21 days of treatment. |
| 1375 | 16184010 | Diabetic rats showed high blood glucose (P less than 0.001), decreased activities of SOD, catalase and Na+/K+ ATPase (P less than 0.01, P less than 0.001 and P less than 0.01), increased levels of GPx and MDA (P less than 0.01 and P less than 0.001) and decreased membrane fluidity (P less than 0.01). |
| 1376 | 16186389 | Mammalian translocase of inner mitochondrial membrane (Tim)44 was identified by upregulation in streptozotocin (STZ)-induced diabetic mouse kidneys; Tim44 functions as a membrane anchor of mtHsp70 to TIM23 complex and is involved in the import of preproteins with mitochondria-targeted presequence into mitochondrial matrix. |
| 1377 | 16186389 | Transfection of siRNA and pcDNA3.1/TIM44 using HASMC culture clarified that import of antioxidative enzymes such as superoxide dismutase and glutathione peroxidase was facilitated by Tim44. |
| 1378 | 16197726 | In diabetics rats, the activities of enzymatic antioxidants such as superoxide dismutase (SOD, EC 1.11.1.1) catalase (CAT, EC 1.11.1.6) were decreased significantly while the activity of glutathione peroxidase (GPx, EC 1.11.1.9) decreased in the liver and increased in the kidney. |
| 1379 | 16202232 | Blood samples were taken from the neck vascular trunk in order to determine the glucose, triglycerides, total cholesterol, HDL-cholesterol (HDL-c), atherogenic index (AI), total protein, blood urea nitrogen (BUN), creatinine, insulin, lipid peroxidation products, reduced glutathione (GSH) and superoxide dismutase (SOD) and glutathione peroxidase (GSH-Px) activities. |
| 1380 | 16202232 | As well, we estimated the lipid peroxidtion, GSH and SOD, GSH-Px and catalase activities in brain and renal homogenates, and the excretion of albumin, proteins and glucose in urine over 24 h period. |
| 1381 | 16202232 | The administration of STZ caused significant increases in levels of glycosuria, proteinuria, albuminuria, glycemia, total cholesterol and AI, as well as in lipid peroxidation products in the brain, plasma and kidney, whereas it decreased the GSH content and SOD, GSH-Px and catalase activities. |
| 1382 | 16202232 | Blood samples were taken from the neck vascular trunk in order to determine the glucose, triglycerides, total cholesterol, HDL-cholesterol (HDL-c), atherogenic index (AI), total protein, blood urea nitrogen (BUN), creatinine, insulin, lipid peroxidation products, reduced glutathione (GSH) and superoxide dismutase (SOD) and glutathione peroxidase (GSH-Px) activities. |
| 1383 | 16202232 | As well, we estimated the lipid peroxidtion, GSH and SOD, GSH-Px and catalase activities in brain and renal homogenates, and the excretion of albumin, proteins and glucose in urine over 24 h period. |
| 1384 | 16202232 | The administration of STZ caused significant increases in levels of glycosuria, proteinuria, albuminuria, glycemia, total cholesterol and AI, as well as in lipid peroxidation products in the brain, plasma and kidney, whereas it decreased the GSH content and SOD, GSH-Px and catalase activities. |
| 1385 | 16202232 | Blood samples were taken from the neck vascular trunk in order to determine the glucose, triglycerides, total cholesterol, HDL-cholesterol (HDL-c), atherogenic index (AI), total protein, blood urea nitrogen (BUN), creatinine, insulin, lipid peroxidation products, reduced glutathione (GSH) and superoxide dismutase (SOD) and glutathione peroxidase (GSH-Px) activities. |
| 1386 | 16202232 | As well, we estimated the lipid peroxidtion, GSH and SOD, GSH-Px and catalase activities in brain and renal homogenates, and the excretion of albumin, proteins and glucose in urine over 24 h period. |
| 1387 | 16202232 | The administration of STZ caused significant increases in levels of glycosuria, proteinuria, albuminuria, glycemia, total cholesterol and AI, as well as in lipid peroxidation products in the brain, plasma and kidney, whereas it decreased the GSH content and SOD, GSH-Px and catalase activities. |
| 1388 | 16214842 | Our data showed that diabetic cardiomyocytes exhibited significantly increased [Zn2+]i (0.87 +/- 0.05 nM ) and [Ca2+]i (49.66 +/- 9.03 nM), decreased levels of MT and reduced glutathione, increased levels of lipid peroxidation and nitric oxide products, and decreased activities of superoxide dismutase, glutathione reductase, and glutathione peroxidase. |
| 1389 | 16217126 | It is a direct scavenger of free radicals and has indirect antioxidant effects due to its stimulation of the expression and activity of antioxidative enzymes such as glutathione peroxidase, superoxide dismutase and catalase, and NO synthase, in mammalian cells. |
| 1390 | 16217126 | It was recently reported that melatonin enhanced insulin-receptor kinase and IRS-1 phosphorylation, suggesting the potential existence of signaling pathway cross-talk between melatonin and insulin. |
| 1391 | 16217126 | Because TNF-alpha has been shown to impair insulin action by suppressing insulin receptor-tyrosine kinase activity and its IRS-1 tyrosine phosphorylation in peripheral tissues such as skeletal muscle cells, it was speculated that melatonin might counteract TNF-alpha-associated insulin resistance in type 2 diabetes. |
| 1392 | 16220078 | Superoxide dismutase and catalase activity were either unchanged or significantly increased during the early stage of diabetes whereas during the medium and late stage were significantly reduced. |
| 1393 | 16220078 | Though curcumin treatment had no significant effect on superoxide dismutase, catalase, and reduced glutathione levels, it significantly reduced lipid peroxidation compared with diabetic control. |
| 1394 | 16220078 | Superoxide dismutase and catalase activity were either unchanged or significantly increased during the early stage of diabetes whereas during the medium and late stage were significantly reduced. |
| 1395 | 16220078 | Though curcumin treatment had no significant effect on superoxide dismutase, catalase, and reduced glutathione levels, it significantly reduced lipid peroxidation compared with diabetic control. |
| 1396 | 16227644 | Intraperitoneal administration of (-)-epicatechin at doses of 15 and 30 mg/kg to diabetic rats for a period of 35 days resulted in a significant decrease in blood glucose, thiobarbituric acid reactive substances and hydroperoxides and a significant increase in the concentration of glutathione and the activities of catalase, superoxide dismutase and glutathione peroxidase. (-)-Epicatechin at a dose of 30 mg/kg was found to be more effective. |
| 1397 | 16258183 | Molecular targets sensitive to the exercise training effect include the endothelial nitric oxide synthase and the antioxidant enzyme superoxide dismutase. |
| 1398 | 16258735 | We have determined the levels of lipid peroxidation expressed as thiobarbituric acid-reactive substances (TBARS), oxidative protein damage as indicated by protein carbonyl (PCO) content and activities of antioxidant enzymes including superoxide dismutase (SOD), catalase (CAT) and glutathione peroxidase (GSHPx) in all patient groups and healthy subjects. |
| 1399 | 16258735 | We found enhanced oxidative stress in all patient groups due to an increase in lipid peroxidation (TBARS) and increased oxidative protein damage in terms of PCO content and reduced activities of SOD, CAT and GSH-Px. |
| 1400 | 16258735 | We have determined the levels of lipid peroxidation expressed as thiobarbituric acid-reactive substances (TBARS), oxidative protein damage as indicated by protein carbonyl (PCO) content and activities of antioxidant enzymes including superoxide dismutase (SOD), catalase (CAT) and glutathione peroxidase (GSHPx) in all patient groups and healthy subjects. |
| 1401 | 16258735 | We found enhanced oxidative stress in all patient groups due to an increase in lipid peroxidation (TBARS) and increased oxidative protein damage in terms of PCO content and reduced activities of SOD, CAT and GSH-Px. |
| 1402 | 16260406 | Oral administration of the ethanolic extract showed significant (p < 0.001) blood glucose lowering effect at 200 mg/kg in alloxan induced diabetic rats (120 mg/kg, i.p.) and the extract was also found to significantly (p < 0.001) scavenge oxygen free radicals, viz., superoxide dismutase (SOD), catalase (CAT) and also protein, malondialdehyde and ascorbic acid in vivo. |
| 1403 | 16286809 | The levels of the renal oxidative stress markers malonaldehyde and glutathione and the antioxidant enzymes superoxide dismutase and catalase were measured in kidney homogenate. |
| 1404 | 16298858 | The activities of the antioxidant enzymes SOD and catalase were decreased in the maternal placental side, catalase activity was enhanced in the fetal placental side and both enzymes were increased in the fetuses from diabetic rats when compared to controls. |
| 1405 | 16320166 | In the present study, antioxidant enzyme activities (SOD, CAT, GSH-Px) and free sialic acid (FSA) levels in saliva were determined before and after training in the elite Turkish judoists (ETJ). |
| 1406 | 16321378 | Puerarin was also found to inhibit the free radicals production induced by H(2)O(2) and to increase catalase and superoxide dismutase (SOD) activities in the isolated pancreatic islets. |
| 1407 | 16342016 | Control of excessive ROS-formation can be obtained by angiotensin converting enzyme (ACE-) inhibitors, by AT (1)-receptor blockers, by statins and other lipid lowering compounds, by improved expression of antioxidative enzymes (superoxide dismutase, catalase etc.), by compounds such as probucol, certain vitamins, pyruvate, by lipid apheresis and by physical exercise training, which displays surprising efficacy. |
| 1408 | 16373499 | Xanthine/xanthine oxidase generated superoxide was reduced by superoxide dismutase or inositols, with db-DCI efficacious in a mechanism requiring chelated Fe(3+). |
| 1409 | 16386542 | Data were collected on oxidative parameters: malondialdehyde (MDA), glutathione peroxidase (GPx), catalase, superoxide dismutase (SOD), glutathione reductase (GR), and lipid profile. |
| 1410 | 16388100 | Effect of coenzyme Q10 on catalase activity and other antioxidant parameters in streptozotocin-induced diabetic rats. |
| 1411 | 16388100 | CoQ10 treatment also reduced lipid peroxidation and increased antioxidant parameters like superoxide dismutase, catalase, and glutathione in the liver homogenates of diabetic rats. |
| 1412 | 16391545 | Adenoviral-mediated intracavernosal transfer of therapeutic genes, such as endothelial nitric oxide synthase (eNOS), calcitonin gene-related peptide (CGRP), superoxide dismutase (SOD), and RhoA/Rho kinase and mesenchymal stem cell-based cell and gene therapy strategy for the treatment of age- and diabetes-related ED are the focus of this review. |
| 1413 | 16404941 | To evaluate LP processes, serum levels of the secondary LP product, malonic dialdehyde, and two antioxidative enzymes, superoxide dismutase and catalase, were measured. |
| 1414 | 16412660 | Effect of tempol on altered angiotensin II and acetylcholine-mediated vascular responses in thoracic aorta isolated from rats with insulin resistance. |
| 1415 | 16412660 | In this regard, the effect of tempol (a membrane permeable superoxide dismutase mimetic/free radical scavenger) on the enhanced Ang II-induced contraction and impaired-ACh mediated relaxation in thoracic aorta of rats with insulin resistance was studied. |
| 1416 | 16412660 | Ang II-induced contraction and ACh-mediated relaxation responses were recorded isometrically in endothelium intact and denuded thoracic aortic ring preparations isolated from male Sprague-Dawley rats which were fed with either normal pellet diet (NPD) (control group) or high fat diet (HFD) (insulin resistant group) for 4 weeks. |
| 1417 | 16412660 | In conclusion, our results indicate that superoxide radicals play crucial role in enhanced contractile and impaired vasodilatory responses to Ang II and ACh, respectively, in thoracic aortic rings isolated from diet-induced insulin resistant rats. |
| 1418 | 16428080 | Immunohistochemistry for ED-1 macrophages marker, intercellular adhesion molecule-1 (ICAM-1) and monocyte chemoattractant protein-1 (MCP-1) was performed. |
| 1419 | 16428080 | Activity of AOE such as glutathione peroxidase (GSH-PX) was markedly elevated while superoxide dismutase (SOD) and catalase (CAT) were not changed by MMF treatment. |
| 1420 | 16428080 | In diabetic animals receiving no treatment, there were increases in ED-1-positive cells, ICAM-1 expression and MCP-1 expression in glomeruli and tubulointerstitium, which were effectively suppressed by MMF treatment. |
| 1421 | 16428080 | Our data suggest that MMF treatment ameliorates early renal injury via the inhibition of oxidative stress and overexpression of ICAM-1, MCP-1 and TGF-beta1 in renal tissue in diabetic rats. |
| 1422 | 16445706 | Superoxide dismutase (SOD), xanthine oxidase (XO) and glutathione peroxidase (GSH-Px) activities were determined to evaluate changes in the anti-oxidant status of kidney tissue. 3. |
| 1423 | 16445706 | Therefore, on the basis of these data, we suggest that urinary NAG, albumin excretion, XO activity and MDA levels are more valuable parameters showing the degree of renal tubular injury than classical markers of oxidative stress, including SOD and GSH-Px, in diabetic rat kidneys. |
| 1424 | 16445706 | Superoxide dismutase (SOD), xanthine oxidase (XO) and glutathione peroxidase (GSH-Px) activities were determined to evaluate changes in the anti-oxidant status of kidney tissue. 3. |
| 1425 | 16445706 | Therefore, on the basis of these data, we suggest that urinary NAG, albumin excretion, XO activity and MDA levels are more valuable parameters showing the degree of renal tubular injury than classical markers of oxidative stress, including SOD and GSH-Px, in diabetic rat kidneys. |
| 1426 | 16459485 | Decreased concentration of reduced glutathione (GSH) and decreased activities of superoxide dismutase (SOD), catalase and glutathione peroxidase (GPx) were also observed in these tissues of diabetic rats. |
| 1427 | 16459485 | Oral administration of aqueous E. littorale whole plant extract (1 and 2 g/kg) to diabetic rats daily for 45 days significantly decreased blood glucose, TBARS, HP and increased GSH, SOD, catalase and GPx. |
| 1428 | 16459485 | Decreased concentration of reduced glutathione (GSH) and decreased activities of superoxide dismutase (SOD), catalase and glutathione peroxidase (GPx) were also observed in these tissues of diabetic rats. |
| 1429 | 16459485 | Oral administration of aqueous E. littorale whole plant extract (1 and 2 g/kg) to diabetic rats daily for 45 days significantly decreased blood glucose, TBARS, HP and increased GSH, SOD, catalase and GPx. |
| 1430 | 16464311 | The diabetic rats had elevated levels of blood glucose and lipid peroxidation markers such as thiobarbituric acid reactive substances (TBARS), conjugated dienes (CD), and lipid hydroperoxide (HP) and decreased levels of nonenzymatic antioxidants (Vitamin C and reduced glutathione [GSH]), elevated levels of vitamin E, and elevated levels of enzymatic antioxidants (superoxide dismutase [SOD], catalase [CAT], glutathione peroxidase [GPx]), elevated glucose-6-phosphate dehydrogenase activity, and altered lipid profile (cholesterol and phospholipids) in erythrocytes. |
| 1431 | 16464472 | Diabetic rats had an elevation in the levels of lipid peroxidation markers (thiobarbituric acid reactive substances (TBARS), lipid hydroperoxides (HP) and conjugated dienes (CD)), and a reduction in nonenzymic antioxidants (vitamin C and reduced glutathione (GSH) except vitamin E in the plasma and liver, and enzymic antioxidants (superoxide dismutase (SOD), catalase (CAT) and glutathione peroxidase (GPx) in the liver. |
| 1432 | 16484570 | AGE scavenges oxidants, increases superoxide dismutase, catalase, glutathione peroxidase, and glutathione levels, and inhibits lipid peroxidation and inflammatory prostaglandins. |
| 1433 | 16508175 | The superoxide dismutase (SOD), catalase, and glutathione-peroxidase (GPx) activities, and glutathione level in the STZ-induced diabetic rats liver decreased significantly compared with those in the age-matched normal rats. |
| 1434 | 16510762 | TIM44 functions as a membrane anchor of mitochondrial heat-shock protein 70 (mtHsp70) to TIM23 complex and is involved in the import of mitochondria-targeted preproteins into mitochondrial matrix. |
| 1435 | 16510762 | Transfection with siRNA and expressing vector of TIM44 revealed that TIM44 facilitates import of antioxidative enzymes such as superoxide dismutase and glutathione peroxidase into mitochondria. |
| 1436 | 16545576 | Lipid peroxidation was significantly enhanced while the superoxide dismutase (SOD) and catalase activity was significantly lower in aorta of diabetic rats as compared to control rats. |
| 1437 | 16545576 | The enhanced systolic pressure, lipid peroxidation and the reduced SOD and catalase activity were restored to control values following 2 weeks edaravone treatment. |
| 1438 | 16545576 | Lipid peroxidation was significantly enhanced while the superoxide dismutase (SOD) and catalase activity was significantly lower in aorta of diabetic rats as compared to control rats. |
| 1439 | 16545576 | The enhanced systolic pressure, lipid peroxidation and the reduced SOD and catalase activity were restored to control values following 2 weeks edaravone treatment. |
| 1440 | 16572112 | Transforming growth factor (TGF)-beta1, fibronectin expression, Ras, ERK, p38, and c-Jun activation of glomerular mesangial cells or urinary albumin secretion were assessed. |
| 1441 | 16572112 | High glucose and AGEs rapidly enhanced Ras activation and progressively increased cytosolic ERK and nuclear c-Jun activation. |
| 1442 | 16572112 | SOD or PD98059 pretreatment reduced high-glucose and AGE promotion of ERK and c-Jun activation. |
| 1443 | 16572112 | Exogenous SOD treatment in diabetic rats significantly attenuated diabetes induction of superoxide, urinary albumin excretion, 8-hydroxy-2'-deoxyguanosine, TGF-beta1, and fibronectin immunoreactivities in renal glomerular mesangial cells. |
| 1444 | 16572112 | Transforming growth factor (TGF)-beta1, fibronectin expression, Ras, ERK, p38, and c-Jun activation of glomerular mesangial cells or urinary albumin secretion were assessed. |
| 1445 | 16572112 | High glucose and AGEs rapidly enhanced Ras activation and progressively increased cytosolic ERK and nuclear c-Jun activation. |
| 1446 | 16572112 | SOD or PD98059 pretreatment reduced high-glucose and AGE promotion of ERK and c-Jun activation. |
| 1447 | 16572112 | Exogenous SOD treatment in diabetic rats significantly attenuated diabetes induction of superoxide, urinary albumin excretion, 8-hydroxy-2'-deoxyguanosine, TGF-beta1, and fibronectin immunoreactivities in renal glomerular mesangial cells. |
| 1448 | 16581090 | Antioxidant enzyme (superoxide dismutase and catalase) levels were reduced and malondialdehyde (MDA) levels were significantly increased in diabetic rats as compared to the age-matched control rats, this indicates the involvement of oxidative stress in diabetic neuropathy. |
| 1449 | 16629371 | Both CRS or NIDDM as such enhanced gastric mucosal LPO, NO and SOD, but decreased CAT levels while CRS plus NIDDM rats caused further increase in LPO and NO level without causing any further changes in SOD and CAT level. |
| 1450 | 16644902 | The plasma insulin, C-peptide, and leptin levels in caffeic acid group were significantly higher than those of the control group, whereas the plasma glucagon level was lower. |
| 1451 | 16644902 | Caffeic acid also markedly increased glucokinase activity and its mRNA expression and glycogen content and simultaneously lowered glucose-6-phosphatase and phosphoenolpyruvate carboxykinase activities and their respective mRNA expressions, accompanied by a reduction in the glucose transporter 2 expression in the liver. |
| 1452 | 16644902 | In contrast to the hepatic glucose transporter 2, adipocyte glucose transporter 4 expression was greater than the control group. |
| 1453 | 16644902 | In addition, caffeic acid significantly increased superoxide dismutase, catalase, and glutathione peroxidase activities and their respective mRNA levels, while lowering the hydrogen peroxide and thiobarbituric acid reactive substances levels in the erythrocyte and liver of db/db mice. |
| 1454 | 16644902 | These results indicate that caffeic acid exhibits a significant potential as an antidiabetic agent by suppressing a progression of type 2 diabetic states that is suggested by an attenuation of hepatic glucose output and enhancement of adipocyte glucose uptake, insulin secretion, and antioxidant capacity. |
| 1455 | 16648296 | The role of circulating IGF-I in skeletal acquisition and the anabolic response to PTH is not well understood. |
| 1456 | 16648296 | We generated IGF-I-deficient mice by gene deletions of IGF ternary complex components including: (1) liver-specific deletion of the IGF-I gene (LID), (2) global deletion of the acid-labile (ALS) gene (ALSKO), and (3) both liver IGF-I and ALS inactivated genes (LA). |
| 1457 | 16648296 | In conclusion, we demonstrated that the presentation of IGF-I as a circulating complex is essential for skeletal remodeling and the anabolic response to PTH. |
| 1458 | 16674981 | The results showed that AGE-BSA could induce significantly the apoptosis of BRPs in a dose-dependent manner compared with controls, associated with an increase in intracellular malondialdehyde level and caspase-3 activity; a decrease in intracellular catalase, SOD activities and Bcl-2/Bax ratio. |
| 1459 | 16674981 | The decreased Bcl-2/Bax ratio and activation of caspase-3 are associated with apoptotic process. |
| 1460 | 16682518 | Catalase, glutathione peroxidase (GPX), and superoxide dismutase (SOD) are some of the antioxidant enzymes that protect the body from oxidative damage. |
| 1461 | 16682518 | The present study investigates the activities of erythrocyte catalase, GPX, and SOD with respect to senile cataract (non-diabetic cataract) and osmotic cataract (diabetic cataract) in a Sri Lankan population. |
| 1462 | 16682518 | Erythrocyte catalase, GPX, and SOD activities were assayed and the data were analysed by t-test (p <0.05 for significance). |
| 1463 | 16682518 | In the non-diabetic group, significantly low levels of catalase, GPX, and SOD activities were associated with cataract when compared with non-cataract. |
| 1464 | 16682518 | No significant changes in catalase, GPX, and SOD activities were observed in the diabetic group between cataract and non-cataract. |
| 1465 | 16682518 | Senile cataract (non-diabetic cataract) was associated with significantly low levels of erythrocyte catalase, GPX, and SOD when compared with osmotic cataract (diabetic cataract). |
| 1466 | 16682518 | Positive correlations were observed between catalase and SOD (r = 0.75), catalase and GPX (r = 0.63), and SOD and GPX (r = 0.59) in subjects with senile cataracts. |
| 1467 | 16682518 | Catalase, glutathione peroxidase (GPX), and superoxide dismutase (SOD) are some of the antioxidant enzymes that protect the body from oxidative damage. |
| 1468 | 16682518 | The present study investigates the activities of erythrocyte catalase, GPX, and SOD with respect to senile cataract (non-diabetic cataract) and osmotic cataract (diabetic cataract) in a Sri Lankan population. |
| 1469 | 16682518 | Erythrocyte catalase, GPX, and SOD activities were assayed and the data were analysed by t-test (p <0.05 for significance). |
| 1470 | 16682518 | In the non-diabetic group, significantly low levels of catalase, GPX, and SOD activities were associated with cataract when compared with non-cataract. |
| 1471 | 16682518 | No significant changes in catalase, GPX, and SOD activities were observed in the diabetic group between cataract and non-cataract. |
| 1472 | 16682518 | Senile cataract (non-diabetic cataract) was associated with significantly low levels of erythrocyte catalase, GPX, and SOD when compared with osmotic cataract (diabetic cataract). |
| 1473 | 16682518 | Positive correlations were observed between catalase and SOD (r = 0.75), catalase and GPX (r = 0.63), and SOD and GPX (r = 0.59) in subjects with senile cataracts. |
| 1474 | 16682518 | Catalase, glutathione peroxidase (GPX), and superoxide dismutase (SOD) are some of the antioxidant enzymes that protect the body from oxidative damage. |
| 1475 | 16682518 | The present study investigates the activities of erythrocyte catalase, GPX, and SOD with respect to senile cataract (non-diabetic cataract) and osmotic cataract (diabetic cataract) in a Sri Lankan population. |
| 1476 | 16682518 | Erythrocyte catalase, GPX, and SOD activities were assayed and the data were analysed by t-test (p <0.05 for significance). |
| 1477 | 16682518 | In the non-diabetic group, significantly low levels of catalase, GPX, and SOD activities were associated with cataract when compared with non-cataract. |
| 1478 | 16682518 | No significant changes in catalase, GPX, and SOD activities were observed in the diabetic group between cataract and non-cataract. |
| 1479 | 16682518 | Senile cataract (non-diabetic cataract) was associated with significantly low levels of erythrocyte catalase, GPX, and SOD when compared with osmotic cataract (diabetic cataract). |
| 1480 | 16682518 | Positive correlations were observed between catalase and SOD (r = 0.75), catalase and GPX (r = 0.63), and SOD and GPX (r = 0.59) in subjects with senile cataracts. |
| 1481 | 16682518 | Catalase, glutathione peroxidase (GPX), and superoxide dismutase (SOD) are some of the antioxidant enzymes that protect the body from oxidative damage. |
| 1482 | 16682518 | The present study investigates the activities of erythrocyte catalase, GPX, and SOD with respect to senile cataract (non-diabetic cataract) and osmotic cataract (diabetic cataract) in a Sri Lankan population. |
| 1483 | 16682518 | Erythrocyte catalase, GPX, and SOD activities were assayed and the data were analysed by t-test (p <0.05 for significance). |
| 1484 | 16682518 | In the non-diabetic group, significantly low levels of catalase, GPX, and SOD activities were associated with cataract when compared with non-cataract. |
| 1485 | 16682518 | No significant changes in catalase, GPX, and SOD activities were observed in the diabetic group between cataract and non-cataract. |
| 1486 | 16682518 | Senile cataract (non-diabetic cataract) was associated with significantly low levels of erythrocyte catalase, GPX, and SOD when compared with osmotic cataract (diabetic cataract). |
| 1487 | 16682518 | Positive correlations were observed between catalase and SOD (r = 0.75), catalase and GPX (r = 0.63), and SOD and GPX (r = 0.59) in subjects with senile cataracts. |
| 1488 | 16682518 | Catalase, glutathione peroxidase (GPX), and superoxide dismutase (SOD) are some of the antioxidant enzymes that protect the body from oxidative damage. |
| 1489 | 16682518 | The present study investigates the activities of erythrocyte catalase, GPX, and SOD with respect to senile cataract (non-diabetic cataract) and osmotic cataract (diabetic cataract) in a Sri Lankan population. |
| 1490 | 16682518 | Erythrocyte catalase, GPX, and SOD activities were assayed and the data were analysed by t-test (p <0.05 for significance). |
| 1491 | 16682518 | In the non-diabetic group, significantly low levels of catalase, GPX, and SOD activities were associated with cataract when compared with non-cataract. |
| 1492 | 16682518 | No significant changes in catalase, GPX, and SOD activities were observed in the diabetic group between cataract and non-cataract. |
| 1493 | 16682518 | Senile cataract (non-diabetic cataract) was associated with significantly low levels of erythrocyte catalase, GPX, and SOD when compared with osmotic cataract (diabetic cataract). |
| 1494 | 16682518 | Positive correlations were observed between catalase and SOD (r = 0.75), catalase and GPX (r = 0.63), and SOD and GPX (r = 0.59) in subjects with senile cataracts. |
| 1495 | 16682518 | Catalase, glutathione peroxidase (GPX), and superoxide dismutase (SOD) are some of the antioxidant enzymes that protect the body from oxidative damage. |
| 1496 | 16682518 | The present study investigates the activities of erythrocyte catalase, GPX, and SOD with respect to senile cataract (non-diabetic cataract) and osmotic cataract (diabetic cataract) in a Sri Lankan population. |
| 1497 | 16682518 | Erythrocyte catalase, GPX, and SOD activities were assayed and the data were analysed by t-test (p <0.05 for significance). |
| 1498 | 16682518 | In the non-diabetic group, significantly low levels of catalase, GPX, and SOD activities were associated with cataract when compared with non-cataract. |
| 1499 | 16682518 | No significant changes in catalase, GPX, and SOD activities were observed in the diabetic group between cataract and non-cataract. |
| 1500 | 16682518 | Senile cataract (non-diabetic cataract) was associated with significantly low levels of erythrocyte catalase, GPX, and SOD when compared with osmotic cataract (diabetic cataract). |
| 1501 | 16682518 | Positive correlations were observed between catalase and SOD (r = 0.75), catalase and GPX (r = 0.63), and SOD and GPX (r = 0.59) in subjects with senile cataracts. |
| 1502 | 16682518 | Catalase, glutathione peroxidase (GPX), and superoxide dismutase (SOD) are some of the antioxidant enzymes that protect the body from oxidative damage. |
| 1503 | 16682518 | The present study investigates the activities of erythrocyte catalase, GPX, and SOD with respect to senile cataract (non-diabetic cataract) and osmotic cataract (diabetic cataract) in a Sri Lankan population. |
| 1504 | 16682518 | Erythrocyte catalase, GPX, and SOD activities were assayed and the data were analysed by t-test (p <0.05 for significance). |
| 1505 | 16682518 | In the non-diabetic group, significantly low levels of catalase, GPX, and SOD activities were associated with cataract when compared with non-cataract. |
| 1506 | 16682518 | No significant changes in catalase, GPX, and SOD activities were observed in the diabetic group between cataract and non-cataract. |
| 1507 | 16682518 | Senile cataract (non-diabetic cataract) was associated with significantly low levels of erythrocyte catalase, GPX, and SOD when compared with osmotic cataract (diabetic cataract). |
| 1508 | 16682518 | Positive correlations were observed between catalase and SOD (r = 0.75), catalase and GPX (r = 0.63), and SOD and GPX (r = 0.59) in subjects with senile cataracts. |
| 1509 | 16682803 | The parameters studied were the mesenteric arteriolar reactivity (intravital microscopy), nitric oxide synthase (NOS) activity (conversion of L-arginine to L-citrulline), eNOS gene expression (RT-PCR), NO production (diaminofluorescein), reactive oxygen species (ROS) generation (intravital fluorescence microscopy) and Cu/Zn superoxide dismutase (SOD) activity (spectrophotometry) and gene expression (RT-PCR). |
| 1510 | 16682803 | NOS activity was decreased by diabetes, but insulin did not correct it. |
| 1511 | 16682803 | However, insulin increased SOD activity but not its expression. |
| 1512 | 16682803 | In contrast to males, however, insulin does not regulate NOS in the microcirculation of diabetic females. |
| 1513 | 16682803 | The parameters studied were the mesenteric arteriolar reactivity (intravital microscopy), nitric oxide synthase (NOS) activity (conversion of L-arginine to L-citrulline), eNOS gene expression (RT-PCR), NO production (diaminofluorescein), reactive oxygen species (ROS) generation (intravital fluorescence microscopy) and Cu/Zn superoxide dismutase (SOD) activity (spectrophotometry) and gene expression (RT-PCR). |
| 1514 | 16682803 | NOS activity was decreased by diabetes, but insulin did not correct it. |
| 1515 | 16682803 | However, insulin increased SOD activity but not its expression. |
| 1516 | 16682803 | In contrast to males, however, insulin does not regulate NOS in the microcirculation of diabetic females. |
| 1517 | 16766854 | In the presence of high glucose and H2O2, the total antioxidative capability, catalase, reduced glutathione, and superoxide dismutase level of rat mesangial cells were significantly decreased, and transforming growth factor beta1 (TGF-beta1) mRNA level, collagen IV, and laminin level were significantly increased. |
| 1518 | 16766854 | When compared with those in the high glucose group, these 4 indexes of cells incubated in 2.0 and/or 20 micromol/L of AS I were significantly enhanced, and levels of TGF-beta1 mRNA, collagen IV and laminin were statistically decreased. |
| 1519 | 16772327 | Moreover, change in area under the curve of cGMP (second messenger of nitric oxide; P < 0.001), superoxide dismutase (index of antioxidant capacity; P < 0.01), and adiponectin levels (P < 0.02) increased, whereas basal endothelin-1 levels (P < 0.01) and leptin-to-adiponectin ratio (P < 0.05) decreased in the L-arginine group. |
| 1520 | 16780994 | After small and large dosage (1 or 10mg/kg/d) carvedilol-administrated for 5 weeks, hemodynamic parameters, the levels of malondialdehyde (MDA), the activities of superoxide dismutase (SOD), catalase (CAT), glutathione peroxidase (GSH-Px) and expression of Bcl-2 mRNA in the cardiac tissues of all six groups were measured. |
| 1521 | 16786186 | A significant (p < 0.05) increase in the levels of fasting plasma glucose, lipid peroxidative products (thiobarbituric acid reactive substances [TBARS] and lipid hydroperoxides [HP]) and a significant (p < 0.05) decrease in plasma insulin, enzymic antioxidants (superoxide dismutase [SOD], catalase, glutathione peroxidase [GPx] and glutathione reductase [GRx]) and nonenzymic antioxidants (reduced glutathione [GSH], vitamin C and E) in diabetic liver, kidney and brain were observed. |
| 1522 | 16790290 | Several antioxidants like SOD, CAT, epigallocatechin-3-O-gallate, lycopene, ellagic acid, coenzyme Q10, indole-3-carbinol, genistein, quercetin, vitamin C and vitamin E have been found to be pharmacologically active as prophylactic and therapeutic agents for above mentioned diseases. |
| 1523 | 16806281 | In addition, THC caused significant increase in the activities of superoxide dismutase, catalase, glutathione peroxidase, glutathione-S-transferase, reduced glutathione, vitamin C and vitamin E in liver and kidney of diabetic rats with significant decrease in thiobarbituric acid reactive substances (TBARS) and hydroperoxides formation in liver and kidney, suggesting its role in protection against lipid peroxidation induced membrane damage. |
| 1524 | 16831449 | Hepatic superoxide dismutase, catalase, and glutathione peroxidase activities of the STZ-induced diabetic rats were significantly decreased in comparison with the control rats. |
| 1525 | 16859669 | Manganese-containing superoxide dismutase (Mn-SOD) plays a critical role in guarding against mitochondrial oxidative stress. |
| 1526 | 16860299 | In aorta and heart of diabetic rats there was a significant increase in the activity of superoxide dismutase, catalase and glutathione peroxidase with an increase in lipid peroxides. |
| 1527 | 16862607 | In other experiments with polyamine-deficient cells containing plasmids that overexpress superoxide dismutases (SOD1, SOD2), ROS decreased but with only a partial protection against cell death. |
| 1528 | 16873692 | Furthermore, the refed rats show, in both SS and IMF muscle mitochondria, a lower aconitase activity (whose inactivation is an index of increased reactive oxygen species [ROS]), associated with higher superoxide dismutase activity and increased proton leak. |
| 1529 | 16895803 | The diabetogenic agent alloxan is selectively accumulated in insulin-producing cells through uptake via the GLUT2 glucose transporter in the plasma membrane. |
| 1530 | 16895803 | Thus, while superoxide dismutase (SOD) only reduced the toxicity, catalase, in particular in the presence of SOD, provided complete protection of insulin-producing cells against the cytotoxic action of alloxan and dialuric acid due to H(2)O(2) destruction and the prevention of hydroxyl radical ((*)OH) formation, indicating that it is the hydroxyl radical ((*)OH) which is the ROS ultimately responsible for cell death. |
| 1531 | 16910316 | Plasma glucose, plasma insulin, thiobarbituricacid reactive substances (TBARS), hydroperoxides, superoxide dismutase (SOD), catalase (CAT), glutathione peroxide (Gpx), reduced glutathione (GSH), glutathione-S-transferase (GST), and vitamins C and E were assayed in liver and kidney. |
| 1532 | 16910316 | In addition, the treated groups also showed a significant increase in the activities of plasma insulin, SOD, CAT, GPx, GST, GSH, vitamin C, and vitamin E in liver and kidney of STZ-nicotinamide-induced diabetic rats. |
| 1533 | 16910316 | Plasma glucose, plasma insulin, thiobarbituricacid reactive substances (TBARS), hydroperoxides, superoxide dismutase (SOD), catalase (CAT), glutathione peroxide (Gpx), reduced glutathione (GSH), glutathione-S-transferase (GST), and vitamins C and E were assayed in liver and kidney. |
| 1534 | 16910316 | In addition, the treated groups also showed a significant increase in the activities of plasma insulin, SOD, CAT, GPx, GST, GSH, vitamin C, and vitamin E in liver and kidney of STZ-nicotinamide-induced diabetic rats. |
| 1535 | 16931797 | HG enhanced superoxide dismutase and suppressed catalase (CAT) expression in HEK293 cells, leading to a significant increase in intracellular ROS. |
| 1536 | 16931797 | The effects of HG were mimicked by hydrogen peroxide (H(2)O(2)), and hSlo functions were restored by CAT gene transfer. |
| 1537 | 16948477 | Several mitochondrial parameters were evaluated: respiratory indexes (state 3 and 4 of respiration, respiratory control and ADP/O ratios), transmembrane potential, depolarization and repolarization levels, ATP, glutathione and coenzyme Q contents, production of hydrogen peroxide, superoxide dismutase, glutathione peroxidase and glutathione reductase activities and the ability of mitochondria to accumulate calcium. |
| 1538 | 16971752 | This study was designed to examine the effects of Cinnamomi cassiae and Rhodiola rosea extracts on blood glucose, lipid peroxidation, the level of reduced glutathione and its related enzymes (glutathione reductase, glutathione S-transferase), and the activity of the antioxidant enzymes (catalase, superoxide dismutase and glutathione peroxidase) in the liver of db/db mice. |
| 1539 | 16971752 | These type II diabetic mice were used to investigate the effects of Cinnamomi cassiae and Rhodiola rosea on blood glucose, reduced glutathione, glutathione reductase, glutathione S-transferase, glutathione peroxidase, lipid peroxidation, catalase and superoxide dismutase. |
| 1540 | 16971752 | Cinnamomi cassiae and Rhodiola rosea extracts significantly decreased on blood glucose, increased levels of reduced glutathione and the activities of glutathione reductase, glutathione S-transferase, glutathione peroxidase, catalase and superoxide dismutase in the liver. |
| 1541 | 16971752 | This study was designed to examine the effects of Cinnamomi cassiae and Rhodiola rosea extracts on blood glucose, lipid peroxidation, the level of reduced glutathione and its related enzymes (glutathione reductase, glutathione S-transferase), and the activity of the antioxidant enzymes (catalase, superoxide dismutase and glutathione peroxidase) in the liver of db/db mice. |
| 1542 | 16971752 | These type II diabetic mice were used to investigate the effects of Cinnamomi cassiae and Rhodiola rosea on blood glucose, reduced glutathione, glutathione reductase, glutathione S-transferase, glutathione peroxidase, lipid peroxidation, catalase and superoxide dismutase. |
| 1543 | 16971752 | Cinnamomi cassiae and Rhodiola rosea extracts significantly decreased on blood glucose, increased levels of reduced glutathione and the activities of glutathione reductase, glutathione S-transferase, glutathione peroxidase, catalase and superoxide dismutase in the liver. |
| 1544 | 16971752 | This study was designed to examine the effects of Cinnamomi cassiae and Rhodiola rosea extracts on blood glucose, lipid peroxidation, the level of reduced glutathione and its related enzymes (glutathione reductase, glutathione S-transferase), and the activity of the antioxidant enzymes (catalase, superoxide dismutase and glutathione peroxidase) in the liver of db/db mice. |
| 1545 | 16971752 | These type II diabetic mice were used to investigate the effects of Cinnamomi cassiae and Rhodiola rosea on blood glucose, reduced glutathione, glutathione reductase, glutathione S-transferase, glutathione peroxidase, lipid peroxidation, catalase and superoxide dismutase. |
| 1546 | 16971752 | Cinnamomi cassiae and Rhodiola rosea extracts significantly decreased on blood glucose, increased levels of reduced glutathione and the activities of glutathione reductase, glutathione S-transferase, glutathione peroxidase, catalase and superoxide dismutase in the liver. |
| 1547 | 16999030 | Oral administration of ethanol extract of N. sativa seeds (300 mg/kg body weight/day) to streptozotocin induced diabetic rats for 30 days significantly reduced the elevated levels of blood glucose, lipids, plasma insulin and improved altered levels of lipid peroxidation products (TBARS and hydroperoxides) and antioxidant enzymes like catalase, superoxide dismutase, reduced glutathione and glutathione peroxidase in liver and kidney. |
| 1548 | 17002667 | The hsp90 inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG; 2 x 10(-7) mol/L) or the nitric oxide synthase (NOS) inhibitor Nomega-nitro-L-arginine methyl ester (1 x 10(-5) mol/L) was added to the perfusate to observe the effects of hsp90 inhibition and hsp90-associated endothelial NOS on ischaemic responses of diabetic hearts. |
| 1549 | 17002667 | Diabetic hearts also had markedly elevated HO-1 and catalase, with no significant change in superoxide dismutase. |
| 1550 | 17004907 | Blood pressure (BP), anthropometric measurements, plasma glucose, glycated hemoglobin (HbA1c), lipid profiles [total cholesterol, low-density lipoprotein cholesterol (LDL-C), and high-density lipoprotein cholesterol, and triglycerides (TG)], lipid peroxidation [thiobarbituric acid-reactive substances (TBARS)], electrolytes (sodium, potassium, and chloride), and enzymic (superoxide dismutase, glutathione peroxidase, and catalase) and nonenzymic (vitamin C, vitamin E, beta-carotene, and reduced glutathione) antioxidants were measured at baseline and after 45 days of sesame oil substitution. |
| 1551 | 17009256 | Diabetic rats fed low-carbohydrate diet had altered activities of renal glutathione reductase and superoxide dismutase, but increased renal glutathione peroxidase activity in diabetic animals was not corrected by the test diet. |
| 1552 | 17015165 | The retina experiences mitochondrial dysfunction in diabetes, superoxide levels are elevated, and mitochondrial superoxide dismutase (MnSOD) activity is decreased. |
| 1553 | 17042909 | A significant decrease in the activity of anti-oxidant enzymes (superoxide dismutase and catalase) and an increase in lipid peroxidation were observed in sciatic nerves from diabetic rats compared with age-matched control rats. |
| 1554 | 17042922 | Simultaneously, changes in lipid peroxidation (LPO), reduced glutathione (GSH) content and the activity of associated endogenous anti-oxidant enzymes, such as superoxide dismuatase (SOD) and catalase (CAT), were investigated in renal and cardiac tissues, which are commonly affected in diabetes mellitus. 3. |
| 1555 | 17042922 | Although administration of dexamethasone (1.0 mg/kg, i.m., for 22 days) caused hyperglycaemia with a parallel increase in serum insulin and tissue LPO, it decreased thyroid hormone concentrations and the activity of SOD and CAT. 4. |
| 1556 | 17042922 | When dexamethasone-induced hyperglycaemic mice were treated with acarbose (10 mg/kg per day, p.o., for 15 days), levels of thyroid hormones were increased and most of the abnormalities, including serum insulin and glucose levels, tissue LPO, SOD and CAT activity and GSH content, were reversed. 5. |
| 1557 | 17042922 | Simultaneously, changes in lipid peroxidation (LPO), reduced glutathione (GSH) content and the activity of associated endogenous anti-oxidant enzymes, such as superoxide dismuatase (SOD) and catalase (CAT), were investigated in renal and cardiac tissues, which are commonly affected in diabetes mellitus. 3. |
| 1558 | 17042922 | Although administration of dexamethasone (1.0 mg/kg, i.m., for 22 days) caused hyperglycaemia with a parallel increase in serum insulin and tissue LPO, it decreased thyroid hormone concentrations and the activity of SOD and CAT. 4. |
| 1559 | 17042922 | When dexamethasone-induced hyperglycaemic mice were treated with acarbose (10 mg/kg per day, p.o., for 15 days), levels of thyroid hormones were increased and most of the abnormalities, including serum insulin and glucose levels, tissue LPO, SOD and CAT activity and GSH content, were reversed. 5. |
| 1560 | 17042922 | Simultaneously, changes in lipid peroxidation (LPO), reduced glutathione (GSH) content and the activity of associated endogenous anti-oxidant enzymes, such as superoxide dismuatase (SOD) and catalase (CAT), were investigated in renal and cardiac tissues, which are commonly affected in diabetes mellitus. 3. |
| 1561 | 17042922 | Although administration of dexamethasone (1.0 mg/kg, i.m., for 22 days) caused hyperglycaemia with a parallel increase in serum insulin and tissue LPO, it decreased thyroid hormone concentrations and the activity of SOD and CAT. 4. |
| 1562 | 17042922 | When dexamethasone-induced hyperglycaemic mice were treated with acarbose (10 mg/kg per day, p.o., for 15 days), levels of thyroid hormones were increased and most of the abnormalities, including serum insulin and glucose levels, tissue LPO, SOD and CAT activity and GSH content, were reversed. 5. |
| 1563 | 17049946 | Superoxide dismutase (SOD) and catalase (CAT) activity was altered in all the groups. |
| 1564 | 17051732 | The extract also causes a significant (P<0.05) increase in superoxide dismutase, catalase, glutathione peroxidase, glutathione-s-transferase glutathione reductase and glucose-6-phosphate dehydrogenase, reduced glutathione, vitamin A, vitamin C, vitamin E, total sulfhydryl groups (TSH) and non protein sulfhydryl groups (NPSH) in liver and kidney of alloxan induced diabetic rats, which clearly shows, the antioxidant property of T. arjuna bark. |
| 1565 | 17065353 | Concurrent administration of polyethylene-glycolated superoxide dismutase (SOD), l-nitroarginine methyl ester, or sepiapterin not only reversed the effects of high glucose on both angiotensin II-induced relaxation and PGI(2) release but also abolished high-glucose-enhanced PGIS nitration, as well as its association with eNOS. |
| 1566 | 17065353 | Furthermore, diabetes significantly suppressed PGIS activity in parallel with increased superoxide and PGIS nitration in the aortas of diabetic C57BL6 mice but had less effect in diabetic mice either lacking eNOS or overexpressing human SOD (hSOD(+/+)), suggesting an eNOS-dependent PGIS nitration in vivo. |
| 1567 | 17065353 | We conclude that diabetes increases PGIS nitration in vivo, likely via dysfunctional eNOS. |
| 1568 | 17065353 | Concurrent administration of polyethylene-glycolated superoxide dismutase (SOD), l-nitroarginine methyl ester, or sepiapterin not only reversed the effects of high glucose on both angiotensin II-induced relaxation and PGI(2) release but also abolished high-glucose-enhanced PGIS nitration, as well as its association with eNOS. |
| 1569 | 17065353 | Furthermore, diabetes significantly suppressed PGIS activity in parallel with increased superoxide and PGIS nitration in the aortas of diabetic C57BL6 mice but had less effect in diabetic mice either lacking eNOS or overexpressing human SOD (hSOD(+/+)), suggesting an eNOS-dependent PGIS nitration in vivo. |
| 1570 | 17065353 | We conclude that diabetes increases PGIS nitration in vivo, likely via dysfunctional eNOS. |
| 1571 | 17066087 | Antioxidant enzymatic activity of Cu/Zn extracellular-superoxide dismutase (SOD) and catalase (CAT) was measured in plasma and glutathione peroxidase 1 in hemolysed erythrocytes. |
| 1572 | 17066087 | In mononuclear cells, total-SOD activity, CAT and glutathione peroxidase 1, were assessed as well. |
| 1573 | 17068205 | Blood glucose, hemoglobin A1c, plasma levels of free fatty acid, triacylglycerol, and plasminogen activator inhibitor-1 in OLETF rats were significantly higher than those in nondiabetic control [Long-Evans Tokushima Otsuka (LETO)] rats at 29 weeks. |
| 1574 | 17068205 | A fibrogenic growth factor, transforming growth factor (TGF)-beta1 in the coronary vessels, endothelial nitric-oxide synthase, and aortic nitrotyrosine were increased in OLETF rats at 42 weeks. |
| 1575 | 17068205 | In contrast, an index of the NO-cGMP pathway, phosphorylated vasodilator-stimulated phosphoprotein, and superoxide dismutase activity in the aorta were significantly diminished. |
| 1576 | 17077515 | MEHZ significantly decreased thiobarbituric acid reactive substances and significantly increased reduced glutathione, superoxide dismutase and catalase in streptozotocin-induced diabetic rats at the end of 14 d of treatment. |
| 1577 | 17085829 | Ethanol, nicotine, or concurrent intake significantly increases lipid peroxidation in liver, and decreased superoxide dismutase activity and increased catalase activity in the kidney. |
| 1578 | 17101252 | In this study we aimed to evaluate the in vivo effects of myrtle oil (myrtii oleum) on the antioxidant enzymes such as superoxide dismutase and catalase, the levels of malondialdehyde in liver tissues as an index of lipid peroxidation and nitrite-nitrate levels in normoglycaemic and alloxan-induced diabetic and MO-treated rabbits. |
| 1579 | 17101252 | Although the levels of superoxide dismutase and catalase enzyme activities did not change during acute studies in diabetes + MO group, there was a significant change at the end of 21 days. |
| 1580 | 17101252 | In this study we aimed to evaluate the in vivo effects of myrtle oil (myrtii oleum) on the antioxidant enzymes such as superoxide dismutase and catalase, the levels of malondialdehyde in liver tissues as an index of lipid peroxidation and nitrite-nitrate levels in normoglycaemic and alloxan-induced diabetic and MO-treated rabbits. |
| 1581 | 17101252 | Although the levels of superoxide dismutase and catalase enzyme activities did not change during acute studies in diabetes + MO group, there was a significant change at the end of 21 days. |
| 1582 | 17109651 | During diabetes progression, we determined glycaemia and antioxidant status, by measuring vitamin C levels and activities of superoxide dismutase (SOD), glutathione peroxidase (GSH-Px) and glutathione reductase (GSSG-Red). |
| 1583 | 17122189 | Metabolic parameters, free 15-F(2t)-isoprostane level, protein expression of NADPH oxidase, superoxide dismutase (SOD), heme oxygenase (HO-1), interleukin-6 (IL-6), and cyclooxygenase-2 (COX-2) were analyzed in control and streptozotocin-induced diabetic rats treated with or without NAC in drinking water for 8 wk. |
| 1584 | 17122189 | The cardiac protein expression of p67(phox) and p22(phox) was increased in diabetic rats, accompanied by increased NADPH-dependent superoxide production. |
| 1585 | 17122189 | As a compensatory response to the increased NADPH oxidase, the protein expression of Cu-Zn-SOD and HO-1 and the total SOD activity were also increased in diabetic rat hearts. |
| 1586 | 17122189 | Cardiac inflammatory markers IL-6 and COX-2 were also increased in diabetic rats. |
| 1587 | 17122189 | NAC treatment prevented the increased expression of p22(phox) and translocation of p67(phox) to the membrane in diabetic rat hearts. |
| 1588 | 17122189 | Subsequently, the levels of cardiac free 15-F(2t)-isoprostane, HO-1, Cu-Zn-SOD, total SOD, IL-6, and COX-2 in diabetic rats were decreased by NAC. |
| 1589 | 17122189 | The protective effects of NAC on diabetic rat hearts may be attributable to its protection of hearts against oxidative damage induced by the increased NADPH oxidase and to its reduction in cardiac inflammatory mediators IL-6 and COX-2. |
| 1590 | 17122189 | Metabolic parameters, free 15-F(2t)-isoprostane level, protein expression of NADPH oxidase, superoxide dismutase (SOD), heme oxygenase (HO-1), interleukin-6 (IL-6), and cyclooxygenase-2 (COX-2) were analyzed in control and streptozotocin-induced diabetic rats treated with or without NAC in drinking water for 8 wk. |
| 1591 | 17122189 | The cardiac protein expression of p67(phox) and p22(phox) was increased in diabetic rats, accompanied by increased NADPH-dependent superoxide production. |
| 1592 | 17122189 | As a compensatory response to the increased NADPH oxidase, the protein expression of Cu-Zn-SOD and HO-1 and the total SOD activity were also increased in diabetic rat hearts. |
| 1593 | 17122189 | Cardiac inflammatory markers IL-6 and COX-2 were also increased in diabetic rats. |
| 1594 | 17122189 | NAC treatment prevented the increased expression of p22(phox) and translocation of p67(phox) to the membrane in diabetic rat hearts. |
| 1595 | 17122189 | Subsequently, the levels of cardiac free 15-F(2t)-isoprostane, HO-1, Cu-Zn-SOD, total SOD, IL-6, and COX-2 in diabetic rats were decreased by NAC. |
| 1596 | 17122189 | The protective effects of NAC on diabetic rat hearts may be attributable to its protection of hearts against oxidative damage induced by the increased NADPH oxidase and to its reduction in cardiac inflammatory mediators IL-6 and COX-2. |
| 1597 | 17122189 | Metabolic parameters, free 15-F(2t)-isoprostane level, protein expression of NADPH oxidase, superoxide dismutase (SOD), heme oxygenase (HO-1), interleukin-6 (IL-6), and cyclooxygenase-2 (COX-2) were analyzed in control and streptozotocin-induced diabetic rats treated with or without NAC in drinking water for 8 wk. |
| 1598 | 17122189 | The cardiac protein expression of p67(phox) and p22(phox) was increased in diabetic rats, accompanied by increased NADPH-dependent superoxide production. |
| 1599 | 17122189 | As a compensatory response to the increased NADPH oxidase, the protein expression of Cu-Zn-SOD and HO-1 and the total SOD activity were also increased in diabetic rat hearts. |
| 1600 | 17122189 | Cardiac inflammatory markers IL-6 and COX-2 were also increased in diabetic rats. |
| 1601 | 17122189 | NAC treatment prevented the increased expression of p22(phox) and translocation of p67(phox) to the membrane in diabetic rat hearts. |
| 1602 | 17122189 | Subsequently, the levels of cardiac free 15-F(2t)-isoprostane, HO-1, Cu-Zn-SOD, total SOD, IL-6, and COX-2 in diabetic rats were decreased by NAC. |
| 1603 | 17122189 | The protective effects of NAC on diabetic rat hearts may be attributable to its protection of hearts against oxidative damage induced by the increased NADPH oxidase and to its reduction in cardiac inflammatory mediators IL-6 and COX-2. |
| 1604 | 17126611 | Superoxide dismutase (SOD; converts superoxide to H(2)O(2)) significantly reduced the contraction in both types of arteries -- an effect abolished by catalase (H(2)O(2) scavenger), suggesting that the SOD effect was mediated by H(2)O(2). |
| 1605 | 17126611 | Treatment with catalase had no effect on the Ang II contraction in euglycaemic arteries, but it raised the contraction in diabetic arteries to euglycaemic levels. |
| 1606 | 17132211 | The activity of superoxide dismutase, catalase, glutathione peroxidase, glutathione-S-transferase and reduced glutathione was significantly decreased in liver and kidney of diabetic animals when compared with normal control. |
| 1607 | 17145126 | The oxidative stress was measured by tissue LPO level, reduced glutathione (GSH) content and by enzymatic activities of superoxide dismutase (SOD), catalase (CAT), glutathione peroxidase (GPx) and glutathione reductase (GR) in liver and pancreas. |
| 1608 | 17151323 | Significantly higher activities of antioxidant enzymes, namely, serum peroxidase, superoxide dismutase (SOD), and catalase (CAT) were found in type 2 diabetic patients as compared to control. |
| 1609 | 17157880 | Topical application of MnTMPyP (SOD mimetic) and apocynin (NADPH oxidase inhibitor) significantly improved the altered arteriolar responses to acetylcholine and bradykinin. |
| 1610 | 17188670 | The levels of glucose and glycosylated hemoglobin in blood and insulin, Vitamin C, Vitamin E, ceruloplasmin, reduced glutathione and TBARS were estimated in plasma of control and experimental groups of rats. |
| 1611 | 17188670 | To assess the changes in the cellular antioxidant defense system such as the level of reduced glutathione and activities of superoxide dismutase, catalase and glutathione peroxidase were assayed in pancreatic tissue homogenate. |
| 1612 | 17188670 | The levels of glucose, glycosylated hemoglobin, insulin, TBARS, enzymatic and non-enzymatic antioxidants were altered in diabetic rats. |
| 1613 | 17193903 | Activities of antioxidant enzymes, such as superoxide dismutase (SOD), catalase (CAT), glutathione peroxidase (GPX) and glutathione S transferase (GST) were assessed in diabetic as well as rats co-administered with ALL. |
| 1614 | 17201632 | The activities of erythrocyte superoxide dismutase (SOD), catalase (CAT), and glutathione peroxidase (GSH-Px) were significantly higher in the Du-zhong group compared with the control group, while glutathione reductase (GR) activity was not different between groups. |
| 1615 | 17205303 | We also compared the activities of antioxidant enzymes like catalase, superoxide dismutase (SOD), glutathione peroxidase (GPX), glutathione reductase (GR) and amount of antioxidant molecules like reduced glutathione (GSH) and uric acid under control and STZ-treated conditions. |
| 1616 | 17209802 | Correlation analysis revealed a strong positive association between IR (insulin resistance) and MDA concentration, but negative correlations with TAC status and SOD activity. |
| 1617 | 17211565 | Parameters involved in the pathogenesis of galactose-induced hyperglycaemia, which included organosomatic index, protein content, antioxidant enzymes superoxide dismutase (SOD), catalase (CAT), glutathione peroxidase (GSH-Px), tryptophan fluorescence, content of protein carbonyls, prooxidant malonaldehyde (MDA) and glutathione (GSH) in hepatic and neuronal tissues were determined at the end of the fourth week. |
| 1618 | 17220473 | Copper zinc-superoxide dismutase and glutathione were raised significantly (P < .001); however, changes in glutathione-S-transferase and glutathione peroxidase activities were nonsignificant. |
| 1619 | 17240813 | Role of anti-oxidant enzymes superoxide dismutase and catalase in the development of cataract : study of serum levels in patients with senile and diabetic cataracts. |
| 1620 | 17240813 | Superoxide dismutase, catalase and glutathione peroxidase are major anti-oxidant enzymes, which protect against free radicals. |
| 1621 | 17240813 | The purpose of this study is to evaluate the role of anti-oxidant enzymes - superoxide dismutase and catalase in the development of cataract in senile and diabetic persons. |
| 1622 | 17240813 | Serum levels of major anti-oxidant enzymes-superoxide dismutase and catalase were estimated in 20 patients with diabetic cataract, and matched with another 20 patients of senile cataract taken as control. |
| 1623 | 17240813 | Estimation of superoxide dismutase was done by improved spectrophotometric assay based on epinephrine auto-oxidation at 480nm, while catalase estimation was done by the method of Hugo Aebi. |
| 1624 | 17240813 | The mean serum levels of superoxide dismutase and catalase were lower as age increased. |
| 1625 | 17240813 | Role of anti-oxidant enzymes superoxide dismutase and catalase in the development of cataract : study of serum levels in patients with senile and diabetic cataracts. |
| 1626 | 17240813 | Superoxide dismutase, catalase and glutathione peroxidase are major anti-oxidant enzymes, which protect against free radicals. |
| 1627 | 17240813 | The purpose of this study is to evaluate the role of anti-oxidant enzymes - superoxide dismutase and catalase in the development of cataract in senile and diabetic persons. |
| 1628 | 17240813 | Serum levels of major anti-oxidant enzymes-superoxide dismutase and catalase were estimated in 20 patients with diabetic cataract, and matched with another 20 patients of senile cataract taken as control. |
| 1629 | 17240813 | Estimation of superoxide dismutase was done by improved spectrophotometric assay based on epinephrine auto-oxidation at 480nm, while catalase estimation was done by the method of Hugo Aebi. |
| 1630 | 17240813 | The mean serum levels of superoxide dismutase and catalase were lower as age increased. |
| 1631 | 17240813 | Role of anti-oxidant enzymes superoxide dismutase and catalase in the development of cataract : study of serum levels in patients with senile and diabetic cataracts. |
| 1632 | 17240813 | Superoxide dismutase, catalase and glutathione peroxidase are major anti-oxidant enzymes, which protect against free radicals. |
| 1633 | 17240813 | The purpose of this study is to evaluate the role of anti-oxidant enzymes - superoxide dismutase and catalase in the development of cataract in senile and diabetic persons. |
| 1634 | 17240813 | Serum levels of major anti-oxidant enzymes-superoxide dismutase and catalase were estimated in 20 patients with diabetic cataract, and matched with another 20 patients of senile cataract taken as control. |
| 1635 | 17240813 | Estimation of superoxide dismutase was done by improved spectrophotometric assay based on epinephrine auto-oxidation at 480nm, while catalase estimation was done by the method of Hugo Aebi. |
| 1636 | 17240813 | The mean serum levels of superoxide dismutase and catalase were lower as age increased. |
| 1637 | 17240813 | Role of anti-oxidant enzymes superoxide dismutase and catalase in the development of cataract : study of serum levels in patients with senile and diabetic cataracts. |
| 1638 | 17240813 | Superoxide dismutase, catalase and glutathione peroxidase are major anti-oxidant enzymes, which protect against free radicals. |
| 1639 | 17240813 | The purpose of this study is to evaluate the role of anti-oxidant enzymes - superoxide dismutase and catalase in the development of cataract in senile and diabetic persons. |
| 1640 | 17240813 | Serum levels of major anti-oxidant enzymes-superoxide dismutase and catalase were estimated in 20 patients with diabetic cataract, and matched with another 20 patients of senile cataract taken as control. |
| 1641 | 17240813 | Estimation of superoxide dismutase was done by improved spectrophotometric assay based on epinephrine auto-oxidation at 480nm, while catalase estimation was done by the method of Hugo Aebi. |
| 1642 | 17240813 | The mean serum levels of superoxide dismutase and catalase were lower as age increased. |
| 1643 | 17240813 | Role of anti-oxidant enzymes superoxide dismutase and catalase in the development of cataract : study of serum levels in patients with senile and diabetic cataracts. |
| 1644 | 17240813 | Superoxide dismutase, catalase and glutathione peroxidase are major anti-oxidant enzymes, which protect against free radicals. |
| 1645 | 17240813 | The purpose of this study is to evaluate the role of anti-oxidant enzymes - superoxide dismutase and catalase in the development of cataract in senile and diabetic persons. |
| 1646 | 17240813 | Serum levels of major anti-oxidant enzymes-superoxide dismutase and catalase were estimated in 20 patients with diabetic cataract, and matched with another 20 patients of senile cataract taken as control. |
| 1647 | 17240813 | Estimation of superoxide dismutase was done by improved spectrophotometric assay based on epinephrine auto-oxidation at 480nm, while catalase estimation was done by the method of Hugo Aebi. |
| 1648 | 17240813 | The mean serum levels of superoxide dismutase and catalase were lower as age increased. |
| 1649 | 17240813 | Role of anti-oxidant enzymes superoxide dismutase and catalase in the development of cataract : study of serum levels in patients with senile and diabetic cataracts. |
| 1650 | 17240813 | Superoxide dismutase, catalase and glutathione peroxidase are major anti-oxidant enzymes, which protect against free radicals. |
| 1651 | 17240813 | The purpose of this study is to evaluate the role of anti-oxidant enzymes - superoxide dismutase and catalase in the development of cataract in senile and diabetic persons. |
| 1652 | 17240813 | Serum levels of major anti-oxidant enzymes-superoxide dismutase and catalase were estimated in 20 patients with diabetic cataract, and matched with another 20 patients of senile cataract taken as control. |
| 1653 | 17240813 | Estimation of superoxide dismutase was done by improved spectrophotometric assay based on epinephrine auto-oxidation at 480nm, while catalase estimation was done by the method of Hugo Aebi. |
| 1654 | 17240813 | The mean serum levels of superoxide dismutase and catalase were lower as age increased. |
| 1655 | 17258921 | MnTMPyP, a metalloporphyrin-based superoxide dismutase/catalase mimetic, protects INS-1 cells and human pancreatic islets from an in vitro oxidative challenge. |
| 1656 | 17261958 | The expression of NADPH oxidase, catalase, and myeloperoxidase (MPO), superoxide dismutase activity, and production of peroxide and hypochlorite were evaluated. |
| 1657 | 17261958 | Catalase was decreased without change in SOD activity, and MPO was enhanced in the kidney of diabetic rats. |
| 1658 | 17261958 | Tempol treatment stimulated SOD activity and increased the conversion of superoxide to hydrogen peroxide, and hydrogen peroxide on its hand was converted to hypochlorite by the increased MPO. |
| 1659 | 17261958 | The expression of NADPH oxidase, catalase, and myeloperoxidase (MPO), superoxide dismutase activity, and production of peroxide and hypochlorite were evaluated. |
| 1660 | 17261958 | Catalase was decreased without change in SOD activity, and MPO was enhanced in the kidney of diabetic rats. |
| 1661 | 17261958 | Tempol treatment stimulated SOD activity and increased the conversion of superoxide to hydrogen peroxide, and hydrogen peroxide on its hand was converted to hypochlorite by the increased MPO. |
| 1662 | 17261958 | The expression of NADPH oxidase, catalase, and myeloperoxidase (MPO), superoxide dismutase activity, and production of peroxide and hypochlorite were evaluated. |
| 1663 | 17261958 | Catalase was decreased without change in SOD activity, and MPO was enhanced in the kidney of diabetic rats. |
| 1664 | 17261958 | Tempol treatment stimulated SOD activity and increased the conversion of superoxide to hydrogen peroxide, and hydrogen peroxide on its hand was converted to hypochlorite by the increased MPO. |
| 1665 | 17282336 | After 5 weeks, hemodynamic parameters, echocardiography characteristics and the levels of malondialdehyde (MDA), the activities of superoxide dismutase (SOD), catalase (CAT), glutathione peroxidase (GSH-Px) in the cardiac tissues of all groups were meassured. |
| 1666 | 17292348 | Increased oxidative stress in the streptozotocin-induced diabetic apoE-deficient mouse: changes in expression of NADPH oxidase subunits and eNOS. |
| 1667 | 17292348 | Glucose-induced changes in the activity of NADPH oxidase and endothelial nitric oxide synthase (eNOS) may result in vascular endothelial cell dysfunction via dysregulation of eNOS and/or changes in the expression of the subunits of NADPH oxidase. |
| 1668 | 17292348 | In this study, we have investigated whether changes in the expression of the subunits of NADPH oxidase, or eNOS mRNA, can be associated with oxidative stress in the streptozotocin-induced type 1 diabetic apolipoprotein E-deficient (apoE(-/-)) diabetic mouse. |
| 1669 | 17292348 | Oxidative stress was assessed in aorta and mesenteric arteries by immunofluorescence labelling with dihydroethidium and levels of NADPH oxidase subunits and eNOS were determined by a real-time polymerase chain reaction protocol. |
| 1670 | 17292348 | In the mesenteric arteries the expression of nox4 (4 weeks) and gp91phox (nox2) (8 weeks) subunits of NADPH oxidase from streptozotocin-apoE(-/-) were enhanced as were eNOS mRNA and protein (P<0.05). |
| 1671 | 17292348 | These data indicate that increased oxidative stress in the vasculature of streptozotocin-apoE(-/-) mice is linked to changes in eNOS, superoxide dismutase (SOD) and NADPH oxidase expression. |
| 1672 | 17331548 | The expression of antioxidant enzymes including alpha-catalase (CAT), Cu-Zn superoxide dismutase (SOD), Mn SOD, and glutathione peroxidase (GPx) were analyzed in the glomeruli of the rats using Western blotting. |
| 1673 | 17331548 | The expression of alpha-CAT and Mn SOD proteins was significantly decreased in isolated glomeruli in the WFR-HS group. |
| 1674 | 17331548 | The expression of antioxidant enzymes including alpha-catalase (CAT), Cu-Zn superoxide dismutase (SOD), Mn SOD, and glutathione peroxidase (GPx) were analyzed in the glomeruli of the rats using Western blotting. |
| 1675 | 17331548 | The expression of alpha-CAT and Mn SOD proteins was significantly decreased in isolated glomeruli in the WFR-HS group. |
| 1676 | 17336007 | Results showed significant reduction in the activities of superoxide dismutase (SOD), catalase (CAT) and pancreatic glutathione (GSH) levels in the diabetic rats compared to the control subjects. |
| 1677 | 17336007 | Furthermore, ASE significantly increased CAT and SOD activities in ASE-treated rats. |
| 1678 | 17336007 | Results showed significant reduction in the activities of superoxide dismutase (SOD), catalase (CAT) and pancreatic glutathione (GSH) levels in the diabetic rats compared to the control subjects. |
| 1679 | 17336007 | Furthermore, ASE significantly increased CAT and SOD activities in ASE-treated rats. |
| 1680 | 17337254 | The PPARgamma ligand, rosiglitazone, reduces vascular oxidative stress and NADPH oxidase expression in diabetic mice. |
| 1681 | 17337254 | Because peroxisome proliferator-activated receptor gamma (PPARgamma) ligands reduced superoxide anion (O(2)(-.)) generation in vascular endothelial cells in vitro by reducing NADPH oxidase and increasing Cu/Zn superoxide dismutase (SOD) expression, the current study examined the effect of PPARgamma ligands on vascular NADPH oxidase and O(2)(-.) generation in vivo. |
| 1682 | 17337254 | Aortic O(2)(-.) generation and mRNA levels of the NADPH oxidase subunits, Nox-1, Nox-2, and Nox-4 as well as Nox-4 protein expression were elevated in db(-)/db(-) compared to db(+)/db(-) mice, whereas aortic Cu/Zn SOD protein and PPARgamma mRNA levels were reduced in db(-)/db(-) mice. |
| 1683 | 17337254 | Treatment with rosiglitazone for 1-week significantly reduced aortic O(2)(-.) production and the expression of Nox-1, 2, and 4 but failed to increase Cu/Zn SOD or PPARgamma in aortic tissue from db(-)/db(-) mice. |
| 1684 | 17337254 | These data demonstrate that the vascular expression of Nox-1, 2, and 4 subunits of NADPH oxidase is increased in db(-)/db(-) mice and that short-term treatment with the PPARgamma agonist, rosiglitazone, has the potential to rapidly suppress vascular NADPH oxidase expression and O(2)(-.) production through mechanisms that do not appear to depend on correction of diabetic metabolic derangements. |
| 1685 | 17337254 | The PPARgamma ligand, rosiglitazone, reduces vascular oxidative stress and NADPH oxidase expression in diabetic mice. |
| 1686 | 17337254 | Because peroxisome proliferator-activated receptor gamma (PPARgamma) ligands reduced superoxide anion (O(2)(-.)) generation in vascular endothelial cells in vitro by reducing NADPH oxidase and increasing Cu/Zn superoxide dismutase (SOD) expression, the current study examined the effect of PPARgamma ligands on vascular NADPH oxidase and O(2)(-.) generation in vivo. |
| 1687 | 17337254 | Aortic O(2)(-.) generation and mRNA levels of the NADPH oxidase subunits, Nox-1, Nox-2, and Nox-4 as well as Nox-4 protein expression were elevated in db(-)/db(-) compared to db(+)/db(-) mice, whereas aortic Cu/Zn SOD protein and PPARgamma mRNA levels were reduced in db(-)/db(-) mice. |
| 1688 | 17337254 | Treatment with rosiglitazone for 1-week significantly reduced aortic O(2)(-.) production and the expression of Nox-1, 2, and 4 but failed to increase Cu/Zn SOD or PPARgamma in aortic tissue from db(-)/db(-) mice. |
| 1689 | 17337254 | These data demonstrate that the vascular expression of Nox-1, 2, and 4 subunits of NADPH oxidase is increased in db(-)/db(-) mice and that short-term treatment with the PPARgamma agonist, rosiglitazone, has the potential to rapidly suppress vascular NADPH oxidase expression and O(2)(-.) production through mechanisms that do not appear to depend on correction of diabetic metabolic derangements. |
| 1690 | 17337254 | The PPARgamma ligand, rosiglitazone, reduces vascular oxidative stress and NADPH oxidase expression in diabetic mice. |
| 1691 | 17337254 | Because peroxisome proliferator-activated receptor gamma (PPARgamma) ligands reduced superoxide anion (O(2)(-.)) generation in vascular endothelial cells in vitro by reducing NADPH oxidase and increasing Cu/Zn superoxide dismutase (SOD) expression, the current study examined the effect of PPARgamma ligands on vascular NADPH oxidase and O(2)(-.) generation in vivo. |
| 1692 | 17337254 | Aortic O(2)(-.) generation and mRNA levels of the NADPH oxidase subunits, Nox-1, Nox-2, and Nox-4 as well as Nox-4 protein expression were elevated in db(-)/db(-) compared to db(+)/db(-) mice, whereas aortic Cu/Zn SOD protein and PPARgamma mRNA levels were reduced in db(-)/db(-) mice. |
| 1693 | 17337254 | Treatment with rosiglitazone for 1-week significantly reduced aortic O(2)(-.) production and the expression of Nox-1, 2, and 4 but failed to increase Cu/Zn SOD or PPARgamma in aortic tissue from db(-)/db(-) mice. |
| 1694 | 17337254 | These data demonstrate that the vascular expression of Nox-1, 2, and 4 subunits of NADPH oxidase is increased in db(-)/db(-) mice and that short-term treatment with the PPARgamma agonist, rosiglitazone, has the potential to rapidly suppress vascular NADPH oxidase expression and O(2)(-.) production through mechanisms that do not appear to depend on correction of diabetic metabolic derangements. |
| 1695 | 17349927 | In untreated STZ rats (vs age-matched control rats): (1) ACh-induced relaxation, cGMP accumulation, phosphorylation of the cGMP-dependent protein kinase substrate vasodilator-stimulated phosphoprotein at Ser-239 [an established biochemical end-point of nitric oxide (NO)/cGMP signaling], and Cu/Zn-superoxide dismutase (SOD) expression and SOD activity were all reduced; (2) aortic superoxide generation, nitrotyrosine expression, and NAD(P)H oxidase activity were increased; (3) plasma endothelin-1 (ET-1) and aortic c-Jun (AP-1 component) protein expressions were increased. |
| 1696 | 17349927 | Collectively, these results suggest that pioglitazone treatment improves endothelium-dependent relaxation by reducing oxidative stress via increased SOD activity, decreased NAD(P)H oxidase activity, and a decreased ET-1 level, and that this decreased ET-1 level may be attributable to an inhibition of the AP-1 signaling pathway. |
| 1697 | 17349927 | In untreated STZ rats (vs age-matched control rats): (1) ACh-induced relaxation, cGMP accumulation, phosphorylation of the cGMP-dependent protein kinase substrate vasodilator-stimulated phosphoprotein at Ser-239 [an established biochemical end-point of nitric oxide (NO)/cGMP signaling], and Cu/Zn-superoxide dismutase (SOD) expression and SOD activity were all reduced; (2) aortic superoxide generation, nitrotyrosine expression, and NAD(P)H oxidase activity were increased; (3) plasma endothelin-1 (ET-1) and aortic c-Jun (AP-1 component) protein expressions were increased. |
| 1698 | 17349927 | Collectively, these results suggest that pioglitazone treatment improves endothelium-dependent relaxation by reducing oxidative stress via increased SOD activity, decreased NAD(P)H oxidase activity, and a decreased ET-1 level, and that this decreased ET-1 level may be attributable to an inhibition of the AP-1 signaling pathway. |
| 1699 | 17381113 | The levels of blood glucose, total antioxidant capacity (TAOC), and malondiadehyde (MDA) and the activities of superoxide dismutase (SOD), glutathione peroxidase (GSH-Px), and xanthine oxidase (XOD) were determined in rat serum, liver, and testes. |
| 1700 | 17394460 | Rosiglitazone treatment curtailed the post-ischemic expression of the pro-inflammatory genes interleukin-1beta, interleukin-6, macrophage inflammatory protein-1alpha, monocyte chemoattractant protein-1, cyclooxygenase-2, inducible nitric oxide synthase, early growth response-1, CCAAT/enhancer binding protein-beta and nuclear factor-kappa B, and increased the expression of the anti-oxidant enzymes catalase and copper/zinc-superoxide dismutase. |
| 1701 | 17394460 | Rosiglitazone also increased the expression of the anti-inflammatory gene suppressor of cytokine signaling-3 and prevented the phosphorylation of the transcription factor signal transducer and activator of transcription-3 after focal ischemia. |
| 1702 | 17406657 | We hypothesized that the enhanced brain injury in GK rats could be caused by differential regulation of the heme degrading enzyme heme oxygenase (HO)-1, known to interact with the expression of other target genes implicated in antioxidant defense, inflammation and neurodegeneration, such as superoxide dismutase (SOD)-1, -2, inducible nitric oxide synthase (iNOS), and tumor necrosis factor-alpha (TNFalpha). |
| 1703 | 17406657 | Baseline expression of HO-1, iNOS, and TNFalpha mRNA was increased in the cortex of sham GK rats. |
| 1704 | 17430642 | The effects of MT-alpha-glucan (450 or 150 mg kg (-1)) on diabetic mice were investigated by observing the changes in body weight, the level of fasting plasma glucose, glycosylated serum protein (GSP), hepatic glycogen, serum insulin, triglycerides, cholesterol, free fatty acid, liver superoxide dismutase (SOD), glutathione peroxidase (GSHpx), reduced glutathione (GSH) and malondialdehyde (MDA). |
| 1705 | 17437032 | A cis-acting transcriptional regulatory element, designated as antioxidant response element (ARE) or electrophile response element (EpRE), mediates the transcriptional activation of genes such as heme oxygenase-1, gamma-glutamylcysteine synthethase, thioredoxin reductase, glutathione-S-transferase and NAD(P)H:quinone oxidoreductase. |
| 1706 | 17437032 | Other antioxidant enzymes such as superoxide dismutase and catalase and non-enzymatic scavengers such as glutathione are also involved in scavenging ROS. |
| 1707 | 17437032 | Nuclear factor-erythroid 2-related factor 2 (Nrf2), a member of the Cap nno Collar family of basic region-leucine zipper (bZIP) transcription factors, plays an important role in ARE-mediated antioxidant gene expression. |
| 1708 | 17437032 | Kelch-like ECH-associated protein-1 (Keap1) normally sequesters Nrf2 in the cytoplasm in association with the actin cytoskeleton, but upon oxidation of cysteine residues Nrf2 dissociates from Keap1, translocates to the nucleus and binds to ARE sequences leading to transcriptional activation of antioxidant and phase II detoxifying genes. |
| 1709 | 17437032 | Protein kinase C (PKC), mitogen-activated protein kinases (MAPKs) and phosphotidylinositol 3-kinase (PI3K) have been implicated in the regulation of Nrf2/ARE signaling. |
| 1710 | 17443690 | Oxidative stress and increased eNOS and NADPH oxidase expression in mouse microvessel endothelial cells. |
| 1711 | 17443690 | In this study, we tested the hypothesis that high glucose-induced oxidative stress was associated with changes in the expression of NADPH oxidase, superoxide dismutase (SOD) and endothelial nitric oxide synthase (eNOS). |
| 1712 | 17443690 | Oxidative stress was assessed in cell cultures of mouse microvessel endothelial cells (MMECs) by fluorescence labelling with dihydroethidium, lucigenin-enhanced chemiluminescence and determining NADPH oxidase subunit and eNOS expression with real-time polymerase chain reaction protocol and Western blotting. |
| 1713 | 17443690 | Oxidative stress and expression of the NADPH oxidase subunit, p22phox, were both increased, SOD1 and 3 expression lowered and eNOS significantly elevated in MMECs treated with 40 mM glucose for 72 h compared to low glucose medium. |
| 1714 | 17443690 | Oxidative stress, p22phox mRNA, eNOS mRNA, and protein were lowered by concurrent incubation with sepiapterin. |
| 1715 | 17443690 | Thus, exposure of MMECs to high glucose results in increased oxidative stress that is associated with increased eNOS and NADPH oxidase subunit expression, notably p22phox, and decreased expression of SOD1 and 3. |
| 1716 | 17443690 | Oxidative stress and increased eNOS and NADPH oxidase expression in mouse microvessel endothelial cells. |
| 1717 | 17443690 | In this study, we tested the hypothesis that high glucose-induced oxidative stress was associated with changes in the expression of NADPH oxidase, superoxide dismutase (SOD) and endothelial nitric oxide synthase (eNOS). |
| 1718 | 17443690 | Oxidative stress was assessed in cell cultures of mouse microvessel endothelial cells (MMECs) by fluorescence labelling with dihydroethidium, lucigenin-enhanced chemiluminescence and determining NADPH oxidase subunit and eNOS expression with real-time polymerase chain reaction protocol and Western blotting. |
| 1719 | 17443690 | Oxidative stress and expression of the NADPH oxidase subunit, p22phox, were both increased, SOD1 and 3 expression lowered and eNOS significantly elevated in MMECs treated with 40 mM glucose for 72 h compared to low glucose medium. |
| 1720 | 17443690 | Oxidative stress, p22phox mRNA, eNOS mRNA, and protein were lowered by concurrent incubation with sepiapterin. |
| 1721 | 17443690 | Thus, exposure of MMECs to high glucose results in increased oxidative stress that is associated with increased eNOS and NADPH oxidase subunit expression, notably p22phox, and decreased expression of SOD1 and 3. |
| 1722 | 17443690 | Oxidative stress and increased eNOS and NADPH oxidase expression in mouse microvessel endothelial cells. |
| 1723 | 17443690 | In this study, we tested the hypothesis that high glucose-induced oxidative stress was associated with changes in the expression of NADPH oxidase, superoxide dismutase (SOD) and endothelial nitric oxide synthase (eNOS). |
| 1724 | 17443690 | Oxidative stress was assessed in cell cultures of mouse microvessel endothelial cells (MMECs) by fluorescence labelling with dihydroethidium, lucigenin-enhanced chemiluminescence and determining NADPH oxidase subunit and eNOS expression with real-time polymerase chain reaction protocol and Western blotting. |
| 1725 | 17443690 | Oxidative stress and expression of the NADPH oxidase subunit, p22phox, were both increased, SOD1 and 3 expression lowered and eNOS significantly elevated in MMECs treated with 40 mM glucose for 72 h compared to low glucose medium. |
| 1726 | 17443690 | Oxidative stress, p22phox mRNA, eNOS mRNA, and protein were lowered by concurrent incubation with sepiapterin. |
| 1727 | 17443690 | Thus, exposure of MMECs to high glucose results in increased oxidative stress that is associated with increased eNOS and NADPH oxidase subunit expression, notably p22phox, and decreased expression of SOD1 and 3. |
| 1728 | 17448894 | The glutathione peroxidase (GSH-Px), catalase (CAT), superoxide dismutase (SOD), glutathione (GSH), and ceruloplasmin levels in the diabetic group were decreased by the effect of diabetes but there was no difference between zinc-supplemented diabetic and control rabbits. |
| 1729 | 17462535 | AGE differentially regulated VSMC NADPH oxidase catalytic subunits, stimulating the transcription of Nox1 (201+/-12.7%, p<0.0001), while having no effect on Nox4. |
| 1730 | 17462535 | Regarding the source of NO, AGE stimulated inducible nitric oxide synthase mRNA (1 vs 9.7+/-3.0, p=0.046), which was abolished by a NF-kappaB inhibitor, SOD, catalase, or siRNA against Nox1. |
| 1731 | 17462535 | This study establishes that AGE activate iNOS in VSMC through a ROS-sensitive, NF-kappaB-dependent mechanism involving ROS generation by a Nox1-based oxidase. |
| 1732 | 17482424 | We aimed to investigate the extent to which maternal diabetes with or without folic acid (FA) supplementation affects mRNA levels and protein distribution of ROS scavenging enzymes, vascular endothelial growth factor-A (Vegf-A), folate binding protein-1 (Folbp-1), and apoptosis-associated proteins in the yolk sacs of rat embryos on gestational days 10 and 11. |
| 1733 | 17482424 | Maternal diabetes also increased the levels of CuZnSOD protein, increased the Bax/Bcl-2 protein ratio and decreased Vegf-A protein distribution. |
| 1734 | 17482424 | FA treatment normalized vascular morphology, decreased mRNA levels of all three SOD isoforms and increased Vegf-A mRNA levels, rectified CuZnSOD protein distribution and Bax/Bcl-2 ratio. |
| 1735 | 17490624 | Reactive species of thiobarbituric acid (TBARS) and total antioxidant reactivity (TAR) as well as antioxidant enzyme activities catalase (CAT) and superoxide dismutase (SOD) were evaluated. |
| 1736 | 17490624 | There were no effects of CAT and SOD activities in erythrocytes from tested animals. |
| 1737 | 17490624 | Reactive species of thiobarbituric acid (TBARS) and total antioxidant reactivity (TAR) as well as antioxidant enzyme activities catalase (CAT) and superoxide dismutase (SOD) were evaluated. |
| 1738 | 17490624 | There were no effects of CAT and SOD activities in erythrocytes from tested animals. |
| 1739 | 17497341 | In the absence of an appropriate compensatory response by the endogenous antioxidants, such as vitamins C and E, catalase, glutathione, and superoxide dismutase, oxidative stress dominates, resulting in the activation of stress-sensitive intracellular signaling pathways. |
| 1740 | 17521626 | The changes in lipid peroxidation status and anti-oxidant enzymes (Superoxide dismutase and Catalase) levels observed in diabetic rats were significantly restored by edaravone treatment. |
| 1741 | 17533199 | NADPH oxidase contributes to vascular inflammation, insulin resistance, and remodeling in the transgenic (mRen2) rat. |
| 1742 | 17533199 | Angiotensin II, acting through its angiotensin type 1 receptor, inhibits the actions of insulin in the vasculature which may lead to deleterious effects such as vascular inflammation, remodeling, endothelial dysfunction, and insulin resistance. |
| 1743 | 17533199 | To explore the impact of angiotensin II on insulin signaling, NADPH oxidase-derived reactive oxygen species formation, vascular inflammation, apoptosis, and remodeling, we used transgenic TG(mRen2)27 (Ren2) rats, which harbor the mouse renin transgene and exhibits elevated tissue angiotensin II levels. |
| 1744 | 17533199 | Compared with Sprague-Dawley controls, Ren2 aortas exhibited greater NADPH oxidase activity, reactive oxygen species levels, C-reactive protein, tumor necrosis factor-alpha expression, apoptosis, and wall thickness, which were significantly attenuated by in vivo treatment with angiotensin type 1 receptor blockade (valsartan) or the superoxide dismutase/catalase mimetic (tempol). |
| 1745 | 17533199 | There was substantially diminished Akt and endothelial NO synthase activation in Ren2 aortas in response to in vivo insulin stimulation, and this was significantly improved by in vivo treatment with valsartan or tempol. |
| 1746 | 17533199 | Further, there was reduced insulin induced Akt activation and increased tumor necrosis factor-alpha levels in vascular smooth muscle cells from Ren2 and Sprague-Dawley rats treated with angiotensin II, abnormalities that were abrogated by angiotensin type 1 receptor blockade with valsartan or antioxidant N-acetylcysteine. |
| 1747 | 17533199 | Collectively, these data suggest that increased angiotensin type 1 receptor/NADPH oxidase activation/reactive oxygen species contribute to vascular insulin resistance, endothelial dysfunction, apoptosis, and inflammation. |
| 1748 | 17537413 | The effect of EMS on glucose, insulin, hemoglobin, glycosylated hemoglobin, TBARS, hydroperoxide, superoxide dismutase (SOD), catalase (CAT), glutathione peroxide (Gpx), glutathione-S-transferase (GST), vitamins C and E, reduced glutathione (GSH) and membrane bound enzymes were studied. |
| 1749 | 17537413 | The levels of glucose, glycosylated hemoglobin, TBARS, hyderoperoxide, and vitamin E were increased significantly whereas the level of insulin and hemoglobin, as well as antioxidants (SOD, CAT, Gpx, GST, vitamin C and GSH) membrane bound total ATPase, Na(+)/K(+)-ATPase, Ca(2+)-ATPase and Mg(2+)-ATPase were decreased significantly in streptozotocin-nicotinamide diabetic rats. |
| 1750 | 17537413 | In addition the levels of insulin, hemoglobin, enzymic antioxidants, vitamin C, and GSH and the activities of membrane bound enzymes also were increased in EMS and metformin treated diabetic rats. |
| 1751 | 17537413 | The effect of EMS on glucose, insulin, hemoglobin, glycosylated hemoglobin, TBARS, hydroperoxide, superoxide dismutase (SOD), catalase (CAT), glutathione peroxide (Gpx), glutathione-S-transferase (GST), vitamins C and E, reduced glutathione (GSH) and membrane bound enzymes were studied. |
| 1752 | 17537413 | The levels of glucose, glycosylated hemoglobin, TBARS, hyderoperoxide, and vitamin E were increased significantly whereas the level of insulin and hemoglobin, as well as antioxidants (SOD, CAT, Gpx, GST, vitamin C and GSH) membrane bound total ATPase, Na(+)/K(+)-ATPase, Ca(2+)-ATPase and Mg(2+)-ATPase were decreased significantly in streptozotocin-nicotinamide diabetic rats. |
| 1753 | 17537413 | In addition the levels of insulin, hemoglobin, enzymic antioxidants, vitamin C, and GSH and the activities of membrane bound enzymes also were increased in EMS and metformin treated diabetic rats. |
| 1754 | 17566145 | Treatment with breviscapine also significantly decreased lipid peroxidation malondiadehyde levels and increased the activities of antioxidative enzymes such as superoxide dismutase, catalase and glutathione peroxidase in diabetic liver. |
| 1755 | 17566145 | Western blot analysis showed that the expression of transforming growth factor-beta1 in diabetic liver was lowered by breviscapine treatment. |
| 1756 | 17581213 | Thiobarbituric acid-reactive substances (TBARS; an index of lipid peroxidation), superoxide dismutase, glutathione peroxidase, catalase, nitrate/nitrite (NO(x)) and reduced glutathione (GSH) were estimated in liver and kidney homogenates. 4. |
| 1757 | 17584062 | In normal physiological condition, ROS production is usually homeostatically controlled by endogenous free radical scavengers such as superoxide dismutase, catalase, and the glutathione peroxidase and thioredoxin reductase systems. |
| 1758 | 17609286 | Of 105 analyzed spots, expression of 40 proteins, including the antioxidative enzymes peroxiredoxin 1 and 3, glutathione peroxidase 1, and SOD-1, was increased with diabetes, suggesting an adaptive response to oxidative stress associated with this diabetic model. |
| 1759 | 17613116 | SO(2) exposure, while markedly increasing Cu-Zn Superoxide dismutase activity, significantly decreased glutathione peroxidase activity in diabetic and non-diabetic groups compared with the C group; hippocampus catalase activity was unaltered. |
| 1760 | 17641739 | Further, the extract also significantly (P < .01) decreased the pancreatic thiobarbituric acid-reactive substances (TBARS) levels and significantly (P < .01) increased the superoxide dismutase, catalase, and glutathione levels as compared to above levels in pancreatic tissue of pathogenic diabetic rats. |
| 1761 | 17665046 | On day 21 of pregnancy, the adult rats (weighing approximately 250 +/- 50 g, minimum number = 13/group) were anesthetized to obtain maternal and fetal liver samples for superoxide dismutase (SOD), catalase (CAT), glutathione peroxidase (GSH-Px), and total glutathione (GSH-t) determinations. |
| 1762 | 17665046 | For G1, maternal GSH-Px = 0.9 +/- 0.2 and SOD = 274.1 +/- 80.3; fetal CAT = 92.6 +/- 82.7 and GSH-t = 0.6 +/- 0.5. |
| 1763 | 17665046 | On day 21 of pregnancy, the adult rats (weighing approximately 250 +/- 50 g, minimum number = 13/group) were anesthetized to obtain maternal and fetal liver samples for superoxide dismutase (SOD), catalase (CAT), glutathione peroxidase (GSH-Px), and total glutathione (GSH-t) determinations. |
| 1764 | 17665046 | For G1, maternal GSH-Px = 0.9 +/- 0.2 and SOD = 274.1 +/- 80.3; fetal CAT = 92.6 +/- 82.7 and GSH-t = 0.6 +/- 0.5. |
| 1765 | 17665974 | High glucose-induced protein kinase C signalling or renal angiotensin II signalling increases the membrane translocation of cytosolic component p47phox. |
| 1766 | 17665974 | NADPH oxidase-derived reactive oxygen species (ROS) in the podocytes damage the glomerular basement membrane and the slit diaphragm causing proteinuria, and mesangial and glomerular endothelial NADPH oxidase increase TGF-beta and cause collagen and fibronectin accumulation. |
| 1767 | 17665974 | Tubular NADPH oxidase stimulated by angiotensin II or aldosterone contributes to sodium retention and to tubulointerstitial damage. |
| 1768 | 17665974 | Thus, inhibition of the renal renin-angiotensin II-aldosterone system with angiotensin-converting enzyme inhibitor, angiotensin II type 1 receptor blocker or selective aldosterone inhibitor indirectly suppresses NADPH oxidase reducing renal ROS, proteinuria and glomerulosclerosis. |
| 1769 | 17665974 | Statins are also effective in blocking the membrane translocation of Rac, especially in diabetes with hypercholesterolemia where ROS is produced by the intrinsic NADPH oxidase and by the activated macrophages. |
| 1770 | 17665974 | A medical herb, picrorhiza, inhibits the membrane translocation of p47phox, is a specific inhibitor of NADPH oxidase and, more so than superoxide dismutase mimetics, may be a promising strategy for the treatment of diabetic nephropathy. |
| 1771 | 17693046 | The effect of THC and curcumin on glucose, insulin, haemoglobin, glycosylated haemoglobin, thiobarbituric acid reactive substances (TBARS), superoxide dismutase (SOD), catalase (CAT), glutathione peroxide (Gpx), glutathione-S-transferase (GST), reduced glutathione (GSH) and membrane bound enzymes were studied. |
| 1772 | 17693046 | The levels of blood glucose, glycosylated haemoglobin, erythrocyte TBARS, were increased significantly whereas the level of plasma insulin and haemoglobin, erythrocyte antioxidants (SOD, CAT, GPx, GST and GSH), membrane bound total ATPase, Na(+)/K(+)-ATPase, Ca(2+)-ATPase, Mg(2+)-ATPase were decreased significantly in diabetic rats. |
| 1773 | 17693046 | The effect of THC and curcumin on glucose, insulin, haemoglobin, glycosylated haemoglobin, thiobarbituric acid reactive substances (TBARS), superoxide dismutase (SOD), catalase (CAT), glutathione peroxide (Gpx), glutathione-S-transferase (GST), reduced glutathione (GSH) and membrane bound enzymes were studied. |
| 1774 | 17693046 | The levels of blood glucose, glycosylated haemoglobin, erythrocyte TBARS, were increased significantly whereas the level of plasma insulin and haemoglobin, erythrocyte antioxidants (SOD, CAT, GPx, GST and GSH), membrane bound total ATPase, Na(+)/K(+)-ATPase, Ca(2+)-ATPase, Mg(2+)-ATPase were decreased significantly in diabetic rats. |
| 1775 | 17697870 | After 5 weeks of diabetes, KO diabetic (D) but not WT-D mice developed marked albuminuria, increases in glomerular content of transforming growth factor beta, collagen alpha1(IV), and nitrotyrosine, and higher glomerular superoxide compared with corresponding values in nondiabetics. |
| 1776 | 17697870 | Treatment of KO-D with the SOD mimetic tempol for 4 weeks suppressed albuminuria, increases in glomerular transforming growth factor beta, collagen alpha1(IV), nitrotyrosine, and glomerular superoxide, and concurrently increased C(In). |
| 1777 | 17850913 | Oxidative stress status parameters [thiobarbituric acid-reacting substances (TBARS), superoxide anion (O(2)(-)), superoxide dismutase (SOD) activity and total sulphydryl groups] and the concentration of leptin were measured in 312 subjects (178 patients and in 134 control subjects). |
| 1778 | 17853336 | The present study was designed to investigate the relationship between the serum levels of oxidant-antioxidant system (malondialdehyde (MDA) level, Paraoxonase (PON1) activity, nitric oxide (NO) level and superoxide dismutase (SOD) activity) and thyroid hormone status in hypothyroidism pre and posttreatment. |
| 1779 | 17853336 | Serum MDA level, PON1 activity, NO level and SOD activity were measured according to an enzymatic spectrophotometric method. |
| 1780 | 17853336 | The present study was designed to investigate the relationship between the serum levels of oxidant-antioxidant system (malondialdehyde (MDA) level, Paraoxonase (PON1) activity, nitric oxide (NO) level and superoxide dismutase (SOD) activity) and thyroid hormone status in hypothyroidism pre and posttreatment. |
| 1781 | 17853336 | Serum MDA level, PON1 activity, NO level and SOD activity were measured according to an enzymatic spectrophotometric method. |
| 1782 | 17873009 | Increasing doses of sorbitol (10(-10)-10(-4) M) elicited dose-dependent constrictions (maximum 22 +/- 3%), which were abolished by endothelium removal, a prostaglandin H(2)/thromboxane A(2) (PGH(2)/TXA(2)) receptor (TP) antagonist SQ-29548, or superoxide dismutase (SOD) plus catalase (CAT). |
| 1783 | 17873009 | Incubation of arterioles with sorbitol (10(-7) M) reduced flow-dependent dilations (from maximum of 39 +/- 2% to 20 +/- 1.5%), which was not further affected by inhibition of nitric oxide synthase by N(omega)-nitro-l-arginine methyl ester but was prevented by SOD plus CAT and mitigated by SQ-29548. |
| 1784 | 17873009 | Nitric oxide donor sodium nitroprusside-induced (10(-9)-10(-6) M) dilations were also decreased in a SQ-29548 and SOD plus CAT-reversible manner, whereas adenosine dilations were not affected by sorbitol exposure. |
| 1785 | 17873009 | Sorbitol significantly increased arterial superoxide production detected by lucigenin-enhanced chemiluminescence, which was inhibited by SOD plus CAT. |
| 1786 | 17873009 | Increasing doses of sorbitol (10(-10)-10(-4) M) elicited dose-dependent constrictions (maximum 22 +/- 3%), which were abolished by endothelium removal, a prostaglandin H(2)/thromboxane A(2) (PGH(2)/TXA(2)) receptor (TP) antagonist SQ-29548, or superoxide dismutase (SOD) plus catalase (CAT). |
| 1787 | 17873009 | Incubation of arterioles with sorbitol (10(-7) M) reduced flow-dependent dilations (from maximum of 39 +/- 2% to 20 +/- 1.5%), which was not further affected by inhibition of nitric oxide synthase by N(omega)-nitro-l-arginine methyl ester but was prevented by SOD plus CAT and mitigated by SQ-29548. |
| 1788 | 17873009 | Nitric oxide donor sodium nitroprusside-induced (10(-9)-10(-6) M) dilations were also decreased in a SQ-29548 and SOD plus CAT-reversible manner, whereas adenosine dilations were not affected by sorbitol exposure. |
| 1789 | 17873009 | Sorbitol significantly increased arterial superoxide production detected by lucigenin-enhanced chemiluminescence, which was inhibited by SOD plus CAT. |
| 1790 | 17873009 | Increasing doses of sorbitol (10(-10)-10(-4) M) elicited dose-dependent constrictions (maximum 22 +/- 3%), which were abolished by endothelium removal, a prostaglandin H(2)/thromboxane A(2) (PGH(2)/TXA(2)) receptor (TP) antagonist SQ-29548, or superoxide dismutase (SOD) plus catalase (CAT). |
| 1791 | 17873009 | Incubation of arterioles with sorbitol (10(-7) M) reduced flow-dependent dilations (from maximum of 39 +/- 2% to 20 +/- 1.5%), which was not further affected by inhibition of nitric oxide synthase by N(omega)-nitro-l-arginine methyl ester but was prevented by SOD plus CAT and mitigated by SQ-29548. |
| 1792 | 17873009 | Nitric oxide donor sodium nitroprusside-induced (10(-9)-10(-6) M) dilations were also decreased in a SQ-29548 and SOD plus CAT-reversible manner, whereas adenosine dilations were not affected by sorbitol exposure. |
| 1793 | 17873009 | Sorbitol significantly increased arterial superoxide production detected by lucigenin-enhanced chemiluminescence, which was inhibited by SOD plus CAT. |
| 1794 | 17873009 | Increasing doses of sorbitol (10(-10)-10(-4) M) elicited dose-dependent constrictions (maximum 22 +/- 3%), which were abolished by endothelium removal, a prostaglandin H(2)/thromboxane A(2) (PGH(2)/TXA(2)) receptor (TP) antagonist SQ-29548, or superoxide dismutase (SOD) plus catalase (CAT). |
| 1795 | 17873009 | Incubation of arterioles with sorbitol (10(-7) M) reduced flow-dependent dilations (from maximum of 39 +/- 2% to 20 +/- 1.5%), which was not further affected by inhibition of nitric oxide synthase by N(omega)-nitro-l-arginine methyl ester but was prevented by SOD plus CAT and mitigated by SQ-29548. |
| 1796 | 17873009 | Nitric oxide donor sodium nitroprusside-induced (10(-9)-10(-6) M) dilations were also decreased in a SQ-29548 and SOD plus CAT-reversible manner, whereas adenosine dilations were not affected by sorbitol exposure. |
| 1797 | 17873009 | Sorbitol significantly increased arterial superoxide production detected by lucigenin-enhanced chemiluminescence, which was inhibited by SOD plus CAT. |
| 1798 | 17877130 | The aim of the study was to evaluate selected parameters of oxidative stress in patients with metabolic compensated or decompensated diabetes by means of marking in red blood cells of the patients in question the activity of antioaxidative enzymes such as: superoxide dysmutase (SOD-1) and catalase (CAT) and concentration of malondialdehyde (MDA). 61 diabetic patients took part in the research, 31 of which met the criteria of metabolic compensation whereas 30 were metabolically decompensated. |
| 1799 | 17877130 | The activity of SOD-1 was marked by Misra and Fridovich's method, the activity of CAT by Beers and Sizer's method and the concentration of MDA in red blood cells was indicated by Placer et al. |
| 1800 | 17877130 | The activity of evaluated antioxidative enzymes SOD-1 and CAT in the erythrocytes of diabetes type 2 patients was statistically lower as compared with the control group. |
| 1801 | 17877130 | The highest activity of SOD-1 and CAT was noted in metabolic decompensated diabetes type 2 group. |
| 1802 | 17877130 | The aim of the study was to evaluate selected parameters of oxidative stress in patients with metabolic compensated or decompensated diabetes by means of marking in red blood cells of the patients in question the activity of antioaxidative enzymes such as: superoxide dysmutase (SOD-1) and catalase (CAT) and concentration of malondialdehyde (MDA). 61 diabetic patients took part in the research, 31 of which met the criteria of metabolic compensation whereas 30 were metabolically decompensated. |
| 1803 | 17877130 | The activity of SOD-1 was marked by Misra and Fridovich's method, the activity of CAT by Beers and Sizer's method and the concentration of MDA in red blood cells was indicated by Placer et al. |
| 1804 | 17877130 | The activity of evaluated antioxidative enzymes SOD-1 and CAT in the erythrocytes of diabetes type 2 patients was statistically lower as compared with the control group. |
| 1805 | 17877130 | The highest activity of SOD-1 and CAT was noted in metabolic decompensated diabetes type 2 group. |
| 1806 | 17877130 | The aim of the study was to evaluate selected parameters of oxidative stress in patients with metabolic compensated or decompensated diabetes by means of marking in red blood cells of the patients in question the activity of antioaxidative enzymes such as: superoxide dysmutase (SOD-1) and catalase (CAT) and concentration of malondialdehyde (MDA). 61 diabetic patients took part in the research, 31 of which met the criteria of metabolic compensation whereas 30 were metabolically decompensated. |
| 1807 | 17877130 | The activity of SOD-1 was marked by Misra and Fridovich's method, the activity of CAT by Beers and Sizer's method and the concentration of MDA in red blood cells was indicated by Placer et al. |
| 1808 | 17877130 | The activity of evaluated antioxidative enzymes SOD-1 and CAT in the erythrocytes of diabetes type 2 patients was statistically lower as compared with the control group. |
| 1809 | 17877130 | The highest activity of SOD-1 and CAT was noted in metabolic decompensated diabetes type 2 group. |
| 1810 | 17877130 | The aim of the study was to evaluate selected parameters of oxidative stress in patients with metabolic compensated or decompensated diabetes by means of marking in red blood cells of the patients in question the activity of antioaxidative enzymes such as: superoxide dysmutase (SOD-1) and catalase (CAT) and concentration of malondialdehyde (MDA). 61 diabetic patients took part in the research, 31 of which met the criteria of metabolic compensation whereas 30 were metabolically decompensated. |
| 1811 | 17877130 | The activity of SOD-1 was marked by Misra and Fridovich's method, the activity of CAT by Beers and Sizer's method and the concentration of MDA in red blood cells was indicated by Placer et al. |
| 1812 | 17877130 | The activity of evaluated antioxidative enzymes SOD-1 and CAT in the erythrocytes of diabetes type 2 patients was statistically lower as compared with the control group. |
| 1813 | 17877130 | The highest activity of SOD-1 and CAT was noted in metabolic decompensated diabetes type 2 group. |
| 1814 | 17879132 | Ethanol extract of G. montanum leaves (GLEt) was administered orally to alloxan-induced diabetic rats for 3 weeks, and the effects on blood glucose, insulin, lipid peroxidation markers, thiobarbituric acid reactive substances, hydroperoxides in plasma and antioxidant enzymes including superoxide dismutase, catalase and glutathione peroxidase activities in erythrocytes were studied. |
| 1815 | 17914354 | STZ-treated rats received insulin, the superoxide dismutase mimetic tempol, or contrast medium. |
| 1816 | 17916927 | Additionally, superoxide dismutase, catalase activities, and copper and zinc concentrations in red cell were determined in each group. |
| 1817 | 17916928 | Total nitrite, nitrite, nitrate, malondialdehyde, copper, zinc concentrations in plasma, superoxide dismutase, and catalase activities and copper, zinc concentrations in red cell were determined both in control and experimental groups. |
| 1818 | 17955223 | Reduced glutathione levels and enzymatic activities of superoxide dismutase and catalase were decreased in both cerebral cortex and hippocampal regions of diabetic rat brain. |
| 1819 | 17976266 | With respect to LPO, while in alloxan-treated animals an increase in hepatic LPO and a decrease in the activity of cellular antioxidants, such as catalase (CAT) and superoxide dismutase (SOD), and in glutathione (GSH) content was observed, administration of apigenin to alloxan-treated mice reversed all these changes, suggesting its hepatoprotective potential. |
| 1820 | 17977678 | At concentration levels of 150 and 250 mg/kg b.wt., POE exerted a protective effect on the significantly decreased levels of antioxidants namely, glutathione (GSH), superoxide dismutase (SOD), glutathione peroxidase (GPx), catalase and nitric oxide (NO). |
| 1821 | 18008141 | In this study, the expression of two antioxidant enzymes, superoxide dismutase (SOD), and catalase which are involved in the detoxification of reactive oxygen species was studied in the streptozotocin-induced diabetic rat liver tissues. |
| 1822 | 18008141 | The RT-PCR and Western-blot analysis results demonstrated that this decrease in activity is regulated at the level of gene expression, as both catalase and Cu-Zn SOD mRNA and protein expressions were also suppressed. |
| 1823 | 18008141 | Supplementing the animals with vitamin C, a powerful antioxidant increased both SOD and catalase activities with no change in both mRNA and protein expressions suggesting a role of post-translational modification. |
| 1824 | 18008141 | However, even though mRNA expressions of both catalase and Cu-Zn SOD were not changed, the protein levels increased in parallel to activities in the case of another antioxidant, alpha-lipoic acid. |
| 1825 | 18008141 | In this study, the expression of two antioxidant enzymes, superoxide dismutase (SOD), and catalase which are involved in the detoxification of reactive oxygen species was studied in the streptozotocin-induced diabetic rat liver tissues. |
| 1826 | 18008141 | The RT-PCR and Western-blot analysis results demonstrated that this decrease in activity is regulated at the level of gene expression, as both catalase and Cu-Zn SOD mRNA and protein expressions were also suppressed. |
| 1827 | 18008141 | Supplementing the animals with vitamin C, a powerful antioxidant increased both SOD and catalase activities with no change in both mRNA and protein expressions suggesting a role of post-translational modification. |
| 1828 | 18008141 | However, even though mRNA expressions of both catalase and Cu-Zn SOD were not changed, the protein levels increased in parallel to activities in the case of another antioxidant, alpha-lipoic acid. |
| 1829 | 18008141 | In this study, the expression of two antioxidant enzymes, superoxide dismutase (SOD), and catalase which are involved in the detoxification of reactive oxygen species was studied in the streptozotocin-induced diabetic rat liver tissues. |
| 1830 | 18008141 | The RT-PCR and Western-blot analysis results demonstrated that this decrease in activity is regulated at the level of gene expression, as both catalase and Cu-Zn SOD mRNA and protein expressions were also suppressed. |
| 1831 | 18008141 | Supplementing the animals with vitamin C, a powerful antioxidant increased both SOD and catalase activities with no change in both mRNA and protein expressions suggesting a role of post-translational modification. |
| 1832 | 18008141 | However, even though mRNA expressions of both catalase and Cu-Zn SOD were not changed, the protein levels increased in parallel to activities in the case of another antioxidant, alpha-lipoic acid. |
| 1833 | 18008141 | In this study, the expression of two antioxidant enzymes, superoxide dismutase (SOD), and catalase which are involved in the detoxification of reactive oxygen species was studied in the streptozotocin-induced diabetic rat liver tissues. |
| 1834 | 18008141 | The RT-PCR and Western-blot analysis results demonstrated that this decrease in activity is regulated at the level of gene expression, as both catalase and Cu-Zn SOD mRNA and protein expressions were also suppressed. |
| 1835 | 18008141 | Supplementing the animals with vitamin C, a powerful antioxidant increased both SOD and catalase activities with no change in both mRNA and protein expressions suggesting a role of post-translational modification. |
| 1836 | 18008141 | However, even though mRNA expressions of both catalase and Cu-Zn SOD were not changed, the protein levels increased in parallel to activities in the case of another antioxidant, alpha-lipoic acid. |
| 1837 | 18057537 | Two candidate genes that affect the oxidative stress are manganese mitochondrial superoxide dismutase (Mn-SOD) and endothelial nitric oxide synthase (eNOS). |
| 1838 | 18057537 | The aim of the present study was to examine the role of the V16A polymorphism of the Mn-SOD gene and the 4a/b polymorphism of the eNOS gene in the development of diabetic retinopathy in Caucasians with type 2 diabetes. |
| 1839 | 18057537 | A significantly higher frequency of the VV genotype of the V16A polymorphism of the Mn-SOD was found in patients with diabetic retinopathy compared to those without diabetic retinopathy (OR=2.1, 95% whereas the 4a/b polymorphism of the eNOS gene failed to yield an association with diabetic retinopathy. |
| 1840 | 18063812 | Here we show that TPr stimulation activates AMP-activated kinase (AMPK), which in turn limits TPr-induced protein synthesis in VSMCs. |
| 1841 | 18063812 | Exposure of cultured VSMCs to either TPr agonists, IBOP and U46619, or exogenous hydrogen peroxide (H2O2) caused time- and dose-dependent AMPK activation, as evidenced by increased phosphorylation of both AMPK-Thr172 and acetyl-coenzyme A carboxylase-Ser79, a downstream enzyme of AMPK, whereas SQ29548, a selective TPr antagonist, significantly attenuated TPr-enhanced AMPK activation. |
| 1842 | 18063812 | Furthermore, adenoviral overexpression of catalase (an H2O2 scavenger) abolished, whereas superoxide dismutase (which catalyzes H2O2 formation) enhanced, IBOP-induced AMPK activation, suggesting that TPr-activated AMPK was mediated by H2O2. |
| 1843 | 18063812 | Consistently, exposure of VSMCs to either TPr agonists or exogenous H2O2 dose-dependently increased the phosphorylation of LKB1 (at serines 428 and 307), an AMPK kinase, as well as coimmunoprecipitation of AMPK with LKB1. |
| 1844 | 18063812 | In addition, direct mutagenesis of either Ser428 or Ser307 of LKB1 into alanine, like the kinase-dead LKB1 mutant, abolished both TPr-stimulated AMPK activation and coimmunoprecipitation. |
| 1845 | 18063812 | We conclude that TPr stimulation triggers reactive oxygen species-mediated LKB1-dependent AMPK activation, which in return inhibits cellular protein synthesis in VSMCs. |
| 1846 | 18066100 | This study aimed to investigate the interrelationship of plasma lipid profile, lipid peroxidation, and erythrocyte antioxidative defense in patients with insulin-dependent (IDDM) and non-insulin-dependent (NIDDM) diabetes mellitus. |
| 1847 | 18066100 | Plasma levels of total cholesterol, triglycerides, and lipid peroxides and the activities of copper, zinc superoxide dismutase (CuZnSOD), catalase, glutathione peroxidase (GSH-Px), as well as the amount of glutathione in erythrocytes, were determined in IDDM, NIDDM, and nondiabetic control subjects. |
| 1848 | 18079207 | To evaluate the biochemical basis of this phenomenon, we aimed to identify defects of the NO/cGMP/cGMP-dependent protein kinase (PKG) pathway in cultured vascular smooth muscle cells (VSMCs) from OZR and lean Zucker rats (LZR) by measuring: 1) NO donor ability to increase cGMP in the absence and presence of inhibitors of soluble guanylate cyclase (sGC) and phosphodiesterases (PDEs); 2) NO and cGMP ability to induce, via PKG, vasodilator-stimulated phosphoprotein (VASP) phosphorylation at serine 239 and PDE5 activity; 3) protein expression of sGC, PKG, total VASP, and PDE5; 4) superoxide anion concentrations and ability of antioxidants (superoxide dismutase+catalase and amifostine) to influence the NO/cGMP/PKG pathway activation; and 5) hydrogen peroxide influence on PDE5 activity and VASP phosphorylation. |
| 1849 | 18079207 | LZR showed: 1) baseline cGMP concentrations higher, at least in part owing to reduced catabolism by PDEs; 2) impairment of NO donor ability to increase cGMP, even in the presence of PDE inhibitors, suggesting a defect in the NO-induced sGC activation; 3) reduction of NO and cGMP ability to activate PKG, indicated by the impaired ability to phosphorylate VASP at serine 239 and to increase PDE5 activity via PKG; 4) similar baseline protein expression of sGC, PKG, total VASP, and PDE5; and 5) higher levels of superoxide anion. |
| 1850 | 18191078 | At the end of the experimental period, lipid peroxidation, superoxide dismutase (SOD), and inducible NOS (iNOS) and endothelial NOS (eNOS) distribution were evaluated. |
| 1851 | 18191078 | Oxidative stress decreased with ALA in diabetic animals, and SOD also increased with ALA. iNOS and eNOS increased in diabetic animals, and ALA prevented iNOS increment in lung tissues. |
| 1852 | 18191078 | At the end of the experimental period, lipid peroxidation, superoxide dismutase (SOD), and inducible NOS (iNOS) and endothelial NOS (eNOS) distribution were evaluated. |
| 1853 | 18191078 | Oxidative stress decreased with ALA in diabetic animals, and SOD also increased with ALA. iNOS and eNOS increased in diabetic animals, and ALA prevented iNOS increment in lung tissues. |
| 1854 | 18206121 | Even though the free radical scavenging enzymes such as superoxide dismutase (SOD) and catalase can handle huge amounts of reactive oxygen species, should these systems fail some reactive molecules will evade the detoxification process and damage potential targets. |
| 1855 | 18277391 | Mitochondrial oxidative damage and antioxidant defence were also considered by measuring lipid peroxidation, aconitase and superoxide dismutase (SOD) specific activity. |
| 1856 | 18291430 | In addition, E2 enhanced superoxide dismutase (SOD), catalase (CAT) and glutathione peroxidase (GPX) (by 207, 52 and 72%, respectively, as compared to diabetic rats), reduced lipid peroxidation in the hepatic tissue (by 54%) and improved the liver dysfunction parameters by the significant decrease of gamma-glytamyl transferase (GGT), phosphatases alkalines (PAL), lactate deshydrogenase (LDH) and aspartate and lactate transaminases (AST and ALT) activities which increased in diabetic rats. |
| 1857 | 18292963 | The results suggest that diabetes-induced oxidative stress parallels an increase in NADPH oxidase-4 (NOX-4) and decrease in superoxide dismutase-1, 2 (SOD-1, 2) expression, in mitochondrial compartment. |
| 1858 | 18292963 | We observed loss of mitochondrial membrane permeability as evidenced by leakage of mitochondrial cytochrome c and prohibitin to the cytosol. |
| 1859 | 18339714 | Superoxide destabilization of beta-catenin augments apoptosis of high-glucose-stressed mesangial cells. |
| 1860 | 18339714 | Although reactive oxygen radicals and Wnt signaling components are potent regulators that modulate renal tissue remodeling and morphogenesis, cross-talk between oxidative stress and Wnt/beta-catenin signaling in controlling high-glucose-impaired mesangial cell survival and renal function have not been tested. |
| 1861 | 18339714 | In this study, high glucose induced Ras and Rac1 activation, superoxide burst, and Wnt5a/beta-catenin destabilization and subsequently promoted caspase-3 and poly (ADP-ribose) polymerase cleavage and apoptosis in mesangial cell cultures. |
| 1862 | 18339714 | The pharmacological and genetic suppression of superoxide synthesis by superoxide dismutase and diphenyloniodium, dominant-negative Ras (S17N), and dominant-negative Rac1 (T17N) abrogated high-glucose-induced glycogen synthase kinase (GSK-3beta) activation and caspase-3 and poly (ADP-ribose) polymerase degradation. |
| 1863 | 18339714 | Inactivation of Ras and Racl also reversed Wnt/beta-catenin expression and survival of mesangial cells. |
| 1864 | 18339714 | Stabilization of beta-catenin by the transfection of stable beta-catenin (Delta45) and kinase-inactive GSK-3beta attenuated high-glucose-mediated mesangial cell apoptosis. |
| 1865 | 18339714 | Immunohistological observation revealed that superoxide dismutase treatment abrogated diabetes-induced caspase-3 cleavage and terminal deoxynucleotidyl transferase-mediated deoxyuridine triphosphate-biotin nick end-labeling (TUNEL) and increased Wnt5a/beta-catenin expression in renal glomeruli. |
| 1866 | 18339714 | The Ras and Rac1 regulation of superoxide appeared to raise apoptotic activity by activating GSK-3beta and inhibiting Wnt5a/beta-catenin signaling. |
| 1867 | 18339714 | Controlling oxidative stress and Wnt/beta-catenin signaling has potential for protecting renal tissue against the deleterious effect of high glucose. |
| 1868 | 18339714 | Superoxide destabilization of beta-catenin augments apoptosis of high-glucose-stressed mesangial cells. |
| 1869 | 18339714 | Although reactive oxygen radicals and Wnt signaling components are potent regulators that modulate renal tissue remodeling and morphogenesis, cross-talk between oxidative stress and Wnt/beta-catenin signaling in controlling high-glucose-impaired mesangial cell survival and renal function have not been tested. |
| 1870 | 18339714 | In this study, high glucose induced Ras and Rac1 activation, superoxide burst, and Wnt5a/beta-catenin destabilization and subsequently promoted caspase-3 and poly (ADP-ribose) polymerase cleavage and apoptosis in mesangial cell cultures. |
| 1871 | 18339714 | The pharmacological and genetic suppression of superoxide synthesis by superoxide dismutase and diphenyloniodium, dominant-negative Ras (S17N), and dominant-negative Rac1 (T17N) abrogated high-glucose-induced glycogen synthase kinase (GSK-3beta) activation and caspase-3 and poly (ADP-ribose) polymerase degradation. |
| 1872 | 18339714 | Inactivation of Ras and Racl also reversed Wnt/beta-catenin expression and survival of mesangial cells. |
| 1873 | 18339714 | Stabilization of beta-catenin by the transfection of stable beta-catenin (Delta45) and kinase-inactive GSK-3beta attenuated high-glucose-mediated mesangial cell apoptosis. |
| 1874 | 18339714 | Immunohistological observation revealed that superoxide dismutase treatment abrogated diabetes-induced caspase-3 cleavage and terminal deoxynucleotidyl transferase-mediated deoxyuridine triphosphate-biotin nick end-labeling (TUNEL) and increased Wnt5a/beta-catenin expression in renal glomeruli. |
| 1875 | 18339714 | The Ras and Rac1 regulation of superoxide appeared to raise apoptotic activity by activating GSK-3beta and inhibiting Wnt5a/beta-catenin signaling. |
| 1876 | 18339714 | Controlling oxidative stress and Wnt/beta-catenin signaling has potential for protecting renal tissue against the deleterious effect of high glucose. |
| 1877 | 18343213 | HG and AGEs had no effects on ECs morphology and inflammatory states as measured by vascular cell adhesion molecule (VCAM)-1 and cyclooxygenase (COX)-2 expressions. |
| 1878 | 18343213 | GO (500muM, 24h) induced cytotoxic morphological changes and protein expression of COX-2 but not VCAM-1. |
| 1879 | 18343213 | GO (500muM, 24h) activated ERK but not JNK, p38 or NF-kappaB. |
| 1880 | 18343213 | However, ERK inhibitor PD98059 was ineffective to GO-induced COX-2. |
| 1881 | 18343213 | While EUK134, synthetic combined superoxide dismutase/catalase mimetic, had no effect on GO-mediated inflammation, sodium nitroprusside inhibited it. |
| 1882 | 18377884 | Then, several key antioxidants such as superoxide dismutase (SOD), reduced glutathione (GSH), catalase (CAT) and the pancreatic exocrine enzyme amylase (AMS) were measured. |
| 1883 | 18387670 | We measured mRNA levels of superoxide dismutase (SOD), catalase (CAT), glutathione peroxidase (GPX), Bcl-2 associated X protein (Bax), B-cell lymphoma protein (Bcl-2), tumor suppressor protein-53 (p53), paired box protein-3 (Pax-3) and vascular endothelial growth factor-A (Vegf-A). |
| 1884 | 18387670 | Moreover, we found that maternal diabetes causes decreased expression of genes involved in the oxidative stress defense system (CuZnSOD in non-malformed D11 embryos, MnSOD at all gestational time points, ECSOD and Gpx-1 at GD11-GD15, CAT and Gpx-2 at GD15), decreased expression of Pax-3 at GD11, and increased expression of Vegf-A at all gestational time points. |
| 1885 | 18387839 | Effects of an oral superoxide dismutase enzyme supplementation on indices of oxidative stress, proviral load, and CD4:CD8 ratios in asymptomatic FIV-infected cats. |
| 1886 | 18387839 | The CD4+ to CD8+ ratio increased significantly (0.66-0.88) in the SOD supplemented FIV-infected cats but not in the unsupplemented FIV-infected cats. |
| 1887 | 18387839 | Effects of an oral superoxide dismutase enzyme supplementation on indices of oxidative stress, proviral load, and CD4:CD8 ratios in asymptomatic FIV-infected cats. |
| 1888 | 18387839 | The CD4+ to CD8+ ratio increased significantly (0.66-0.88) in the SOD supplemented FIV-infected cats but not in the unsupplemented FIV-infected cats. |
| 1889 | 18398869 | Hepatic glucokinase activity was significantly higher in the curcumin-supplemented db/db group than in the db/db group, whereas glucose-6-phosphatase and phosphoenolpyruvate carboxykinase activities were significantly lower. |
| 1890 | 18398869 | Curcumin normalized erythrocyte and hepatic antioxidant enzyme activities (superoxide dismutase, catalase, gluthathione peroxidase) in db/db mice that resulted in a significant reduction in lipid peroxidation. |
| 1891 | 18404309 | Postprandial blood glucose levels, malondialdehyde, reduced glutathione (GSH), nitrate, nitrite, ascorbic acid, retinol, beta-carotene, superoxide dismutase, and catalase levels were measured, and immunohistochemical studies were performed in all of the groups. |
| 1892 | 18413155 | The effects of sulfonylurea glyburide on superoxide dismutase, catalase, and glutathione peroxidase activities in the brain tissue of streptozotocin-induced diabetic rat. |
| 1893 | 18414053 | Resveratrol has also been shown to activate various transcription factor (e.g; NFkappaB, STAT3, HIF-1alpha, beta-catenin and PPAR-gamma), suppress the expression of antiapoptotic gene products (e.g; Bcl-2, Bcl-X(L), XIAP and survivin), inhibit protein kinases (e.g; src, PI3K, JNK, and AKT), induce antioxidant enzymes (e,g; catalase, superoxide dismutase and hemoxygenase-1), suppress the expression of inflammatory biomarkers (e.g., TNF, COX-2, iNOS, and CRP), inhibit the expression of angiogenic and metastatic gene products (e.g., MMPs, VEGF, cathepsin D, and ICAM-1), and modulate cell cycle regulatory genes (e.g., p53, Rb, PTEN, cyclins and CDKs). |
| 1894 | 18418439 | To assess the level of myocardial reactive oxygen species, we measured malondialdehyde, a surrogate marker of oxidative stress, which was increased in the hearts of NTG and Gsalpha diabetic mice. |
| 1895 | 18418439 | In addition, chronic hyperglycemia also increased the activity of catalase and superoxide dismutase in the hearts of NTG and Gsalpha diabetic mice. |
| 1896 | 18418439 | Hearts of NTG diabetic mice, but not Gsalpha mice, showed increased expression of proapoptosis Bax, downregulation in Bcl2, and an increase in the Bax/Bcl2 ratio. |
| 1897 | 18437679 | We used immunohistochemistry to evaluate parameters of oxidative stress (superoxide dismutase [SOD]) and inducible nitric oxide synthase (iNOS) protein expression. |
| 1898 | 18437679 | Our results indicated that A) Diabetic myocardium appears more vulnerable to ischemia/reperfusion damage concerning ultrastructure of cardiomyocytes (sarcomeres, vacuoles, mitochondria), expression of antioxidative enzymes (CuZnSOD, MnSOD), and iNOS than normal myocardium; B) Pre-treatment of diabetic myocardium with EGb and additional ischemia/reperfusion leads to a relative improvement in myocardial ultrastructure compared to unprotected myocardium. |
| 1899 | 18514628 | We investigated the effects of a specific oral mixture of amino acid (AA) supplements on the antioxidant defense system, superoxide dismutase (SOD), and heat shock proteins (HSPs: HspB1, similar to Hsp 20 kDa, and HspB7) in the soleus muscle of streptozotocin (STZ)-diabetic mice by bidimensional electrophoresis and mass spectrometry. |
| 1900 | 18514628 | AA supplements in the nondiabetic animals were associated with a statistical increase of SOD and no changes in expression of HSPs. |
| 1901 | 18514628 | Diabetes mellitus decreased antioxidant SOD and increased cellular stress as demonstrated by the overall upregulated HSPs. |
| 1902 | 18514628 | Administration of AAs counteracted the effects of diabetes, producing upregulation of SOD and downregulation of HSPs. |
| 1903 | 18514628 | We investigated the effects of a specific oral mixture of amino acid (AA) supplements on the antioxidant defense system, superoxide dismutase (SOD), and heat shock proteins (HSPs: HspB1, similar to Hsp 20 kDa, and HspB7) in the soleus muscle of streptozotocin (STZ)-diabetic mice by bidimensional electrophoresis and mass spectrometry. |
| 1904 | 18514628 | AA supplements in the nondiabetic animals were associated with a statistical increase of SOD and no changes in expression of HSPs. |
| 1905 | 18514628 | Diabetes mellitus decreased antioxidant SOD and increased cellular stress as demonstrated by the overall upregulated HSPs. |
| 1906 | 18514628 | Administration of AAs counteracted the effects of diabetes, producing upregulation of SOD and downregulation of HSPs. |
| 1907 | 18514628 | We investigated the effects of a specific oral mixture of amino acid (AA) supplements on the antioxidant defense system, superoxide dismutase (SOD), and heat shock proteins (HSPs: HspB1, similar to Hsp 20 kDa, and HspB7) in the soleus muscle of streptozotocin (STZ)-diabetic mice by bidimensional electrophoresis and mass spectrometry. |
| 1908 | 18514628 | AA supplements in the nondiabetic animals were associated with a statistical increase of SOD and no changes in expression of HSPs. |
| 1909 | 18514628 | Diabetes mellitus decreased antioxidant SOD and increased cellular stress as demonstrated by the overall upregulated HSPs. |
| 1910 | 18514628 | Administration of AAs counteracted the effects of diabetes, producing upregulation of SOD and downregulation of HSPs. |
| 1911 | 18514628 | We investigated the effects of a specific oral mixture of amino acid (AA) supplements on the antioxidant defense system, superoxide dismutase (SOD), and heat shock proteins (HSPs: HspB1, similar to Hsp 20 kDa, and HspB7) in the soleus muscle of streptozotocin (STZ)-diabetic mice by bidimensional electrophoresis and mass spectrometry. |
| 1912 | 18514628 | AA supplements in the nondiabetic animals were associated with a statistical increase of SOD and no changes in expression of HSPs. |
| 1913 | 18514628 | Diabetes mellitus decreased antioxidant SOD and increased cellular stress as demonstrated by the overall upregulated HSPs. |
| 1914 | 18514628 | Administration of AAs counteracted the effects of diabetes, producing upregulation of SOD and downregulation of HSPs. |
| 1915 | 18543386 | The rats treated with S. baicalensis and metformin + S. baicalensis had elevated hepatic activities of the antioxidant enzymes--superoxide dismutase (SOD), catalase (CAT), and glutathione peroxidase (GPx) compared to the vehicle- and metformin-treated diabetic groups (p < 0.05). |
| 1916 | 18544912 | In the diabetic liver, the activities of superoxide dismutase (SOD), catalase and ATP levels decreased, and the microsomal CYP2E1 activity increased. |
| 1917 | 18557423 | In diabetic animals, an increase in the activity of anti-oxidative enzymes: superoxide dismutase (Cu,Zn-SOD), catalase (CAT), glutathione peroxidase (GSH-Px) and glutathione reductase (GSSG-R), and in the level of glutathione (GSH) but a decrease in the level of ascorbic acid (AA) were observed. |
| 1918 | 18563351 | The levels of malondialdehyde, protein carbonyl and nitric oxide with activities of xanthine oxidase and myeloperoxidase were increased in liver tissues of diabetic and non-diabetic IR groups. |
| 1919 | 18563351 | The activities of catalase and superoxide dismutase were increased in IR groups in comparison with control and DM. |
| 1920 | 18585396 | Non-protein thiol levels and enzymatic activities of superoxide dismutase and catalase were decreased in both cerebral cortex and hippocampal regions of diabetic rat brain. |
| 1921 | 18586837 | In this study, these effects, and the protective effects of pigment epithelium-derived factor (PEDF), were defined in a primary human pericyte model. |
| 1922 | 18586837 | To assess pro-inflammatory effects, monocyte chemoattractant protein-1 (MCP-1) secretion was measured by ELISA, and nuclear factor-kappaB (NF-kappaB) activation was detected by immunocytochemistry. |
| 1923 | 18586837 | The results showed that MCP-1 was significantly increased by HOG-LDL, and the effect was attenuated by PEDF in a dose-dependent manner. |
| 1924 | 18586837 | PEDF also attenuated the HOG-LDL-induced NF-kappaB activation, suggesting that the inhibitory effect of PEDF on MCP-1 was at least partially through the blockade of NF-kappaB activation. |
| 1925 | 18586837 | Moreover, PEDF significantly ameliorated HOG-LDL-induced ROS generation through up-regulation of superoxide dismutase 1 expression. |
| 1926 | 18586837 | Suppressing MCP-1 production and thus inhibiting macrophage recruitment may represent a new mechanism for the salutary effect of PEDF in diabetic retinopathy and warrants more studies in future. |
| 1927 | 18621448 | In the diabetic group, a decrease in the pancreatic glutathione levels, glutathione peroxidase and superoxide dismutase activities and an increase in the pancreatic lipid peroxidation level and catalase activities were observed. |
| 1928 | 18633101 | Elevated toll-like receptor 4 expression and signaling in muscle from insulin-resistant subjects. |
| 1929 | 18633101 | However, it is not known whether insulin-resistant subjects have abnormal TLR4 signaling. |
| 1930 | 18633101 | We examined whether insulin-resistant subjects have abnormal TLR4 expression and TLR4-driven (IkappaB/NFkappaB) signaling in skeletal muscle. |
| 1931 | 18633101 | TLR4 muscle protein content correlated with the severity of insulin resistance. |
| 1932 | 18633101 | The increase in TLR4 and NFkappaB signaling was accompanied by elevated expression of the NFkappaB-regulated genes interleukin (IL)-6 and superoxide dismutase (SOD)2. |
| 1933 | 18633101 | Increased TLR4 content and gene expression observed in muscle from insulin-resistant subjects were reproduced by treating myotubes from lean, normal-glucose-tolerant subjects with palmitate. |
| 1934 | 18633101 | Palmitate also increased IL-6 and SOD2 gene expression, and this effect was prevented by inhibiting NFkappaB. |
| 1935 | 18633101 | CONCLUSIONS- Abnormal TLR4 expression and signaling, possibly caused by elevated plasma FFA levels, may contribute to the pathogenesis of insulin resistance in humans. |
| 1936 | 18669160 | Dyslipidemia and insulin resistance in obese LDL receptor-deficient mice were associated with increased oxidative stress and impaired HDL-associated antioxidant defence associated with accelerated atherosclerosis due to increased macrophage infiltration and accumulation of oxidized LDL in the aorta. |
| 1937 | 18669160 | Weight loss in leptin-deficient, obese, and insulin-resistant mice was associated with expressional changes of key genes regulating adipocyte differentiation, glucose transport and insulin sensitivity, lipid metabolism, oxidative stress and inflammation, most of which are under the transcriptional control of PPARs. |
| 1938 | 18669160 | We established an important relationship between PPAR-gamma and SOD1 for the prevention of the oxidation of LDL in the arterial wall. |
| 1939 | 18669160 | For example we showed that rosuvastatin decreased the oxidized LDL accumulation by increasing the expression of PPAR-gamma and SOD1. |
| 1940 | 18669160 | Oxidized LDL correlated positively with the expression of IRF1 and TLR2 suggesting a relation between oxidative stress and inflammation in coronary atherosclerotic plaques. |
| 1941 | 18669160 | Oxidized LDL induced further the expression of TLR2 and IRF1 in macrophages in vitro suggesting a causative link. |
| 1942 | 18669160 | We showed that TLR2, CXCR4 and MYC are overexpressed in monocytes of obese women at high cardiovascular risk and that weight loss was associated with a concomitant decrease of their expression. |
| 1943 | 18669160 | The increased expression of TLR2 and CXCR4 were observed in the absence of an increase in ox-LDL but in the presence of an increase in SOD1. |
| 1944 | 18669160 | We identified paraoxonase, interferon regulatory factor-1, toll-like receptors, CXCR4 and SOD1 as possible targets for intervention. |
| 1945 | 18669160 | Dyslipidemia and insulin resistance in obese LDL receptor-deficient mice were associated with increased oxidative stress and impaired HDL-associated antioxidant defence associated with accelerated atherosclerosis due to increased macrophage infiltration and accumulation of oxidized LDL in the aorta. |
| 1946 | 18669160 | Weight loss in leptin-deficient, obese, and insulin-resistant mice was associated with expressional changes of key genes regulating adipocyte differentiation, glucose transport and insulin sensitivity, lipid metabolism, oxidative stress and inflammation, most of which are under the transcriptional control of PPARs. |
| 1947 | 18669160 | We established an important relationship between PPAR-gamma and SOD1 for the prevention of the oxidation of LDL in the arterial wall. |
| 1948 | 18669160 | For example we showed that rosuvastatin decreased the oxidized LDL accumulation by increasing the expression of PPAR-gamma and SOD1. |
| 1949 | 18669160 | Oxidized LDL correlated positively with the expression of IRF1 and TLR2 suggesting a relation between oxidative stress and inflammation in coronary atherosclerotic plaques. |
| 1950 | 18669160 | Oxidized LDL induced further the expression of TLR2 and IRF1 in macrophages in vitro suggesting a causative link. |
| 1951 | 18669160 | We showed that TLR2, CXCR4 and MYC are overexpressed in monocytes of obese women at high cardiovascular risk and that weight loss was associated with a concomitant decrease of their expression. |
| 1952 | 18669160 | The increased expression of TLR2 and CXCR4 were observed in the absence of an increase in ox-LDL but in the presence of an increase in SOD1. |
| 1953 | 18669160 | We identified paraoxonase, interferon regulatory factor-1, toll-like receptors, CXCR4 and SOD1 as possible targets for intervention. |
| 1954 | 18669160 | Dyslipidemia and insulin resistance in obese LDL receptor-deficient mice were associated with increased oxidative stress and impaired HDL-associated antioxidant defence associated with accelerated atherosclerosis due to increased macrophage infiltration and accumulation of oxidized LDL in the aorta. |
| 1955 | 18669160 | Weight loss in leptin-deficient, obese, and insulin-resistant mice was associated with expressional changes of key genes regulating adipocyte differentiation, glucose transport and insulin sensitivity, lipid metabolism, oxidative stress and inflammation, most of which are under the transcriptional control of PPARs. |
| 1956 | 18669160 | We established an important relationship between PPAR-gamma and SOD1 for the prevention of the oxidation of LDL in the arterial wall. |
| 1957 | 18669160 | For example we showed that rosuvastatin decreased the oxidized LDL accumulation by increasing the expression of PPAR-gamma and SOD1. |
| 1958 | 18669160 | Oxidized LDL correlated positively with the expression of IRF1 and TLR2 suggesting a relation between oxidative stress and inflammation in coronary atherosclerotic plaques. |
| 1959 | 18669160 | Oxidized LDL induced further the expression of TLR2 and IRF1 in macrophages in vitro suggesting a causative link. |
| 1960 | 18669160 | We showed that TLR2, CXCR4 and MYC are overexpressed in monocytes of obese women at high cardiovascular risk and that weight loss was associated with a concomitant decrease of their expression. |
| 1961 | 18669160 | The increased expression of TLR2 and CXCR4 were observed in the absence of an increase in ox-LDL but in the presence of an increase in SOD1. |
| 1962 | 18669160 | We identified paraoxonase, interferon regulatory factor-1, toll-like receptors, CXCR4 and SOD1 as possible targets for intervention. |
| 1963 | 18702952 | The activities of the antioxidant enzymes superoxide dismutase and catalase were measured. |
| 1964 | 18702952 | Oxidative damage was evaluated by measuring lipid peroxidation and protein oxidation. (1) In all animals fed HSD, the levels of LMWAs were decreased in most organs, although not plasma. (2) A significant difference was consistently found in antioxidant enzymes' activities in the pancreas of HSD-fed CDs rats, but not in other tissues. (3) The activities of superoxide dismutase and catalase and the levels of malondialdehyde and protein carbonyl group increased, whereas the levels of LMWAs decreased, in the pancreas of HSD-fed CDs rats. |
| 1965 | 18702952 | The activities of the antioxidant enzymes superoxide dismutase and catalase were measured. |
| 1966 | 18702952 | Oxidative damage was evaluated by measuring lipid peroxidation and protein oxidation. (1) In all animals fed HSD, the levels of LMWAs were decreased in most organs, although not plasma. (2) A significant difference was consistently found in antioxidant enzymes' activities in the pancreas of HSD-fed CDs rats, but not in other tissues. (3) The activities of superoxide dismutase and catalase and the levels of malondialdehyde and protein carbonyl group increased, whereas the levels of LMWAs decreased, in the pancreas of HSD-fed CDs rats. |
| 1967 | 18716028 | However, miR-377 led to reduced expressions of p21-activated kinase and superoxide dismutase, which enhanced fibronectin protein production. |
| 1968 | 18723759 | Endothelial dysfunction was reversed by addition of superoxide dismutase or the NADPH oxidase inhibitor apocynin. |
| 1969 | 18723759 | An increase in superoxide production and increased expression of the NADPH oxidase regulatory subunit p47(phox) were also found in pulmonary arteries from diabetic rats. |
| 1970 | 18726685 | Extracellular superoxide dismutase (EC-SOD) is the main SOD isoform in the arterial wall contributing to cardiovascular defense against oxidative stress by removing the superoxide anion. |
| 1971 | 18726685 | In our study, the Thr40Ala and Arg213Gly polymorphic variants of the EC-SOD gene (SOD ( 3 )) were investigated for associations with atherosclerosis and other related factors in 144 subjects with significant atheroma (having one, two, or three major coronary arteries with >50% obstruction, and/or peripheral artery lesions, and/or carotid artery stenosis demonstrated by angiography and echography) and in 150 subjects with no significant atheroma. |
| 1972 | 18726685 | Extracellular superoxide dismutase (EC-SOD) is the main SOD isoform in the arterial wall contributing to cardiovascular defense against oxidative stress by removing the superoxide anion. |
| 1973 | 18726685 | In our study, the Thr40Ala and Arg213Gly polymorphic variants of the EC-SOD gene (SOD ( 3 )) were investigated for associations with atherosclerosis and other related factors in 144 subjects with significant atheroma (having one, two, or three major coronary arteries with >50% obstruction, and/or peripheral artery lesions, and/or carotid artery stenosis demonstrated by angiography and echography) and in 150 subjects with no significant atheroma. |
| 1974 | 18797155 | Serum glucose, glycated hemoglobin, advanced glycation end products (AGEs), and tissue malondialdehyde (MDA) and superoxide dismutase (SOD) were determined. |
| 1975 | 18800899 | Induction of diabetes mellitus in rats caused an increase in blood lipid peroxide levels that was associated with the reduced activity of red blood cell (RBC) antioxidant enzymes--namely, superoxide dismutase, catalase, glutathione reductase, and glutathione peroxidase--along with depletion of plasma reduced glutathione (GSH) and copper, zinc, iron, magnesium, and selenium levels. |
| 1976 | 18800902 | Changes in antioxidant status were evaluated by determining catalase (CAT) and superoxide dismutase (SOD) activities and the level of reduced glutathione (GSH) in pancreatic tissue. |
| 1977 | 18800902 | The diabetic rats also exhibited pancreatic GSH depletion along with significant reductions in activities of CAT and SOD. |
| 1978 | 18800902 | Rats treated with T. polium extract had significantly higher GSH levels along with enhanced CAT and SOD activities in pancreatic tissue. |
| 1979 | 18800902 | Changes in antioxidant status were evaluated by determining catalase (CAT) and superoxide dismutase (SOD) activities and the level of reduced glutathione (GSH) in pancreatic tissue. |
| 1980 | 18800902 | The diabetic rats also exhibited pancreatic GSH depletion along with significant reductions in activities of CAT and SOD. |
| 1981 | 18800902 | Rats treated with T. polium extract had significantly higher GSH levels along with enhanced CAT and SOD activities in pancreatic tissue. |
| 1982 | 18800902 | Changes in antioxidant status were evaluated by determining catalase (CAT) and superoxide dismutase (SOD) activities and the level of reduced glutathione (GSH) in pancreatic tissue. |
| 1983 | 18800902 | The diabetic rats also exhibited pancreatic GSH depletion along with significant reductions in activities of CAT and SOD. |
| 1984 | 18800902 | Rats treated with T. polium extract had significantly higher GSH levels along with enhanced CAT and SOD activities in pancreatic tissue. |
| 1985 | 18802743 | This was accompanied by decrease in glutathione and total thiol content along with decrease in the activities of superoxide dismutase, catalase and glutathione reductase. |
| 1986 | 18813861 | Therefore, we directly investigated exercise training to determine whether it was able to ameliorate the molecular pathogenic phenotypes in the brain using a neuron-specific enolase (NSE)/Swedish mutation of amyloid precursor protein (APPsw) transgenic (Tg) mice as a novel AD model. |
| 1987 | 18813861 | The results indicated (i) that amyloid beta-42 (Abeta-42) peptides were significantly decreased in the NSE/APPsw Tg mice following exercise training; (ii) that exercise training inhibited the apoptotic biochemical cascades, including cytochrome c, caspase-9, caspase-3 and Bax; (iii) that the glucose transporter-1 (GLUT-1) and brain-derived neurotrophic factor (BDNF) proteins induced by exercise training protected the neurons from injury by inducing the concomitant expression of genes that encode proteins such as superoxide dismutase-1 (SOD-1), catalase and Bcl-2, which suppress oxidative stress and excitotoxic injury; (iv) that heat-shock protein-70 (HSP-70) and glucose-regulated protein-78 (GRP-78) were significantly increased in the exercise (EXE) group when compared to the sedentary (SED) group, and that these proteins may benefit the brain by making it more resistant to stress-induced neuron cell damage; (v) and that exercise training contributed to the restoration of normal levels of serum total cholesterol, insulin and glucose. |
| 1988 | 18814208 | However, there was a decrease in serum concentration of thyroid hormones and in the endogenous antioxidant enzymes, such as superoxide dismutase (SOD), catalase (CAT) and reduced glutathione (GSH) in liver. |
| 1989 | 18814208 | Dexamethasone-induced alterations in the levels of thyroid hormones as well as in hepatic LPO, SOD, CAT and GSH were also reversed by the plant extract. |
| 1990 | 18814208 | However, there was a decrease in serum concentration of thyroid hormones and in the endogenous antioxidant enzymes, such as superoxide dismutase (SOD), catalase (CAT) and reduced glutathione (GSH) in liver. |
| 1991 | 18814208 | Dexamethasone-induced alterations in the levels of thyroid hormones as well as in hepatic LPO, SOD, CAT and GSH were also reversed by the plant extract. |
| 1992 | 18814490 | Forty days of orally feeding the aqueous E. ribes extract (100 and 200 mg/kg) to streptozotocin (40 mg/kg, iv, single dose) induced diabetic rats produced significant decrease in heart rate, systolic blood pressure, blood glucose, blood glycosylated hemoglobin, serum lactate dehydrogenase, creatine kinase and increase in blood glutathione levels as compared to pathogenic diabetic rats. |
| 1993 | 18814490 | Further, the extract significantly decreased the levels of pancreatic lipid peroxides and increased the levels of pancreatic superoxide dismutase, catalase and glutathione. |
| 1994 | 18830445 | This was accompanied by a significant increase in reduced glutathione and superoxide dismutase activity and a decrease in catalase activity and in the total antioxidant capacity of the kidneys. |
| 1995 | 18830445 | In addition, B. oleracea extract attenuated the adverse effect of diabetes on malondialdehyde, glutathione and superoxide dismutase activity as well as catalase activity and total antioxidant capacity of diabetic kidneys. |
| 1996 | 18830445 | This was accompanied by a significant increase in reduced glutathione and superoxide dismutase activity and a decrease in catalase activity and in the total antioxidant capacity of the kidneys. |
| 1997 | 18830445 | In addition, B. oleracea extract attenuated the adverse effect of diabetes on malondialdehyde, glutathione and superoxide dismutase activity as well as catalase activity and total antioxidant capacity of diabetic kidneys. |
| 1998 | 18842828 | Methylglyoxal mediates vascular inflammation via JNK and p38 in human endothelial cells. |
| 1999 | 18842828 | MGO induced mRNA and protein expression of cyclooxygenase (COX)-2 in a concentration (0-420 microM)- and time (6-24 h)-dependent manner. |
| 2000 | 18842828 | Acute treatment with MGO (20 min) induced concentration-dependent (0-420 microM) activation of JNK and p38 MAP kinase but not ERK or NF-kappaB. |
| 2001 | 18842828 | Both the JNK inhibitor SP600125 and the p38 inhibitor SB203580 prevented the MGO induction of COX-2. |
| 2002 | 18842828 | However, inhibiting JNK and p38 or COX-2 was ineffective to the morphological damage by MGO (420 microM, 24 h). |
| 2003 | 18842828 | EUK134, a synthetic combined superoxide dismutase/catalase mimetic, had no effect on MGO-induced COX-2. |
| 2004 | 18842828 | Present results indicated that MGO mediates JNK- and p38-dependent EC inflammatory responses, which might be independent of oxidative stress. |
| 2005 | 18850202 | Downstream targets of this pathway include genes that encode antioxidative enzymes such as Superoxide dismutase (SOD) whose transcription is activated when receptor activation by insulin/IGF is low or when sirtuins are active and the ability of cells to resist oxidative damage appears to determine their life span. |
| 2006 | 18997283 | While in alloxan treated animals, an increase in the concentration of serum glucose with a parallel decrease in insulin level was observed, administration of 15 mg/kg/day of isolated quercetin-3-O-glucoside for 10 consecutive days to the hyperglycemic animals reversed these effects and simultaneously inhibited the activity of hepatic glucose-6-phosphatase. |
| 2007 | 18997283 | It further decreased the hepatic and renal LPO with a concomitant increase in the activities of antioxidative enzymes, such as catalase (CAT) and superoxide dismutase (SOD) and in glutathione (GSH) content, indicating its safe and antiperoxidative effects. |
| 2008 | 19001772 | The activity of catalase of the erythrocyte sample decreased in the XOS group, but not the activities of superoxide dismutase and glutathione peroxidase. |
| 2009 | 19010140 | Data were collected on oxidative parameters: malondialdehyde, glutathione peroxidase, catalase, superoxide dismutase, glutathione reductase, lipid profile, and renal function (creatinine concentration, Cockroft-Gault formula, and Modified Diet in Renal Disease study). |
| 2010 | 19027117 | We determined the plasma concentrations of kynurenine (KYN), kynurenic acid (KYNA) and quinolinic acid (QA); three distinct SOX markers: Cu/Zn superoxide dismutase (Cu/Zn SOD), total peroxide and malondialdehyde (MDA), high sensitivity C-reactive protein (hs CRP) as a indicator of inflammation, and intima-media thickness (IMT)--an early reflection of the systemic atherosclerosis in the population of 124 patients with ESRD. |
| 2011 | 19049670 | Superoxide dismutase and catalase activities in the ALR (230 +/- 13 and 131 +/- 15 U/mg protein) liver showed a marked increase when compared with the ALS liver (148 +/- 13 and 68 +/- 5 U/mg protein). |
| 2012 | 19074570 | We found that in untrained animals, the levels of TRX-1 (TRX1) protein and activity, and thioredoxin-interacting protein (TXNip) were similar in diabetic and nondiabetic animals. |
| 2013 | 19074570 | Exercise training, however, increased TRX1 protein in nondiabetic animals without affecting TXNip levels, whereas diabetes inhibited the effect of training on TRX1 protein and also increased TXNip mRNA. |
| 2014 | 19074570 | Both diabetes and exercise training decreased glutathione reductase (GRD) activity and cytosolic superoxide dismutase (Cu,Zn-SOD) levels. |
| 2015 | 19074570 | Nevertheless, diabetes or training had no effect on Cu,Zn-SOD mRNA, Mn-SOD protein, total SOD activity, or catalase mRNA, protein, or activity. |
| 2016 | 19074570 | Our findings suggest that exercise training increases TRX1 levels in brain without a concomitant rise in TXNip, and that experimental diabetes is associated with an incomplete TRX response to training. |
| 2017 | 19074570 | We found that in untrained animals, the levels of TRX-1 (TRX1) protein and activity, and thioredoxin-interacting protein (TXNip) were similar in diabetic and nondiabetic animals. |
| 2018 | 19074570 | Exercise training, however, increased TRX1 protein in nondiabetic animals without affecting TXNip levels, whereas diabetes inhibited the effect of training on TRX1 protein and also increased TXNip mRNA. |
| 2019 | 19074570 | Both diabetes and exercise training decreased glutathione reductase (GRD) activity and cytosolic superoxide dismutase (Cu,Zn-SOD) levels. |
| 2020 | 19074570 | Nevertheless, diabetes or training had no effect on Cu,Zn-SOD mRNA, Mn-SOD protein, total SOD activity, or catalase mRNA, protein, or activity. |
| 2021 | 19074570 | Our findings suggest that exercise training increases TRX1 levels in brain without a concomitant rise in TXNip, and that experimental diabetes is associated with an incomplete TRX response to training. |
| 2022 | 19076258 | A number of vectors have been used to insert genes to increase the expression of nitric oxide synthase, superoxide dismutase, maxi-K channel (hSlo), neurotrophin-3, and vasoactive intestinal polypeptide for the treatment of erectile function. |
| 2023 | 19130858 | Erythrocyte glutathione (GSH), superoxide dismutase (SOD) and thiobarbituric acid reactive substances (TBARS), plasma vitamins C and E and serum total glutathione-S-transferase (GST), protein thiols and ceruloplasmin (Cp) were estimated spectrophotometrically in maternal blood of age matched controls and mothers with GDM and also in cord blood samples of the above. |
| 2024 | 19130858 | There was a significant increase in the erythrocytic GSH, serum total GST and protein thiols in GDM maternal blood when compared to controls whereas erythrocytic SOD exhibited a marked decrease in GDM cases. |
| 2025 | 19130858 | Erythrocyte glutathione (GSH), superoxide dismutase (SOD) and thiobarbituric acid reactive substances (TBARS), plasma vitamins C and E and serum total glutathione-S-transferase (GST), protein thiols and ceruloplasmin (Cp) were estimated spectrophotometrically in maternal blood of age matched controls and mothers with GDM and also in cord blood samples of the above. |
| 2026 | 19130858 | There was a significant increase in the erythrocytic GSH, serum total GST and protein thiols in GDM maternal blood when compared to controls whereas erythrocytic SOD exhibited a marked decrease in GDM cases. |
| 2027 | 19148834 | Compared to the normoglycaemic group, the treatment of rats with a single dose of STZ (65 mg/kg body weight) revealed a significant increase (p<0.05) only in plasma hydrogen peroxide (H(2)O(2)), i.e. by 230%; it increased the thiobarbituric acid reactive substances (TBARS) as index of the lipid peroxidation level by 69%, while total antioxidant activity was decreased by 36%, with a consistently significant decrease (p<0.05) in the activity of erythrocytes antioxidative enzymes catalase (CAT), superoxide dismutase (SOD) and glutathione peroxidase (GPx). |
| 2028 | 19148834 | Exogenous administration of individual gradual doses of lycopene to hyperglycaemic rats causes a dose-dependent decrease in glucose level, an increase of insulin concentration, a decrease of H(2)O(2) and TBARS levels, as well as increased total antioxidant status with increased antioxidant enzyme activities (CAT, SOD and GPx) with improvement in serum lipid profile. |
| 2029 | 19148834 | Compared to the normoglycaemic group, the treatment of rats with a single dose of STZ (65 mg/kg body weight) revealed a significant increase (p<0.05) only in plasma hydrogen peroxide (H(2)O(2)), i.e. by 230%; it increased the thiobarbituric acid reactive substances (TBARS) as index of the lipid peroxidation level by 69%, while total antioxidant activity was decreased by 36%, with a consistently significant decrease (p<0.05) in the activity of erythrocytes antioxidative enzymes catalase (CAT), superoxide dismutase (SOD) and glutathione peroxidase (GPx). |
| 2030 | 19148834 | Exogenous administration of individual gradual doses of lycopene to hyperglycaemic rats causes a dose-dependent decrease in glucose level, an increase of insulin concentration, a decrease of H(2)O(2) and TBARS levels, as well as increased total antioxidant status with increased antioxidant enzyme activities (CAT, SOD and GPx) with improvement in serum lipid profile. |
| 2031 | 19168420 | Diabetes was induced with single intraperitoneal injection of streptozotocin (45 mg/kg, i.p) dissolved in freshly prepared citrate buffer (pH 4.5), resulted in elevation of blood glucose levels, decrease in the superoxide dismutase and catalase activity. |
| 2032 | 19170137 | It decreased serum triiodothyronine (T3), thyroxine (T4) and high-density lipoprotein cholesterol (HDL-C) levels as well as renal superoxide dismutase (SOD); catalase (CAT) and reduced glutathione (GSH) content. |
| 2033 | 19182373 | By using Escherichia coli mutant strains, we observed that cyclohexyl-DHP exposure strongly reduced the survival rate of a cytosolic sodium dodecyl sulfate (SOD)-deficient strain (sodA sodB), significantly reduced the survival rates of DNA repair-deficient strains (recA and uvrB) and mildly reduced the survival rate of a catalase-deficient strain (katE katG) compared with the survival rate of the wild-type strain. |
| 2034 | 19190261 | Since oxidative stress depletes adiponectin and insulin levels, we investigated whether an upregulated heme oxygenase (HO) system would attenuate the oxidative destruction of adiponectin/insulin and improve insulin sensitivity and glucose metabolism in streptozotocin (STZ)-induced type 1 diabetes. |
| 2035 | 19190261 | Interestingly, the antidiabetic effects of hemin lasted for 2 mo after termination of therapy and were accompanied by enhanced HO-1 and HO activity of the soleus muscle, along with potentiation of plasma antioxidants like bilirubin, ferritin, and superoxide dismutase, with corresponding elevation of the total antioxidant capacity. |
| 2036 | 19190261 | Importantly, hemin abated c-Jun NH2-terminal kinase (JNK), a substance known to inhibit insulin biosynthesis, and suppressed markers/mediators of oxidative stress including 8-isoprostane, nuclear-factor (NF)-kappaB, activating protein (AP)-1, and AP-2 of the soleus muscle. |
| 2037 | 19190261 | Correspondingly, hemin increased plasma insulin and potentiated agents implicated in insulin sensitization and insulin signaling such as adiponectin, adenosine monophosphate-activated protein kinase (AMPK), cAMP, cGMP, and glucose transporter (GLUT)4, a protein required for glucose uptake. |
| 2038 | 19198268 | Concentrations of lipid peroxidation products (primary--diene conjugates and secondary--malonic dialdehyde) as well as the activity of the antioxidant system (catalase and superoxide dismutase) were evaluated in 118 patients suffering from type II diabetes mellitus complicated with pyonecrotic affection of the lower limbs. |
| 2039 | 19202557 | Light treatment was ineffective as an antioxidant therapy in chronic diabetes, but light treatment for 18 days in acutely diabetic rats resulted in the normalization of hepatic glutathione reductase and superoxide dismutase activities and a significant increase in glutathione peroxidase and glutathione-S transferase activities. |
| 2040 | 19228889 | Insulin-mediated signal transduction is positively correlated to adiponectin, adenosine monophosphate-activated protein kinase (AMPK), and glucose-transporter-4 (GLUT4) but negatively to oxidative/inflammatory mediators such as nuclear factor-kappaB, activating-protein (AP)-1, AP-2, and c-Jun-N-terminal-kinase. |
| 2041 | 19228889 | Although hemeoxygenase (HO) suppresses oxidative insults, its effects on insulin-sensitizing agents like AMPK and GLUT4 remains unclear and were investigated using Goto-Kakizaki rats (GK), a nonobese insulin-resistant type-2 diabetic model. |
| 2042 | 19228889 | Interestingly, the antidiabetic was accompanied by a paradoxical increase of insulin alongside the potentiation of insulin-sensitizing agents such as adiponectin, AMPK, and GLUT4 in the gastrocnemius muscle. |
| 2043 | 19228889 | Furthermore, hemin enhanced mediators/regulators of insulin signaling like cGMP and cAMP and suppressed oxidative insults by up-regulating HO-1, HO activity, superoxide dismutase, catalase, and the total antioxidant capacity in the gastrocnemius muscle. |
| 2044 | 19228889 | Accordingly, oxidative markers/mediators including nuclear factor-kappaB, AP-1, AP-2, c-Jun-N-terminal-kinase, and 8-isoprostane were abated, whereas CrMP annulled the cytoprotective and antidiabetic effects of hemin. |
| 2045 | 19228889 | Our study unveils a 3-month enduring antidiabetic effect of hemin and unmasks the synergistic interaction among the HO system, adiponectin, AMPK, and GLUT4 that could be explored to enhance insulin signaling and improve glucose metabolism in insulin-resistant diabetes. |
| 2046 | 19229592 | Gene expressions of Mn-SOD and GPx-1 in streptozotocin-induced diabetes: effect of antioxidants. |
| 2047 | 19229592 | These results together with our previous findings about the gene expressions of catalase and Cu-Zn SOD indicate the presence of very intricate control mechanisms regulating the activities of antioxidant enzymes in order to prevent the damaging effects of oxidative stress. |
| 2048 | 19244937 | Besides, a fall in testicular antioxidant capacity appeared by a decrease in both antioxidant (superoxide dismutase (SOD), catalase (CAT) and glutathione peroxidase (GPx) activities) and nonenzymatic antioxidant (copper (Cu), magnesium (Mg) and iron (Fe) levels). |
| 2049 | 19262996 | Since the dismutation of superoxide is catalyzed by superoxide dismutase enzymes, we tested the association between obesity and Ala16Val manganese-dependent superoxide dismutase gene (MnSOD) polymorphism. |
| 2050 | 19298203 | The treatment with PF showed improved hepatic glutathione S-transferase, superoxide dismutase, and xanthine oxidase activities as well as glutathione and lipid peroxide levels in the diabetic animals. |
| 2051 | 19339227 | In addition, there was significant elevation in pancreatic lipid peroxides measured as malondialdehyde (MDA) and serum nitric oxide (NO) amounting to 185% and 224%, respectively with marked reduction in serum reduced glutathione (GSH) and catalase (CAT) (66% and 31%, respectively) and pancreatic superoxide dismutase (SOD) (54%) in STZ-treated rats. |
| 2052 | 19339227 | On the other hand, oral daily treatment of animals with EEP in a dose of 200 mg/kg bwt for a period of 5 weeks ameliorated STZ-induced alterations in the animal body weight as well as in serum glucose, lipids, lipoproteins, NO, GSH & CAT and pancreatic MDA & SOD. |
| 2053 | 19339227 | In addition, there was significant elevation in pancreatic lipid peroxides measured as malondialdehyde (MDA) and serum nitric oxide (NO) amounting to 185% and 224%, respectively with marked reduction in serum reduced glutathione (GSH) and catalase (CAT) (66% and 31%, respectively) and pancreatic superoxide dismutase (SOD) (54%) in STZ-treated rats. |
| 2054 | 19339227 | On the other hand, oral daily treatment of animals with EEP in a dose of 200 mg/kg bwt for a period of 5 weeks ameliorated STZ-induced alterations in the animal body weight as well as in serum glucose, lipids, lipoproteins, NO, GSH & CAT and pancreatic MDA & SOD. |
| 2055 | 19339234 | Superoxide dimutase (SOD), glutathione (GSH), catalase (CAT) and MDA were measured in the renal tissue. |
| 2056 | 19339234 | Moreover, renal tissue MDA was markedly increased while SOD, GSH and CAT were significantly decreased. |
| 2057 | 19339234 | Renal GSH, SOD and CAT were significantly increased while MDA was markedly reduced. |
| 2058 | 19339234 | Superoxide dimutase (SOD), glutathione (GSH), catalase (CAT) and MDA were measured in the renal tissue. |
| 2059 | 19339234 | Moreover, renal tissue MDA was markedly increased while SOD, GSH and CAT were significantly decreased. |
| 2060 | 19339234 | Renal GSH, SOD and CAT were significantly increased while MDA was markedly reduced. |
| 2061 | 19339234 | Superoxide dimutase (SOD), glutathione (GSH), catalase (CAT) and MDA were measured in the renal tissue. |
| 2062 | 19339234 | Moreover, renal tissue MDA was markedly increased while SOD, GSH and CAT were significantly decreased. |
| 2063 | 19339234 | Renal GSH, SOD and CAT were significantly increased while MDA was markedly reduced. |
| 2064 | 19364111 | The rats treated with baicalin and metformin + baicalin had significantly elevated (p < 0.05) hepatic activities of superoxide dismutase, catalase, and glutathione peroxidase compared with the vehicle- and metformin-treated groups. |
| 2065 | 19393637 | The administration of OMW extract fractions (F1) and (F2) as well as purified (HT) in diabetic rats caused a decrease in glucose level in plasma and an increase in renal superoxide dismutase (SOD), catalase (CAT) and glutathione peroxidase (GPX) activities in liver and kidney. |
| 2066 | 19406193 | The effect of bark extract on glucose, insulin, haemoglobin, glycosylated haemoglobin, TBARS, hydroperoxide, superoxide dismutase (SOD), catalase (CAT), glutathione peroxide (GPx), glutathione-S-transferase (GST), vitamins C and E, reduced glutathione (GSH) and membrane bound enzymes were studied. |
| 2067 | 19427773 | The result showed that the dose of 300 mg/kg and 450 mg/kg resulted significant hypoglycemic effect on normal mice, the dose of 300 mg/kg induced significant decrease in plasma glucose concentration (PGC), glycosylated serum protein (GSP), total cholesterol (TC) and triglyceride (TG), and significant increase in superoxide dismutase (SOD) activity and serum insulin level in streptozotocin-diabetic mice. |
| 2068 | 19429317 | Furthermore, TTA increased the superoxide dismutase activity (SOD) and the serum insulin level of diabetic mice. |
| 2069 | 19429815 | Our aim was to determine whether NADPH oxidase (Nox) is a source of O(2)(-) and whether glucose-6-phosphate dehydrogenase (G6PD)-derived NADPH plays a role in augmenting O(2)(-) generation in diabetes. |
| 2070 | 19429815 | We found that myocardial G6PD activity was significantly higher in fa/fa than in lean rats, whereas superoxide dismutase and glutathione peroxidase activities were decreased (P < 0.05). |
| 2071 | 19429815 | Notably, the activities of Nox and G6PD in the fa/fa rat heart were inhibited by chelerythrine, a protein kinase C inhibitor. |
| 2072 | 19458120 | I/R significantly increased interstitial extension, collagen deposition, apoptosis of tubular epithelial cells, nitrotyrosine expression, hydrogen peroxide production, and lipid peroxidation and decreased copper-zinc SOD, manganese SOD, and glucose 6-phosphate dehydrogenase activities in the kidneys 16 days after the procedure. |
| 2073 | 19458120 | In addition, MnTMPyP administration significantly attenuated the increases of alpha-smooth muscle actin, PCNA, S100A4, CD68, and heat shock protein 47 expression following I/R. |
| 2074 | 19468831 | Efficacy of BDMCA was determined by evaluating blood glucose, thiobarbituric acid reactive substances (TBARS), hydroperoxides (HP), activities of marker enzymes alkaline phosphatase (ALP), and lactate dehydrogenase (LDH) and activities of antioxidant enzymes superoxide dismutase (SOD), catalase (CAT) and glutathione peroxidase (GPx). |
| 2075 | 19470681 | We observed down-regulation of cytosolic CuZn-SOD (SOD1) and extracellular CuZn-SOD (SOD3), but not mitochondrial Mn-SOD (SOD2), in the kidney of KK/Ta-Akita mice which exhibit progressive DN. |
| 2076 | 19470681 | Collectively, these results indicate that down-regulation of renal SOD1 and SOD3 may play a key role in the pathogenesis of DN. |
| 2077 | 19470681 | We observed down-regulation of cytosolic CuZn-SOD (SOD1) and extracellular CuZn-SOD (SOD3), but not mitochondrial Mn-SOD (SOD2), in the kidney of KK/Ta-Akita mice which exhibit progressive DN. |
| 2078 | 19470681 | Collectively, these results indicate that down-regulation of renal SOD1 and SOD3 may play a key role in the pathogenesis of DN. |
| 2079 | 19475334 | Compared with control subjects, superoxide dismutase, glutathione peroxidase, catalase, vitamin C were decreased (P < 0.01). |
| 2080 | 19478420 | Our results investigate that Ajuga iva extract supplementation increased the levels of both enzymatic antioxidant (superoxide dismutase, catalase and glutathione peroxidase) and metals antioxidants (iron, copper, magnesium, calcium) and decreased lipid peroxidation level (TBARs). |
| 2081 | 19497592 | In hypertensive outpatients, on top of typical clinical workup, we assessed ET-1 levels, glucose handling parameters (glycated hemoglobin [HbA(1c)], homeostasis model assessment [HOMA] index, and insulin level), and antioxidative protection (ferric reducing ability of plasma [FRAP], superoxide dismutase [SOD], and vitamin C). |
| 2082 | 19497592 | Serum ET-1 level averaged 1.09 (0.48) pg/mL and correlated positively with glucose handling-associated parameters (insulin, r = 0.22; HOMA, r = 0.21; HbA(1c), r = 0.23; all Ps < .05) and negatively with constituents of antioxidative protection system (FRAP, r = -0.45; SOD, r = -0.47; both Ps < .0001; vitamin C, r = -0.27; P < or = .01). |
| 2083 | 19497592 | In sex-, age-, blood pressure-, and creatinine-adjusted models, with interchangeable introduction of antioxidative parameters on top of interchangeable introduction of glucose handling-associated parameters, ET-1 levels were each time only significantly associated with FRAP in the context of HbA(1c); FRAP, SOD, or vitamin C in the context of HOMA; and FRAP or SOD in the context of insulin concentration. |
| 2084 | 19497592 | In hypertensive outpatients, on top of typical clinical workup, we assessed ET-1 levels, glucose handling parameters (glycated hemoglobin [HbA(1c)], homeostasis model assessment [HOMA] index, and insulin level), and antioxidative protection (ferric reducing ability of plasma [FRAP], superoxide dismutase [SOD], and vitamin C). |
| 2085 | 19497592 | Serum ET-1 level averaged 1.09 (0.48) pg/mL and correlated positively with glucose handling-associated parameters (insulin, r = 0.22; HOMA, r = 0.21; HbA(1c), r = 0.23; all Ps < .05) and negatively with constituents of antioxidative protection system (FRAP, r = -0.45; SOD, r = -0.47; both Ps < .0001; vitamin C, r = -0.27; P < or = .01). |
| 2086 | 19497592 | In sex-, age-, blood pressure-, and creatinine-adjusted models, with interchangeable introduction of antioxidative parameters on top of interchangeable introduction of glucose handling-associated parameters, ET-1 levels were each time only significantly associated with FRAP in the context of HbA(1c); FRAP, SOD, or vitamin C in the context of HOMA; and FRAP or SOD in the context of insulin concentration. |
| 2087 | 19497592 | In hypertensive outpatients, on top of typical clinical workup, we assessed ET-1 levels, glucose handling parameters (glycated hemoglobin [HbA(1c)], homeostasis model assessment [HOMA] index, and insulin level), and antioxidative protection (ferric reducing ability of plasma [FRAP], superoxide dismutase [SOD], and vitamin C). |
| 2088 | 19497592 | Serum ET-1 level averaged 1.09 (0.48) pg/mL and correlated positively with glucose handling-associated parameters (insulin, r = 0.22; HOMA, r = 0.21; HbA(1c), r = 0.23; all Ps < .05) and negatively with constituents of antioxidative protection system (FRAP, r = -0.45; SOD, r = -0.47; both Ps < .0001; vitamin C, r = -0.27; P < or = .01). |
| 2089 | 19497592 | In sex-, age-, blood pressure-, and creatinine-adjusted models, with interchangeable introduction of antioxidative parameters on top of interchangeable introduction of glucose handling-associated parameters, ET-1 levels were each time only significantly associated with FRAP in the context of HbA(1c); FRAP, SOD, or vitamin C in the context of HOMA; and FRAP or SOD in the context of insulin concentration. |
| 2090 | 19531637 | Moreover, expression of p22phox (catalytic subunit of NADPH oxidase) as well as nitrotyrosine and superoxide content were all reduced in the aortas of rosiglitazone-treated SHR. |
| 2091 | 19531637 | Acute pretreatment of MVB from vehicle-treated SHR with apocynin (NADPH oxidase inhibitor) enhanced vasodilator actions of insulin (results comparable to those in MVB from rosiglitazone-treated SHR). |
| 2092 | 19531637 | We conclude that rosiglitazone therapy in SHR increases SOD activity and decreases p22phox expression in the vasculature to reduce oxidant stress leading to an improved cardiovascular phenotype. |
| 2093 | 19540215 | Lipids peroxidation level and activities of catalase, superoxide-dismutase and glutathione peroxidase were then measured in liver and kidney. |
| 2094 | 19540215 | In addition, eucalyptus extract appears to exert an antioxidative activity demonstrated (1) by the increase of catalase, superoxide-dismutase and gluthatione-peroxidase activities in liver and kidney, and (2) a lowering of lipids peroxidation level in these organs. |
| 2095 | 19540215 | Lipids peroxidation level and activities of catalase, superoxide-dismutase and glutathione peroxidase were then measured in liver and kidney. |
| 2096 | 19540215 | In addition, eucalyptus extract appears to exert an antioxidative activity demonstrated (1) by the increase of catalase, superoxide-dismutase and gluthatione-peroxidase activities in liver and kidney, and (2) a lowering of lipids peroxidation level in these organs. |
| 2097 | 19554009 | To test this hypothesis, reactive oxygen species-related genes (SOD1, SOD2, GP x 1, CAT, NOS2, NOS3) were tested, erectile functional studies and immunohistochemical analysis were carried out in diabetic rats treated with or without Tempol. |
| 2098 | 19554009 | To confirm the RT-PCR results, we carried out immunohistochemistry (IHC) for catalase (CAT) and iNOS (NOS2). |
| 2099 | 19556978 | There was a striking increase in the expression of proteins involved in glucose transporter-4 (GLUT4) granule transport and fusion (actin, myosin-9, tubulin, vimentin, annexins, moesin, LIM, and SH3 domain protein-1), signaling (calmodulin, guanine nucleotide-binding proteins), redox regulation (superoxide dismutase, catalase, ferritin, transferrin, heat shock proteins), and adipogenesis (collagens, galectin-1, nidogen-1, laminin, lamin A/C). |
| 2100 | 19556978 | Thus, the major changes observed were among proteins involved in cytoskeletal rearrangement, insulin and calcium signaling, and inflammatory and redox signals that decisively upregulate GLUT4 granule trafficking in human adipose tissue. |
| 2101 | 19581077 | Oral administration of CCl(4) at a dose of 1.2g/kg body weight 3 times a week for 3 weeks significantly induced marked hepatic injury as revealed by increased activity of the serum enzymes ALT, AST, SALP and gamma-GT. |
| 2102 | 19581077 | Methanolic extract of V. amygdalina administered 5 times a week for 2 weeks before CCl(4) treatment at 250 and 500 mg/kg doses of the extract ameliorated the increase in the activities of these enzymes. |
| 2103 | 19581077 | Similarly, administration of the extract increased the activities of the antioxidant enzymes: superoxide dismutase, glutathione S-transferase and reduced glutathione concentration significantly at 500 mg/kg (P<0.05) and catalase activity at 500-1000 mg/kg doses. |
| 2104 | 19616598 | The GLEt and glibenclamide were administered orally for 3 weeks and the effects on glucose, insulin, renal markers including urea, creatinine and uric acid, lipid peroxidation markers including thiobarbituric reactive substances (TBARS) and hydroperoxides and antioxidant enzymes superoxide dismutase (SOD), catalase (CAT), glutathione peroxidase (GPx) and glutathione-S-transferase (GST) activities in kidney were studied. |
| 2105 | 19662717 | When compared with diabetic hyperlipid-emic rats, plasma TBARS and LOOH levels decreased, the activities of enzymic antioxidants (SOD, CAT, GPx) and plasma GSH levels increased in the S-Frf fed group. |
| 2106 | 19662717 | The activities of plasma hepatic markers serum aspartate aminotransferase, alanine aminotransferase, and alkaline phosphatase, and levels of plasma urea, uric acid, creatinine, globulin, A/G ratio significantly decreased, whereas liver weight, total protein, and albumin increased. |
| 2107 | 19698781 | Protection of insulin-producing cells against toxicity of dexamethasone by catalase overexpression. |
| 2108 | 19698781 | Therefore we investigated the toxicity of dexamethasone in RINm5F insulin-producing cells and its dependence on the expression level of the antioxidant enzyme catalase, which inactivates hydrogen peroxide. |
| 2109 | 19698781 | Interestingly, exposure to dexamethasone increased the cytosolic superoxide dismutase Cu/ZnSOD protein expression and activity, whereas the mitochondrial MnSOD isoform was not affected by the glucocorticoid. |
| 2110 | 19698781 | Catalase overexpression in insulin-producing cells prevented all the cytotoxic effects of dexamethasone. |
| 2111 | 19698781 | Increased ROS scavenging capacity in insulin-producing cells, through overexpression of catalase, prevents a deleterious increase in hydrogen peroxide generation and thus prevents dexamethasone-induced apoptosis. |
| 2112 | 19758795 | Activity of antioxidant enzyme such as SOD, CAT was markedly elevated by TGP treatment with 200mg/kg. |
| 2113 | 19758795 | Western blot analysis showed that p-p38 MAPK and NF-kappaB p65 protein expression increased in diabetic rat kidney, which were significantly decreased by TGP treatment. |
| 2114 | 19761040 | There was a significant decrease in reduced glutathione, superoxide dismutase, catalase levels and increase in thiobarbituiric acid reactive species levels in the liver of STZ-induced diabetic rats. |
| 2115 | 19767827 | Glucagon-like peptide-1 (GLP-1) ameliorates the symptoms of diabetes through stimulation of insulin secretion. |
| 2116 | 19767827 | With exendin-4 treatment on diabetic mice, the following results were noted: (i) exendin-4 suppressed the increase in plasma glucose and inhibited somatostatin expression induced by STZ, (ii) reduction of insulin prevalence was inhibited, while expression of p75 neurotrophin receptor (p75NTR), pancreatic nerve growth factor (NGF), and NGF-positive islet cell prevalence increased, (iii) there were no alterations in the severity of proliferated cell nuclear antigen positive or apoptotic beta cells in pancreatic islets, and (iv) pancreatic catalase, glutathione peroxidase, and superoxide dismutase activities significantly increased. |
| 2117 | 19767827 | In conclusion, these data suggest that exendin-4 might exert its actions through the NGF/p75NTR system and decrease somatostatin expression. |
| 2118 | 19780024 | Expression (RT-PCR and radioligand binding) and functional (calcium mobilization with fura-2AM, and p42/p44MAPK and Akt phosphorylation assays) experiments revealed the presence of functional B2R in pig cerebral microvascular endothelial cells (pCMVEC). |
| 2119 | 19780024 | BK treatment coincided with enhanced expression of the cytoprotective proteins COX-2, Bcl-2, and (Cu/Zn)SOD. |
| 2120 | 19785000 | The anti-diabetic effect of anthocyanins in streptozotocin-induced diabetic rats through glucose transporter 4 regulation and prevention of insulin resistance and pancreatic apoptosis. |
| 2121 | 19785000 | ANT not only enhanced STZ-mediated insulin level decreases, but also decreased the triglyceride levels induced by STZ injection in serum. |
| 2122 | 19785000 | Diabetic rats exhibited a lower expression of glucose transporter 4 proteins in the membrane fractions of heart and skeletal muscle tissues, which was enhanced by ANT. |
| 2123 | 19785000 | In addition, ANT activated insulin receptor phosphorylation, suggesting an increased utilization of glucose by tissues. |
| 2124 | 19785000 | Moreover, ANT protected pancreatic tissue from STZ-induced apoptosis through regulation of caspase-3, Bax, and Bcl-2 proteins. |
| 2125 | 19785000 | Furthermore, ANT significantly suppressed malondialdehyde levels and restored superoxide dismutase and catalase activities in diabetic rats. |
| 2126 | 19785000 | Taken together, ANT from black soybean seed coat have anti-diabetic effects that are due, in part, to the regulation of glucose transporter 4 and prevention of insulin resistance and pancreatic apoptosis, suggesting a possible use as a drug to regulate diabetes. |
| 2127 | 19786892 | Waist circumference, body mass index, blood pressure, and glucose and insulin values were obtained; and fasting serum lipids, malondialdehyde, nitric oxide, glutathione peroxidase and superoxide dismutase activity were determined before and after 12 weeks of treatment. |
| 2128 | 19798452 | Furthermore, RS treatment decreased malondialdehyde levels, while increasing superoxide dismutase, catalase and glutathione peroxidase activities of the liver and kidney of diabetic rats. |
| 2129 | 19805130 | In particular, insulin resistance was rapidly reversible upon exposure to agents that act as mitochondrial uncouplers, ETC inhibitors, or mitochondrial superoxide dismutase (MnSOD) mimetics. |
| 2130 | 19805130 | Furthermore, acute induction of mitochondrial superoxide production using the complex III antagonist antimycin A caused rapid attenuation of insulin action independently of changes in the canonical PI3K/Akt pathway. |
| 2131 | 19805130 | These results were validated in vivo in that MnSOD transgenic mice were partially protected against HFD induced insulin resistance and MnSOD+/- mice were glucose intolerant on a standard chow diet. |
| 2132 | 19815948 | This was associated with a depression of glutathione (GSH) concentration as well as superoxide dismutase (SOD) and catalase (CAT) activities in the pylorus and ileum. |
| 2133 | 19815948 | L-arginine supplementation (0.15 mg/ml) through drinking water until eight weeks after alloxan injection significantly ameliorated the oxidative stress, as evidenced by lower MDA levels as well as higher levels of endogenous GSH, SOD, and CAT (p < 0.001). |
| 2134 | 19815948 | This was associated with a depression of glutathione (GSH) concentration as well as superoxide dismutase (SOD) and catalase (CAT) activities in the pylorus and ileum. |
| 2135 | 19815948 | L-arginine supplementation (0.15 mg/ml) through drinking water until eight weeks after alloxan injection significantly ameliorated the oxidative stress, as evidenced by lower MDA levels as well as higher levels of endogenous GSH, SOD, and CAT (p < 0.001). |
| 2136 | 19837064 | In these cells, reduced glutathione levels and mitochondrial and superoxide dismutase activities increased markedly while reactive oxygen species generation decreased significantly in presence of PEDF as compared with cells grown in the absence of PEDF under high glucose conditions (10-20 nM, *p < 0.01&**p < 0.001; 30-50 nM, ***p < 0.0001). |
| 2137 | 19842839 | In the present study, hyperglycemia inhibited pulmonary antioxidants, including superoxide dismutase, catalase, glutathione peroxidase, and glutathione. |
| 2138 | 19865527 | Effects of sage consumption on erythrocytes' SOD and CAT activities and on Hsp70 expression in lymphocytes were also evaluated. |
| 2139 | 19865527 | Sage tea also increased lymphocyte Hsp70 expression and erythrocyte SOD and CAT activities. |
| 2140 | 19865527 | Effects of sage consumption on erythrocytes' SOD and CAT activities and on Hsp70 expression in lymphocytes were also evaluated. |
| 2141 | 19865527 | Sage tea also increased lymphocyte Hsp70 expression and erythrocyte SOD and CAT activities. |
| 2142 | 19948220 | Decreases on Mn-superoxide dismutase (SOD), catalase, and heme oxygenase-1 levels by I/R were increased by sulforaphane treatment and pretreatment of 5-HD blocked the sulforaphane effects. |
| 2143 | 19948220 | Increases in Bax and caspase-3 levels, and decrease in Bcl-2 level by I/R were attenuated by sulforaphane treatment. |
| 2144 | 19957886 | The changes in lipid peroxidation status and anti-oxidant enzymes (superoxide dismutase and catalase) levels observed in diabetic rats were significantly restored by E. officinalis extract and quercetin treatment. |
| 2145 | 20004234 | This treatment increased the activities of antioxidant enzymes namely, catalase, glutathione reductase and superoxide dismutase and reduced serum triglyceride and cholesterol levels as compared to those found in uncontrolled diabetic mice. |
| 2146 | 20011081 | Extracellular SOD and VEGF are increased in vitreous bodies from proliferative diabetic retinopathy patients. |
| 2147 | 20020514 | PJ treatment also caused a significant decrease in levels of thiobarbituric acid reactive substances (TBARS) in kidney and pancreas while activities of enzymes superoxide dismutase (SOD), catalase (CAT), and glutathione reductase (GSH) showed significant elevation. |
| 2148 | 20020514 | The results suggest that the PJ extract could prevent the development of high blood pressure induced by Ang II in diabetic rats probably by combating the oxidative stress induced by diabetes and Ang II and by inhibiting ACE activity. |
| 2149 | 20027866 | The antioxidant defense system was also found to be improved in CLEt-treated (400 mg/kg) MD and SD rats, as revealed by significant increase in activities of erythrocyte's antioxidant enzymes, i.e., superoxide dismutase (SOD) and catalase (CAT) with a concomitant elevation in erythrocyte's reduced glutathione (GSH) content. |
| 2150 | 20072924 | The observed elevated level of lipid peroxidation (LPO) comes down significantly (p < 0.05) and decreased activities of antioxidant enzymes such as catalase (CAT), superoxide dismutase (SOD), glutathione peroxidase (GPx), and glutathione-S-transferase (GST) got increased (p < 0.05) significantly of diabetic rats on extract treatment. |
| 2151 | 20097730 | To test the hypothesis that polymorphic variants of antioxidant genes modify the risk of pancreatic cancer, we examined seven single-nucleotide polymorphisms (SNPs) of genes coding for superoxide dismutase (SOD) 2, glutathione S-transferase alpha 4 (GSTA4), catalase and glutathione peroxidase in 575 patients with pancreatic adenocarcinoma and 648 healthy controls in a case-control study. |
| 2152 | 20100065 | Moreover, diabetic rats showed low activities of superoxide dismutase, catalase, glutathione peroxidase, and reduced glutathione content in kidney, which were restored to near normal levels by treatment with fenugreek oil. |
| 2153 | 20112810 | The drug had enzyme induction effect with respect to catalase (CAT) and glutathione peroxidase (GSH-Px) activity, however decreased the exaggerated activity of superoxide dismutase (SOD) in type 2 diabetic rats. |
| 2154 | 20126367 | Catalase and glutathione peroxidase activities with seaweed supplementation were higher than the controls (p<0.05), but superoxide dismutase activity was not affected. |
| 2155 | 20126586 | The purpose of this study is to investigate the effect of HBO exposure on the gene expression of three important antioxidant enzymes, cytosolic superoxide dismutase (Cu-Zn SOD), cytosolic glutathione peroxidase (GPx-1), and catalase (CAT) in DM rats, respectively. |
| 2156 | 20126586 | The mRNA expressions of Cu-Zn SOD and CAT decreased significantly (p < 0.001), and GPx increased significantly (p < 0.001) in all the studied organs of DM rats under HBO exposure compared to those from DM-induced rats not exposed to HBO. |
| 2157 | 20126586 | The purpose of this study is to investigate the effect of HBO exposure on the gene expression of three important antioxidant enzymes, cytosolic superoxide dismutase (Cu-Zn SOD), cytosolic glutathione peroxidase (GPx-1), and catalase (CAT) in DM rats, respectively. |
| 2158 | 20126586 | The mRNA expressions of Cu-Zn SOD and CAT decreased significantly (p < 0.001), and GPx increased significantly (p < 0.001) in all the studied organs of DM rats under HBO exposure compared to those from DM-induced rats not exposed to HBO. |
| 2159 | 20127524 | PPAR-gamma, by increasing superoxide dismutase/catalase and decreasing nicotinamide adenine dinucleotide phosphate oxidase levels, attenuated ischemia-induced reactive oxygen species and subsequently alleviated the postischemic degradation of Bcl-2, Bcl-xl, and Akt. |
| 2160 | 20130740 | The aim of this study was to determine the antidiabetic properties of 4 purified fractions of different molecular weight range HPSs (HPS1, HPS2, HPS3, HPS4). |
| 2161 | 20130740 | The interleukin-6, tumor necrosis factor-alpha, leptin, and free fatty acid levels were significantly lower in the HPS3-treated groups and HPS3 + metformin (HPS3+MET) group than in the DM control group, while plasma insulin, hepatic glycogen, superoxide dismutase, and nitric oxide synthetase activity were significantly higher. |
| 2162 | 20136451 | Feeding rats with these diets for 5 weeks resulted in reduction of plasma glucose and changes in biomarkers of oxidative stress-namely, superoxide dismutase (SOD), peroxidase (PER), and thiobarbituric acid-reactive substances (TBARS). |
| 2163 | 20136451 | A decrease in the activities of PER and SOD was observed in the kidneys of the diabetic rats. |
| 2164 | 20136451 | Feeding rats with these diets for 5 weeks resulted in reduction of plasma glucose and changes in biomarkers of oxidative stress-namely, superoxide dismutase (SOD), peroxidase (PER), and thiobarbituric acid-reactive substances (TBARS). |
| 2165 | 20136451 | A decrease in the activities of PER and SOD was observed in the kidneys of the diabetic rats. |
| 2166 | 20154258 | Prostacyclin was the predominant prostaglandin produced by ACh-stimulated CCAs, with greater than twofold more prostacyclin released from SHR versus WKY rats, and its production was unaffected by ROCK inhibition. |
| 2167 | 20154258 | Augmentation of chemical superoxide quenching with tiron or inhibition of the NADPH oxidase-derived superoxide-producing pathway with apocynin reduced ACh-stimulated contractile activity in SHR more than in WKY rats, whereas the SOD mimetic tempol amplified the response. |
| 2168 | 20162039 | Post-euthanization, hepatic tissues were excised and processed biochemically for antioxidant enzymes and lipid profiles, such as catalase (CAT), reactive oxygen species (ROS), glutathione (GSH), superoxide dismutase (SOD), glutathione peroxidase (GSH-Px), thiobarbituric acid reactive substances (TBARS), triglycerides (TG), total cholesterol (TC), high density lipoprotein (HDL) and low density lipoprotein (LDL), respectively. |
| 2169 | 20162039 | STZ treatment also significantly decreased (p<0.05) CAT, GSH, SOD, GSH-Px activities, and HDL levels. |
| 2170 | 20162039 | Post-euthanization, hepatic tissues were excised and processed biochemically for antioxidant enzymes and lipid profiles, such as catalase (CAT), reactive oxygen species (ROS), glutathione (GSH), superoxide dismutase (SOD), glutathione peroxidase (GSH-Px), thiobarbituric acid reactive substances (TBARS), triglycerides (TG), total cholesterol (TC), high density lipoprotein (HDL) and low density lipoprotein (LDL), respectively. |
| 2171 | 20162039 | STZ treatment also significantly decreased (p<0.05) CAT, GSH, SOD, GSH-Px activities, and HDL levels. |
| 2172 | 20162074 | The pancreases of the sacrificed rats were excised and randomly processed for histological staining and biochemical assays for antioxidant enzymes [such as glutathione peroxidase (GSHPx), superoxide dismutase (SOD), catalase (CAT), malondialdehyde (MDA) and serum nitric oxide (NO)]. |
| 2173 | 20162074 | STZ treatment significantly decreased (p<0.05) GSHPx, SOD, CAT and pancreatic insulin content. |
| 2174 | 20162074 | The pancreases of the sacrificed rats were excised and randomly processed for histological staining and biochemical assays for antioxidant enzymes [such as glutathione peroxidase (GSHPx), superoxide dismutase (SOD), catalase (CAT), malondialdehyde (MDA) and serum nitric oxide (NO)]. |
| 2175 | 20162074 | STZ treatment significantly decreased (p<0.05) GSHPx, SOD, CAT and pancreatic insulin content. |
| 2176 | 20170713 | The present study was carried out to find the effects of Aegle marmelose leaf extract and insulin alone and in combination with pyridoxine on the cerebellar 5-HT through 5-HT(2A) receptor subtype, gene expression studies on the status of antioxidants-superoxide dismutase (SOD), glutathione peroxidase (GPx), 5-HT(2A) and 5-HT transporter (5-HTT) and immunohistochemical studies in streptozotocin induced diabetic rats. 5-HT and 5-HT(2A) receptor binding parameters, B(max) and K(d), showed a significant decrease (p<0.001) in the cerebellum of diabetic rats compared to control. |
| 2177 | 20170713 | Gene expression studies of SOD, GPx, 5-HT(2A) and 5-HTT in cerebellum showed a significant down regulation (p<0.001) in diabetic rats compared to control. |
| 2178 | 20170713 | Pyridoxine treated alone and in combination with insulin, A. marmelose to diabetic rats reversed the B(max), K(d) of 5-HT, 5-HT(2A) and the gene expression of SOD, GPx, 5-HT(2A) and 5-HTT in cerebellum to near control. |
| 2179 | 20170713 | The gene expression of 5-HT(2A) and 5-HTT were confirmed by immunohistochemical studies. |
| 2180 | 20170713 | Our results suggest that pyridoxine treated alone and in combination with insulin and A. marmelose has a role in the regulation of insulin synthesis and release, normalizing diabetic related oxidative stress and neurodegeneration affecting the motor ability of an individual by serotonergic receptors through 5-HT(2A) function. |
| 2181 | 20170713 | The present study was carried out to find the effects of Aegle marmelose leaf extract and insulin alone and in combination with pyridoxine on the cerebellar 5-HT through 5-HT(2A) receptor subtype, gene expression studies on the status of antioxidants-superoxide dismutase (SOD), glutathione peroxidase (GPx), 5-HT(2A) and 5-HT transporter (5-HTT) and immunohistochemical studies in streptozotocin induced diabetic rats. 5-HT and 5-HT(2A) receptor binding parameters, B(max) and K(d), showed a significant decrease (p<0.001) in the cerebellum of diabetic rats compared to control. |
| 2182 | 20170713 | Gene expression studies of SOD, GPx, 5-HT(2A) and 5-HTT in cerebellum showed a significant down regulation (p<0.001) in diabetic rats compared to control. |
| 2183 | 20170713 | Pyridoxine treated alone and in combination with insulin, A. marmelose to diabetic rats reversed the B(max), K(d) of 5-HT, 5-HT(2A) and the gene expression of SOD, GPx, 5-HT(2A) and 5-HTT in cerebellum to near control. |
| 2184 | 20170713 | The gene expression of 5-HT(2A) and 5-HTT were confirmed by immunohistochemical studies. |
| 2185 | 20170713 | Our results suggest that pyridoxine treated alone and in combination with insulin and A. marmelose has a role in the regulation of insulin synthesis and release, normalizing diabetic related oxidative stress and neurodegeneration affecting the motor ability of an individual by serotonergic receptors through 5-HT(2A) function. |
| 2186 | 20170713 | The present study was carried out to find the effects of Aegle marmelose leaf extract and insulin alone and in combination with pyridoxine on the cerebellar 5-HT through 5-HT(2A) receptor subtype, gene expression studies on the status of antioxidants-superoxide dismutase (SOD), glutathione peroxidase (GPx), 5-HT(2A) and 5-HT transporter (5-HTT) and immunohistochemical studies in streptozotocin induced diabetic rats. 5-HT and 5-HT(2A) receptor binding parameters, B(max) and K(d), showed a significant decrease (p<0.001) in the cerebellum of diabetic rats compared to control. |
| 2187 | 20170713 | Gene expression studies of SOD, GPx, 5-HT(2A) and 5-HTT in cerebellum showed a significant down regulation (p<0.001) in diabetic rats compared to control. |
| 2188 | 20170713 | Pyridoxine treated alone and in combination with insulin, A. marmelose to diabetic rats reversed the B(max), K(d) of 5-HT, 5-HT(2A) and the gene expression of SOD, GPx, 5-HT(2A) and 5-HTT in cerebellum to near control. |
| 2189 | 20170713 | The gene expression of 5-HT(2A) and 5-HTT were confirmed by immunohistochemical studies. |
| 2190 | 20170713 | Our results suggest that pyridoxine treated alone and in combination with insulin and A. marmelose has a role in the regulation of insulin synthesis and release, normalizing diabetic related oxidative stress and neurodegeneration affecting the motor ability of an individual by serotonergic receptors through 5-HT(2A) function. |
| 2191 | 20174975 | Antioxidant status was examined by measuring the superoxide dismutase (SOD), catalase, glutathione, and lipid peroxidation in kidney tissues. |
| 2192 | 20174975 | Selenium-treated groups significantly increased antioxidant enzyme activities (SOD, catalase, and glutathione) in kidneys of diabetic rats. |
| 2193 | 20174975 | Antioxidant status was examined by measuring the superoxide dismutase (SOD), catalase, glutathione, and lipid peroxidation in kidney tissues. |
| 2194 | 20174975 | Selenium-treated groups significantly increased antioxidant enzyme activities (SOD, catalase, and glutathione) in kidneys of diabetic rats. |
| 2195 | 20186490 | After the treatment, the levels of urine sugar, blood glucose, liver glycogen, and antioxidants like vitamin C and E in plasma and superoxide dismutase (SOD), catalase (CAT), thiobarbituric acid reactive substances (TBARS), glutathione peroxidase (GPx), glutathione-S-transferase (GST) and reduced glutathione (GSH) in liver, kidney and heart were determined. |
| 2196 | 20186490 | Diabetic rats showed a significant (p < 0.05) elevation in glucose and TBARS and a significant (p < 0.05) reduction in glycogen, vitamin C and E, SOD, CAT, GPx, GST, and GSH levels when compared to normal control rats. |
| 2197 | 20186490 | After the treatment, the levels of urine sugar, blood glucose, liver glycogen, and antioxidants like vitamin C and E in plasma and superoxide dismutase (SOD), catalase (CAT), thiobarbituric acid reactive substances (TBARS), glutathione peroxidase (GPx), glutathione-S-transferase (GST) and reduced glutathione (GSH) in liver, kidney and heart were determined. |
| 2198 | 20186490 | Diabetic rats showed a significant (p < 0.05) elevation in glucose and TBARS and a significant (p < 0.05) reduction in glycogen, vitamin C and E, SOD, CAT, GPx, GST, and GSH levels when compared to normal control rats. |
| 2199 | 20307140 | Activity of the three primary scavenger enzymes (superoxide dismutase, catalase, and glutathione peroxidase), levels of glutathione, and lipid peroxidation were estimated in plasma and pancreas of diabetic rats and compared to the reference drug, glibenclamide (600 microg/kg body weight/day). |
| 2200 | 20307515 | Telmisartan, an angiotensin II-receptor blocker (ARB), is a partial agonist of the peroxisome proliferator-activated receptor-gamma (PPAR-gamma). |
| 2201 | 20307515 | Compared with diabetic controls, diabetic rats with myocardial infarction exhibited altered hemodynamic profiles and reduction in the activities of creatine kinase-MB isoenzyme, lactate dehydrogenase, superoxide dismutase, catalase, and glutathione level along with increased level of malondialdehyde in the heart. |
| 2202 | 20307516 | After the experimental period of 30 days, the pathophysiological markers such as serum bilirubin and hepatic aspartate transaminase (AST), alanine transaminase (ALT) and alkaline phosphatase (ALP) were studied in addition to hepatic TNF-alpha, IL-1 beta, IL-6, NF-kappaB p65 and nitric oxide (NO) levels in control and experimental groups of rats. |
| 2203 | 20307516 | The levels of vitamin C, vitamin E and reduced glutathione (GSH) and activities of superoxide dismutase (SOD), catalase, glutathione peroxidase (GPx), glutathione-S-transferase (GST) and glutathione reductase (GR) were determined in the liver tissues. |
| 2204 | 20333650 | Oral administration of resveratrol (5 mg/kg body weight) to diabetic rats for 30 days showed a significant decline in the levels of blood glucose, glycosylated hemoglobin (HbA1c), TNF-alpha, IL-1beta, IL-6, NF-kappaB p65 unit and nitric oxide (NO) with concomitant elevation in plasma insulin. |
| 2205 | 20333650 | The diminished activities of pancreatic superoxide dismutase (SOD), catalase, glutathione peroxidase (GPx) and glutathione-S-transferase (GST) as well as the decreased levels of plasma ceruloplasmin, vitamin C, vitamin E and reduced glutathione (GSH) in diabetic rats were reverted to near normalcy by resveratrol administration. |
| 2206 | 20339905 | Diabetic rats showed an increase in the levels of fasting plasma glucose, lipid peroxidative products such as thiobarbituric acid reactive substances and lipid hydroperoxides and a decrease in plasma insulin, and enzymic antioxidants viz., superoxide dismutase, catalase, glutathione peroxidase and glutathione-S-transferase. |
| 2207 | 20361141 | An excessive glucose supply to embryonic tissues leads to a state of oxidative stress, which affects the expression of genes encoding scavenging enzymes such as super oxide dismutase (SOD) and catastases and activates development genes such as PAX3, involved in neural tube defects. |
| 2208 | 20361141 | There is an increase of apoptotic Bax and caspase-3 proteins and a low expression of Bcl-Z ant apoptotic protein in embryos exposed to a diabetic environment. |
| 2209 | 20368212 | TheTBARS, carbonylated proteins, were measured in the plasma and in the supernatant of liver homogenisates, and superoxide dismutase and catalase were measured in the haemolysates of RBCs and supernatant of liver homogenisates. |
| 2210 | 20376213 | The lipid peroxidation, superoxide dismutase, and catalase were measured in liver homogenate and serum glutamic pyruvic transaminase, serum glutamic oxaloacetic transaminase, alkaline phosphatase, lipid profile were measured in blood serum. |
| 2211 | 20376213 | Administration of single dose of streptozotozin (55 mg/kg, i.p.) caused significant increases in lipid peroxidation, serum glutamic pyruvic transaminase, serum glutamic oxaloacetic transaminase, alkaline phosphatase, cholesterol and triglyceride levels, while superoxide dismutase and catalase levels were significantly decreased. |
| 2212 | 20376213 | Consequently, superoxide dismutase and catalase levels were significantly increased. |
| 2213 | 20376213 | It was observed that the effect of chloroform extracts of Calotropis gigantea on alkaline phosphatase, cholesterol, superoxide dismutase, serum glutamic pyruvic transaminase, serum glutamic oxaloacetic transaminase, levels are comparable to that of those produced by the positive control. |
| 2214 | 20376213 | The lipid peroxidation, superoxide dismutase, and catalase were measured in liver homogenate and serum glutamic pyruvic transaminase, serum glutamic oxaloacetic transaminase, alkaline phosphatase, lipid profile were measured in blood serum. |
| 2215 | 20376213 | Administration of single dose of streptozotozin (55 mg/kg, i.p.) caused significant increases in lipid peroxidation, serum glutamic pyruvic transaminase, serum glutamic oxaloacetic transaminase, alkaline phosphatase, cholesterol and triglyceride levels, while superoxide dismutase and catalase levels were significantly decreased. |
| 2216 | 20376213 | Consequently, superoxide dismutase and catalase levels were significantly increased. |
| 2217 | 20376213 | It was observed that the effect of chloroform extracts of Calotropis gigantea on alkaline phosphatase, cholesterol, superoxide dismutase, serum glutamic pyruvic transaminase, serum glutamic oxaloacetic transaminase, levels are comparable to that of those produced by the positive control. |
| 2218 | 20376213 | The lipid peroxidation, superoxide dismutase, and catalase were measured in liver homogenate and serum glutamic pyruvic transaminase, serum glutamic oxaloacetic transaminase, alkaline phosphatase, lipid profile were measured in blood serum. |
| 2219 | 20376213 | Administration of single dose of streptozotozin (55 mg/kg, i.p.) caused significant increases in lipid peroxidation, serum glutamic pyruvic transaminase, serum glutamic oxaloacetic transaminase, alkaline phosphatase, cholesterol and triglyceride levels, while superoxide dismutase and catalase levels were significantly decreased. |
| 2220 | 20376213 | Consequently, superoxide dismutase and catalase levels were significantly increased. |
| 2221 | 20376213 | It was observed that the effect of chloroform extracts of Calotropis gigantea on alkaline phosphatase, cholesterol, superoxide dismutase, serum glutamic pyruvic transaminase, serum glutamic oxaloacetic transaminase, levels are comparable to that of those produced by the positive control. |
| 2222 | 20376213 | The lipid peroxidation, superoxide dismutase, and catalase were measured in liver homogenate and serum glutamic pyruvic transaminase, serum glutamic oxaloacetic transaminase, alkaline phosphatase, lipid profile were measured in blood serum. |
| 2223 | 20376213 | Administration of single dose of streptozotozin (55 mg/kg, i.p.) caused significant increases in lipid peroxidation, serum glutamic pyruvic transaminase, serum glutamic oxaloacetic transaminase, alkaline phosphatase, cholesterol and triglyceride levels, while superoxide dismutase and catalase levels were significantly decreased. |
| 2224 | 20376213 | Consequently, superoxide dismutase and catalase levels were significantly increased. |
| 2225 | 20376213 | It was observed that the effect of chloroform extracts of Calotropis gigantea on alkaline phosphatase, cholesterol, superoxide dismutase, serum glutamic pyruvic transaminase, serum glutamic oxaloacetic transaminase, levels are comparable to that of those produced by the positive control. |
| 2226 | 20384568 | Direct inhibition by angiotensin II of insulin-dependent glucose transport activity in mammalian skeletal muscle involves a ROS-dependent mechanism. |
| 2227 | 20384568 | No previous study has investigated how the vaso-constrictive peptide Ang II impacts insulin action in isolated mammalian skeletal muscle. |
| 2228 | 20384568 | We investigated the molecular actions of Ang II on insulin signalling and glucose transport in skeletal muscle from lean Zucker rats. |
| 2229 | 20384568 | Soleus strips were incubated with insulin (5 mU/ml) and/or Ang II (500 nM) for 2 hours. |
| 2230 | 20384568 | Ang II caused significant (p < 0.05) inhibition of insulin-stimulated glucose transport (39%) and decreased phosphorylation of Akt Ser(473) (37%) and glycogen synthase kinase-3beta Ser(9) (42%) without affecting phosphorylation of IRS-1 Ser(307) or p38 MAPK. |
| 2231 | 20384568 | We used the superoxide dismutase mimetic, tempol (1 mM), to determine if reactive oxygen species (ROS) contribute to Ang II-mediated insulin resistance. |
| 2232 | 20384568 | Tempol partially reversed (42%) Ang II-induced inhibition of insulin-stimulated glucose transport. |
| 2233 | 20384568 | These results indicate that Ang II inhibits distal insulin signalling and insulin-stimulated glucose transport in isolated mammalian skeletal muscle, and that this effect is partially mediated by ROS. |
| 2234 | 20395699 | Apolipoprotein A-I mimetic peptides: a potential new therapy for the prevention of atherosclerosis. |
| 2235 | 20395699 | The beneficial effects of high-density lipoprotein (HDL) on atherosclerosis have largely been attributed to its major protein, apolipoprotein A-I (apoA-I). |
| 2236 | 20395699 | In a rat model of diabetes, D-4F increased arterial concentrations of heme oxygenase-1 (HO-1) and superoxide dismutase, decreased superoxide levels, reduced levels of circulating endothelial cells, decreased endothelial cell fragmentation, and restored arterial vasoreactivity to normal. |
| 2237 | 20397104 | Besides this, the ethanol extracts from the DMCB treatment significantly increased catalase, superoxide dismutase and glutathione peroxidase activities, except for decreasing the maleic dialdehyde level in diabetic mice. |
| 2238 | 20399771 | Also, telmisartan significantly reduced the elevations of total gastric acid output, pepsin activity, gastric ulcer index and gastric mucosal tumor necrosis factor-alpha, nitric oxide, malondialdehyde and caspase-3 activity, and restored the depleted antioxidant defenses (reduced glutathione level, and superoxide dismutase and catalase activities) caused by indomethacin administration in diabetic rats. |
| 2239 | 20399771 | Immunohistochemical analysis revealed that telmisartan markedly attenuated the reduction in insulin content of pancreatic islet beta-cells, and prevented the indomethacin-induced overexpression of inducible nitric oxide synthase and nuclear factor-kappaB in gastric mucosa of diabetic rats. |
| 2240 | 20399799 | At the end of 4, 8, and 12 weeks, hydroxyproline content, NADPH oxidase activity and the expression of phosphorylation of inositol-requiring enzyme-1alpha (p-IRE1alpha), p47phox, nitrotyrosine (NT) and NF-E2-related factor 2 (Nrf2) in the kidneys of all rats were determined; malondialdehyde (MDA) levels and superoxide dismutase (SOD) activity in serum and urine were also detected; renal nuclear factor kappaB (NF-kappaB) activity in all of the rats was examined at the end of 12 weeks. |
| 2241 | 20399799 | Compared with the NC group, the DN rats showed a significant increase in hydroxyproline content, NADPH oxidase activity, NF-kappaB activity, the expression of p-IRE1alpha, p47phox, NT and Nrf2 in renal tissue; markedly, MDA levels were higher and SOD activity was lower in serum and urine of DN rats than in NC rats for the indicated time. |
| 2242 | 20399799 | At the end of 4, 8, and 12 weeks, hydroxyproline content, NADPH oxidase activity and the expression of phosphorylation of inositol-requiring enzyme-1alpha (p-IRE1alpha), p47phox, nitrotyrosine (NT) and NF-E2-related factor 2 (Nrf2) in the kidneys of all rats were determined; malondialdehyde (MDA) levels and superoxide dismutase (SOD) activity in serum and urine were also detected; renal nuclear factor kappaB (NF-kappaB) activity in all of the rats was examined at the end of 12 weeks. |
| 2243 | 20399799 | Compared with the NC group, the DN rats showed a significant increase in hydroxyproline content, NADPH oxidase activity, NF-kappaB activity, the expression of p-IRE1alpha, p47phox, NT and Nrf2 in renal tissue; markedly, MDA levels were higher and SOD activity was lower in serum and urine of DN rats than in NC rats for the indicated time. |
| 2244 | 20422335 | The absence of cardiomyopathy is accompanied by increased activities of CAT, MnSOD and GST in long-term diabetes in rats. |
| 2245 | 20422335 | The activities of the antioxidant enzymes superoxide dismutase (SOD), catalase (CAT) and glutathione S-transferase (GST), the incidence of DNA damage, the activation of poly (ADP-ribose) polymerase-1 (PARP-1), a marker of DNA repair, and connective tissue growth factor (CTGF), a marker of tissue fibrosis, were examined in the hearts of rats for 16 weeks after diabetes induction by streptozotocin (STZ) administration. |
| 2246 | 20422335 | While total SOD and CuZn-SOD exhibited progressively decreasing activities, those of Mn-SOD and GST were elevated. |
| 2247 | 20422335 | Neither DNA strand breaks (apoptosis or necrosis) nor changes in PARP-1 activity and in CTGF levels (fibrosis) were observed in the diabetic heart. |
| 2248 | 20422335 | The absence of cardiomyopathy is accompanied with increased activities of CAT, MnSOD and GST. |
| 2249 | 20422335 | The absence of cardiomyopathy is accompanied by increased activities of CAT, MnSOD and GST in long-term diabetes in rats. |
| 2250 | 20422335 | The activities of the antioxidant enzymes superoxide dismutase (SOD), catalase (CAT) and glutathione S-transferase (GST), the incidence of DNA damage, the activation of poly (ADP-ribose) polymerase-1 (PARP-1), a marker of DNA repair, and connective tissue growth factor (CTGF), a marker of tissue fibrosis, were examined in the hearts of rats for 16 weeks after diabetes induction by streptozotocin (STZ) administration. |
| 2251 | 20422335 | While total SOD and CuZn-SOD exhibited progressively decreasing activities, those of Mn-SOD and GST were elevated. |
| 2252 | 20422335 | Neither DNA strand breaks (apoptosis or necrosis) nor changes in PARP-1 activity and in CTGF levels (fibrosis) were observed in the diabetic heart. |
| 2253 | 20422335 | The absence of cardiomyopathy is accompanied with increased activities of CAT, MnSOD and GST. |
| 2254 | 20422735 | The oxidants arise from NADPH oxidase, xanthine oxidase, and mitochondria. |
| 2255 | 20422735 | With some important vascular proteins, for example, endothelial nitric oxide synthase, prostacycline synthase, and superoxide dismutase, oxidation of a single susceptible amino acid inactivates the enzyme. |
| 2256 | 20425759 | We measured inflammatory markers (high sensitivity C-Reactive Protein, Monocyte Chemotactic Protein-1, Macrophage Inflammatory Protein 1-β, and Regulated upon Activation, Normal T cell Expressed and Secreted), superoxide dismutase, and micronutrients (β-carotene, vitamin C, and vitamin E). |
| 2257 | 20425759 | Results showed Monocyte Chemotactic Protein-1, Macrophage Inflammatory Protein 1-β, and RANTES levels were significantly reduced and superoxide dismutase and micronutrient levels were significantly increased in subjects consuming both FV and FVB, relative to placebo. |
| 2258 | 20425759 | We measured inflammatory markers (high sensitivity C-Reactive Protein, Monocyte Chemotactic Protein-1, Macrophage Inflammatory Protein 1-β, and Regulated upon Activation, Normal T cell Expressed and Secreted), superoxide dismutase, and micronutrients (β-carotene, vitamin C, and vitamin E). |
| 2259 | 20425759 | Results showed Monocyte Chemotactic Protein-1, Macrophage Inflammatory Protein 1-β, and RANTES levels were significantly reduced and superoxide dismutase and micronutrient levels were significantly increased in subjects consuming both FV and FVB, relative to placebo. |
| 2260 | 20435848 | Resistin decreases expression of endothelial nitric oxide synthase through oxidative stress in human coronary artery endothelial cells. |
| 2261 | 20435848 | Resistin is a newly discovered adipocyte-derived cytokine that may play an important role in insulin resistance, diabetes, adipogenesis, inflammation, and cardiovascular disease. |
| 2262 | 20435848 | However, it is largely unknown whether resistin impairs endothelial functions by affecting the endothelial nitric oxide synthase (eNOS) system. |
| 2263 | 20435848 | Mitochondrial membrane potential and the activities of catalase and superoxide dismutase were reduced. |
| 2264 | 20435848 | Three antioxidants, seleno-L-methionine, ginsenoside Rb1, and MnTBAP (superoxide dismutase mimetic), effectively blocked resistin-induced eNOS downregulation. |
| 2265 | 20435848 | Meanwhile, resistin activated the mitogen-activated protein kinases p38 and c-Jun NH(2)-terminal kinase (JNK), and the specific p38 inhibitor SB-239063 effectively blocked resistin-induced ROS production and eNOS downregulation. |
| 2266 | 20435848 | Thus resistin directly induces eNOS downregulation through overproduction of ROS and activation of p38 and JNK in HCAECs. |
| 2267 | 20435848 | Resistin decreases expression of endothelial nitric oxide synthase through oxidative stress in human coronary artery endothelial cells. |
| 2268 | 20435848 | Resistin is a newly discovered adipocyte-derived cytokine that may play an important role in insulin resistance, diabetes, adipogenesis, inflammation, and cardiovascular disease. |
| 2269 | 20435848 | However, it is largely unknown whether resistin impairs endothelial functions by affecting the endothelial nitric oxide synthase (eNOS) system. |
| 2270 | 20435848 | Mitochondrial membrane potential and the activities of catalase and superoxide dismutase were reduced. |
| 2271 | 20435848 | Three antioxidants, seleno-L-methionine, ginsenoside Rb1, and MnTBAP (superoxide dismutase mimetic), effectively blocked resistin-induced eNOS downregulation. |
| 2272 | 20435848 | Meanwhile, resistin activated the mitogen-activated protein kinases p38 and c-Jun NH(2)-terminal kinase (JNK), and the specific p38 inhibitor SB-239063 effectively blocked resistin-induced ROS production and eNOS downregulation. |
| 2273 | 20435848 | Thus resistin directly induces eNOS downregulation through overproduction of ROS and activation of p38 and JNK in HCAECs. |
| 2274 | 20458637 | That led to use of catalytic antioxidants such as SOD/CAT mimetics. |
| 2275 | 20479714 | The effect of inhibiting diabetes-induced retinal superoxide accumulation on MMP2 and its regulators was investigated in diabetic mice overexpressing mitochondrial superoxide dismutase (MnSOD). |
| 2276 | 20479714 | Inhibition of MMP2 ameliorated glucose-induced increase in mitochondrial superoxide and membrane permeability, prevented cytochrome c leakage from the mitochondria, and inhibited capillary cell apoptosis. |
| 2277 | 20479714 | Overexpression of MnSOD protected the retina from diabetes-induced increase in MMP2 and its membrane activator (MT1-MMP), and decrease in its tissue inhibitor (TIMP-2). |
| 2278 | 20493573 | Oxidative antioxidant markers, immunohistochemical inducible nitric oxide synthase (iNOS) stain, nitric oxide (NO), MDA, Superoxide dismutase (SOD) activity in liver was measured. |
| 2279 | 20493573 | Furthermore, salicylate reversed IH-induced (1) increase in iNOS and NO expression in the liver; (2) increase in MDA/SOD in the liver. |
| 2280 | 20493573 | Oxidative antioxidant markers, immunohistochemical inducible nitric oxide synthase (iNOS) stain, nitric oxide (NO), MDA, Superoxide dismutase (SOD) activity in liver was measured. |
| 2281 | 20493573 | Furthermore, salicylate reversed IH-induced (1) increase in iNOS and NO expression in the liver; (2) increase in MDA/SOD in the liver. |
| 2282 | 20511130 | Glutathione peroxidase (GSH-Px), catalase (CAT), superoxide dismutase (SOD), glutathione (GSH), vitamin A and beta-carotene in brain were decreased (p<0.05) when compared with control in OVX but MDA in brain and glucose in plasma were elevated (p<0.05). |
| 2283 | 20511130 | The activities of GSH-Px (p<0.001, p<0.01), CAT (p<005, p<0.001) and SOD (p<0.001) and the levels of GSH (p<0.001), vitamin A (p<0.05) and beta-carotene (p<0.001, p<0.05) were lower in the brain of OVX diabetic rats, while MDA in the brain and glucose in the plasma were higher (p<0.001). |
| 2284 | 20511130 | Glutathione peroxidase (GSH-Px), catalase (CAT), superoxide dismutase (SOD), glutathione (GSH), vitamin A and beta-carotene in brain were decreased (p<0.05) when compared with control in OVX but MDA in brain and glucose in plasma were elevated (p<0.05). |
| 2285 | 20511130 | The activities of GSH-Px (p<0.001, p<0.01), CAT (p<005, p<0.001) and SOD (p<0.001) and the levels of GSH (p<0.001), vitamin A (p<0.05) and beta-carotene (p<0.001, p<0.05) were lower in the brain of OVX diabetic rats, while MDA in the brain and glucose in the plasma were higher (p<0.001). |
| 2286 | 20521624 | The decrease of lipids and apoprotein levels of VLDL and LDL were followed by stimulation of plasma post-heparin lipolytic activity and lecithin cholesterol acyltransferase as well as hepatic superoxide dismutase and catalase activities. |
| 2287 | 20559501 | Diabetic rats had significantly elevated levels of lipid peroxidation (TBARS), up-regulated activities of superoxide dismutase (SOD) and glutathione peroxidase (GPx) while catalase (CAT) activity was significantly reduced. |
| 2288 | 20570704 | Antioxidant enzyme activities such as catalase (CAT), superoxide dismutase (SOD) and non-enzymatic levels of reduced glutathione (GSH) significantly decreased in the plasma and kidney of diabetic rats compared to those of controls. |
| 2289 | 20585363 | Lipoperoxidation (LPO), and superoxide dismutase (SOD), catalase, and glutathione peroxidase activities were measured in the pulmonary tissue, as well as the presence of inducible nitric oxide synthase (iNOS), through immunohistochemistry. |
| 2290 | 20586612 | Knockouts of SOD1 and GPX1 exert different impacts on murine islet function and pancreatic integrity. |
| 2291 | 20586612 | Using single knockout of Cu,Zn-superoxide dismutase (SOD1(-/-)) or Se-glutathione peroxidase-1 (GPX1(-/-)) and their double-knockout (DKO) mouse models, we determined if elevating endogenously-derived superoxide and hydroperoxide exerted distinct impacts and mechanisms on body glucose homeostasis. |
| 2292 | 20586612 | Whereas the three knockout groups displayed decreased plasma insulin concentrations and islet β-cells mass, only SOD1(-/-) showed decreased body weight, increased blood glucose, and blocked glucose-stimulated insulin secretion. |
| 2293 | 20586612 | Null of SOD1 and GPX1 elevated respective islet superoxide and hydroperoxide production, and upregulated p53 phosphorylation. |
| 2294 | 20586612 | Knockout of SOD1 downregulated the foxhead box A2/pancreatic and duodenal homeobox 1 pathway in a superoxide-dependent fashion at epigenetic, mRNA, and protein levels in islets, but improved insulin signaling in liver and muscle. |
| 2295 | 20586612 | The SOD1(-/-) mice showed more apparent pancreatitis than the GPX1(-/-) mice that were more susceptible to the cerulein-induced amylase increase. |
| 2296 | 20586612 | Knockout of SOD1 impaired islet function, pancreas integrity, and body glucose homeostasis more than that of GPX1. |
| 2297 | 20586612 | Knockouts of SOD1 and GPX1 exert different impacts on murine islet function and pancreatic integrity. |
| 2298 | 20586612 | Using single knockout of Cu,Zn-superoxide dismutase (SOD1(-/-)) or Se-glutathione peroxidase-1 (GPX1(-/-)) and their double-knockout (DKO) mouse models, we determined if elevating endogenously-derived superoxide and hydroperoxide exerted distinct impacts and mechanisms on body glucose homeostasis. |
| 2299 | 20586612 | Whereas the three knockout groups displayed decreased plasma insulin concentrations and islet β-cells mass, only SOD1(-/-) showed decreased body weight, increased blood glucose, and blocked glucose-stimulated insulin secretion. |
| 2300 | 20586612 | Null of SOD1 and GPX1 elevated respective islet superoxide and hydroperoxide production, and upregulated p53 phosphorylation. |
| 2301 | 20586612 | Knockout of SOD1 downregulated the foxhead box A2/pancreatic and duodenal homeobox 1 pathway in a superoxide-dependent fashion at epigenetic, mRNA, and protein levels in islets, but improved insulin signaling in liver and muscle. |
| 2302 | 20586612 | The SOD1(-/-) mice showed more apparent pancreatitis than the GPX1(-/-) mice that were more susceptible to the cerulein-induced amylase increase. |
| 2303 | 20586612 | Knockout of SOD1 impaired islet function, pancreas integrity, and body glucose homeostasis more than that of GPX1. |
| 2304 | 20586612 | Knockouts of SOD1 and GPX1 exert different impacts on murine islet function and pancreatic integrity. |
| 2305 | 20586612 | Using single knockout of Cu,Zn-superoxide dismutase (SOD1(-/-)) or Se-glutathione peroxidase-1 (GPX1(-/-)) and their double-knockout (DKO) mouse models, we determined if elevating endogenously-derived superoxide and hydroperoxide exerted distinct impacts and mechanisms on body glucose homeostasis. |
| 2306 | 20586612 | Whereas the three knockout groups displayed decreased plasma insulin concentrations and islet β-cells mass, only SOD1(-/-) showed decreased body weight, increased blood glucose, and blocked glucose-stimulated insulin secretion. |
| 2307 | 20586612 | Null of SOD1 and GPX1 elevated respective islet superoxide and hydroperoxide production, and upregulated p53 phosphorylation. |
| 2308 | 20586612 | Knockout of SOD1 downregulated the foxhead box A2/pancreatic and duodenal homeobox 1 pathway in a superoxide-dependent fashion at epigenetic, mRNA, and protein levels in islets, but improved insulin signaling in liver and muscle. |
| 2309 | 20586612 | The SOD1(-/-) mice showed more apparent pancreatitis than the GPX1(-/-) mice that were more susceptible to the cerulein-induced amylase increase. |
| 2310 | 20586612 | Knockout of SOD1 impaired islet function, pancreas integrity, and body glucose homeostasis more than that of GPX1. |
| 2311 | 20586612 | Knockouts of SOD1 and GPX1 exert different impacts on murine islet function and pancreatic integrity. |
| 2312 | 20586612 | Using single knockout of Cu,Zn-superoxide dismutase (SOD1(-/-)) or Se-glutathione peroxidase-1 (GPX1(-/-)) and their double-knockout (DKO) mouse models, we determined if elevating endogenously-derived superoxide and hydroperoxide exerted distinct impacts and mechanisms on body glucose homeostasis. |
| 2313 | 20586612 | Whereas the three knockout groups displayed decreased plasma insulin concentrations and islet β-cells mass, only SOD1(-/-) showed decreased body weight, increased blood glucose, and blocked glucose-stimulated insulin secretion. |
| 2314 | 20586612 | Null of SOD1 and GPX1 elevated respective islet superoxide and hydroperoxide production, and upregulated p53 phosphorylation. |
| 2315 | 20586612 | Knockout of SOD1 downregulated the foxhead box A2/pancreatic and duodenal homeobox 1 pathway in a superoxide-dependent fashion at epigenetic, mRNA, and protein levels in islets, but improved insulin signaling in liver and muscle. |
| 2316 | 20586612 | The SOD1(-/-) mice showed more apparent pancreatitis than the GPX1(-/-) mice that were more susceptible to the cerulein-induced amylase increase. |
| 2317 | 20586612 | Knockout of SOD1 impaired islet function, pancreas integrity, and body glucose homeostasis more than that of GPX1. |
| 2318 | 20586612 | Knockouts of SOD1 and GPX1 exert different impacts on murine islet function and pancreatic integrity. |
| 2319 | 20586612 | Using single knockout of Cu,Zn-superoxide dismutase (SOD1(-/-)) or Se-glutathione peroxidase-1 (GPX1(-/-)) and their double-knockout (DKO) mouse models, we determined if elevating endogenously-derived superoxide and hydroperoxide exerted distinct impacts and mechanisms on body glucose homeostasis. |
| 2320 | 20586612 | Whereas the three knockout groups displayed decreased plasma insulin concentrations and islet β-cells mass, only SOD1(-/-) showed decreased body weight, increased blood glucose, and blocked glucose-stimulated insulin secretion. |
| 2321 | 20586612 | Null of SOD1 and GPX1 elevated respective islet superoxide and hydroperoxide production, and upregulated p53 phosphorylation. |
| 2322 | 20586612 | Knockout of SOD1 downregulated the foxhead box A2/pancreatic and duodenal homeobox 1 pathway in a superoxide-dependent fashion at epigenetic, mRNA, and protein levels in islets, but improved insulin signaling in liver and muscle. |
| 2323 | 20586612 | The SOD1(-/-) mice showed more apparent pancreatitis than the GPX1(-/-) mice that were more susceptible to the cerulein-induced amylase increase. |
| 2324 | 20586612 | Knockout of SOD1 impaired islet function, pancreas integrity, and body glucose homeostasis more than that of GPX1. |
| 2325 | 20586612 | Knockouts of SOD1 and GPX1 exert different impacts on murine islet function and pancreatic integrity. |
| 2326 | 20586612 | Using single knockout of Cu,Zn-superoxide dismutase (SOD1(-/-)) or Se-glutathione peroxidase-1 (GPX1(-/-)) and their double-knockout (DKO) mouse models, we determined if elevating endogenously-derived superoxide and hydroperoxide exerted distinct impacts and mechanisms on body glucose homeostasis. |
| 2327 | 20586612 | Whereas the three knockout groups displayed decreased plasma insulin concentrations and islet β-cells mass, only SOD1(-/-) showed decreased body weight, increased blood glucose, and blocked glucose-stimulated insulin secretion. |
| 2328 | 20586612 | Null of SOD1 and GPX1 elevated respective islet superoxide and hydroperoxide production, and upregulated p53 phosphorylation. |
| 2329 | 20586612 | Knockout of SOD1 downregulated the foxhead box A2/pancreatic and duodenal homeobox 1 pathway in a superoxide-dependent fashion at epigenetic, mRNA, and protein levels in islets, but improved insulin signaling in liver and muscle. |
| 2330 | 20586612 | The SOD1(-/-) mice showed more apparent pancreatitis than the GPX1(-/-) mice that were more susceptible to the cerulein-induced amylase increase. |
| 2331 | 20586612 | Knockout of SOD1 impaired islet function, pancreas integrity, and body glucose homeostasis more than that of GPX1. |
| 2332 | 20586612 | Knockouts of SOD1 and GPX1 exert different impacts on murine islet function and pancreatic integrity. |
| 2333 | 20586612 | Using single knockout of Cu,Zn-superoxide dismutase (SOD1(-/-)) or Se-glutathione peroxidase-1 (GPX1(-/-)) and their double-knockout (DKO) mouse models, we determined if elevating endogenously-derived superoxide and hydroperoxide exerted distinct impacts and mechanisms on body glucose homeostasis. |
| 2334 | 20586612 | Whereas the three knockout groups displayed decreased plasma insulin concentrations and islet β-cells mass, only SOD1(-/-) showed decreased body weight, increased blood glucose, and blocked glucose-stimulated insulin secretion. |
| 2335 | 20586612 | Null of SOD1 and GPX1 elevated respective islet superoxide and hydroperoxide production, and upregulated p53 phosphorylation. |
| 2336 | 20586612 | Knockout of SOD1 downregulated the foxhead box A2/pancreatic and duodenal homeobox 1 pathway in a superoxide-dependent fashion at epigenetic, mRNA, and protein levels in islets, but improved insulin signaling in liver and muscle. |
| 2337 | 20586612 | The SOD1(-/-) mice showed more apparent pancreatitis than the GPX1(-/-) mice that were more susceptible to the cerulein-induced amylase increase. |
| 2338 | 20586612 | Knockout of SOD1 impaired islet function, pancreas integrity, and body glucose homeostasis more than that of GPX1. |
| 2339 | 20614191 | At the end, alterations in serum glucose, insulin, triiodothyronine, thyroxine, total cholesterol, triglyceride, high density lipoprotein, low density lipoprotein, very low density lipoprotein, hepatic lipid peroxidation, superoxide dismutase and catalase were studied. |
| 2340 | 20618069 | Pancreatic islets contain low activities of catalase, selenium-dependent glutathione peroxidase 1 (GPX1), and Cu,Zn-superoxide dismutase 1 (SOD1). |
| 2341 | 20618069 | While β cell-specific overexpression of Sod1 enhanced mouse resistance to streptozotocin-induced diabetes, the same manipulation of catalase aggravated onset of type 1 diabetes in nonobese diabetic mice. |
| 2342 | 20618069 | Although knockouts of Gpx1 and Sod1 each alone or together decreased pancreatic β cell mass and plasma insulin concentrations, these knockouts improved body insulin sensitivity to different extents. |
| 2343 | 20618069 | Pancreatic duodenal homeobox 1, forkhead box A2, and uncoupling protein 2 are three key regulators of β cell mass, insulin synthesis, and glucose-stimulated insulin secretion. |
| 2344 | 20618069 | Phenotypes resulted from altering GPX1 and/or SOD1 were partly mediated through these factors, along with protein kinase B and c-jun terminal kinase. |
| 2345 | 20618069 | Pancreatic islets contain low activities of catalase, selenium-dependent glutathione peroxidase 1 (GPX1), and Cu,Zn-superoxide dismutase 1 (SOD1). |
| 2346 | 20618069 | While β cell-specific overexpression of Sod1 enhanced mouse resistance to streptozotocin-induced diabetes, the same manipulation of catalase aggravated onset of type 1 diabetes in nonobese diabetic mice. |
| 2347 | 20618069 | Although knockouts of Gpx1 and Sod1 each alone or together decreased pancreatic β cell mass and plasma insulin concentrations, these knockouts improved body insulin sensitivity to different extents. |
| 2348 | 20618069 | Pancreatic duodenal homeobox 1, forkhead box A2, and uncoupling protein 2 are three key regulators of β cell mass, insulin synthesis, and glucose-stimulated insulin secretion. |
| 2349 | 20618069 | Phenotypes resulted from altering GPX1 and/or SOD1 were partly mediated through these factors, along with protein kinase B and c-jun terminal kinase. |
| 2350 | 20618069 | Pancreatic islets contain low activities of catalase, selenium-dependent glutathione peroxidase 1 (GPX1), and Cu,Zn-superoxide dismutase 1 (SOD1). |
| 2351 | 20618069 | While β cell-specific overexpression of Sod1 enhanced mouse resistance to streptozotocin-induced diabetes, the same manipulation of catalase aggravated onset of type 1 diabetes in nonobese diabetic mice. |
| 2352 | 20618069 | Although knockouts of Gpx1 and Sod1 each alone or together decreased pancreatic β cell mass and plasma insulin concentrations, these knockouts improved body insulin sensitivity to different extents. |
| 2353 | 20618069 | Pancreatic duodenal homeobox 1, forkhead box A2, and uncoupling protein 2 are three key regulators of β cell mass, insulin synthesis, and glucose-stimulated insulin secretion. |
| 2354 | 20618069 | Phenotypes resulted from altering GPX1 and/or SOD1 were partly mediated through these factors, along with protein kinase B and c-jun terminal kinase. |
| 2355 | 20618069 | Pancreatic islets contain low activities of catalase, selenium-dependent glutathione peroxidase 1 (GPX1), and Cu,Zn-superoxide dismutase 1 (SOD1). |
| 2356 | 20618069 | While β cell-specific overexpression of Sod1 enhanced mouse resistance to streptozotocin-induced diabetes, the same manipulation of catalase aggravated onset of type 1 diabetes in nonobese diabetic mice. |
| 2357 | 20618069 | Although knockouts of Gpx1 and Sod1 each alone or together decreased pancreatic β cell mass and plasma insulin concentrations, these knockouts improved body insulin sensitivity to different extents. |
| 2358 | 20618069 | Pancreatic duodenal homeobox 1, forkhead box A2, and uncoupling protein 2 are three key regulators of β cell mass, insulin synthesis, and glucose-stimulated insulin secretion. |
| 2359 | 20618069 | Phenotypes resulted from altering GPX1 and/or SOD1 were partly mediated through these factors, along with protein kinase B and c-jun terminal kinase. |
| 2360 | 20626057 | All rats were examined for body weight, serum and hepatic biochemical indices, content of malondialdehyde (MDA), activities of superoxide dismutase (SOD) and pathological changes in liver and pancreas, as well as protein tyrosine phosphatase 1B (PTP1B) expression in liver. |
| 2361 | 20626057 | Treatment with TFLC showed a significant increase in insulin sensitivity, serum HDL-C level and SOD activities, meanwhile marked decrease in body weight, serum FFA, TC, TG, LDL-C, CRP, MDA content. |
| 2362 | 20626057 | All rats were examined for body weight, serum and hepatic biochemical indices, content of malondialdehyde (MDA), activities of superoxide dismutase (SOD) and pathological changes in liver and pancreas, as well as protein tyrosine phosphatase 1B (PTP1B) expression in liver. |
| 2363 | 20626057 | Treatment with TFLC showed a significant increase in insulin sensitivity, serum HDL-C level and SOD activities, meanwhile marked decrease in body weight, serum FFA, TC, TG, LDL-C, CRP, MDA content. |
| 2364 | 20632216 | The activities of superoxide dismutase, catalase and glyoxalase I were assayed. |
| 2365 | 20632216 | Catalase and glyoxalase I had a decrease in their activities. |
| 2366 | 20656571 | Most up-regulated proteins like Ubiquinol-cytochrome-c reductase complex core protein I (UQCRC1), ATP synthase D chain, Superoxide dismutase (SOD), Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), Sulfotransferase 1A1 (SULT1A1), Carnitine O-palmitoyltransferase 2 (CPT2) and Heat-shock protein beta 1 (HSPB1) across the three depots were found to be associated with lipid metabolism and metabolic activity. |
| 2367 | 20669150 | Their parotid (PA) and submandibular (SM) glands were removed soon after the sacrifice and the total protein and malondialdehyde (MDA) concentrations, as well as, the superoxide dismutase (SOD), glutathione peroxidase (GPx), and catalase (CAT) activities were determined. |
| 2368 | 20669150 | Twenty-one days after the diabetes induction, the SM glands showed an increase in SOD, CAT, and GPx activities, as well as, MDA concentration. |
| 2369 | 20669150 | Their parotid (PA) and submandibular (SM) glands were removed soon after the sacrifice and the total protein and malondialdehyde (MDA) concentrations, as well as, the superoxide dismutase (SOD), glutathione peroxidase (GPx), and catalase (CAT) activities were determined. |
| 2370 | 20669150 | Twenty-one days after the diabetes induction, the SM glands showed an increase in SOD, CAT, and GPx activities, as well as, MDA concentration. |
| 2371 | 20685284 | The present study was aimed to investigate the possible effects of beta-casomorphin-7, against hyperglycemia and free radical-mediated oxidative stress in streptozotocin-induced diabetic rats by assaying the blood glucose level and the activity of plasma enzymatic antioxidants, such as superoxide dismutase (SOD), catalase and glutathione peroxidase (GSH-Px). |
| 2372 | 20705622 | Oxidative stress is one of the major markers of inflammatory response and oxidative stress markers such as lipid peroxidation, thiobarbituric acid reactive substance (TBARS), Superoxide Dismutase (SOD), Catalase, G Peroxidase, G-S Peroxidase and plasma total antioxidant play a major role in the nonhealing of diabetic foot ulcers. |
| 2373 | 20705622 | Growth factors such as platelet-derived growth factor (PDGF), transforming growth factor (VEGF), and epidermal growth factor (EGF) are needed for normal wound repair, while proteases such as matrix metalloproteinase (MMP) and serine proteases found in chronic wounds delay the healing process. |
| 2374 | 20709041 | The oxidative stress was measured by tissue thiobarbituric acid reactive substances (TBARS), reduced glutathione (GSH) content and enzymatic activities of superoxide dismutase (SOD), catalase (CAT) and glutathione peroxidase (GPx) in brain, liver, heart, kidney and pancreas. |
| 2375 | 20709041 | An increase in TBARS level, a significant reduction in GSH content along with decreased enzymatic activities of SOD, CAT, and GPx were seen in untreated diabetic rats. |
| 2376 | 20709041 | Administration of either costunolide (20mg/kg day) or eremanthin (20mg/kg day) for 60 days caused a significant reduction in TBARS level and a significant increase in GSH content along with increased enzymatic activities of SOD, CAT and GPx in the treated rats when compared to untreated diabetic rats. |
| 2377 | 20709041 | The oxidative stress was measured by tissue thiobarbituric acid reactive substances (TBARS), reduced glutathione (GSH) content and enzymatic activities of superoxide dismutase (SOD), catalase (CAT) and glutathione peroxidase (GPx) in brain, liver, heart, kidney and pancreas. |
| 2378 | 20709041 | An increase in TBARS level, a significant reduction in GSH content along with decreased enzymatic activities of SOD, CAT, and GPx were seen in untreated diabetic rats. |
| 2379 | 20709041 | Administration of either costunolide (20mg/kg day) or eremanthin (20mg/kg day) for 60 days caused a significant reduction in TBARS level and a significant increase in GSH content along with increased enzymatic activities of SOD, CAT and GPx in the treated rats when compared to untreated diabetic rats. |
| 2380 | 20709041 | The oxidative stress was measured by tissue thiobarbituric acid reactive substances (TBARS), reduced glutathione (GSH) content and enzymatic activities of superoxide dismutase (SOD), catalase (CAT) and glutathione peroxidase (GPx) in brain, liver, heart, kidney and pancreas. |
| 2381 | 20709041 | An increase in TBARS level, a significant reduction in GSH content along with decreased enzymatic activities of SOD, CAT, and GPx were seen in untreated diabetic rats. |
| 2382 | 20709041 | Administration of either costunolide (20mg/kg day) or eremanthin (20mg/kg day) for 60 days caused a significant reduction in TBARS level and a significant increase in GSH content along with increased enzymatic activities of SOD, CAT and GPx in the treated rats when compared to untreated diabetic rats. |
| 2383 | 20728477 | Lipid peroxidation, xanthine oxidase activity, myeloperoxidase activity and nitric oxide level in renal tissue were significantly (p < 0.05, p < 0.001, p < 0.01, p < 0.05 respectively) decreased after renal I/R in sitagliptin treated rats compared to diabetic rats. |
| 2384 | 20728477 | Antioxidant enzymes like glutathione (p < 0.05), glutathione peroxidase (p < 0.001), superoxide dismutase (p < 0.05) and catalase (p < 0.001) were significantly increased after renal I/R in sitagliptin treated diabetic rats compared to non treated diabetic rats. |
| 2385 | 20734144 | The anti-diabetic effect was examined by blood glucose, triglycerides, lipid peroxidation, total cholesterol levels in the serum, glycogen content of liver and skeletal muscles, superoxide dismutase (SOD), catalase (CAT), glutathione (GSH) and oxidized glutathione (GSSG) levels. |
| 2386 | 20734144 | Hexane and chloroform extracts from fruits and seeds of Byrsonima crassifolia increased the levels of SOD, GSH, GSSG and CAT, hepatic glycogen content, glucose-6-phosphatase (G6Pase) and the plasma insulin levels. |
| 2387 | 20734144 | The anti-diabetic effect was examined by blood glucose, triglycerides, lipid peroxidation, total cholesterol levels in the serum, glycogen content of liver and skeletal muscles, superoxide dismutase (SOD), catalase (CAT), glutathione (GSH) and oxidized glutathione (GSSG) levels. |
| 2388 | 20734144 | Hexane and chloroform extracts from fruits and seeds of Byrsonima crassifolia increased the levels of SOD, GSH, GSSG and CAT, hepatic glycogen content, glucose-6-phosphatase (G6Pase) and the plasma insulin levels. |
| 2389 | 20823566 | After 8 weeks of COS treatment, the changes in glycometabolism, insulin sensitivity, serum hepatic marker enzyme levels, liver glycogen content, expressions of glucose transporter GLUT-4, malonaldehyde content, superoxide dismutase activity and morphology of the pancreas were observed. |
| 2390 | 20823566 | COS increased liver glucokinase activity and glycogen content and upregulated the expressions of GLUT-4 mRNA in adipose and soleus muscle. |
| 2391 | 20823566 | It was found that COS played important roles in INS-1 cells by promoting proliferation, increasing glucose stimulated insulin release, upregulating the expressions of GLUT-2 mRNA and protecting against STZ-induced apoptosis. |
| 2392 | 20838862 | The activities of the antioxidant enzymes catalase, superoxide dismutase and glutathione peroxidase showed no significant differences among all groups of animals. |
| 2393 | 20839055 | To assess the changes in the cellular antioxidant defense system, the level of reduced glutathione in plasma and pancreas and activities of superoxide dismutase and catalase were assayed in pancreatic tissue homogenate. |
| 2394 | 20844835 | The reduced expression of angiotensin-converting enzyme (ACE) 2 in the kidneys of animal models and patients with diabetes suggests ACE2 involvement in diabetic nephrology. |
| 2395 | 20844835 | To explore the renoprotective effects of ACE2 overexpression, ACE inhibition (ACEI) or both on diabetic nephropathy and the potential mechanisms involved, 50 Wistar rats were randomly divided into a normal group that received an injection of sodium citrate buffer and a diabetic model group that received an injection of 60 mg/kg streptozotocin. |
| 2396 | 20844835 | An experiment in cultured glomerular mesangial cells was performed to examine the effects of ACE2 on cellular proliferation, oxidative stress and collagen IV synthesis. |
| 2397 | 20844835 | In comparison with the Ad-GFP group, the Ad-ACE2 group exhibited reduced systolic blood pressure, urinary albumin excretion, creatinine clearance, glomeruli sclerosis index and renal malondialdehyde level; downregulated transforming growth factor (TGF)-β1, vascular endothelial growth factor (VEGF) and collagen IV protein expression; and increased renal superoxide dismutase activity. |
| 2398 | 20844835 | ACE2 transfection attenuated angiotensin (Ang) II-induced glomerular mesangial cell proliferation, oxidative stress and collagen IV protein synthesis. |
| 2399 | 20851292 | Polymorphisms of superoxide dismutase, glutathione peroxidase and catalase genes in patients with post-transplant diabetes mellitus. |
| 2400 | 20863784 | The pancreatic thiobarbituric acid reactive substances and lipid hydroperoxides were significantly (P<0.05) increased and the activities of pancreatic superoxide dismutase, catalase and glutathione peroxidase were significantly (P<0.05) decreased in diabetic rats. |
| 2401 | 20878014 | However, when neutrophils were stimulated by receptor-bypassing phorbol 12-myristate 13-acetate (PMA), gangliosides above their critical micellar concentrations prolonged the lag time preceding the production in a concentration-dependent way, without affecting total extracellular O₂·⁻ generation detected by superoxide dismutase-inhibitable cytochrome c reduction. |
| 2402 | 20878014 | The effect of ganglioside GT1b (100 µM) on the increase in lag time was shown to be significant by means of both superoxide dismutase-inhibitable cytochrome c reduction assay and electron paramagnetic resonance spectroscopy (P < 0.0001 and P < 0.005, respectively). |
| 2403 | 20878014 | However, when neutrophils were stimulated by receptor-bypassing phorbol 12-myristate 13-acetate (PMA), gangliosides above their critical micellar concentrations prolonged the lag time preceding the production in a concentration-dependent way, without affecting total extracellular O₂·⁻ generation detected by superoxide dismutase-inhibitable cytochrome c reduction. |
| 2404 | 20878014 | The effect of ganglioside GT1b (100 µM) on the increase in lag time was shown to be significant by means of both superoxide dismutase-inhibitable cytochrome c reduction assay and electron paramagnetic resonance spectroscopy (P < 0.0001 and P < 0.005, respectively). |
| 2405 | 20929060 | Increased level of lipid peroxidation, protein oxidation, superoxide dismutase and catalase activities under diabetic condition remained unchanged in arsenic exposed diabetic group compared to unexposed diabetic group. |
| 2406 | 20931083 | (Lamiaceae) (PPE) was studied to evaluate the effects of antidiabetic potential, by measuring fasting blood glucose, insulin, total antioxidant power (TAP), using ferric reducing antioxidant power (FRAP), lipid peroxidation (using thiobarbituric acid reactive substances, TBARS), superoxide dismutase (SOD), catalase (CAT), and glutathione peroxidase (GPx) on streptozotocin-induced diabetes in rats. |
| 2407 | 20931083 | The extract at 100 and 200 mg/kg increased the activity of hepatic SOD, CAT, and GPx in diabetic rats. |
| 2408 | 20931083 | (Lamiaceae) (PPE) was studied to evaluate the effects of antidiabetic potential, by measuring fasting blood glucose, insulin, total antioxidant power (TAP), using ferric reducing antioxidant power (FRAP), lipid peroxidation (using thiobarbituric acid reactive substances, TBARS), superoxide dismutase (SOD), catalase (CAT), and glutathione peroxidase (GPx) on streptozotocin-induced diabetes in rats. |
| 2409 | 20931083 | The extract at 100 and 200 mg/kg increased the activity of hepatic SOD, CAT, and GPx in diabetic rats. |
| 2410 | 20951120 | The effects of SAC on glucose, plasma insulin, thiobarbituric acid reactive substances (TBARS), hydroperoxide, superoxide dismutase (SOD), catalase (CAT), glutathione peroxidase (GPx), reduced glutathione (GSH), oxidized glutathione (GSSG) and GSH/GSSG ratio were studied. |
| 2411 | 20951120 | The levels of glucose, TBARS, hydroperoxide, and GSSG were increased significantly whereas the levels of plasma insulin, reduced glutathione, GSH/GSSG ratio, superoxide dismutase, catalase and GPx were decreased in STZ induced diabetic rats. |
| 2412 | 20951120 | In addition, the levels of plasma insulin, superoxide dismutase, catalase, GPx and reduced glutathione (GSH) were increased in SAC treated diabetic rats. |
| 2413 | 20951120 | The effects of SAC on glucose, plasma insulin, thiobarbituric acid reactive substances (TBARS), hydroperoxide, superoxide dismutase (SOD), catalase (CAT), glutathione peroxidase (GPx), reduced glutathione (GSH), oxidized glutathione (GSSG) and GSH/GSSG ratio were studied. |
| 2414 | 20951120 | The levels of glucose, TBARS, hydroperoxide, and GSSG were increased significantly whereas the levels of plasma insulin, reduced glutathione, GSH/GSSG ratio, superoxide dismutase, catalase and GPx were decreased in STZ induced diabetic rats. |
| 2415 | 20951120 | In addition, the levels of plasma insulin, superoxide dismutase, catalase, GPx and reduced glutathione (GSH) were increased in SAC treated diabetic rats. |
| 2416 | 20951120 | The effects of SAC on glucose, plasma insulin, thiobarbituric acid reactive substances (TBARS), hydroperoxide, superoxide dismutase (SOD), catalase (CAT), glutathione peroxidase (GPx), reduced glutathione (GSH), oxidized glutathione (GSSG) and GSH/GSSG ratio were studied. |
| 2417 | 20951120 | The levels of glucose, TBARS, hydroperoxide, and GSSG were increased significantly whereas the levels of plasma insulin, reduced glutathione, GSH/GSSG ratio, superoxide dismutase, catalase and GPx were decreased in STZ induced diabetic rats. |
| 2418 | 20951120 | In addition, the levels of plasma insulin, superoxide dismutase, catalase, GPx and reduced glutathione (GSH) were increased in SAC treated diabetic rats. |
| 2419 | 20956460 | Additionally, Chinese propolis induced an increase in the serum superoxide dismutase (SOD) level significantly while Brazilian propolis raised serum SOD and reduced level of malonaldehyde (MDA) and nitric synthetase (NOS). |
| 2420 | 21035442 | Elevated free fatty acids and impaired adiponectin bioactivity contribute to reduced SOD2 protein in monocytes of type 2 diabetes patients. |
| 2421 | 21035442 | Monocytes are critically important in the pathogenesis of CVD and antioxidant enzymes like superoxide dismutase (SOD2) protect these cells from excessive reactive oxygen species (ROS). |
| 2422 | 21035442 | Adiponectin is an adipocyte-derived protein with atheroprotective function and the effect of adiponectin on monocyte SOD2 was analyzed herein. |
| 2423 | 21035442 | Adiponectin upregulated SOD2 mRNA and dose- and time-dependently induced SOD2 protein in primary human monocytes. |
| 2424 | 21035442 | Adiponectin mediated upregulation of SOD2, however, was not affected by FFA incubation. |
| 2425 | 21035442 | Adiponectin still induced SOD2 in T2D monocytes but efficiency tended to be reduced. |
| 2426 | 21035442 | In summary this study indicates that elevated systemic free fatty acids and impaired adiponectin activity contribute to reduced SOD2 and most likely increased oxidative stress in T2D monocytes. |
| 2427 | 21050844 | Aortic inducible (iNOS) and endothelial nitric oxide synthase (eNOS) protein content was measured by western immunoblotting. |
| 2428 | 21050844 | Finally it restored the iNOS and eNOS content and the superoxide dismutase activity in thoracic aorta. |
| 2429 | 21080139 | When compared to those of the untreated diabetic rats, the superoxide dismutase, catalase, and glutathione peroxidase levels in the pancreas of the rats treated with this supplement were also enhanced by 330%, 170%, and 301%, respectively. |
| 2430 | 21086547 | Lipid peroxidation levels and the activities of superoxide-dismutase, catalase and glutathione peroxidase were then measured in liver and pancreas. |
| 2431 | 21086547 | In addition, treatment with garlic extract or α-tocopherol + magnesium appeared to exert an antioxidative activity demonstrated (1) by the increase of catalase, superoxide-dismutase and glutathione-peroxidase activities in liver and pancreas, and (2) a lowering of lipid peroxidation level in these organs. |
| 2432 | 21086547 | Lipid peroxidation levels and the activities of superoxide-dismutase, catalase and glutathione peroxidase were then measured in liver and pancreas. |
| 2433 | 21086547 | In addition, treatment with garlic extract or α-tocopherol + magnesium appeared to exert an antioxidative activity demonstrated (1) by the increase of catalase, superoxide-dismutase and glutathione-peroxidase activities in liver and pancreas, and (2) a lowering of lipid peroxidation level in these organs. |
| 2434 | 21086754 | In addition, changes in renal lipid peroxidation (LPO), activities of superoxide dismutase (SOD) and catalase (CAT), reduced glutathione (GSH) content, as well as renal somatic index (RSI) and daily rate of water consumption were also investigated. |
| 2435 | 21086754 | While dexamethasone administration (1.0 mg/kg for 21 days) expressed two renal proteins (43 kDa and 63.23 kDa), in addition to the increased fasting serum levels of glucose and insulin, renal LPO, RSI and daily rate of water consumption, a parallel decrease in renal SOD, CAT and GSH was also observed. |
| 2436 | 21086754 | In addition, changes in renal lipid peroxidation (LPO), activities of superoxide dismutase (SOD) and catalase (CAT), reduced glutathione (GSH) content, as well as renal somatic index (RSI) and daily rate of water consumption were also investigated. |
| 2437 | 21086754 | While dexamethasone administration (1.0 mg/kg for 21 days) expressed two renal proteins (43 kDa and 63.23 kDa), in addition to the increased fasting serum levels of glucose and insulin, renal LPO, RSI and daily rate of water consumption, a parallel decrease in renal SOD, CAT and GSH was also observed. |
| 2438 | 21108110 | The soy isoflavones were also protected hepatic-kidney functions showed by the significant increase in superoxide dismutase, catalase and glutathione peroxidase activities and the decrease in thiobarbituric acid reactive substances, total bilirubin, creatinine and transaminases content. |
| 2439 | 21120613 | It also showed an improved antioxidant potential as evidenced by decreased lipid peroxidation and a significant increase in the activity of various antioxidant enzymes such as catalase, superoxide dismutase, glutathione peroxidase and glutathione reductase. |
| 2440 | 21151615 | Shen-Fu injection preconditioning inhibits myocardial ischemia-reperfusion injury in diabetic rats: activation of eNOS via the PI3K/Akt pathway. |
| 2441 | 21151615 | SFI preconditioning significantly decreased infarct size, apoptosis, caspase-3 protein expression, MDA level in myocardial tissues, and plasma level of CK and LDH but increased p-Akt, p-eNOS, bcl-2 protein expression, and SOD activity compared to I/R group. |
| 2442 | 21153246 | Abnormal serum IGF-II transport in non-islet cell tumor hypoglycemia results from abnormalities of both IGF binding protein-3 and acid labile subunit and leads to elevation of serum free IGF-II. |
| 2443 | 21153246 | This is attributable to abnormalities of the IGF binding proteins (IGFBPs) present in NICTH which is characterized by a marked decrease in the fraction of IGFBP-3 present in the 150 kD complex with acid labile subunit (ALS) and a 2- to 4-fold increase in IGFBP-2. |
| 2444 | 21153246 | We studied the impact of these changes in IGFBPs on the concentration of free IGF-II using a neutral C-18 Sep-Pak extraction procedure. |
| 2445 | 21153246 | We conclude that both a functional deficiency of ALS and IGFBP-3 are present in NICTH sera. |
| 2446 | 21154199 | Administration of bacosine and glibenclamide significantly decreased the levels of malondialdehyde (MDA), and increased the levels of reduced glutathione (GSH) and the activities of superoxide dismutase (SOD) and catalase (CAT) in the liver of diabetic rats. |
| 2447 | 21174950 | Antioxidant activities (superoxide dismutase, catalase, reduced glutathione content and glutathione-s-transferase) and lipid peroxidation levels were measured in heart, kidney and liver tissues of normal, diabetic and experimental animals (diabetics + treatment). |
| 2448 | 21184796 | A marked decrease in anti-oxidant marker enzymes, superoxide dismutase (SOD), catalase (CAT), glutathione peroxidase (GPx), glutathione reductase (GR), reduced glutathione (GSH) and increase in malondialdehyde (MDA) was observed in the diabetic rats. |
| 2449 | 21189167 | Effect of natural polyphenols, pycnogenol® on superoxide dismutase and nitric oxide synthase in diabetic rats. |
| 2450 | 21189167 | The work is focused on clarifying the impact of diabetes and natural plant polyphenols contained in Pycnogenol® (PYC) on the activity and synthesis of Cu/Zn-SOD and synthesis of nNOS and eNOS in the cerebellum and cerebral cortex in rats with induced diabetes. |
| 2451 | 21204649 | We measured levels of glycosylated hemoglobin (HbA1c), plasma lipid peroxides, superoxide dismutase, glutathione peroxidase, total antioxidants, and tumor necrosis factor-alpha (TNF-α). |
| 2452 | 21234421 | Fenofibrate treatment restored the impaired endothelium-dependent relaxation and increased basal nitric oxide availability in diabetic aorta, enhanced erythrocyte/liver superoxide dismutase and catalase levels, ameliorated the abnormal serum/aortic thiobarbituric acid reactive substances, and prevented the increased aortic myeloperoxidase without a significant change in serum total cholesterol and triglyceride levels. |
| 2453 | 21240568 | LPO level was higher in diabetic pregnant rats than in control, although superoxide dismutase, catalase, and glutathione peroxidase activities were lower in diabetic pregnant animals than in control. |
| 2454 | 21249318 | Superoxide dismutase-dependent production of hydrogen peroxide led to increased cell invasive and migratory ability and the expression of urokinase plasminogen activator. |
| 2455 | 21251685 | Arterial levels of the antioxidant enzymes, superoxide dismutase, catalase, and heme oxygenase-1 were not higher in STZ-DM, although superoxide was higher, suggesting impaired antioxidant response. |
| 2456 | 21307644 | Lipid peroxidation (TBARS), catalase and superoxide dismutase were measured to evaluate the oxidative stress and the BrdU-positive cells were assessed to measure changes in cellular proliferation. |
| 2457 | 21314459 | In addition, licorice extract modulated the adverse effect of diabetes on renal malondialdehyde, glutathione, superoxide dismutase, and catalase activity. |
| 2458 | 21322281 | [Study of SOD and PON-1 expression in type 2 diabetes mellitus nephropathy and its clinical significance]. |
| 2459 | 21327985 | Control versus patient results in the univariate analysis were the following: pre-gestational body mass index [BMI] 23.31 ± 4.2 vs. 27.13 ± 4.6 kg/m(2) (P = 0.001); weeks at delivery 39.2 ± 3.05 vs. 38.9 ± 1.8 (P = 0.09); Caesarean delivery 12.5 vs. 43% (P = 0.004); macrosomia 4 vs. 9.4% (P = 0.6); lipoperoxides [LPO] 2.06 ± 1.00 vs. 3.14 ± 1.55 μmol/mg (P = 0.001); catalase 3.23 ± 1.41 vs. 2.52 ± 1.3 nmol/min/ml (P = 0.03); superoxide dismutase [SOD] 0.11 ± 0.04 vs. 0.08 ± 0.01 U/ml (P = 0.0003); glutathione peroxidase [GPX] 0.03 ± 0.006 vs. 0.025 ± 0.006 nmol/min/ml (P = 0.01); glutathione reductase [GSH] 0.004 ± 0.002 vs. 0.004 ± 0.004 nmol/min/ml (P = 0.9)]; and glutathione transferase [GST] 0.0025 ± 0.0012 vs. 0.0027 ± 0.00017 nmol/min/ml (P = 0.7). |
| 2460 | 21336648 | Serum levels of basic fibroblast growth factor (b-FGF) was measured by immunosorbent assay kit; advanced glycosylation end products, platelet-derived endothelial cell growth factor (PD-ECGF), cathepsin-D (CD), gangliosides, hyaluronic acid (HA), nitric oxide (NO), lipid peroxides (LPER), superoxide dismutase, and total thiols by chemical methods; and copper (Cu) by atomic absorption flame photometry. |
| 2461 | 21340016 | Malondialdehyde (MDA) levels, glutathione peroxidase (GPx) and superoxide dismutase (SOD) activities were significantly elevated while catalase (CAT) activity, total antioxidant status (TAS), reduced glutathione (GSH), and GSH:oxidized glutathione (GSSG) ratio was significantly reduced in the diabetic kidneys. |
| 2462 | 21340016 | CAT, glutathione reductase (GR), TAS, and GSH remained significantly reduced in the diabetic rats treated with metformin and/or glibenclamide. |
| 2463 | 21364932 | Cerium oxide nanoparticles (nanoceria) catalytically scavenge ROS by mimicking the activities of superoxide dismutase and catalase. |
| 2464 | 21366960 | Its effect on gene expression level of the tissue—specific cytochrome P450 (CYP) was also studied. |
| 2465 | 21366960 | The elevated level of lipid peroxidation was decreased and the decreased activities of antioxidant enzymes such as catalase, superoxide dismutase, glutathione peroxidase and glutathione-S-transferase were increased significantly (p<0.05) in treated rats. |
| 2466 | 21378371 | The activities of catalase, superoxide dismutase, and glyoxalase I were also assessed. |
| 2467 | 21428214 | The aqueous banaba leaf extract (150 mg/kg bodyweight) duly reduced STZ generated reactive intermediates and radical species helping to regulate normal levels of antioxidative markers like superoxide dismutase, catalase, glutathione-S-transferase and reduced glutathione. |
| 2468 | 21439372 | Oral administration of resveratrol to diabetic rats showed a significant normalization on the levels of creatinine clearance, plasma adiponectin, C-peptide and renal superoxide anion, hydroxyl radical, nitric oxide, TNF-α, IL-1β, IL-6 and NF-κB p65 subunit and activities of renal aspartate transaminase, alanine transaminase and alkaline phosphatase in comparison with diabetic rats. |
| 2469 | 21439372 | The altered activities of renal aldose reductase, sorbitol dehydrogenase and glyoxalase-I and elevated level of serum advanced glycation end products in diabetic rats were also reverted back to near normalcy. |
| 2470 | 21439372 | Further, resveratrol treatment revealed a significant improvement in superoxide dismutase, catalase, glutathione peroxidase, glutathione-S-transferase and glutathione reductase activities and vitamins C and E, and reduced glutathione levels, with a significant decline in lipid peroxides, hydroperoxides and protein carbonyls levels in diabetic kidneys. |
| 2471 | 21454169 | There is significant increases in the pancreatic enzyme like SOD, CAT and Glutathione expression when compare with the untreated group. |
| 2472 | 21479831 | Antioxidant enzymes, superoxide dismutase (SOD), catalase (CAT), glutathione reductase (GR), glutathione peroxidase (GPx), glutathione-S-transferase (GST), as well as carbonic anhydrase (CA), myeloperoxidase (MPO) activities and protein carbonyl content (PCC) were determined in muscle tissue. |
| 2473 | 21484408 | The aim of this study was to investigate the effects of vitamin E (alpha-tocopherol) and 17β-estradiol (E(2)) supplementation on malondialdehyde (MDA), glutathione (GSH), vitamin A, beta carotene, selenium-dependent glutathione peroxidase (GSH-Px), zinc-dependent superoxide dismutase (SOD), and copper/zinc-dependent catalase (CAT) values in the kidney of ovariectomized (OVX) diabetic rats. |
| 2474 | 21484408 | GSH-Px, CAT, SOD, GSH levels, vitamin A, and beta carotene levels were decreased in OVX group compared to those in the control group but MDA level was elevated via ovariectomy. |
| 2475 | 21484408 | However, GSH, GSH-Px, CAT, SOD, vitamin A, and beta carotene levels in kidney were lower in OVX diabetic rats. |
| 2476 | 21484408 | On the other hand, E(2) and E(2)+alpha-tocopherol supplementations to OVX diabetic rats have caused an increase in GSH-Px, CAT and SOD, GSH, vitamin A, and beta carotene levels but a decrease in MDA levels. |
| 2477 | 21484408 | The aim of this study was to investigate the effects of vitamin E (alpha-tocopherol) and 17β-estradiol (E(2)) supplementation on malondialdehyde (MDA), glutathione (GSH), vitamin A, beta carotene, selenium-dependent glutathione peroxidase (GSH-Px), zinc-dependent superoxide dismutase (SOD), and copper/zinc-dependent catalase (CAT) values in the kidney of ovariectomized (OVX) diabetic rats. |
| 2478 | 21484408 | GSH-Px, CAT, SOD, GSH levels, vitamin A, and beta carotene levels were decreased in OVX group compared to those in the control group but MDA level was elevated via ovariectomy. |
| 2479 | 21484408 | However, GSH, GSH-Px, CAT, SOD, vitamin A, and beta carotene levels in kidney were lower in OVX diabetic rats. |
| 2480 | 21484408 | On the other hand, E(2) and E(2)+alpha-tocopherol supplementations to OVX diabetic rats have caused an increase in GSH-Px, CAT and SOD, GSH, vitamin A, and beta carotene levels but a decrease in MDA levels. |
| 2481 | 21484408 | The aim of this study was to investigate the effects of vitamin E (alpha-tocopherol) and 17β-estradiol (E(2)) supplementation on malondialdehyde (MDA), glutathione (GSH), vitamin A, beta carotene, selenium-dependent glutathione peroxidase (GSH-Px), zinc-dependent superoxide dismutase (SOD), and copper/zinc-dependent catalase (CAT) values in the kidney of ovariectomized (OVX) diabetic rats. |
| 2482 | 21484408 | GSH-Px, CAT, SOD, GSH levels, vitamin A, and beta carotene levels were decreased in OVX group compared to those in the control group but MDA level was elevated via ovariectomy. |
| 2483 | 21484408 | However, GSH, GSH-Px, CAT, SOD, vitamin A, and beta carotene levels in kidney were lower in OVX diabetic rats. |
| 2484 | 21484408 | On the other hand, E(2) and E(2)+alpha-tocopherol supplementations to OVX diabetic rats have caused an increase in GSH-Px, CAT and SOD, GSH, vitamin A, and beta carotene levels but a decrease in MDA levels. |
| 2485 | 21484408 | The aim of this study was to investigate the effects of vitamin E (alpha-tocopherol) and 17β-estradiol (E(2)) supplementation on malondialdehyde (MDA), glutathione (GSH), vitamin A, beta carotene, selenium-dependent glutathione peroxidase (GSH-Px), zinc-dependent superoxide dismutase (SOD), and copper/zinc-dependent catalase (CAT) values in the kidney of ovariectomized (OVX) diabetic rats. |
| 2486 | 21484408 | GSH-Px, CAT, SOD, GSH levels, vitamin A, and beta carotene levels were decreased in OVX group compared to those in the control group but MDA level was elevated via ovariectomy. |
| 2487 | 21484408 | However, GSH, GSH-Px, CAT, SOD, vitamin A, and beta carotene levels in kidney were lower in OVX diabetic rats. |
| 2488 | 21484408 | On the other hand, E(2) and E(2)+alpha-tocopherol supplementations to OVX diabetic rats have caused an increase in GSH-Px, CAT and SOD, GSH, vitamin A, and beta carotene levels but a decrease in MDA levels. |
| 2489 | 21514684 | Epigallocatechin-3-O-gallate (EGCG) attenuates FFAs-induced peripheral insulin resistance through AMPK pathway and insulin signaling pathway in vivo. |
| 2490 | 21514684 | Co-injection with EGCG significantly prevented FFAs-induced peripheral insulin resistance, decreased plasma markers of oxidative stress: malondialdehyde (MDA) and 8-isoprostaglandin, and increased antioxidant enzymes: superoxide dismutases (SOD) and Glutathione peroxidase (GPx). |
| 2491 | 21514684 | Furthermore, EGCG treatment reversed IH-induced: (1) decrease in Thr172 phosphorylation of AMP activated protein kinase (AMPK); (2) increase in protein kinase Cθ(PKCθ) membrane translocation and Ser307 phosphorylation of insulin receptor substrate-1 (IRS-1); (3) decrease in Ser473 phosphorylation of Akt and Glucose transporter 4 (GLUT4) translocation in skeletal muscle and adipose tissue. |
| 2492 | 21514684 | Our data suggest that EGCG treatment ameliorated FFAs-induced peripheral insulin resistance in vivo, and this might be through decreasing oxidative stress and PKCθ membrane translocation, activating the AMPK pathway and improving insulin signaling pathway in vivo. |
| 2493 | 21525262 | Epicatechin treatment caused changes in diabetic mice that are associated with a healthier and longer lifespan, including improved skeletal muscle stress output, reduced systematic inflammation markers and serum LDL cholesterol, increased hepatic antioxidant glutathione concentration and total superoxide dismutase activity, decreased circulating insulin-like growth factor-1 (from 303 ± 21 mg/L in the diabetic control group to 189 ± 21 mg/L in the epicatechin-treated group), and improved AMP-activated protein kinase-α activity in the liver and skeletal muscle. |
| 2494 | 21525431 | The present study was performed to investigate the underlying mechanism, particularly the roles of reactive oxygen species (ROS) and protein kinase C (PKC), in the diabetes-induced canonical transient receptor potential 6 (TRPC6) downregulation. |
| 2495 | 21525431 | Catalase as well as superoxide dismutase were able to prevent the inhibitory effect of HG on TRPC6. |
| 2496 | 21525431 | Specific knockdown of Nox4, a component of NADPH oxidase, increased TRPC6 protein expression. |
| 2497 | 21525431 | Furthermore, either knockdown of TRPC6 or HG treatment significantly decreased ANG II-stimulated MC contraction, and the HG-impaired MC contraction was rescued by overexpression of TRPC6. |
| 2498 | 21525431 | These results suggest that hyperglycemia in diabetes downregulated TRPC6 protein expression in MCs through a NADPH oxidase Nox4-ROS-PKC pathway, proving a mechanism for impaired MC contraction in diabetes. |
| 2499 | 21538233 | Oral treatment of TC (100 and 200 mg/kg body weight) for 14 days regulated blood glucose, provoked insulin secretion and also suppressed oxidative stress marker, thiobarbituric acid reactive substances (TBARS), formation and restored cellular defence anti-oxidant markers including superoxide dismutase (SOD), glutathione peroxidase (GPx) and glutathione (GSH), in liver. |
| 2500 | 21544882 | At day 60, the serum glutathione (GSH) level, superoxide dismutase (SOD), Paraoxonase (PONase) and glutathione reductase (GSSG-R) activities increased markedly in the treatment group compared with the placebo group. |
| 2501 | 21576908 | Minimal differences were observed in the number of cells positive for cytoplasmic superoxide dismutase (SOD)1 or mitochondrial SOD2. |
| 2502 | 21584231 | Our results suggested that protection against development of diabetic nephropathy by luteolin treatment involved changes in superoxide dismutase (SOD) activity, the malondialdehyde (MDA) content and expression of Heme Oxygenase-1 (HO-1) protein. |
| 2503 | 21602470 | Although the protein expression of endothelial nitric oxide synthase did not increase, ET reduced both IFN-γ and superoxide production by inhibiting gp91(phox) protein levels. |
| 2504 | 21602470 | In addition, ET increased the expression of adiponectin (APN) and the antioxidant enzyme, SOD-1. |
| 2505 | 21602470 | APNKO mice also showed increased protein expression of IFN-γ, gp91(phox), and nitrotyrosine but protein expression of SOD-1 and -3 were comparable between wild-type and APNKO. |
| 2506 | 21602470 | These findings in the aorta imply that APN suppresses inflammation and oxidative stress in the aorta, but not SOD-1 and -3. |
| 2507 | 21602470 | Although the protein expression of endothelial nitric oxide synthase did not increase, ET reduced both IFN-γ and superoxide production by inhibiting gp91(phox) protein levels. |
| 2508 | 21602470 | In addition, ET increased the expression of adiponectin (APN) and the antioxidant enzyme, SOD-1. |
| 2509 | 21602470 | APNKO mice also showed increased protein expression of IFN-γ, gp91(phox), and nitrotyrosine but protein expression of SOD-1 and -3 were comparable between wild-type and APNKO. |
| 2510 | 21602470 | These findings in the aorta imply that APN suppresses inflammation and oxidative stress in the aorta, but not SOD-1 and -3. |
| 2511 | 21602470 | Although the protein expression of endothelial nitric oxide synthase did not increase, ET reduced both IFN-γ and superoxide production by inhibiting gp91(phox) protein levels. |
| 2512 | 21602470 | In addition, ET increased the expression of adiponectin (APN) and the antioxidant enzyme, SOD-1. |
| 2513 | 21602470 | APNKO mice also showed increased protein expression of IFN-γ, gp91(phox), and nitrotyrosine but protein expression of SOD-1 and -3 were comparable between wild-type and APNKO. |
| 2514 | 21602470 | These findings in the aorta imply that APN suppresses inflammation and oxidative stress in the aorta, but not SOD-1 and -3. |
| 2515 | 21630391 | In experimental rats, the levels of plasma glucose, insulin, and the levels of thiobarbituric acid reactive substances, lipid hydroperoxides, conjugated dienes, and the activities of superoxide dismutase, catalase, glutathione-S-transferase, and glutathione peroxidase were assayed in liver and kidney. |
| 2516 | 21633835 | The levels of vascular endothelial growth factor, superoxide dismutase, lipid peroxide, and connexins were analyzed in wound tissues taken from diabetic and non-diabetic mice before and after sodium selenite administration. |
| 2517 | 21633835 | In diabetic wounds, the low levels of vascular endothelial growth factor and extracellular superoxide dismutase were restored to normal level following selenium administration. |
| 2518 | 21666113 | We measured the responses of cerebral arterioles in untreated and resveratrol-treated (10 mg·kg(-1)·day(-1)) nondiabetic and diabetic rats to endothelial (eNOS) and neuronal (nNOS) nitric oxide synthase (NOS)-dependent agonists and to a NOS-independent agonist. |
| 2519 | 21666113 | Furthermore, we used Western blot analysis to determine the protein expression of eNOS, nNOS, SOD-1, and SOD-2 in cerebral arterioles and/or brain tissue from untreated and resveratrol-treated nondiabetic and diabetic rats. |
| 2520 | 21666113 | We found that T1D impaired eNOS- and nNOS-dependent reactivity of cerebral arterioles but did not alter NOS-independent vasodilation. |
| 2521 | 21666113 | While resveratrol did not alter responses in nondiabetic rats, resveratrol prevented T1D-induced impairment in eNOS- and nNOS-dependent vasodilation. |
| 2522 | 21666113 | Furthermore, eNOS and nNOS protein were increased in diabetic rats and resveratrol produced a further increased eNOS and nNOS proteins. |
| 2523 | 21666113 | SOD-1 and SOD-2 proteins were not altered by T1D, but resveratrol treatment produced a decrease in SOD-2 protein. |
| 2524 | 21666113 | We measured the responses of cerebral arterioles in untreated and resveratrol-treated (10 mg·kg(-1)·day(-1)) nondiabetic and diabetic rats to endothelial (eNOS) and neuronal (nNOS) nitric oxide synthase (NOS)-dependent agonists and to a NOS-independent agonist. |
| 2525 | 21666113 | Furthermore, we used Western blot analysis to determine the protein expression of eNOS, nNOS, SOD-1, and SOD-2 in cerebral arterioles and/or brain tissue from untreated and resveratrol-treated nondiabetic and diabetic rats. |
| 2526 | 21666113 | We found that T1D impaired eNOS- and nNOS-dependent reactivity of cerebral arterioles but did not alter NOS-independent vasodilation. |
| 2527 | 21666113 | While resveratrol did not alter responses in nondiabetic rats, resveratrol prevented T1D-induced impairment in eNOS- and nNOS-dependent vasodilation. |
| 2528 | 21666113 | Furthermore, eNOS and nNOS protein were increased in diabetic rats and resveratrol produced a further increased eNOS and nNOS proteins. |
| 2529 | 21666113 | SOD-1 and SOD-2 proteins were not altered by T1D, but resveratrol treatment produced a decrease in SOD-2 protein. |
| 2530 | 21669272 | After six weeks, the serum insulin, blood biochemical indices, superoxide dismutase, malondialdehyde, monoamine neurotransmitters, and BAEP were measured. |
| 2531 | 21679740 | Moreover, PG also markedly inhibited pancreatic nuclear factor-kappa B protein expression induced by STZ and restored the activities of antioxidant enzymes, including superoxide dismutase, catalase, and glutathione peroxidase. |
| 2532 | 21713411 | A significant (P < 0.05) increase in the levels of fasting plasma glucose and lipid peroxidative products (thiobarbituric acid reactive substances and lipid hydroperoxides) and a significant (P < 0.05) decrease in plasma insulin, enzymic antioxidants (superoxide dismutase, catalase, glutathione peroxidase, and glutathione reductase), and nonenzymic antioxidants (reduced glutathione, vitamin C, and E) in diabetic pancreas, liver, and kidney were observed. |
| 2533 | 21716679 | The RMD-treated diabetic rats showed higher activities of glutathione disulfide reductase, glutathione reductase, catalase and superoxide dismutase (P < .05) in the pancreas compared with the diabetic control rats. |
| 2534 | 21716679 | RMD also inhibited diabetes-induced elevation in the levels of interleukin (IL)-1β, IL-6, interferon-γ and tumor necrosis factor-α. |
| 2535 | 21718105 | Antioxidant activities of superoxide dismutase, catalase and glutathione are significantly increased in kidneys of irradiated db/db mice. |
| 2536 | 21731194 | Superoxide dismutase (SOD), glutathione peroxidase and catalase are termed as primary antioxidants as these scavenge superoxide anion and hydrogen peroxide. |
| 2537 | 21737173 | The aim of the present study was to investigate the effects of Syzygium cumini leaf extract (ASc), on Adenosine deaminase (ADA) and Acetylcholinesterase (AChE) activities, and also on oxidative stress parameters in erythrocytes hemolysates (RBCs) and erythrocytes membranes (ghosts) from type 2 diabetics patients (Type 2 DM) under in vitro conditions. |
| 2538 | 21737173 | Non protein thiol groups (NP-SH), AChE, Catalase (CAT) and Superoxide Dismutase (SOD) activities were measure in RBCs. |
| 2539 | 21737173 | The results demonstrated that ADA and AChE activities, besides TBARS levels were higher in erythrocytes of Type 2 DM, while SOD activity and NP-SH levels were decreased when compared to control group. |
| 2540 | 21737173 | The aim of the present study was to investigate the effects of Syzygium cumini leaf extract (ASc), on Adenosine deaminase (ADA) and Acetylcholinesterase (AChE) activities, and also on oxidative stress parameters in erythrocytes hemolysates (RBCs) and erythrocytes membranes (ghosts) from type 2 diabetics patients (Type 2 DM) under in vitro conditions. |
| 2541 | 21737173 | Non protein thiol groups (NP-SH), AChE, Catalase (CAT) and Superoxide Dismutase (SOD) activities were measure in RBCs. |
| 2542 | 21737173 | The results demonstrated that ADA and AChE activities, besides TBARS levels were higher in erythrocytes of Type 2 DM, while SOD activity and NP-SH levels were decreased when compared to control group. |
| 2543 | 21748304 | Furthermore, oxidative stress in rats was also investigated in terms of superoxide dismutase (SOD), catalase, lipid peroxidation, and glutathione (GSH). |
| 2544 | 21748304 | Treatment with above complex decreased the lipid peroxidation and the antioxidant enzymes such as SOD, CAT, and GSH to near-control levels. |
| 2545 | 21748304 | Furthermore, oxidative stress in rats was also investigated in terms of superoxide dismutase (SOD), catalase, lipid peroxidation, and glutathione (GSH). |
| 2546 | 21748304 | Treatment with above complex decreased the lipid peroxidation and the antioxidant enzymes such as SOD, CAT, and GSH to near-control levels. |
| 2547 | 21756187 | After the experimental period, thiobarbituric acid reacting substances (TBARS) and antioxidant enzymes such as catalase, superoxide dismutase (SOD) and glutathione peroxidase were measured. |
| 2548 | 21756187 | Administration of O. sanctum to streptozocin-induced diabetic rats for 30 days significantly reduced the plasma level of TBARS and improved the status of the antioxidant enzymes catalase, SOD and glutathione peroxidase in vital organs such as the liver and kidney. |
| 2549 | 21756187 | After the experimental period, thiobarbituric acid reacting substances (TBARS) and antioxidant enzymes such as catalase, superoxide dismutase (SOD) and glutathione peroxidase were measured. |
| 2550 | 21756187 | Administration of O. sanctum to streptozocin-induced diabetic rats for 30 days significantly reduced the plasma level of TBARS and improved the status of the antioxidant enzymes catalase, SOD and glutathione peroxidase in vital organs such as the liver and kidney. |
| 2551 | 21782842 | Similarly, the administration of polysaccharide levan in diabetic rats caused a decrease in the thiobarbituric acid-reactive substances (TBARS) by 31%, 41%, 39% and 25%, an increase in superoxide dismutase (SOD) by 40%, 50%, 44% and 34%, and in catalase (CAT) by 18%, 20%, 12% and 18% in liver, kidney, pancreas and heart, respectively. |
| 2552 | 21804221 | Treatment with cobalt chloride (CoCl(2)) decreased the expression of EC-SOD but not other SOD isozymes in pericytes accompanied with an increase of intracellular ROS production. |
| 2553 | 21804221 | EC-SOD enhancer 4-phenyl butyric acid also suppressed the caspase-3 activation. |
| 2554 | 21823905 | Biochemistry results (lipid peroxidase (LPO); catalase (CAT); superoxide dismutase (SOD); total glutatyon (GSH); and myeloperoxidase (MPO) values) in Group C-DO were determined as 12.27, 21.88, 23.08 and 29.90 nmol/gr tissue; 59.3, 70.06, 69.7 and 78.1 mmol/min/mg tissue; 174.2, 156.4, 159.7 and 154.6 mmol/min/mg tissue; 3.63, 3.61, 4.21 and 3.97 nmol/mg tissue; and 5.05, 5.68, 5.58 and 6.19 µmol/min/mg tissue, respectively. |
| 2555 | 21840472 | Diabetic rats showed decreased activities of superoxide dismutase and catalase, increased concentrations of malondialdehyde in the serum and kidney, and increased levels of 8-hydroxy-2'-deoxyguanosine in urine and renal cortex DNA. |
| 2556 | 21925206 | The oral administration of levan in diabetic rats caused a decrease in glucose level in plasma and an increase of superoxide dismutase (SOD), catalase (CAT) and glutathione peroxidase (GPX) activities in both pancreas and liver. |
| 2557 | 21940665 | Angiotensin II-NADPH oxidase-derived superoxide mediates diabetes-attenuated cell excitability of aortic baroreceptor neurons. |
| 2558 | 21940665 | The present study examined the effects of an angiotensin II type I receptor (AT(1)R) antagonist (losartan), a NADPH oxidase inhibitor (apocynin), and a superoxide dismutase mimetic (tempol) on the enhanced HCN currents and attenuated cell excitability in diabetic nodose neurons. |
| 2559 | 21940665 | These findings suggest that endogenous angiotensin II-NADPH oxidase-superoxide signaling contributes to the enhanced HCN currents and the depressed cell excitation in the aortic baroreceptor neurons of diabetic rats. |
| 2560 | 21966119 | There was significant (P > 0.05) increase in the level of Thio Barbituric Acid Reactive Substances (TBARS), hydroperoxide and conjugated dienes and significant (P > 0.05) decrease in the catalase, superoxide dismutase and glutathione peroxidase activities and in the level of ascorbic acid, vitamin E and reduced glutathione in diabetic rats. |
| 2561 | 21966119 | The flower powder of Cassia auriculata significantly (P > 0.05) decreased the TBARS, hydroperoxide and conjugated dienes and increased the antioxidant enzymes (catalase, superoxide dismutase and glutathione peroxidase) and non enzymic anti oxidants (ascorbic acid, vitamin E and reduced glutathione). |
| 2562 | 21966119 | There was significant (P > 0.05) increase in the level of Thio Barbituric Acid Reactive Substances (TBARS), hydroperoxide and conjugated dienes and significant (P > 0.05) decrease in the catalase, superoxide dismutase and glutathione peroxidase activities and in the level of ascorbic acid, vitamin E and reduced glutathione in diabetic rats. |
| 2563 | 21966119 | The flower powder of Cassia auriculata significantly (P > 0.05) decreased the TBARS, hydroperoxide and conjugated dienes and increased the antioxidant enzymes (catalase, superoxide dismutase and glutathione peroxidase) and non enzymic anti oxidants (ascorbic acid, vitamin E and reduced glutathione). |
| 2564 | 21969757 | The erythrocytes membrane lipid peroxide and catalase activity was increased where as the activities of superoxide dismutase, glutathione peroxidase were found to be decreased significantly (P<0.01) in alloxan-induced diabetic rats. |
| 2565 | 21969757 | The levels of lipid peroxide in liver of diabetic rats increased significantly (P<0.01) and catalase, superoxide dismutase, glutathione peroxidase in liver was significantly decreased in alloxan-induced diabetic rats, when compared to normal rats. |
| 2566 | 21969757 | The erythrocytes membrane lipid peroxide and catalase activity was increased where as the activities of superoxide dismutase, glutathione peroxidase were found to be decreased significantly (P<0.01) in alloxan-induced diabetic rats. |
| 2567 | 21969757 | The levels of lipid peroxide in liver of diabetic rats increased significantly (P<0.01) and catalase, superoxide dismutase, glutathione peroxidase in liver was significantly decreased in alloxan-induced diabetic rats, when compared to normal rats. |
| 2568 | 22001983 | Telmisartan successfully prevented oxidative stress, which was evidenced by a decrease in malondialdehyde and an increase in glutathione, catalase, superoxide dismutase levels. |
| 2569 | 22015457 | Administration of superoxide dismutase (to scavenge superoxide anions) or L-N(G)-nitroarginine methyl ester (L-NAME, a nonselective nitric oxide synthase inhibitor) restored PGIS activity and attenuated pericyte apoptosis. |
| 2570 | 22053564 | We measured the concentrations of superoxide dismutase (SOD), glutathione peroxidase (GPOD), catalase, and total antioxidative status (TAS). |
| 2571 | 22053564 | The concentrations of SOD, GPOD, catalase, and TAS were significantly lower in the diabetic patients with DR after retinal scatter LF, which could be the consequence of retinal oxidative stress caused by the LF thermal effect. |
| 2572 | 22053564 | We measured the concentrations of superoxide dismutase (SOD), glutathione peroxidase (GPOD), catalase, and total antioxidative status (TAS). |
| 2573 | 22053564 | The concentrations of SOD, GPOD, catalase, and TAS were significantly lower in the diabetic patients with DR after retinal scatter LF, which could be the consequence of retinal oxidative stress caused by the LF thermal effect. |
| 2574 | 22056428 | Moreover, the antioxidant enzymic activities of glutathione peroxidase, glutathione reductase, and superoxide dismutase also improved significantly after treatment with the extract. |
| 2575 | 22056647 | The activities of antioxidant enzymes superoxide dismutase (SOD), catalase (CAT), glutathione peroxidase (GPx), glutathione-S-transferase (GST) and the levels of low-molecular weight antioxidants vitamin C, vitamin E and reduced glutathione (GSH) were decreased while increases in the levels of LPO markers were observed in liver and kidney tissues of diabetic control rats as compared to normal control rats. |
| 2576 | 22063193 | When atria were paced at 1.2 Hz, N-acetyl cystein (antioxidant, NAC), α-lipoic acid (antioxidant), tempol (superoxide dismutase mimic), and apocynin (NADPH oxidase inhibitor; NOX inhibitor) did not affect ANP secretion and atrial contractility. |
| 2577 | 22065939 | There was a decrease in antioxidant enzyme levels (in superoxide dismutase, reduced glutathione and catalase) in diabetic hearts, which could be improved by treatment with fruit juice. |
| 2578 | 22072110 | In this study, we treated non-obese and hypoinsulinemic C57BL/6-Ins2(Akita) (C57BL/6-Akita) diabetic mice with telmisartan (5 mg kg(-1) per day), an angiotensin II type 1 receptor blocker, or amlodipine (5 mg kg(-1) per day), a calcium channel blocker, for 4 weeks and compared the effects of these two anti-hypertensive drugs on renal NAD(P)H oxidase, SOD and transcription factor Nrf2 (NF-E2-related factor 2), which is known to upregulate several antioxidant enzymes including SOD. |
| 2579 | 22072110 | Furthermore, telmisartan-treated C57BL/6-Akita mice increased the renal protein expression of SOD and Nrf2. |
| 2580 | 22072110 | In contrast, treatment with amlodipine failed to modulate renal NAD(P)H oxidase, SOD and Nrf2. |
| 2581 | 22072110 | Finally, treatment of C57BL/6-Akita mice with apocynin, an NAD(P)H oxidase inhibitor, also increased the renal protein expression of SOD and Nrf2. |
| 2582 | 22072110 | Collectively, our data suggest that NAD(P)H oxidase negatively regulates renal SOD, possibly by downregulation of Nrf2, and that telmisartan could upregulate renal SOD by the suppression of NAD(P)H oxidase and subsequent upregulation of Nrf2, leading to the amelioration of renal oxidative stress and diabetic renal changes. |
| 2583 | 22072110 | In this study, we treated non-obese and hypoinsulinemic C57BL/6-Ins2(Akita) (C57BL/6-Akita) diabetic mice with telmisartan (5 mg kg(-1) per day), an angiotensin II type 1 receptor blocker, or amlodipine (5 mg kg(-1) per day), a calcium channel blocker, for 4 weeks and compared the effects of these two anti-hypertensive drugs on renal NAD(P)H oxidase, SOD and transcription factor Nrf2 (NF-E2-related factor 2), which is known to upregulate several antioxidant enzymes including SOD. |
| 2584 | 22072110 | Furthermore, telmisartan-treated C57BL/6-Akita mice increased the renal protein expression of SOD and Nrf2. |
| 2585 | 22072110 | In contrast, treatment with amlodipine failed to modulate renal NAD(P)H oxidase, SOD and Nrf2. |
| 2586 | 22072110 | Finally, treatment of C57BL/6-Akita mice with apocynin, an NAD(P)H oxidase inhibitor, also increased the renal protein expression of SOD and Nrf2. |
| 2587 | 22072110 | Collectively, our data suggest that NAD(P)H oxidase negatively regulates renal SOD, possibly by downregulation of Nrf2, and that telmisartan could upregulate renal SOD by the suppression of NAD(P)H oxidase and subsequent upregulation of Nrf2, leading to the amelioration of renal oxidative stress and diabetic renal changes. |
| 2588 | 22072110 | In this study, we treated non-obese and hypoinsulinemic C57BL/6-Ins2(Akita) (C57BL/6-Akita) diabetic mice with telmisartan (5 mg kg(-1) per day), an angiotensin II type 1 receptor blocker, or amlodipine (5 mg kg(-1) per day), a calcium channel blocker, for 4 weeks and compared the effects of these two anti-hypertensive drugs on renal NAD(P)H oxidase, SOD and transcription factor Nrf2 (NF-E2-related factor 2), which is known to upregulate several antioxidant enzymes including SOD. |
| 2589 | 22072110 | Furthermore, telmisartan-treated C57BL/6-Akita mice increased the renal protein expression of SOD and Nrf2. |
| 2590 | 22072110 | In contrast, treatment with amlodipine failed to modulate renal NAD(P)H oxidase, SOD and Nrf2. |
| 2591 | 22072110 | Finally, treatment of C57BL/6-Akita mice with apocynin, an NAD(P)H oxidase inhibitor, also increased the renal protein expression of SOD and Nrf2. |
| 2592 | 22072110 | Collectively, our data suggest that NAD(P)H oxidase negatively regulates renal SOD, possibly by downregulation of Nrf2, and that telmisartan could upregulate renal SOD by the suppression of NAD(P)H oxidase and subsequent upregulation of Nrf2, leading to the amelioration of renal oxidative stress and diabetic renal changes. |
| 2593 | 22072110 | In this study, we treated non-obese and hypoinsulinemic C57BL/6-Ins2(Akita) (C57BL/6-Akita) diabetic mice with telmisartan (5 mg kg(-1) per day), an angiotensin II type 1 receptor blocker, or amlodipine (5 mg kg(-1) per day), a calcium channel blocker, for 4 weeks and compared the effects of these two anti-hypertensive drugs on renal NAD(P)H oxidase, SOD and transcription factor Nrf2 (NF-E2-related factor 2), which is known to upregulate several antioxidant enzymes including SOD. |
| 2594 | 22072110 | Furthermore, telmisartan-treated C57BL/6-Akita mice increased the renal protein expression of SOD and Nrf2. |
| 2595 | 22072110 | In contrast, treatment with amlodipine failed to modulate renal NAD(P)H oxidase, SOD and Nrf2. |
| 2596 | 22072110 | Finally, treatment of C57BL/6-Akita mice with apocynin, an NAD(P)H oxidase inhibitor, also increased the renal protein expression of SOD and Nrf2. |
| 2597 | 22072110 | Collectively, our data suggest that NAD(P)H oxidase negatively regulates renal SOD, possibly by downregulation of Nrf2, and that telmisartan could upregulate renal SOD by the suppression of NAD(P)H oxidase and subsequent upregulation of Nrf2, leading to the amelioration of renal oxidative stress and diabetic renal changes. |
| 2598 | 22072110 | In this study, we treated non-obese and hypoinsulinemic C57BL/6-Ins2(Akita) (C57BL/6-Akita) diabetic mice with telmisartan (5 mg kg(-1) per day), an angiotensin II type 1 receptor blocker, or amlodipine (5 mg kg(-1) per day), a calcium channel blocker, for 4 weeks and compared the effects of these two anti-hypertensive drugs on renal NAD(P)H oxidase, SOD and transcription factor Nrf2 (NF-E2-related factor 2), which is known to upregulate several antioxidant enzymes including SOD. |
| 2599 | 22072110 | Furthermore, telmisartan-treated C57BL/6-Akita mice increased the renal protein expression of SOD and Nrf2. |
| 2600 | 22072110 | In contrast, treatment with amlodipine failed to modulate renal NAD(P)H oxidase, SOD and Nrf2. |
| 2601 | 22072110 | Finally, treatment of C57BL/6-Akita mice with apocynin, an NAD(P)H oxidase inhibitor, also increased the renal protein expression of SOD and Nrf2. |
| 2602 | 22072110 | Collectively, our data suggest that NAD(P)H oxidase negatively regulates renal SOD, possibly by downregulation of Nrf2, and that telmisartan could upregulate renal SOD by the suppression of NAD(P)H oxidase and subsequent upregulation of Nrf2, leading to the amelioration of renal oxidative stress and diabetic renal changes. |
| 2603 | 22128218 | Compared to control animals, diabetic rats exhibited lower levels of mRNA coding for Zn-superoxide dismutase, glutathione peroxidase and gamma-glutamylcysteine synthetase and higher levels of reactive oxygen species production by neutrophils, thiobarbituric acid-reactive substances and carbonyl proteins in hepatic tissues. |
| 2604 | 22138721 | The aim of this study was to investigate (i) the cholecystokinin, somatostatin and apelin mRNA levels, (ii) the changes in levels and localization of these peptides, (iii) relation between these peptides, (iv) antiapoptotic effects and (v) antioxidant effects of ghrelin. |
| 2605 | 22138721 | Cholecystokinin mRNA and peptide, somatostatin mRNA, release to duodenal lumen of apelin peptide and apelin mRNA signals decreased in ghrelin-treated diabetic rats compared to the diabetic group. |
| 2606 | 22138721 | There was no statistically significant difference among the four groups for somatostatin and apelin peptides. |
| 2607 | 22138721 | Caspase-3 signals were not observed only in diabetic group treated with ghrelin. |
| 2608 | 22138721 | Caspase-8 signals were increased while PCNA signals were decreased in diabetic group given ghrelin compared to diabetic group. |
| 2609 | 22138721 | Small intestine CAT, SOD, GP(x) and GST activities and GSH levels were decreased and LPO, PC levels were increased in diabetic rats. |
| 2610 | 22178680 | The decrease in lipid peroxides and increase in superoxide dismutase (SOD) and catalase (CAT) in liver illustrated the antioxidant potential of bergenin. |
| 2611 | 22231435 | Total antioxidants status, paraoxonase-1 (PON1) and erythrocyte superoxide dismutase activities significantly decreased in the diabetic rats compared to the controls, while a higher fasting plasma glucose level was observed in the diabetic animals. |
| 2612 | 22237966 | Moreover, concentration of GSH and the activity of both superoxide dismutase and catalase were considerably increased in the diabetic treated groups compared with the diabetic untreated group. |
| 2613 | 22285432 | In this study, we attempt to reveal how sodium arsenite (iAs) could induce stress mediated impaired insulin signaling in mice and if an isolated active fraction of ginger, [6]-gingerol could attenuate the iAs intoxicated hyperglycemic condition of mice and bring about improvement in their impaired insulin signaling. [6]-Gingerol treatment reduced elevated blood glucose level and oxidative stress by enhancing activity of super oxide dismutase (SOD), catalase, glutathione peroxidase (GPx) and GSH. [6]-Gingerol also helped in increasing plasma insulin level, brought down after iAs exposure. iAs treatment to primary cell culture of β-cells and hepatocytes in vitro produced cyto-degenerative effect and accumulated reactive oxygen species (ROS) in pancreatic β-cells and hepatocytes of mice. [6]-Gingerol appeared to inhibit/intervene iAs induced cyto-degeneration of pancreatic β-cells and hepatocytes, helped in scavenging the free radicals. |
| 2614 | 22285432 | The over-expression of TNFα and IL6 in iAs intoxicated mice was down-regulated by [6]-gingerol treatment. iAs intoxication reduced expression levels of GLUT4, IRS-1, IRS-2, PI3K, AKT, PPARγ signaling molecules; [6]-gingerol mediated its action through enhancing the expressions of these signaling molecules, both at protein and mRNA levels. |
| 2615 | 22308229 | Elevated angiotensin II in rat nodose ganglia primes diabetes-blunted arterial baroreflex sensitivity: involvement of NADPH oxidase-derived superoxide. |
| 2616 | 22308229 | Our previous study has shown that angiotensin II (Ang II)-NADPH oxidase-superoxide signaling is associated with the reduced cell excitability in the aortic baroreceptor neurons (a primary afferent limb of the arterial baroreflex) from diabetic rats. |
| 2617 | 22308229 | Using Ang II (125)I radioimmunoassay and lucigenin chemiluminescence method, we found Ang II concentration, NADPH oxidase activity, and superoxide production in the nodose ganglia were enhanced in diabetic rats, compared to sham rats. |
| 2618 | 22308229 | Local microinjection (50 nl) of losartan (an AT(1) receptor antagonist, 1 nmol), apocynin (a NADPH oxidase inhibitor, 1 nmol), and tempol (a superoxide dismutase mimetic, 10 nmol) into the nodose ganglia significantly improved the arterial baroreflex sensitivity in diabetic rats. |
| 2619 | 22308229 | These results indicate that overactivation of the Ang II-NADPH oxidase-superoxide signal pathway in the nodose ganglia contributes to the blunted baroreflex sensitivity in diabetes. |
| 2620 | 22355488 | Myocardial oxidative stress was assessed by measuring the activity of superoxide dismutase (SOD), the level of malondialdehyde (MDA) as well as heme oxygenase-1 (HO-1) protein level. |
| 2621 | 22355488 | The level of SOD decreased, CTGF and HO-1 protein expression and MDA content rose. |
| 2622 | 22355488 | Riboflavin treatment significantly improved left ventricular systolic and diastolic function in diabetic rats, there were persistent increases in significant activation of SOD and the level of HO-1 protein, and a decrease in the level of CTGF. |
| 2623 | 22355488 | These results suggest that riboflavin treatment ameliorates myocardial function and improves heart oxidant status, whereas raising myocardial HO-1 and decreasing myocardial CTGF levels have beneficial effects on diabetic cardiomyopathy. |
| 2624 | 22355488 | Myocardial oxidative stress was assessed by measuring the activity of superoxide dismutase (SOD), the level of malondialdehyde (MDA) as well as heme oxygenase-1 (HO-1) protein level. |
| 2625 | 22355488 | The level of SOD decreased, CTGF and HO-1 protein expression and MDA content rose. |
| 2626 | 22355488 | Riboflavin treatment significantly improved left ventricular systolic and diastolic function in diabetic rats, there were persistent increases in significant activation of SOD and the level of HO-1 protein, and a decrease in the level of CTGF. |
| 2627 | 22355488 | These results suggest that riboflavin treatment ameliorates myocardial function and improves heart oxidant status, whereas raising myocardial HO-1 and decreasing myocardial CTGF levels have beneficial effects on diabetic cardiomyopathy. |
| 2628 | 22355488 | Myocardial oxidative stress was assessed by measuring the activity of superoxide dismutase (SOD), the level of malondialdehyde (MDA) as well as heme oxygenase-1 (HO-1) protein level. |
| 2629 | 22355488 | The level of SOD decreased, CTGF and HO-1 protein expression and MDA content rose. |
| 2630 | 22355488 | Riboflavin treatment significantly improved left ventricular systolic and diastolic function in diabetic rats, there were persistent increases in significant activation of SOD and the level of HO-1 protein, and a decrease in the level of CTGF. |
| 2631 | 22355488 | These results suggest that riboflavin treatment ameliorates myocardial function and improves heart oxidant status, whereas raising myocardial HO-1 and decreasing myocardial CTGF levels have beneficial effects on diabetic cardiomyopathy. |
| 2632 | 22375253 | Common antioxidants include the vitamins A, C, and E, glutathione (GSH), and the enzymes superoxide dismutase (SOD), catalase (CAT), glutathione peroxidase (GPx), and glutathione reductase (GRx). |
| 2633 | 22384308 | Exercise did not change body weight of db/db, but superoxide dismutase (SOD1 and SOD2) and phosphorylated- eNOS protein (Ser1177) expression in heart tissue was up-regulated whereas tumor necrosis factor-alpha (TNF-α) protein level was decreased by ET. |
| 2634 | 22386881 | The inhibition of respiration provoked a rapid and sustained increase in superoxide levels, despite the increase in UCP2 and superoxide dismutase activity. |
| 2635 | 22435145 | Oxidative damage in the tissues of diabetic mice was evidenced by a marked increase in the level of thiobarbituric acid reactive substances (TBARS), distinct decrease in reduced glutathione (GSH) content and declined activity of antioxidant enzymes, such as superoxide dismutase (SOD), catalase (CAT) and glutathione peroxidase (GSH-Px). |
| 2636 | 22484523 | The enzymes under study were: superoxide dismutase, catalase, glutathione peroxidase and glutathione reductase. |
| 2637 | 22484523 | The activities of glutathione reductase, superoxide dismutase and catalase decreased during the LPD period and increased in the LPD+dealcoholized wine period. |
| 2638 | 22484523 | On the third day of intervention, significant changes were observed in glutathione reductase and superoxide dismutase activity for both intervention periods under study. |
| 2639 | 22484523 | The enzymes under study were: superoxide dismutase, catalase, glutathione peroxidase and glutathione reductase. |
| 2640 | 22484523 | The activities of glutathione reductase, superoxide dismutase and catalase decreased during the LPD period and increased in the LPD+dealcoholized wine period. |
| 2641 | 22484523 | On the third day of intervention, significant changes were observed in glutathione reductase and superoxide dismutase activity for both intervention periods under study. |
| 2642 | 22484523 | The enzymes under study were: superoxide dismutase, catalase, glutathione peroxidase and glutathione reductase. |
| 2643 | 22484523 | The activities of glutathione reductase, superoxide dismutase and catalase decreased during the LPD period and increased in the LPD+dealcoholized wine period. |
| 2644 | 22484523 | On the third day of intervention, significant changes were observed in glutathione reductase and superoxide dismutase activity for both intervention periods under study. |
| 2645 | 22489155 | The shape and structure of islet cells were observed with Hematine-Eosin staining, and the expression of superoxide dismutase (SOD) and inducible nitric oxide synthase (iNOS) in islet cells were detected by immunohistochemical assay. |
| 2646 | 22489155 | The shape and structure of islet cells improved with the up-expressing SOD and down-expressing iNOS in the medium-high dose treated groups compared to those in the DM-model group (P < 0.05). |
| 2647 | 22489155 | The shape and structure of islet cells were observed with Hematine-Eosin staining, and the expression of superoxide dismutase (SOD) and inducible nitric oxide synthase (iNOS) in islet cells were detected by immunohistochemical assay. |
| 2648 | 22489155 | The shape and structure of islet cells improved with the up-expressing SOD and down-expressing iNOS in the medium-high dose treated groups compared to those in the DM-model group (P < 0.05). |
| 2649 | 22492942 | Also, renal levels of interleukin-6 (IL-6), tumor necrosis factor-α (TNF-α), ED-1, hypoxia-inducible factor-1α (HIF-1α), and neutrophil gelatinase-associated lipocalin (NGAL) were determined by immunohistochemistry and immunoblotting. |
| 2650 | 22492942 | Additionally, ANG-(1-7) reduced renal fibrosis, decreased thiobarbituric acid-reactive substances, and restored the activity of both renal superoxide dismutase and catalase in ZDF. |
| 2651 | 22492942 | This attenuation of renal oxidative stress proceeded with decreased renal immunostaining of IL-6, TNF-α, ED-1, HIF-1α, and NGAL to values similar to those displayed by LZR. |
| 2652 | 22492942 | Angiotensin-converting enzyme type 2 (ACE2) and ANG II levels remained unchanged after treatment with ANG-(1-7). |
| 2653 | 22495601 | Additionally, levels of antioxidant enzymes (AOEs) namely superoxide dismutase, catalase, glutathione peroxidase, and glutathione reductase were also estimated. |
| 2654 | 22527888 | The levels of malondialdehyde (MDA), interleukin 6 (IL-6), tumor necrosis factor α (TNF-α) and activities of superoxide dismutase (SOD), glutathione peroxidase (GSH-Px) in kidney were determined. |
| 2655 | 22527888 | Compared to diabetic rats treated with insulin alone, the diabetic rats treated with combination of insulin and RA showed: (1) significantly lower levels of MDA, IL-6, TNF-α, and Scr (p < 0.05); (2) significantly higher SOD and GSH-Px activities (p < 0.05); (3) significantly lower NF-κB activation and lower expression levels of PKCα (p < 0.05); (4) significantly smaller kidney-to-body weight ratio (p < 0.05). |
| 2656 | 22527888 | The levels of malondialdehyde (MDA), interleukin 6 (IL-6), tumor necrosis factor α (TNF-α) and activities of superoxide dismutase (SOD), glutathione peroxidase (GSH-Px) in kidney were determined. |
| 2657 | 22527888 | Compared to diabetic rats treated with insulin alone, the diabetic rats treated with combination of insulin and RA showed: (1) significantly lower levels of MDA, IL-6, TNF-α, and Scr (p < 0.05); (2) significantly higher SOD and GSH-Px activities (p < 0.05); (3) significantly lower NF-κB activation and lower expression levels of PKCα (p < 0.05); (4) significantly smaller kidney-to-body weight ratio (p < 0.05). |
| 2658 | 22561229 | Levels of nitric oxide (NO), tissue plasminogen activator (t-PA), plasminogen activator inhibitor-1 (PAI-1), prostaglandin I(2) (PGI(2)), vascular endothelial growth factor (VEGF) and the activity of SOD were measured by enzyme-linked immunosorbent assay (ELISA). |
| 2659 | 22561229 | Under high glucose stress conditions, late EPCs exhibited lower levels of NO, t-PA, PAI-1, PGI(2) and VEGF compared to control medium (5 mmol/L glucose). |
| 2660 | 22573545 | The levels of superoxide dismutase and glutathione peroxidase did not change, but the levels of glutathione-S-transferase (GST) were increased in diabetic prostate. |
| 2661 | 22576019 | The blood glucose, plasma insulin, hemoglobin, glycated hemoglobin, activities of the various antioxidant enzymes (catalase, superoxide dismutase, glutathione peroxidase and glutathione reductase) and lipid peroxidation markers (malondialdehyde, hydroperoxides and conjugated dienes) were evaluated in all the groups. |
| 2662 | 22581434 | The present study was undertaken to evaluate the effect of ethanol extract of Commiphora mukul gum resin (CMEE) on blood glucose, plasma insulin, lipid profiles, reduced glutathione, lipid peroxidation, protein oxidation and enzymatic antioxidants like superoxide dismutase, catalase, glutathione reductase, glutathione peroxidase, glutathione-S-transferase in fructose-induced type-2 diabetic rats. |
| 2663 | 22593683 | The 14-day repeated oral administration of the ethyl acetate fraction significantly reduced the fasting blood glucose and pancreatic TBARS level and significantly increased the liver glycogen, pancreatic superoxide dismutase, and catalase activities as well as reduced glutathione levels. |
| 2664 | 22614816 | Endogenous antioxidants include the antioxidant enzymes superoxide dismutase, catalase, glutathione peroxidase, paraoxanase, and glutathione S-transferase. |
| 2665 | 22644639 | Moreover, EHE treatment increased activities of antioxidant enzymes including catalase (CAT), superoxide dismutase (SOD), and glutathione peroxidase (GSH-px) in high glucose pretreated INS-1 pancreatic β-cells. |
| 2666 | 22644639 | EHE slightly reduced the expression of pro-apoptotic protein Bax induced by high glucose but increased the expression of Bcl-2, an anti-apoptotic protein. |
| 2667 | 22645603 | The oxidative stress parameters and the activity of antioxidant enzymes, superoxide dismutase (SOD), and catalase (CAT) were measured in the rat brain. |
| 2668 | 22688013 | The superoxide dismutase manganese dependent (SOD2) catalyzes O(2)(-) in H(2)O(2) into mitochondria and is encoded by a single gene that presents a common polymorphism that results in the replacement of alanine (A) with a valine (V) in the 16 codon. |
| 2669 | 22688013 | To test our hypothesis, we evaluated the in vitro cytokines production by human peripheral blood mononuclear cells (PBMCs) carrier's different Ala16Val-SOD2 genotypes (IL-1, IL-6, IL-10, TNF-α, IFN-γ). |
| 2670 | 22688338 | The proapoptotic c-Jun NH(2)-terminal kinases (JNK)1/2 activation is associated with diabetic embryopathy. |
| 2671 | 22688338 | We sought to determine whether 1) hyperglycemia-induced oxidative stress is responsible for the activation of JNK1/2 signaling, 2) JNK1 contributes to the teratogenicity of hyperglycemia, and 3) both JNK1 and JNK2 activation cause activation of downstream transcription factors, caspase activation, and apoptosis, resulting in neural tube defects (NTDs). |
| 2672 | 22688338 | Wild-type (WT) embryos from nondiabetic WT dams and WT, superoxide dismutase (SOD)1-overexpressing, jnk1(+/-), jnk1(-/-), and jnk2(-/-) embryos exposed to maternal hyperglycemia were used to assess JNK1/2 activation, NTDs, activation of transcription factors downstream of JNK1/2, caspase cascade, and apoptosis. |
| 2673 | 22688338 | SOD1 overexpression abolished diabetes-induced activation of JNK1/2 and their downstream effectors: phosphorylation of c-Jun, activating transcription factor 2, and E twenty-six-like transcription factor 1 and dephosphorylation of forkhead box class O3a. jnk1(-/-) embryos had significantly lower incidences of NTDs than those of WT or jnk1(+/-) embryos. |
| 2674 | 22688338 | Our results show that JNK1 and JNK2 are equally involved in diabetic embryopathy and that the oxidative stress-JNK1/2-caspase pathway mediates the proapoptotic signals and the teratogenicity of maternal diabetes. |
| 2675 | 22688338 | The proapoptotic c-Jun NH(2)-terminal kinases (JNK)1/2 activation is associated with diabetic embryopathy. |
| 2676 | 22688338 | We sought to determine whether 1) hyperglycemia-induced oxidative stress is responsible for the activation of JNK1/2 signaling, 2) JNK1 contributes to the teratogenicity of hyperglycemia, and 3) both JNK1 and JNK2 activation cause activation of downstream transcription factors, caspase activation, and apoptosis, resulting in neural tube defects (NTDs). |
| 2677 | 22688338 | Wild-type (WT) embryos from nondiabetic WT dams and WT, superoxide dismutase (SOD)1-overexpressing, jnk1(+/-), jnk1(-/-), and jnk2(-/-) embryos exposed to maternal hyperglycemia were used to assess JNK1/2 activation, NTDs, activation of transcription factors downstream of JNK1/2, caspase cascade, and apoptosis. |
| 2678 | 22688338 | SOD1 overexpression abolished diabetes-induced activation of JNK1/2 and their downstream effectors: phosphorylation of c-Jun, activating transcription factor 2, and E twenty-six-like transcription factor 1 and dephosphorylation of forkhead box class O3a. jnk1(-/-) embryos had significantly lower incidences of NTDs than those of WT or jnk1(+/-) embryos. |
| 2679 | 22688338 | Our results show that JNK1 and JNK2 are equally involved in diabetic embryopathy and that the oxidative stress-JNK1/2-caspase pathway mediates the proapoptotic signals and the teratogenicity of maternal diabetes. |
| 2680 | 22690296 | To create a base for and to develop antioxidant therapy, various SOD isozymes, catalase (CAT), methods of gene therapy, and combined applications of enzymes are used. |
| 2681 | 22701336 | The study demonstrated that SF has a cardioprotective effect via increasing SOD activity and NO levels in plasma and myocardium, inhibiting oxidative stress in plasma and myocardium, and inhibiting the expression of CTGF in myocardium in diabetes rats. |
| 2682 | 22718504 | The study was conducted to determine the activity of antioxidant enzymes: catalase (CAT), superoxide dismutase (SOD), glutathione peroxidase (GPX) and total antioxidant status (TAS) in the examined groups. |
| 2683 | 22718504 | A significant decrease of SOD (P < 0.05), GPX (P < 0.05) and nonsignificant decrease of CAT (P > 0.05), and TAS status (P > 0.05) were seen in T2DM patients with neuropathy compared to T2DM patients as well as controls. |
| 2684 | 22718504 | The study was conducted to determine the activity of antioxidant enzymes: catalase (CAT), superoxide dismutase (SOD), glutathione peroxidase (GPX) and total antioxidant status (TAS) in the examined groups. |
| 2685 | 22718504 | A significant decrease of SOD (P < 0.05), GPX (P < 0.05) and nonsignificant decrease of CAT (P > 0.05), and TAS status (P > 0.05) were seen in T2DM patients with neuropathy compared to T2DM patients as well as controls. |
| 2686 | 22771295 | At the end of the experimental periods, diabetic rats exhibited significant increase in the levels of plasma glucose, glycosylated hemoglobin with significant decrease in insulin and total hemoglobin. |
| 2687 | 22771295 | The activities of antioxidant enzymes such as superoxide dismutase, catalase, glutathione peroxidase, glutathione-S-transferase and the levels of reduced glutathione were decreased while increases in the levels of lipid peroxidation markers were observed in aortic tissues of diabetic rats. |
| 2688 | 22789789 | In comparison with the control group, diaphragmatic breathing resulted in significant reduction in body mass index, waist-hip ratio, fasting and post prandial plasma glucose, glycated hemoglobin, malondialdehyde, superoxide dismutase and improvement in glutathione and vitamin C. |
| 2689 | 22791351 | Liver from diabetic rats exhibited significant increase in malondialdehyde level and significant decrease in reduced glutathione, glutathione-S-transferase, quinone reductase, catalase, and superoxide dismutase. |
| 2690 | 22795334 | Coenzyme Q10 significantly increased the serum levels of glutathione (GSH) and serum activity of catalase (CAT) and superoxide dismutase (SOD) in treated group compared with the diabetic untreated group. |
| 2691 | 22796592 | Exposure of human brain microvascular endothelial cells to high glucose (25 mmol/L D-glucose), but not to high osmotic conditions (20 mmol/L L-glucose plus 5 mmol/L D-glucose), for 2h to 1 week significantly increased the permeability of the blood-brain barrier in parallel with lowered expression levels of zonula occludens-1, occludin, and claudin-5, three proteins that are essential to maintaining endothelial cell tight junctions. |
| 2692 | 22796592 | Adenoviral overexpression of superoxide dismutase or catalase significantly attenuated the high-glucose-induced reduction of endothelial cell tight-junction proteins. |
| 2693 | 22803325 | The extract also increased catalase, superoxide dismutase, glutathione reductase, glutathione peroxidase activities significantly and reduced lipid peroxidation. |
| 2694 | 22808343 | Plasma glucose, insulin, adiponectin, and lipid profiles, and lipid peroxidation of the liver were determined. |
| 2695 | 22808343 | Consumption of low and high quercetin reduced thiobarbituric acid reactive substances (TBARS) levels and elevated activities of superoxide dismutase (SOD), catalase (CAT), and glutathione peroxidase (GSH-Px) in the liver. |
| 2696 | 22815043 | The serum levels of glucose, insulin, interleukin 6 (IL-6), tumor necrosis factor α (TNF-α), MDA, SOD, and GSH-Px were determined. |
| 2697 | 22815043 | Compared with diabetic rats receiving BMSCs, diabetic rats receiving EGB before BMSCs transplantation showed (1) significantly lower levels of blood glucose, serum MDA, IL-6, and TNF-α, and higher levels of insulin, SOD, and GSH-Px activities; (2) significantly lower PKCα expression and NF-κB activation in the kidney. |
| 2698 | 22815043 | The serum levels of glucose, insulin, interleukin 6 (IL-6), tumor necrosis factor α (TNF-α), MDA, SOD, and GSH-Px were determined. |
| 2699 | 22815043 | Compared with diabetic rats receiving BMSCs, diabetic rats receiving EGB before BMSCs transplantation showed (1) significantly lower levels of blood glucose, serum MDA, IL-6, and TNF-α, and higher levels of insulin, SOD, and GSH-Px activities; (2) significantly lower PKCα expression and NF-κB activation in the kidney. |
| 2700 | 22819562 | In liver, postnatal EO programmed for lower catalase (-42%), superoxide dismutase (-45%) and glutathione peroxidase (-65%) activities. |
| 2701 | 22819562 | Regarding insulin signaling pathway in liver, SL offspring showed lower IRβ (-66%), IRS1 (-50%), phospho-IRS1 (-73%), PI3-K (-30%) and Akt1 (-58%). |
| 2702 | 22820670 | The plasma level of malondialdehyde was lower in CR rats than that in control rats, while the activities of superoxide dismutase, catalase and glutathione peroxidase in plasma were higher in CR rats than control rats. |
| 2703 | 22825027 | Malondialdehyde (MDA) content, superoxide dismutase (SOD) and caspase 3 activities were measured. |
| 2704 | 22825027 | In addition, with the development of diabetic cardiomyopathy, the contents of MDA and caspase 3 were increased, whereas SOD activity and Mfn-2 mRNA levels were further reduced. |
| 2705 | 22825027 | Malondialdehyde (MDA) content, superoxide dismutase (SOD) and caspase 3 activities were measured. |
| 2706 | 22825027 | In addition, with the development of diabetic cardiomyopathy, the contents of MDA and caspase 3 were increased, whereas SOD activity and Mfn-2 mRNA levels were further reduced. |
| 2707 | 22842119 | Lipid profile, MDA, GSH, SOD, FRAP, HMG CoA reductase and acetyl CoA carboxylase activities were estimated in blood and tissues. |
| 2708 | 22842119 | Administration of aqWC to diabetic animals also showed significant increase in antioxidant levels i.e., GSH, SOD, FRAP and reduced level of MDA in blood and tissue homogenates as compared to diabetic controls (p<0.05). |
| 2709 | 22842119 | Lipid profile, MDA, GSH, SOD, FRAP, HMG CoA reductase and acetyl CoA carboxylase activities were estimated in blood and tissues. |
| 2710 | 22842119 | Administration of aqWC to diabetic animals also showed significant increase in antioxidant levels i.e., GSH, SOD, FRAP and reduced level of MDA in blood and tissue homogenates as compared to diabetic controls (p<0.05). |
| 2711 | 22860400 | It was shown that the activity of superoxide dismutase, catalase is reduced in the plasma and testes of animals with streptozotocin-induced (50 mg/kg) diabetes (blood glucose 8-10 mmol/L). |
| 2712 | 22860400 | The per os administration of the NSE aqueous suspension in a dose of 50 mg/kg during 10 days to the rats with induced diabetes contributed to the normalization of catalase activity in the testis, which correlated with a decrease in the amount of TBA-reacting products and activity of superoxide dismutase and catalase in the blood plasma of animals; the use of NSE also contributed to the reduction of nitrite content in the gonads and to normalization of both nitrite and nitrate in the blood plasma of rats. |
| 2713 | 22860400 | It was shown that the activity of superoxide dismutase, catalase is reduced in the plasma and testes of animals with streptozotocin-induced (50 mg/kg) diabetes (blood glucose 8-10 mmol/L). |
| 2714 | 22860400 | The per os administration of the NSE aqueous suspension in a dose of 50 mg/kg during 10 days to the rats with induced diabetes contributed to the normalization of catalase activity in the testis, which correlated with a decrease in the amount of TBA-reacting products and activity of superoxide dismutase and catalase in the blood plasma of animals; the use of NSE also contributed to the reduction of nitrite content in the gonads and to normalization of both nitrite and nitrate in the blood plasma of rats. |
| 2715 | 22865358 | Glutathione peroxidase, superoxide dismutase and catalase activity were significantly increased in SME treated rats. |
| 2716 | 22878185 | In addition, the dieckol treatment increased the activities of antioxidative enzymes including catalase (CAT), superoxide dismutase (SOD) and glutathione peroxidase (GSH-px) in high glucose-pretreated rat insulinoma cells. |
| 2717 | 22878185 | These effects were mediated by suppressing apoptosis and were associated with increased anti-apoptotic Bcl-2 expression, and reduced pro-apoptotic cleaved caspase-3 expression. |
| 2718 | 22888397 | Simultaneous determination of antioxidant enzymes activities, namely glutathione peroxidase (GSH-Px), glutathione reductase (GSH-red), superoxide dismutase (SOD), total antioxidant, and lipid peroxides measured as thiobarbituric acid-reactive substances (TBARS) levels, were carried out in maternal plasma during labor. |
| 2719 | 22956978 | Hepatic antioxidant activities of glutathione peroxidase (GSH-Px), superoxide dismutase (SOD), and catalase (CAT) were also determined. |
| 2720 | 22956978 | Liver MDA content and serum levels of ALT, AST, ALP, and bilirubin in Group 3 significantly increased compared to Group 1 (P < 0.05) and significantly decreased in Group 4 compared to Group 3 (P < 0.05). |
| 2721 | 22956978 | Serum albumin level and GSH, SOD, CAT, and GSH-Px contents of the liver in Group 3 were significantly decreased compared to Group 1 (P < 0.05) and were significantly increased in Group 4 compared to Group 3 (P < 0.05). |
| 2722 | 22956978 | Hepatic antioxidant activities of glutathione peroxidase (GSH-Px), superoxide dismutase (SOD), and catalase (CAT) were also determined. |
| 2723 | 22956978 | Liver MDA content and serum levels of ALT, AST, ALP, and bilirubin in Group 3 significantly increased compared to Group 1 (P < 0.05) and significantly decreased in Group 4 compared to Group 3 (P < 0.05). |
| 2724 | 22956978 | Serum albumin level and GSH, SOD, CAT, and GSH-Px contents of the liver in Group 3 were significantly decreased compared to Group 1 (P < 0.05) and were significantly increased in Group 4 compared to Group 3 (P < 0.05). |
| 2725 | 22972774 | Association of copper-zinc superoxide dismutase (SOD1) and manganese superoxide dismutase (SOD2) genes with nonsyndromic myelomeningocele. |
| 2726 | 22975494 | To analyse cellular damage by high glucose, activation of Annexin V and p38 mitogen-activated protein kinase (MAPK) and extracellular signal-regulated kinase (ERK) were examined. |
| 2727 | 22975494 | Our results showed that a significant cellular damage on ARPE-19 cells after 48 h treatment with high glucose, accompanied by a decrease in SOD activity and GSH concentration; high glucose also caused ARPE-19 cell apoptosis and activation of p38MAPK and ERK. |
| 2728 | 22975503 | Diabetic rats were treated with 1 for 28 d and a set of biochemical parameters were studied including: glucose level, total cholesterol, triglycerides, lipid peroxidation, liver and muscle glycogen, superoxide dismutase, catalase, glutathione peroxidase and glutathione reductase. |
| 2729 | 22975503 | We also looked into liver function by determining glucose-6-phosphatase, glucokinase and hexokinase activities, and the effect on insulin level. |
| 2730 | 22987311 | Cisplatin exposure induced oxidative stress as indicated by decreased levels of non-enzymatic antioxidant defenses [glutathione (GSH) and ascorbic acid levels] and components of the enzymatic antioxidant defenses [superoxide dismutase (SOD), catalase (CAT) glutathione peroxidase (GPx), glutathione reductase (GR) and and glutathione S-transferase(GST) activities)] in renal tissue. |
| 2731 | 22987311 | Pioglitazone protected against the inhibition of CAT, SOD, GPx, GR and GST activities induced by cisplatin in the kidneys of mice. |
| 2732 | 22987311 | Cisplatin exposure induced oxidative stress as indicated by decreased levels of non-enzymatic antioxidant defenses [glutathione (GSH) and ascorbic acid levels] and components of the enzymatic antioxidant defenses [superoxide dismutase (SOD), catalase (CAT) glutathione peroxidase (GPx), glutathione reductase (GR) and and glutathione S-transferase(GST) activities)] in renal tissue. |
| 2733 | 22987311 | Pioglitazone protected against the inhibition of CAT, SOD, GPx, GR and GST activities induced by cisplatin in the kidneys of mice. |
| 2734 | 23024468 | Serum total cholesterol (TC), triglycerides (TG), LDL + VLDL cholesterol [(LDL + VLDL)C], HDL cholesterol [(HDL)C], total tissue lipids, glycogen and enzymes of carbohydrate metabolism (glycolysis, gluconeogenesis, polyol pathway) hexokinase, glucokinase, pyruvate kinase, malic enzyme, glucose-6-phosphatase, glucose-6-phosphate dehydrogenase, aldose reductase and sorbitol dehydrogenase and antioxidant enzymes glutathione peroxidase, glutathione reductase and superoxide dismutase were estimated. |
| 2735 | 23024468 | Treatment with GII for 15 days in the subdiabetic and moderately diabetic rabbits and for 30 days in the severely diabetic rabbits (i) decreased the elevated lipids TC, TG, (LDL + VLDL)C and increased the decreased (HDL)C, (ii) decreased the elevated liver and heart total lipids, TC and TG, (iii) increased the decreased liver and muscle glycogen, (iv) increased the decreased hexokinase, glucokinase, pyruvate kinase, malic enzyme, glucose-6-phosphate dehydrogenase, superoxide dismutase, glutathione peroxidase, (v) decreased the increased glucose-6-phosphatase, sorbitol dehydrogenase, aldose reductase. |
| 2736 | 23024468 | Serum total cholesterol (TC), triglycerides (TG), LDL + VLDL cholesterol [(LDL + VLDL)C], HDL cholesterol [(HDL)C], total tissue lipids, glycogen and enzymes of carbohydrate metabolism (glycolysis, gluconeogenesis, polyol pathway) hexokinase, glucokinase, pyruvate kinase, malic enzyme, glucose-6-phosphatase, glucose-6-phosphate dehydrogenase, aldose reductase and sorbitol dehydrogenase and antioxidant enzymes glutathione peroxidase, glutathione reductase and superoxide dismutase were estimated. |
| 2737 | 23024468 | Treatment with GII for 15 days in the subdiabetic and moderately diabetic rabbits and for 30 days in the severely diabetic rabbits (i) decreased the elevated lipids TC, TG, (LDL + VLDL)C and increased the decreased (HDL)C, (ii) decreased the elevated liver and heart total lipids, TC and TG, (iii) increased the decreased liver and muscle glycogen, (iv) increased the decreased hexokinase, glucokinase, pyruvate kinase, malic enzyme, glucose-6-phosphate dehydrogenase, superoxide dismutase, glutathione peroxidase, (v) decreased the increased glucose-6-phosphatase, sorbitol dehydrogenase, aldose reductase. |
| 2738 | 23059602 | The group of patients receiving intra-arterial administration of urokinase showed that the examined parameters on day 20 of treatment as compared with basic therapy alone increased: those of coagulability by 6% (p<0.05), activated partial thromboplastin time by 14% (p<0.01), thrombin time by 9.2% (p<0.01), antithrombin III by 7% (p<0.001). |
| 2739 | 23059602 | The fibrinogen level decreased by 9% (p<0.05), malonic dialdehyde concentration dropped by 30% (p<0.001), the concentrations of catalase and superoxide dismutase elevated by 55% (p<0.001) and 42%, respectively (p<0.05). |
| 2740 | 23079581 | The CDs fetuses responded to the HSD with lower catalase like activity, and less reduced superoxide dismutase levels compared to the Sabra strain, and had high malondialdehyde levels even when fed regular chow. |
| 2741 | 23105316 | The aqueous extract also decreased LPO formation (thiobarbituric acid reactive substances TBARS) and increased antioxidant enzymes superoxide dismutase (SOD), catalase (CAT), glutathione peroxidase (GPX), glutathione transferase (GT) and one antioxidant reduced glutathione (GSH) in plasma and rat liver, lung, kidney and brain. |
| 2742 | 23105316 | The decrease in TBARS and increase in GSH, SOD, CAT, GPX, and GT clearly shows the antioxidant property ofOcimum sanctum. |
| 2743 | 23105316 | The aqueous extract also decreased LPO formation (thiobarbituric acid reactive substances TBARS) and increased antioxidant enzymes superoxide dismutase (SOD), catalase (CAT), glutathione peroxidase (GPX), glutathione transferase (GT) and one antioxidant reduced glutathione (GSH) in plasma and rat liver, lung, kidney and brain. |
| 2744 | 23105316 | The decrease in TBARS and increase in GSH, SOD, CAT, GPX, and GT clearly shows the antioxidant property ofOcimum sanctum. |
| 2745 | 23105348 | The aqueous extract also resulted in decreased free radical formation in the tissues studied.The decrease in thiobarbituric acid reactive substances (TBARS) and increase in reduced glutathione (GSH), superoxide dismutase (SOD) and catalase (CAT) clearly showed the antioxidant property of the mixture. |
| 2746 | 23105374 | Lipid peroxidation by measurement of Thiobarbituric Acid Reactive Substances (TBARS) and antioxidant status by determining the activities of the enzymes, Catalase (Cat), Glutathione Peroxidase (GPx) and Superoxide Dismutase (SOD) and the level of Reduced Glutathione (GSH) in the erythrocytes of patients with type 2 Diabetes Mellitus were investigated. |
| 2747 | 23105641 | Biochemical parameters like plasma glucose, oral glucose tolerance and glycosylated hemoglobin HbA(1c), were measured along with lipid profile, and enzymes like glutathione peroxidase (GPX), lipid peroxidase (LPO), superoxide dismutase (SOD), catalase (CAT) and glutathione-S-transferase (GST) in normal, untreated diabetic rats and diabetic rats treated withOcimum sanctum L extracts and vitamin E. |
| 2748 | 23105641 | Evaluation of biochemical profile in treated groups showed statistically significant reduction in plasma levels of glucose, HbA(1c), lipid profile and LPO, and elevation of GPX, SOD, CAT and GST. |
| 2749 | 23105641 | Biochemical parameters like plasma glucose, oral glucose tolerance and glycosylated hemoglobin HbA(1c), were measured along with lipid profile, and enzymes like glutathione peroxidase (GPX), lipid peroxidase (LPO), superoxide dismutase (SOD), catalase (CAT) and glutathione-S-transferase (GST) in normal, untreated diabetic rats and diabetic rats treated withOcimum sanctum L extracts and vitamin E. |
| 2750 | 23105641 | Evaluation of biochemical profile in treated groups showed statistically significant reduction in plasma levels of glucose, HbA(1c), lipid profile and LPO, and elevation of GPX, SOD, CAT and GST. |
| 2751 | 23105723 | The effect of oral administration of vitamin E for twenty-eight consecutive days on blood glucose, reduced glutathione levels, antioxidant enzymes (superoxide dismutase and catalase activities), and levels of malondialdehyde (as an index of free radical-mediated lipid peroxidation) was observed in the whole blood and liver of normal and alloxan-induced diabetic rats. |
| 2752 | 23105761 | The oral administration of aqueous and methanol extracts of P. kurrooa rhizomes (250 and 500 mg / kg body weight / day) for 15 days significantly reduced blood glucose, glycosylated haemoglobin and increased total hemoglobin, plasma insulin in alloxan-induced diabetes in albino rats. |
| 2753 | 23105761 | The treatment also showed significant correction in the level of nitric oxide radicals, superoxide radicals, peroxynitrite radical, lipid peroxidation, glutathione, glutathione reductase, glutathione-S-transferase, glutathione peroxidase, superoxide dismutase and catalase in the pancreas of alloxan diabetic rats. |
| 2754 | 23105908 | Cellular antioxidant enzymes such as glutathione peroxidase (GSHPx), superoxide dismutase (SOD) and catalase (CAT) activities were measured in pancreatic homogenates. |
| 2755 | 23112392 | The combination groups proved to be effective in normalizing the levels of superoxide dismutase, catalase, glutathione reductase and lipid peroxidation in liver homogenates may be due to antioxidant effects of melatonin and decreased hyperglycemia induced insulin resistance by thiazolidinediones. |
| 2756 | 23112392 | The glucose uptake in the isolated hemidiaphragm of mice was significantly increased in combination treated groups (PM and RM) than dexamethasone alone treated mice as well as individual (pioglitazone, rosiglitazone, melatonin) treated groups probably via increased in expression of GLUT-4 by melatonin and thiazolidinediones as well as increased in insulin sensitivity by thiazolidinediones. |
| 2757 | 23128413 | In addition, treatment with glabridin resulted in a significant elevation of alkaline phosphatase (ALP) activity, collagen contents and osteoblast differentiation genes [ALP, collagen, osteopontin (OPN), osteoprotegerin (OPG) and osteocalcin (OC)] and bone morphogenetic protein (BMP) genes (BMP2, BMP4 and BMP7). |
| 2758 | 23128413 | Glabridin also upregulated the gene expression of antioxidant enzymes, superoxide dismutase 1 (SOD1) and glutathione peroxidase 4 (GPX4), which were inhibited by dRib. |
| 2759 | 23181120 | The mRNA levels of the glucose-stimulated insulin secretion (GSIS) genes glucokinase, glucose transporter 2 and Kir6.2 were downregulated under co-culture and co-culture plus LA conditions. |
| 2760 | 23181120 | The mRNA levels of superoxide dismutase and catalase were reduced under co-culture conditions and these reductions were eliminated by the addition of LA. |
| 2761 | 23202932 | We studied the effects of GBR on antioxidant status in type 2 diabetic rats, induced using a high-fat diet and streptozotocin injection, and also evaluated the effects of WR, BR and GBR on catalase and superoxide dismutase genes. |
| 2762 | 23207812 | The study was undertaken on 278 Algerian diabetic subjects who were divided in 2 groups according to glycated hemoglobin (HbA(1c)) <7% or >7% value, attesting for a good or poor metabolic control of diabetes, respectively. |
| 2763 | 23207812 | In conclusion, our results suggest that Mn play a crucial role in antioxidant capacity and we hypothesize that antioxidant defense is preserved in the cytosol (superoxide dismutase Cu/Zn -SOD), whereas it is impaired in mitochondria (Mn-SOD), which makes this cell organelle a true therapeutic target in diabetes. |
| 2764 | 23207871 | Here we conclude that after MkL treatment, not only the antioxidant parameters like SOD, CAT, GSH and MDA, but also PON1 may be involved in decreasing the oxidative stress associated with diabetes. |
| 2765 | 23261675 | Furthermore, reduced thiobarbituric acid reactive substraces (TBARS), as well as increased activities of antioxidant enzymes, including superoxide dismutase (SOD), catalase (CAT) and glutathione peroxidase (GSH-px) in liver tissues were observed in the dieckol administered group. |
| 2766 | 23261675 | In addition, increased levels of the phosphorylation of AMPK and Akt were observed in the muscle tissues of the dieckol administered group in a Western blotting analysis. |
| 2767 | 23265517 | After 12 weeks, RBBO significantly decreased malondialdehyde and restored superoxide dismutase, catalase, glutathione peroxidase, coenzyme Q(10) and ORAC levels in diabetic rats. |
| 2768 | 23285670 | Oxidative stress was measured by tissue LPO levels, reduced glutathione (GSH) contents and by enzymatic activities of glutathione peroxidase (GPx), glutathione reductase (GR), glutathione-S-transferase (GST), superoxide dismutase (SOD) and catalase (CAT). |
| 2769 | 23285670 | In addition, WS treated rats also showed a significant increase in the activities of antioxidant enzymes namely GPx, GR, GST, SOD and CAT when compared with type 2 diabetic control rats. |
| 2770 | 23285670 | Oxidative stress was measured by tissue LPO levels, reduced glutathione (GSH) contents and by enzymatic activities of glutathione peroxidase (GPx), glutathione reductase (GR), glutathione-S-transferase (GST), superoxide dismutase (SOD) and catalase (CAT). |
| 2771 | 23285670 | In addition, WS treated rats also showed a significant increase in the activities of antioxidant enzymes namely GPx, GR, GST, SOD and CAT when compared with type 2 diabetic control rats. |
| 2772 | 23292544 | In addition, decreased activities of hepatic antioxidant enzymes, i.e. glucose-6-phosphate dehydrogenase (G6PDH), glutathione peroxidase (GPx), glutathinone-S-tranferase (GST) and superoxide dismutase (SOD) were significantly increased by 34%, 61%, 19% and 53% respectively in mulberry leaves-treated diabetic rats as compared with diabetic control rats. |
| 2773 | 23304193 | Serum glucose, serum insulin, insulin sensitivity index, lipid parameters, body weight, sciatic nerve conduction velocity, nociception, glucagon-like peptide-1 receptor mRNA and protein, total and phosphorylated p38 mitogen-activated protein kinases protein expression, malonaldehyde content, and superoxide dismutase activity were altered in diabetic rats, and were near control levels treated with trigonelline. |
| 2774 | 23304193 | These findings suggest that trigonelline has beneficial effects for diabetic peripheral neuropathy through glucagon-like peptide-1 receptor/p38 mitogen-activated protein kinases signaling pathway, nerve conduction velocity, antioxidant enzyme activity, improving micropathological changes of sciatic nerve and decreasing lipid peroxidation. |
| 2775 | 23350204 | Natural dicarbonyls, which may be accumulated during oxidative stress in atherosclerosis (e.g. malondialdehyde) or carbonyl stress in diabetes mellitus (glyoxal and methylglyoxal) effectively inhibited the activities of commercial preparations of antioxidant enzymes: catalase, Cu, Zn-superoxide dismutase (Cu, Zn-SOD) and Se-contained glutathione peroxidase from human and bovine erythrocytes and also rat liver glutathione-S-transferase. |
| 2776 | 23354458 | Malondialdehyde and 4-hydroxynonenal adducts are not formed on cardiac ryanodine receptor (RyR2) and sarco(endo)plasmic reticulum Ca2+-ATPase (SERCA2) in diabetes. |
| 2777 | 23354458 | Recently, we reported an elevated level of glucose-generated carbonyl adducts on cardiac ryanodine receptor (RyR2) and sarco(endo)plasmic reticulum Ca(2+)-ATPase (SERCA2) in hearts of streptozotocin(STZ)-induced diabetic rats. |
| 2778 | 23354458 | We also showed these adduct impaired RyR2 and SERCA2 activities, and altered evoked Ca(2+) transients. |
| 2779 | 23354458 | What is less clear is if lipid-derived malondialdehyde (MDA) and 4-hydroxy-2-nonenal (4-HNE) also chemically react with and impair RyR2 and SERCA2 activities in diabetes? |
| 2780 | 23354458 | This study used western blot assays with adduct-specific antibodies and confocal microscopy to assess levels of MDA, 4-HNE, N (ε)-carboxy(methyl)lysine (CML), pentosidine, and pyrraline adducts on RyR2 and SERCA2 and evoked intracellular transient Ca(2+) kinetics in myocytes from control, diabetic, and treated-diabetic rats. |
| 2781 | 23354458 | MDA and 4-HNE adducts were not detected on RyR2 and SERCA2 from either control or 8 weeks diabetic rats with altered evoked Ca(2+) transients. |
| 2782 | 23354458 | Treating diabetic rats with pyridoxamine (a scavenger of reactive carbonyl species, RCS) or aminoguanidine (a mixed reactive oxygen species-RCS scavenger) reduced CML, pentosidine, and pyrraline adducts on RyR2 and SERCA2 and blunted SR Ca(2+) cycling changes. |
| 2783 | 23354458 | Treating diabetic rats with the superoxide dismutase mimetic tempol had no impact on MDA and 4-HNE adducts on RyR2 and SERCA2, and on SR Ca(2+) cycling. |
| 2784 | 23354458 | From these data we conclude that lipid-derived MDA and 4-HNE adducts are not formed on RyR2 and SERCA2 in this model of diabetes, and are therefore unlikely to be directly contributing to the SR Ca(2+) dysregulation. |
| 2785 | 23376836 | The Hsp treatment (100 mg/kg body weight) was carried for twenty four weeks in STZ-induced diabetic rats and evaluated for antioxidant (Superoxide dismutase; SOD, Catalase; CAT and glutathione; GSH) enzymes, inflammatory cytokines (TNF-α, IL-1β), caspase-3, glial fibrillary acidic protein (GFAP) and aquaporin-4(AQP4) expression. |
| 2786 | 23376836 | Diabetic retinae showed increased caspase-3, GFAP and AQP4 expression. |
| 2787 | 23376836 | However, Hsp-treated retinae showed inhibitory effect on caspase-3, GFAP and AQP4 expression. |
| 2788 | 23392947 | Also there was a marked increase in catalase activity (≥90%); and clear decreases in nitrite (≥40%), glutathione redox status (≥67%), and glutathione peroxidase (≥66%) and superoxide dismutase (≥51%) activities in both the aorta and heart. |
| 2789 | 23421041 | To enzymatic ones belong: catalase, superoxide dismutase, glutathione reductase and glutathione peroxidase. |
| 2790 | 23428743 | Weekly slit lamp examination was done during 21 days experimental period and then all rats were sacrificed; Ca/Mg ratio and antioxidant parameters including reduced glutathione (GSH), catalase and superoxide dismutase (SOD) activities were measured in the isolated lenses using ELISA. |
| 2791 | 23428743 | Lenticular GSH and catalase activities were significantly lower and SOD activity was significantly higher in all galactose fed groups. |
| 2792 | 23428743 | Weekly slit lamp examination was done during 21 days experimental period and then all rats were sacrificed; Ca/Mg ratio and antioxidant parameters including reduced glutathione (GSH), catalase and superoxide dismutase (SOD) activities were measured in the isolated lenses using ELISA. |
| 2793 | 23428743 | Lenticular GSH and catalase activities were significantly lower and SOD activity was significantly higher in all galactose fed groups. |
| 2794 | 23444338 | On the 60th day, skin tissue samples were taken, glutathione (GSH), lipid peroxidation (LPO), nonenzymatic glycosylation (NEG) and protein levels, catalase (CAT), superoxide dismutase (SOD) and glutathione-S-transferase (GST) activities were determined. |
| 2795 | 23444338 | Blood glucose, skin LPO and NEG levels increased, but skin GSH levels and CAT, SOD and GST activities decreased in the STZ group. |
| 2796 | 23444338 | On the 60th day, skin tissue samples were taken, glutathione (GSH), lipid peroxidation (LPO), nonenzymatic glycosylation (NEG) and protein levels, catalase (CAT), superoxide dismutase (SOD) and glutathione-S-transferase (GST) activities were determined. |
| 2797 | 23444338 | Blood glucose, skin LPO and NEG levels increased, but skin GSH levels and CAT, SOD and GST activities decreased in the STZ group. |
| 2798 | 23475448 | Ulcer tissues were harvested on days 7 and 14 to determine oxidative stress by measuring malondialdehyde (MDA) and antioxidant enzyme (superoxide dismutase [SOD], catalase [CAT], and glutathione peroxidase [GPx]) levels. |
| 2799 | 23475448 | MDA levels, SOD, and CAT were all significantly higher in the HBO than in the control group on day 14 (P<0.05). |
| 2800 | 23475448 | Ulcer tissues were harvested on days 7 and 14 to determine oxidative stress by measuring malondialdehyde (MDA) and antioxidant enzyme (superoxide dismutase [SOD], catalase [CAT], and glutathione peroxidase [GPx]) levels. |
| 2801 | 23475448 | MDA levels, SOD, and CAT were all significantly higher in the HBO than in the control group on day 14 (P<0.05). |
| 2802 | 23485614 | Both interventions restored the liver function markers (alanine transaminase: ALT, aspartate transaminase: AST, alkaline phosphatase: ALP, total bilirubin and total protein) and hepatic antioxidants (superoxide dismutase: SOD, catalase: CAT, reduced glutathione: GSH and glutathione peroxidase: GPx) to the normal levels than elevated levels noticed on paracetamol control at P<0.001. |
| 2803 | 23492555 | Palmitate decreased glucokinase activity and mRNA expression of genes involved in secretory function but up-regulated mRNA expression of HSPA5, EIF2A, and EIF2AK3, implicating activation of the endoplasmic reticulum stress response. |
| 2804 | 23492555 | These responses were accompanied by increased gene expression of the antioxidant enzymes SOD1, SOD2, CAT and GPX1. |
| 2805 | 23500100 | Finally, the serum levels of glucose, insulin, superoxide dismutase and 8-hydroxy-2'-deoxyguanosine (8-OHdG) were measured. |
| 2806 | 23500100 | While the probiotics administration enhanced the activation of superoxide dismutase and increased the insulin level of serum it decreased both the glucose level of serum and the 8-OHdG factor. |
| 2807 | 23500100 | Finally, the serum levels of glucose, insulin, superoxide dismutase and 8-hydroxy-2'-deoxyguanosine (8-OHdG) were measured. |
| 2808 | 23500100 | While the probiotics administration enhanced the activation of superoxide dismutase and increased the insulin level of serum it decreased both the glucose level of serum and the 8-OHdG factor. |
| 2809 | 23500382 | In the in vitro assay, kinsenoside (20 and 50 μg/mL) markedly inhibited changes in various biochemical substances (nitric oxide (NO), lactic dehydrogenase (LDH), superoxide dismutase (SOD), and catalase (CAT)) in human umbilical vein endothelial cells (HUVECs) damaged by high glucose (35 mM) and restored vascular endothelial structure by balancing the matrix metalloproteinases-the tissue inhibitors of matrix metalloproteinases (MMP-TIMP) system. |
| 2810 | 23500772 | In DM groups, SOD activity, ALDH2 mRNA and protein levels were reduced, MDA content was increased compared with control group; which decreased further as diabetes progressed. |
| 2811 | 23500772 | Compared with DM8W group, SOD and ALDH2 in EtOH+DM8W group was increased, MDA was decreased. |
| 2812 | 23500772 | In DM groups, SOD activity, ALDH2 mRNA and protein levels were reduced, MDA content was increased compared with control group; which decreased further as diabetes progressed. |
| 2813 | 23500772 | Compared with DM8W group, SOD and ALDH2 in EtOH+DM8W group was increased, MDA was decreased. |
| 2814 | 23514549 | The present study investigates the antioxidant enzyme activities such as SOD, CAT, GSH-Px and lipid peroxidation products in cardiac tissues of streptozotosin (STZ)-induced diabetic rats before and after thyroidectomy. |
| 2815 | 23534291 | The study was undertaken to investigate the influence of specific inhibitors of poly(ADP-ribose)polymerase-1 (PARP-1), in particular nicotinamide and 1,5-isoqinolinediol on white blood cells of rats with diabetes. |
| 2816 | 23534291 | Administration of PARP-1 inhibitors prevented the development of oxidative stress in leukocytes and increased their viability. |
| 2817 | 23534291 | Investigated PARP-1 inhibitors had no effect on the activity of superoxide dismutase and glucose levels in the blood. |
| 2818 | 23535541 | No alternation in the CuZn-superoxide dismutase (SOD) or Mn-SOD gene expression was found in the liver of GK rats as compared with that in the controls. |
| 2819 | 23545843 | To further investigate the protective effects of LWE on SIN-1‑induced oxidative stress in HIT-T15 cells, the cellular levels of ROS, lipid peroxidation and endogenous antioxidant enzymes, including superoxide dismutase (SOD), catalase (CAT) and glutathione peroxidase (GSH-px), were determined. |
| 2820 | 23562714 | The present work studies the efficacy of β-CM-7 against myocardial injury in streptozotocin-induced diabetic rats, focusing on the following assays: (1) the level of blood glucose and advanced glycosylation end product (AGE), the activity of lactate dehydrogenase (LDH) in serum; (2) the level of hydrogen peroxide (H2O2), the activity of Na(+)K(+)-ATPase, Ca(2+)Mg(2+)-ATPase and enzymatic antioxidants such as superoxide dismutase (SOD), catalase (CAT), glutathione peroxidase (GSH-Px) in myocardial tissue; (3) the protein expression of glucose transporter-4 (GLUT-4) in myocardial tissue. |
| 2821 | 23562714 | In the antioxidant and oxidant levels, β-CM-7 treatment group signified a remarkable increase in the activity of GSH-Px, SOD and CAT of the anti-oxidation system and meanwhile demonstrated a considerable reduction in H2O2 content (all P<0.05) in comparison with model group. |
| 2822 | 23562714 | The present work studies the efficacy of β-CM-7 against myocardial injury in streptozotocin-induced diabetic rats, focusing on the following assays: (1) the level of blood glucose and advanced glycosylation end product (AGE), the activity of lactate dehydrogenase (LDH) in serum; (2) the level of hydrogen peroxide (H2O2), the activity of Na(+)K(+)-ATPase, Ca(2+)Mg(2+)-ATPase and enzymatic antioxidants such as superoxide dismutase (SOD), catalase (CAT), glutathione peroxidase (GSH-Px) in myocardial tissue; (3) the protein expression of glucose transporter-4 (GLUT-4) in myocardial tissue. |
| 2823 | 23562714 | In the antioxidant and oxidant levels, β-CM-7 treatment group signified a remarkable increase in the activity of GSH-Px, SOD and CAT of the anti-oxidation system and meanwhile demonstrated a considerable reduction in H2O2 content (all P<0.05) in comparison with model group. |
| 2824 | 23565214 | QHYH markedly decreased serum MDA concentration, increased serum catalase (CAT) and SOD activities on week 4. |
| 2825 | 23566555 | Regulation of oxidative stress and somatostatin, cholecystokinin, apelin gene expressions by ghrelin in stomach of newborn diabetic rats. |
| 2826 | 23566555 | The gene expressions of: somatostatin, cholecystokinin, apelin and the altered active caspase-3, active caspase-8, proliferating cell nuclear antigen, were investigated in the pyloric region of the stomach and antioxidant parameters were measured in all the stomach. |
| 2827 | 23566555 | Exogenous ghrelin caused an increased activities of stomach catalase, superoxide dismutase, glutathione reductase and glutathione peroxidase in diabetic rats. |
| 2828 | 23566555 | Numbers of somatostatin, cholecystokinin and proliferating cell nuclear antigen immunoreactive cells decreased in the diabetic+ghrelin group compared to the diabetic group. |
| 2829 | 23566555 | Apelin mRNA expressions were remarkably less in the diabetic+ghrelin rats than in diabetic rats. |
| 2830 | 23580160 | In all rats, serum vitamin E, total cholesterol (TC), triglycerides (TG), low (LDL) and high (HDL) density lipoproteins, alanine (ALT) and aspartate (AST) transaminases, alkaline phosphatase (ALP), and gamma glutamyl transpeptidase (GGT) as well as cardiac and hepatic thiobarbituric acid-reactive substances (TBARS) and antioxidants (reduced glutathione (GSH), superoxide dismutase (SOD), and catalase (CAT)) were measured. |
| 2831 | 23580160 | HFD significantly increased QTc interval, heart rate (HR), serum TC, TG, LDL, ALT, AST, ALP, GGT, liver TG, and cardiac and hepatic TBARS but decreased antioxidants and HDL, while SIM decreased HR, liver TG, serum TC, TG, and LDL and increased HDL in HFD rats. |
| 2832 | 23580160 | Moreover, SIM and vitamin E decreased QTc interval, serum ALT, AST, ALP, GGT, and cardiac and hepatic TBARS and increased antioxidants in HFD rats. |
| 2833 | 23597490 | Furthermore, embelin treatment at both the doses significantly decreased the elevated malondialdehyde, restored depleted glutathione, antioxidant enzymes, superoxide dismutase and catalase in liver. |
| 2834 | 23606892 | ASEAF-treated diabetic rats showed higher pancreatic insulin content and pancreatic total superoxide dismutase activity compared to the untreated diabetic rats. |
| 2835 | 23612842 | Inflammatory markers like TNF-α, IL-6, IL-10, and myeloperoxidase were estimated and histological characters were studied. |
| 2836 | 23612842 | With resveratrol of 20 mg/kg dose, levels of oxidative stress markers and inflammatory markers like malondialdehyde, TNF-α, IL-6, and myeloperoxidase were reduced and there was a significant increase in the levels of antioxidant and anti-inflammatory markers like catalase, superoxide dismutase, and IL-10. |
| 2837 | 23624165 | Our results show that treatment with levan positively changed plasma antioxidant enzyme activities by increasing superoxide dismutase (SOD) and catalase (CAT) by 40% and 28%, respectively, in heart. |
| 2838 | 23625696 | At the end of the experimental period, the diabetic rats were killed, and levels of serum insulin, malondialdehyde, and nitric oxide, activities of glutathione peroxidase, total superoxide dismutase, copper/zinc-superoxide dismutase, and nitric oxide synthase were determined; pancreas was examined histopathologically as well. |
| 2839 | 23627599 | In addition, at 12.5 mg/(kg bw), CO significantly ameliorated pancreatic values of thiobarbituric acid reactive substances and activities of superoxide dismutase and glutathione reductase in diabetics to an extent greater than that of higher CO doses. |
| 2840 | 23652227 | Activities of hepatic and renal superoxide dismutase (SOD) and catalase (CAT), serum alkaline phosphatase, lactate dehydrogenase and alanine aminotransferase were not significantly (p>0.05) affected in MET and GB-treated rats, whereas testicular SOD, CAT, glutathione, serum aspartate aminotransferase and conjugated bilirubin were markedly affected by MET treatment. |
| 2841 | 23652775 | In addition, treatment with CZE resulted in a significant increase in alkaline phosphatase (ALP) activity and collagen content, as well as in the expression of genes associated with osteoblast differentiation [ALP, collagen, osteopontin (OPN), osteoprotegerin (OPG), bone sialoprotein (BSP), osteocalcin (OC) and bone morphogenetic protein (BMP)2, BMP4 and BMP7]. |
| 2842 | 23652775 | In mechanistic studies of the antioxidative potential of CZE, we found that CZE reversed the dRib-induced decrease in the expression of phosphatidylinositol 3-kinase (PI3K) and protein kinase B (AKT)1 and AKT2 genes, which are master regulators of survival-related signaling pathways. |
| 2843 | 23652775 | CZE also upregulated the gene expression of the antioxidant enzymes, superoxide dismutase (SOD)2, SOD3 and glutathione peroxidase 4 (GPx4), which was inhibited by dRib. |
| 2844 | 23662616 | The diabetic control rats exhibited elevated levels of lipid peroxidation and lower activities of copper/zinc superoxide dismutase (SOD), catalase (CAT), glutathione peroxidase (GPx), and reduced glutathione (GSH) content in pancreatic, hepatic, and renal tissues compared with normal tissues. |
| 2845 | 23662616 | The activities of SOD, CAT, GPx, and GSH were found to be increased in diabetic rats treated with the extract. |
| 2846 | 23662616 | The diabetic control rats exhibited elevated levels of lipid peroxidation and lower activities of copper/zinc superoxide dismutase (SOD), catalase (CAT), glutathione peroxidase (GPx), and reduced glutathione (GSH) content in pancreatic, hepatic, and renal tissues compared with normal tissues. |
| 2847 | 23662616 | The activities of SOD, CAT, GPx, and GSH were found to be increased in diabetic rats treated with the extract. |
| 2848 | 23691521 | After the treatment with nateglinide, significant decreases in FPG, PPG, GA, HbA1C, endothelin-1(ET-1), malondialdehyde (MDA), and HOMA-IRI were observed, whereas FMEDD, NO, and SOD increased (P < 0.01). |
| 2849 | 23709595 | Cytokine array revealed that Ex-4-sensitive inflammatory cytokines were ICAM-1 and macrophage colony-stimulating factor. |
| 2850 | 23709595 | Ex-4 ameliorated myocardial oxidative stress via suppression of NADPH oxidase 4 with concomitant elevation of antioxidants (SOD-1 and glutathione peroxidase). |
| 2851 | 23715526 | Therefore, in vitro superoxide dismutase activity of redox active complex 1 was evaluated by using a xanthine/xanthine oxidase-NBT assay which showed an IC50 value of 2.26 μM. |
| 2852 | 23716880 | Superoxide dismutase, catalase, glutathione peroxidase, glutathione-S-transferase, vitamins C, vitamin E, plasma reduced glutathione and erythrocyte glutathione, reduced glutathione content in the tissues was also assayed. |
| 2853 | 23716880 | The activities of catalase, superoxide dismutase and glutathione peroxidase and glutathione-S-transferase in erythrocytes were decreased significantly (F>0.05; P<0.001) in diabetic rats. |
| 2854 | 23716880 | Superoxide dismutase, catalase, glutathione peroxidase, glutathione-S-transferase, vitamins C, vitamin E, plasma reduced glutathione and erythrocyte glutathione, reduced glutathione content in the tissues was also assayed. |
| 2855 | 23716880 | The activities of catalase, superoxide dismutase and glutathione peroxidase and glutathione-S-transferase in erythrocytes were decreased significantly (F>0.05; P<0.001) in diabetic rats. |
| 2856 | 23734996 | The hepatic malondialdehyde, superoxide dismutase, catalase, and glutathione peroxidase activities were significantly increased in diabetic rats as compared with those in intact rats; however, in amitriptyline- and berberine-treated rats, they were significantly decreased as compared to the STZ control. |
| 2857 | 23737649 | In addition, genistein treatment decreased inflammatory markers such as nuclear factor kappa B (p65), phosphorylated inhibitory kappa B alpha, C-reactive protein, monocyte chemotactic protein-1, cyclooxygenase-2, and tumor necrosis factor-alpha and improved oxidative stress markers (nuclear-related factor E2, heme oxygenase-1, glutathione peroxidase, and superoxide dismutase isoforms) in treatment groups, regardless of the genistein treatment dose. |
| 2858 | 23737649 | Furthermore, genistein supplementation inhibited the fibrosis-related markers (protein kinase C, protein kinase C-beta II, and transforming growth factor-beta I) in the DN state. |
| 2859 | 23750273 | We chose two distinct models to test our hypothesis: 1) the leptin receptor deficient mouse (dbdb) model of diabetic polyneuropathy and 2) superoxide dismutase 1 knockout (Sod1(-/-) ) mouse model of in vivo oxidative stress. |
| 2860 | 23762845 | Fasudil significantly reduced the abundances of the Rho A, ROCK 1, and ROCK 2 proteins, restored the activities of succinate dehydrogenase (SDH) and monoamine oxidase (MAO) in cardiac mitochondria, inhibited the opening of the mitochondrial permeability transition pore, and decreased the total antioxidant capacity, as well as levels of malonyldialdehyde, hydroxy radical, reduced glutathione, and superoxide dismutase in heart. |
| 2861 | 23792234 | The activity of enzymatic antioxidants (superoxide dismutase, catalase and glutathione peroxidase) and the levels of non enzymatic antioxidants (vitamin C, vitamin E and reduced glutathione) were decreased in diabetic rats. |
| 2862 | 23792339 | Resveratrol, an activator of silent information regulator 2-related enzymes 1 (sirtuin1, SIRT1), has received attention for its valuable effects in cancer, neurodegenerative diseases, longevity and cardiovascular disease. |
| 2863 | 23792339 | Erectile function, cavernous structure, tissue protein expression of silent information regulator 2-related enzymes 1 (sirtuin1, SIRT1), p53 and forkhead transcription factor O 3a (FOXO3a), superoxide dismutase (SOD) activity and malondialdehyde (MDA) levels in the corpora cavernosa were studied. |
| 2864 | 23792339 | In contrast, resveratrol downregulated the expression of p53 and FOXO3a, which regulate apoptosis and oxidative stress. |
| 2865 | 23796219 | The content of serum insulin, hepatic glycogen, and reduced glutathione and the activity of superoxide dismutase and glutathione peroxidase increased significantly when MT-α-glucan was administered to T2DM mice. |
| 2866 | 23812874 | In this study, the effects of MR on the antioxidation system, including anti-lipid peroxidation; on the activities of superoxide dismutase (SOD), catalase (CAT), and glutathione peroxidase; and on glutathione content in the livers and uteri of β-naphthoflavone (BNF)-treated mice were determined. |
| 2867 | 23812874 | The results showed that MR improved the antioxidant activities of SOD and CAT in the livers and uteri of both normal and BNF-treated mice, while estradiol (E2) increased SOD activity in the uteri of normal mice and CAT activity in the livers of both normal and BNF-treated mice. |
| 2868 | 23812874 | In this study, the effects of MR on the antioxidation system, including anti-lipid peroxidation; on the activities of superoxide dismutase (SOD), catalase (CAT), and glutathione peroxidase; and on glutathione content in the livers and uteri of β-naphthoflavone (BNF)-treated mice were determined. |
| 2869 | 23812874 | The results showed that MR improved the antioxidant activities of SOD and CAT in the livers and uteri of both normal and BNF-treated mice, while estradiol (E2) increased SOD activity in the uteri of normal mice and CAT activity in the livers of both normal and BNF-treated mice. |
| 2870 | 23834171 | The transcription factor NF-E2-related factor 2/antioxidant response element (Nrf2/ARE) regulates the expression of many detoxifying genes such as catalase, superoxide dismutase, UDP-glucuronosyltransferase, c-glutamylcysteine synthetase, NAD(P)H quinone oxidoreductase 1, glutathione- S-transferase, glutathione peroxidase-1 and heme oxygenase-1. |
| 2871 | 23842942 | The anti obesity effect of water soluble fraction of Gymnema sylvestre extract (120 mg/kg, p.o. for 21 days) in HFD fed rats was evaluated by the measurement of body weight gain, food intake, hemodynamic changes (systolic, diastolic, mean blood pressure and heart rate), serum lipid profiles (triglycerides, total cholesterol, LDL-cholesterol, HDL-cholesterol), leptin, insulin, glucose, apolipoproteins A1 and B, lactate dehydrogenase (LDH) and antioxidant enzymes such as reduced glutathione (GSH), glutathione peroxidase (GPx), glutathione reductase (GR), glutathione-S transferase (GST), superoxide dismutase (SOD) and catalase (CAT) levels in liver tissues. |
| 2872 | 23842942 | Water soluble fraction of G. sylvestre ethanolic extract and rimonabant significantly reduced serum lipids, leptin, insulin, glucose, apolipoprotein B and LDH levels while it significantly increased the HDL-cholesterol, apolipoprotein A1 and antioxidant enzymes levels in liver tissue as compared to the HFD fed rats. |
| 2873 | 23871829 | In addition, the OPA pretreatment increased the activities of antioxidant enzymes such as catalase, superoxide dismutase, and glutathione peroxidase in STZ-treated pancreatic β cells. |
| 2874 | 23871829 | These effects were mediated by suppressing apoptosis and were associated with increased anti-apoptotic Bcl-xL expression and reduced pro-apoptotic Bax and cleaved caspase-3 expression. |
| 2875 | 23872067 | Here, we tested whether increased expression of CuZn-superoxide dismutase (Sod1) or Mn-superoxide dismutase (Sod2) prevented obesity-induced changes in oxidative stress and metabolism. |
| 2876 | 23872067 | Both Sod1 and Sod2 overexpressing mice were protected from high fat diet-induced glucose intolerance. |
| 2877 | 23872067 | Mice with increased expression of either Sod1 or Sod2 showed a significant reduction in this oxidative damage. |
| 2878 | 23872067 | Here, we tested whether increased expression of CuZn-superoxide dismutase (Sod1) or Mn-superoxide dismutase (Sod2) prevented obesity-induced changes in oxidative stress and metabolism. |
| 2879 | 23872067 | Both Sod1 and Sod2 overexpressing mice were protected from high fat diet-induced glucose intolerance. |
| 2880 | 23872067 | Mice with increased expression of either Sod1 or Sod2 showed a significant reduction in this oxidative damage. |
| 2881 | 23872067 | Here, we tested whether increased expression of CuZn-superoxide dismutase (Sod1) or Mn-superoxide dismutase (Sod2) prevented obesity-induced changes in oxidative stress and metabolism. |
| 2882 | 23872067 | Both Sod1 and Sod2 overexpressing mice were protected from high fat diet-induced glucose intolerance. |
| 2883 | 23872067 | Mice with increased expression of either Sod1 or Sod2 showed a significant reduction in this oxidative damage. |
| 2884 | 23880309 | BTB and CNC homology 1 (Bach1) is a transcriptional repressor of antioxidative enzymes, such as heme oxygenase-1 (HO-1). |
| 2885 | 23880309 | Unexpectedly, glucose and insulin tolerance tests showed no differences in obese wild-type (WT) and obese Bach1-deficient mice after high-fat diet loading for 6 wk, suggesting minimal roles of Bach1 in the development of insulin resistance. |
| 2886 | 23880309 | In contrast, Bach1 deficiency significantly suppressed alloxan-induced pancreatic insulin content reduction and the resultant glucose elevation. |
| 2887 | 23880309 | HO-1 expression in islets was significantly upregulated in alloxan-injected Bach1-deficient mice, whereas expression of other antioxidative enzymes, e.g., catalase, superoxide dismutase, and glutathione peroxidase, was not changed by either alloxan administration or Bach1 deficiency. |
| 2888 | 23880309 | Our results suggest that Bach1 deficiency protects pancreatic β-cells from oxidative stress-induced apoptosis and that the enhancement of HO-1 expression plays an important role in this protection. |
| 2889 | 23884884 | Copper transporter ATP7A protects against endothelial dysfunction in type 1 diabetic mice by regulating extracellular superoxide dismutase. |
| 2890 | 23884884 | Extracellular superoxide dismutase (SOD3) is one of the key antioxidant enzymes that obtains copper via copper transporter ATP7A. |
| 2891 | 23884884 | The role of SOD3 and ATP7A in endothelial dysfunction in type 1 diabetes mellitus (T1DM) is entirely unknown. |
| 2892 | 23884884 | Here we show that the specific activity of SOD3, but not SOD1, is decreased, which is associated with increased O2(•-) production in aortas of streptozotocin-induced and genetically induced Ins2(Akita) T1DM mice. |
| 2893 | 23884884 | Functionally, acetylcholine-induced, endothelium-dependent relaxation is impaired in T1DM mesenteric arteries, which is rescued by SOD mimetic tempol or gene transfer of SOD3. |
| 2894 | 23884884 | T1DM-induced endothelial dysfunction and decrease of SOD3 activity are rescued in transgenic mice overexpressing ATP7A. |
| 2895 | 23884884 | Furthermore, SOD3-deficient T1DM mice or ATP7A mutant T1DM mice augment endothelial dysfunction and vascular O2(•-) production versus T1DM mice. |
| 2896 | 23884884 | These effects are in part due to hypoinsulinemia in T1DM mice, since insulin treatment, but not high glucose, increases ATP7A expression in VSMCs and restores SOD3 activity in the organoid culture of T1DM vessels. |
| 2897 | 23884884 | In summary, a decrease in ATP7A protein expression contributes to impaired SOD3 activity, resulting in O2(•-) overproduction and endothelial dysfunction in blood vessels of T1DM. |
| 2898 | 23884884 | Copper transporter ATP7A protects against endothelial dysfunction in type 1 diabetic mice by regulating extracellular superoxide dismutase. |
| 2899 | 23884884 | Extracellular superoxide dismutase (SOD3) is one of the key antioxidant enzymes that obtains copper via copper transporter ATP7A. |
| 2900 | 23884884 | The role of SOD3 and ATP7A in endothelial dysfunction in type 1 diabetes mellitus (T1DM) is entirely unknown. |
| 2901 | 23884884 | Here we show that the specific activity of SOD3, but not SOD1, is decreased, which is associated with increased O2(•-) production in aortas of streptozotocin-induced and genetically induced Ins2(Akita) T1DM mice. |
| 2902 | 23884884 | Functionally, acetylcholine-induced, endothelium-dependent relaxation is impaired in T1DM mesenteric arteries, which is rescued by SOD mimetic tempol or gene transfer of SOD3. |
| 2903 | 23884884 | T1DM-induced endothelial dysfunction and decrease of SOD3 activity are rescued in transgenic mice overexpressing ATP7A. |
| 2904 | 23884884 | Furthermore, SOD3-deficient T1DM mice or ATP7A mutant T1DM mice augment endothelial dysfunction and vascular O2(•-) production versus T1DM mice. |
| 2905 | 23884884 | These effects are in part due to hypoinsulinemia in T1DM mice, since insulin treatment, but not high glucose, increases ATP7A expression in VSMCs and restores SOD3 activity in the organoid culture of T1DM vessels. |
| 2906 | 23884884 | In summary, a decrease in ATP7A protein expression contributes to impaired SOD3 activity, resulting in O2(•-) overproduction and endothelial dysfunction in blood vessels of T1DM. |
| 2907 | 23940092 | Relaxation to levcromakalim (ATP-sensitive potassium channel KATP opener, 10(-9)-10(-5) mol/l) and (+/-)-naringenin (large conductance calcium-activated channel BKCa opener, 10(-8)-10(-3) mol/l) were recorded in phenylephrine (1 µmol/l) pre-contracted segments in the absence and presence of superoxide dismutase (SOD, 100 µmol/l) and apocynin (an antioxidant and inhibitor of NADPH oxidase, 100 µmol/l). |
| 2908 | 23951261 | Diabetes-induced superoxide anion and breakdown of the blood-retinal barrier: role of the VEGF/uPAR pathway. |
| 2909 | 23951261 | We have shown that VEGF increases permeability of retinal endothelial cells (REC) by inducing expression of urokinase plasminogen activator receptor (uPAR). |
| 2910 | 23951261 | The purpose of this study was to define the role of superoxide anion in VEGF/uPAR expression and BRB breakdown in diabetes. |
| 2911 | 23951261 | The superoxide dismutase (SOD) mimetic tempol blocked diabetes-induced permeability and uPAR expression in rats and the cell permeable SOD inhibited HG-induced expression of uPAR and VEGF in REC. |
| 2912 | 23951261 | Inhibiting VEGFR blocked HG-induced expression of VEGF and uPAR and GSK-3β phosphorylation in REC. |
| 2913 | 23951261 | Moreover, deletion of uPAR blocked diabetes-induced BRB breakdown and activation of MMP-9 in mice. |
| 2914 | 23951261 | Together, these data indicate that diabetes-induced oxidative stress triggers BRB breakdown by a mechanism involving uPAR expression through VEGF-induced activation of the GSK3β/β-catenin signaling pathway. |
| 2915 | 23994945 | Moreover, RF decreased the activities of glutathione peroxidase (GPx, -33.33% and -49.40%) catalase (CAT, -43.39% and -39.62%) and the superoxide dismutase (SOD, -59.29% and -68.53%) and groups thiol amount (-62.68% and -34.85%), respectively in liver and kidneys. |
| 2916 | 23994945 | Olive leaves extract administration (100 mg/kg, ip) in RF-exposed rats prevented glucose metabolism disruption and restored the activities of GPx, CAT and SOD and thiol group amount in liver and kidneys. |
| 2917 | 23994945 | Moreover, RF decreased the activities of glutathione peroxidase (GPx, -33.33% and -49.40%) catalase (CAT, -43.39% and -39.62%) and the superoxide dismutase (SOD, -59.29% and -68.53%) and groups thiol amount (-62.68% and -34.85%), respectively in liver and kidneys. |
| 2918 | 23994945 | Olive leaves extract administration (100 mg/kg, ip) in RF-exposed rats prevented glucose metabolism disruption and restored the activities of GPx, CAT and SOD and thiol group amount in liver and kidneys. |