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Gene Information
Gene symbol: CYP2B6
Gene name: cytochrome P450, family 2, subfamily B, polypeptide 6
HGNC ID: 2615
Synonyms: CPB6, CYPIIB6
Related Genes
Related Sentences
| # | PMID | Sentence |
| 1 | 19220 | Furthermore, hepatic microsomal protein and cytochrome P-450 contents were not significantly different in any of the diabetic animals from those of the control animals. |
| 2 | 35327 | Cytochrome P-450 levels were similarly increased. |
| 3 | 152519 | In streptozotocin-induced diabetic male rats, hepatic microsomal aminopyrine N-demethylase activity was depressed, whereas aniline hydroxylase activity and cytochrome P-450 content were increased over control values. 2. |
| 4 | 152519 | In diabetic female rats, hepatic microsomal aminopyrine N-demethylase activity, aniline hydroxylase activity, biphenyl 4-hydroxylase activity, and cytochrome P-450 content were increased over control values. 3. |
| 5 | 152519 | Methyl analogues of streptozotocin did not produce a diabetic state when injected into female rats, and resulted in no changes in aminopyrine N-demethylase activity, aniline hydroxylase activity, or cytochrome P-450 content. 5. |
| 6 | 152519 | Insulin treatment of non-diabetic female rats resulted in slight decreases in aminopyrine N-demethylase and aniline hydroxylase activities, but no changes in cytochrome P-450 content. |
| 7 | 152519 | In streptozotocin-induced diabetic male rats, hepatic microsomal aminopyrine N-demethylase activity was depressed, whereas aniline hydroxylase activity and cytochrome P-450 content were increased over control values. 2. |
| 8 | 152519 | In diabetic female rats, hepatic microsomal aminopyrine N-demethylase activity, aniline hydroxylase activity, biphenyl 4-hydroxylase activity, and cytochrome P-450 content were increased over control values. 3. |
| 9 | 152519 | Methyl analogues of streptozotocin did not produce a diabetic state when injected into female rats, and resulted in no changes in aminopyrine N-demethylase activity, aniline hydroxylase activity, or cytochrome P-450 content. 5. |
| 10 | 152519 | Insulin treatment of non-diabetic female rats resulted in slight decreases in aminopyrine N-demethylase and aniline hydroxylase activities, but no changes in cytochrome P-450 content. |
| 11 | 152519 | In streptozotocin-induced diabetic male rats, hepatic microsomal aminopyrine N-demethylase activity was depressed, whereas aniline hydroxylase activity and cytochrome P-450 content were increased over control values. 2. |
| 12 | 152519 | In diabetic female rats, hepatic microsomal aminopyrine N-demethylase activity, aniline hydroxylase activity, biphenyl 4-hydroxylase activity, and cytochrome P-450 content were increased over control values. 3. |
| 13 | 152519 | Methyl analogues of streptozotocin did not produce a diabetic state when injected into female rats, and resulted in no changes in aminopyrine N-demethylase activity, aniline hydroxylase activity, or cytochrome P-450 content. 5. |
| 14 | 152519 | Insulin treatment of non-diabetic female rats resulted in slight decreases in aminopyrine N-demethylase and aniline hydroxylase activities, but no changes in cytochrome P-450 content. |
| 15 | 152519 | In streptozotocin-induced diabetic male rats, hepatic microsomal aminopyrine N-demethylase activity was depressed, whereas aniline hydroxylase activity and cytochrome P-450 content were increased over control values. 2. |
| 16 | 152519 | In diabetic female rats, hepatic microsomal aminopyrine N-demethylase activity, aniline hydroxylase activity, biphenyl 4-hydroxylase activity, and cytochrome P-450 content were increased over control values. 3. |
| 17 | 152519 | Methyl analogues of streptozotocin did not produce a diabetic state when injected into female rats, and resulted in no changes in aminopyrine N-demethylase activity, aniline hydroxylase activity, or cytochrome P-450 content. 5. |
| 18 | 152519 | Insulin treatment of non-diabetic female rats resulted in slight decreases in aminopyrine N-demethylase and aniline hydroxylase activities, but no changes in cytochrome P-450 content. |
| 19 | 537273 | Hepatic cholesterol synthesis was markedly depressed, while cholesterol 7 alpha-hydroxylase activity did not change and cytochrome P-450 content was elevated by about 40%. |
| 20 | 1441586 | A polyclonal, monospecific antibody to a constitutive, diabetes-inducible and insulin-reversible cytochrome P-450 isozyme (RLM6) was used to screen a male rat liver cDNA library in lambda gt 11. |
| 21 | 1457080 | Angiotensin II regulates cytochrome P-450 steroid hydroxylase enzyme expression in human adrenal glomerulosa cells. |
| 22 | 1457080 | We have examined the regulation of cytochrome P-450 side chain cleavage enzyme (P-450SCC) and P-45011 beta (18) hydroxylase (P-450(11) beta) enzyme expression by angiotensin II (AII), the major regulator of aldosterone biosynthesis, in cultured human adrenal glomerulosa cells. |
| 23 | 1457080 | AII (10(-7) mol/L) induced a 3-fold stimulation of P-450SCC and over a 2-fold increase in P-450(11) beta protein expression. |
| 24 | 1457080 | The 12-lipoxygenase product, 12-hydroxyeicosatetraenoic acid (12-HETE) caused a 2-fold increase in P-450(11) beta levels without altering P-450SCC levels. |
| 25 | 1457080 | These results show for the first time that AII can directly increase the levels of P-450SCC and P-450(11) beta enzymes in glomerulosa cells. |
| 26 | 1457080 | Angiotensin II regulates cytochrome P-450 steroid hydroxylase enzyme expression in human adrenal glomerulosa cells. |
| 27 | 1457080 | We have examined the regulation of cytochrome P-450 side chain cleavage enzyme (P-450SCC) and P-45011 beta (18) hydroxylase (P-450(11) beta) enzyme expression by angiotensin II (AII), the major regulator of aldosterone biosynthesis, in cultured human adrenal glomerulosa cells. |
| 28 | 1457080 | AII (10(-7) mol/L) induced a 3-fold stimulation of P-450SCC and over a 2-fold increase in P-450(11) beta protein expression. |
| 29 | 1457080 | The 12-lipoxygenase product, 12-hydroxyeicosatetraenoic acid (12-HETE) caused a 2-fold increase in P-450(11) beta levels without altering P-450SCC levels. |
| 30 | 1457080 | These results show for the first time that AII can directly increase the levels of P-450SCC and P-450(11) beta enzymes in glomerulosa cells. |
| 31 | 1457080 | Angiotensin II regulates cytochrome P-450 steroid hydroxylase enzyme expression in human adrenal glomerulosa cells. |
| 32 | 1457080 | We have examined the regulation of cytochrome P-450 side chain cleavage enzyme (P-450SCC) and P-45011 beta (18) hydroxylase (P-450(11) beta) enzyme expression by angiotensin II (AII), the major regulator of aldosterone biosynthesis, in cultured human adrenal glomerulosa cells. |
| 33 | 1457080 | AII (10(-7) mol/L) induced a 3-fold stimulation of P-450SCC and over a 2-fold increase in P-450(11) beta protein expression. |
| 34 | 1457080 | The 12-lipoxygenase product, 12-hydroxyeicosatetraenoic acid (12-HETE) caused a 2-fold increase in P-450(11) beta levels without altering P-450SCC levels. |
| 35 | 1457080 | These results show for the first time that AII can directly increase the levels of P-450SCC and P-450(11) beta enzymes in glomerulosa cells. |
| 36 | 1457080 | Angiotensin II regulates cytochrome P-450 steroid hydroxylase enzyme expression in human adrenal glomerulosa cells. |
| 37 | 1457080 | We have examined the regulation of cytochrome P-450 side chain cleavage enzyme (P-450SCC) and P-45011 beta (18) hydroxylase (P-450(11) beta) enzyme expression by angiotensin II (AII), the major regulator of aldosterone biosynthesis, in cultured human adrenal glomerulosa cells. |
| 38 | 1457080 | AII (10(-7) mol/L) induced a 3-fold stimulation of P-450SCC and over a 2-fold increase in P-450(11) beta protein expression. |
| 39 | 1457080 | The 12-lipoxygenase product, 12-hydroxyeicosatetraenoic acid (12-HETE) caused a 2-fold increase in P-450(11) beta levels without altering P-450SCC levels. |
| 40 | 1457080 | These results show for the first time that AII can directly increase the levels of P-450SCC and P-450(11) beta enzymes in glomerulosa cells. |
| 41 | 1457080 | Angiotensin II regulates cytochrome P-450 steroid hydroxylase enzyme expression in human adrenal glomerulosa cells. |
| 42 | 1457080 | We have examined the regulation of cytochrome P-450 side chain cleavage enzyme (P-450SCC) and P-45011 beta (18) hydroxylase (P-450(11) beta) enzyme expression by angiotensin II (AII), the major regulator of aldosterone biosynthesis, in cultured human adrenal glomerulosa cells. |
| 43 | 1457080 | AII (10(-7) mol/L) induced a 3-fold stimulation of P-450SCC and over a 2-fold increase in P-450(11) beta protein expression. |
| 44 | 1457080 | The 12-lipoxygenase product, 12-hydroxyeicosatetraenoic acid (12-HETE) caused a 2-fold increase in P-450(11) beta levels without altering P-450SCC levels. |
| 45 | 1457080 | These results show for the first time that AII can directly increase the levels of P-450SCC and P-450(11) beta enzymes in glomerulosa cells. |
| 46 | 1459481 | The former can be produced by enzymatic pathways through the cytochrome P-450 system, while the latter is reported to be solely formed by direct hydroxyl radical attack. |
| 47 | 1471220 | Sex-specific cytochrome P450 as a cause of sex- and species-related differences in drug toxicity. |
| 48 | 1471220 | Recent studies indicate the existence of sex-specific cytochrome P450, such as P450-male (2C11) and P450-female (2C12) and P450(6) beta (3A2) in rat livers, and also show that their expression levels are markedly different between male and female rats. |
| 49 | 1471220 | Sex-specific cytochrome P450 as a cause of sex- and species-related differences in drug toxicity. |
| 50 | 1471220 | Recent studies indicate the existence of sex-specific cytochrome P450, such as P450-male (2C11) and P450-female (2C12) and P450(6) beta (3A2) in rat livers, and also show that their expression levels are markedly different between male and female rats. |
| 51 | 1484345 | In pancreatic beta cells, alloxan anion radicals are generated from alloxan probably mediated by the action of microsomal cytochrome P-450 system. |
| 52 | 1492403 | Content of cytochromes P450 and b5, activities of amidopyrine-N-demethylase, alanine- and p-nitrophenol hydroxylases, NADPH-cytochrome c reductase were studied in the liver, kidney, small intestine and lung tissues of rats and rabbits in insulin-dependent hypoglycemia and alloxan diabetes. |
| 53 | 1494889 | Induction of rat hepatic mixed-function oxidases by acetone and other physiological ketones: their role in diabetes-induced changes in cytochrome P450 proteins. |
| 54 | 1494889 | To evaluate the role of ketone bodies in diabetes-induced changes in hepatic cytochrome P450 composition, rats were treated with acetone, 3-hydroxybutyrate or 1,3-butanediol. 2. |
| 55 | 1494889 | On the basis of work from our own and other laboratories a mechanism for the diabetes-induced changes in hepatic cytochrome P450 proteins is proposed. |
| 56 | 1494889 | Induction of rat hepatic mixed-function oxidases by acetone and other physiological ketones: their role in diabetes-induced changes in cytochrome P450 proteins. |
| 57 | 1494889 | To evaluate the role of ketone bodies in diabetes-induced changes in hepatic cytochrome P450 composition, rats were treated with acetone, 3-hydroxybutyrate or 1,3-butanediol. 2. |
| 58 | 1494889 | On the basis of work from our own and other laboratories a mechanism for the diabetes-induced changes in hepatic cytochrome P450 proteins is proposed. |
| 59 | 1494889 | Induction of rat hepatic mixed-function oxidases by acetone and other physiological ketones: their role in diabetes-induced changes in cytochrome P450 proteins. |
| 60 | 1494889 | To evaluate the role of ketone bodies in diabetes-induced changes in hepatic cytochrome P450 composition, rats were treated with acetone, 3-hydroxybutyrate or 1,3-butanediol. 2. |
| 61 | 1494889 | On the basis of work from our own and other laboratories a mechanism for the diabetes-induced changes in hepatic cytochrome P450 proteins is proposed. |
| 62 | 1575780 | Cytochrome P-450-dependent mixed-function oxidase and glutathione S-transferase activities in spontaneous obesity-diabetes. |
| 63 | 1575780 | The effect of non-insulin-dependent diabetes on the hepatic microsomal cytochrome P450-dependent mixed-function oxidase system and on cytosolic glutathione S-transferase activity was determined using the spontaneously obese-diabetic (ob/ob) mouse model. |
| 64 | 1575780 | The activities of the xenobiotic-metabolizing cytochrome P450 proteins were monitored by the use of chemical probes. |
| 65 | 1575780 | Non-insulin-dependent diabetes did not influence the hepatic metabolism of substrates associated with the P450 I, IIB, IIE, III and IV families of cytochromes. |
| 66 | 1575780 | Cytochrome P-450-dependent mixed-function oxidase and glutathione S-transferase activities in spontaneous obesity-diabetes. |
| 67 | 1575780 | The effect of non-insulin-dependent diabetes on the hepatic microsomal cytochrome P450-dependent mixed-function oxidase system and on cytosolic glutathione S-transferase activity was determined using the spontaneously obese-diabetic (ob/ob) mouse model. |
| 68 | 1575780 | The activities of the xenobiotic-metabolizing cytochrome P450 proteins were monitored by the use of chemical probes. |
| 69 | 1575780 | Non-insulin-dependent diabetes did not influence the hepatic metabolism of substrates associated with the P450 I, IIB, IIE, III and IV families of cytochromes. |
| 70 | 1575780 | Cytochrome P-450-dependent mixed-function oxidase and glutathione S-transferase activities in spontaneous obesity-diabetes. |
| 71 | 1575780 | The effect of non-insulin-dependent diabetes on the hepatic microsomal cytochrome P450-dependent mixed-function oxidase system and on cytosolic glutathione S-transferase activity was determined using the spontaneously obese-diabetic (ob/ob) mouse model. |
| 72 | 1575780 | The activities of the xenobiotic-metabolizing cytochrome P450 proteins were monitored by the use of chemical probes. |
| 73 | 1575780 | Non-insulin-dependent diabetes did not influence the hepatic metabolism of substrates associated with the P450 I, IIB, IIE, III and IV families of cytochromes. |
| 74 | 1676625 | Purification and aminopyrine monooxygenase activity of liver microsomal cytochrome P-450 from alloxan-induced diabetic rats. |
| 75 | 1676625 | We purified two diabetes-inducible and insulin-sensitive forms of cytochrome P-450, named P-450AL-1 and AL-2, from the liver microsomes of alloxan-diabetic male rats, using sodium cholate solubilization, octylamino-Sepharose 4B chromatography, and HPLC with diethylaminoethyl-5PW and hydroxyapatite columns. |
| 76 | 1676625 | Purification and aminopyrine monooxygenase activity of liver microsomal cytochrome P-450 from alloxan-induced diabetic rats. |
| 77 | 1676625 | We purified two diabetes-inducible and insulin-sensitive forms of cytochrome P-450, named P-450AL-1 and AL-2, from the liver microsomes of alloxan-diabetic male rats, using sodium cholate solubilization, octylamino-Sepharose 4B chromatography, and HPLC with diethylaminoethyl-5PW and hydroxyapatite columns. |
| 78 | 1693736 | The only significant drug interactions with felodipine occur with inducers and inhibitors of the cytochrome P-450 system, which is responsible for the metabolism of felodipine. |
| 79 | 1698138 | Effects of vanadate on hepatic cytochrome P-450 expression in streptozotocin-diabetic rats. |
| 80 | 1698138 | The ability of sodium metavanadate to reverse the effects of streptozotocin-induced diabetes on hepatic cytochrome P-450 isozymes was examined in male rats. |
| 81 | 1698138 | Effects of vanadate on hepatic cytochrome P-450 expression in streptozotocin-diabetic rats. |
| 82 | 1698138 | The ability of sodium metavanadate to reverse the effects of streptozotocin-induced diabetes on hepatic cytochrome P-450 isozymes was examined in male rats. |
| 83 | 1706265 | Growth hormone-dependent and -independent regulation of cytochrome P-450 isozyme expression in streptozotocin-diabetic rats. |
| 84 | 1845601 | Microsomal ethanol oxidizing system: transcriptional and posttranscriptional regulation of cytochrome P450, CYP2E1. |
| 85 | 1845601 | CYP2E1 is solely responsible for microsomal P450-mediated ethanol oxidation activity. |
| 86 | 1845601 | Microsomal ethanol oxidizing system: transcriptional and posttranscriptional regulation of cytochrome P450, CYP2E1. |
| 87 | 1845601 | CYP2E1 is solely responsible for microsomal P450-mediated ethanol oxidation activity. |
| 88 | 1909958 | Similarly, inhibition of lipoxygenase with BW755C or NDGA, or inhibition of cytochrome P450-dependent enzymes with NDGA, clotrimazole or 7-ethoxyresorufin were without effect on autoregulatory responses. |
| 89 | 1909958 | In vivo treatment with stannous chloride to deplete renal cytochrome P450-dependent enzymes also failed to modify autoregulatory responses. |
| 90 | 1909958 | Similarly, inhibition of lipoxygenase with BW755C or NDGA, or inhibition of cytochrome P450-dependent enzymes with NDGA, clotrimazole or 7-ethoxyresorufin were without effect on autoregulatory responses. |
| 91 | 1909958 | In vivo treatment with stannous chloride to deplete renal cytochrome P450-dependent enzymes also failed to modify autoregulatory responses. |
| 92 | 2005876 | In contrast, obesity had no significant effect on cytochrome b5 content, P450 reductase activity, benzphetamine demethylation, or erythromycin demethylation, with the latter two reactions being linked with rat IIC11 and IIIA1, respectively. |
| 93 | 2012352 | Toxicity was increased in the presence of an epoxide hydrolase inhibitor (17.5% +/- 0.3% dead cells) and abolished by an inhibitor of cytochrome P-450. |
| 94 | 2079689 | Studies on the enzymology of NDMA metabolism show that some Cytochrome P-450 isozymes exhibit significant NDMA-demethylase activity only at high NDMA concentrations. |
| 95 | 2093363 | H2-antagonists such as cimetidine and ranitidine are metabolized by cytochrome P-450. |
| 96 | 2105452 | The profile of hepatic microsomal cytochrome P450 expressed in the male and female rat was dramatically altered by streptozotocin-induced diabetes. |
| 97 | 2121801 | To determine whether Type II diabetes or glyburide affect hepatic drug metabolism, the authors used 13C-labeled aminopyrine and caffeine breath tests as in vivo probes of the hepatic cytochrome P450 and P(1)450 enzyme activities respectively in six subjects with Type II diabetes (4 women, 2 men). |
| 98 | 2165405 | Studies on induction of delta-aminolevulinic acid synthase, ferrochelatase, cytochrome P-450 and cyclic AMP by phenformin. |
| 99 | 2165405 | The present work demonstrates that phenformin exerted an inducing effect on delta-aminolevulinic acid synthase (ALA-S) and ferrochelatase activities and on cytochrome P-450 content in isolated hepatocytes from rats with experimental diabetes. |
| 100 | 2165405 | Similar results were obtained with respect to ALA-S activity and cytochrome P-450 content when chlorpropamide was used. |
| 101 | 2165405 | The inducing effect exerted by allylisopropylacetamide (AIA) on ALA-S and ferrochelatase activities in diabetic hepatic cells was markedly greater than that observed in normal hepatocytes. |
| 102 | 2165405 | When phenformin was added to isolated rat hepatocytes of normal rats, induction of ALA-S and ferrochelatase activities and cytochrome P-450 content was observed only in the presence of added dibutyryl cAMP. |
| 103 | 2165405 | Studies on induction of delta-aminolevulinic acid synthase, ferrochelatase, cytochrome P-450 and cyclic AMP by phenformin. |
| 104 | 2165405 | The present work demonstrates that phenformin exerted an inducing effect on delta-aminolevulinic acid synthase (ALA-S) and ferrochelatase activities and on cytochrome P-450 content in isolated hepatocytes from rats with experimental diabetes. |
| 105 | 2165405 | Similar results were obtained with respect to ALA-S activity and cytochrome P-450 content when chlorpropamide was used. |
| 106 | 2165405 | The inducing effect exerted by allylisopropylacetamide (AIA) on ALA-S and ferrochelatase activities in diabetic hepatic cells was markedly greater than that observed in normal hepatocytes. |
| 107 | 2165405 | When phenformin was added to isolated rat hepatocytes of normal rats, induction of ALA-S and ferrochelatase activities and cytochrome P-450 content was observed only in the presence of added dibutyryl cAMP. |
| 108 | 2165405 | Studies on induction of delta-aminolevulinic acid synthase, ferrochelatase, cytochrome P-450 and cyclic AMP by phenformin. |
| 109 | 2165405 | The present work demonstrates that phenformin exerted an inducing effect on delta-aminolevulinic acid synthase (ALA-S) and ferrochelatase activities and on cytochrome P-450 content in isolated hepatocytes from rats with experimental diabetes. |
| 110 | 2165405 | Similar results were obtained with respect to ALA-S activity and cytochrome P-450 content when chlorpropamide was used. |
| 111 | 2165405 | The inducing effect exerted by allylisopropylacetamide (AIA) on ALA-S and ferrochelatase activities in diabetic hepatic cells was markedly greater than that observed in normal hepatocytes. |
| 112 | 2165405 | When phenformin was added to isolated rat hepatocytes of normal rats, induction of ALA-S and ferrochelatase activities and cytochrome P-450 content was observed only in the presence of added dibutyryl cAMP. |
| 113 | 2165405 | Studies on induction of delta-aminolevulinic acid synthase, ferrochelatase, cytochrome P-450 and cyclic AMP by phenformin. |
| 114 | 2165405 | The present work demonstrates that phenformin exerted an inducing effect on delta-aminolevulinic acid synthase (ALA-S) and ferrochelatase activities and on cytochrome P-450 content in isolated hepatocytes from rats with experimental diabetes. |
| 115 | 2165405 | Similar results were obtained with respect to ALA-S activity and cytochrome P-450 content when chlorpropamide was used. |
| 116 | 2165405 | The inducing effect exerted by allylisopropylacetamide (AIA) on ALA-S and ferrochelatase activities in diabetic hepatic cells was markedly greater than that observed in normal hepatocytes. |
| 117 | 2165405 | When phenformin was added to isolated rat hepatocytes of normal rats, induction of ALA-S and ferrochelatase activities and cytochrome P-450 content was observed only in the presence of added dibutyryl cAMP. |
| 118 | 2168718 | In the present work we demonstrate that insulin decreases the phenobarbital-induced activities of delta-aminolevulinic acid synthase and ferrochelatase in isolated hepatocytes from normal and experimental-diabetic rats. |
| 119 | 2168718 | Under similar experimental conditions, insulin decreased the basal activities of delta-aminolevulinic acid synthase and ferrochelatase in hepatocytes from normal rats; no inhibitory effect was observed on the basal activity of delta-aminolevulinic acid synthase in hepatocytes from diabetic rats. |
| 120 | 2168718 | Cytochrome P-450 content of both normal and diabetic cells was not affected by insulin in absence or presence of phenobarbital. |
| 121 | 2205622 | Cytochrome P450IIE1, a member of the cytochrome P450 supergene family, was measured in peripheral lymphocytes of 14 patients with insulin-dependent diabetes mellitus who were in poor metabolic control, as evidenced by elevated hemoglobin A1 levels (mean, 11.9 +/- 2.8%; normal, less than 7.8). |
| 122 | 2256435 | In addition to increased glycosylation of hemoglobin, abnormalities of other heme proteins such as cytochrome P-450 might also occur in patients with insulin-dependent diabetes mellitus. |
| 123 | 2256435 | Antipyrine is a useful marker drug for cytochrome P-450 dependent hepatic drug metabolism. |
| 124 | 2256435 | In addition to increased glycosylation of hemoglobin, abnormalities of other heme proteins such as cytochrome P-450 might also occur in patients with insulin-dependent diabetes mellitus. |
| 125 | 2256435 | Antipyrine is a useful marker drug for cytochrome P-450 dependent hepatic drug metabolism. |
| 126 | 2392953 | The effect of alloxan-induced diabetes on the duration of hexobarbital sleep (HB sleep) the activity of ethylmorphine-N-demethylase (EMND), aniline hydroxylase (AH), the content of microsomal cytochrome P-450 and b5, on the activity of ethoxycumarine-0-deethylase (ECOD) and ethoxyresorufine-0-deethylase (EROD) after induction with beta naphthoflavone (beta-NF), as well as the activity of benzphetamine-N-demethylase and pentoxyresorufine-O-dealkylase (PROD) after induction with phenobarbital (PB), was studied in experiments on male Wistar rats. |
| 127 | 2501061 | The demand for NADPH in drug oxidation reactions, caused by the induction phenomenon, was reflected in the elevated activities of the NADPH producing enzymes in pentose phosphate pathway and in the activities of isocitrate dehydrogenase and malic enzyme from mitochondrial oxidation reactions. |
| 128 | 2501061 | Hepatic glucose production rate was related to plasma glucose, NADPH producing enzyme activities and cytochrome P450 content in the obese and lean mice. |
| 129 | 2521554 | Cytochrome P450 in livers of diabetic rats: regulation by growth hormone and insulin. |
| 130 | 2521554 | However, the treatment of hypophysectomized rats with insulin had no effect, and treatment of diabetic rats with growth hormone or a suppressing agent of somatostatin, cysteamine, showed trivial effects on P450-male and P450b. |
| 131 | 2559756 | In the present work we have been able to demonstrate the existence of some interrelationship between intracellular level of cAMP content and phenobarbital induction of delta-aminolevulinic acid synthase, ferrochelatase, and cytochrome P-450 biosynthesis in isolated rat hepatocytes. |
| 132 | 2586489 | The mechanism of the suppression of an ethanol-inducible cytochrome P-450 (P-450DM/j) by pituitary hormone has been studied in rats. |
| 133 | 2806076 | Physiological and pathophysiological alterations in rat hepatic cytochrome P-450. |
| 134 | 2818618 | Similarities and differences in the regulation of hepatic cytochrome P-450 enzymes by diabetes and fasting in male rats. |
| 135 | 2818618 | The effects of streptozotocin-induced diabetes and fasting on hepatic cytochrome P-450 enzymes in sexually mature male rats were studied by immunochemical techniques and enzyme assays. |
| 136 | 2818618 | In contrast, P-450 UT-A (a male specific form) decreased drastically from 295 pmol/mg in the control group to about 10% of this value in diabetic rats and to 50% in fasting rats. |
| 137 | 2818618 | Slight changes in cytochromes P-450 UT-F, P-450 UT-I and P-450 PB-C were also observed under these conditions, but the biological significance is not known. |
| 138 | 2818618 | These results suggest that different mechanisms exist for the regulation of the expression of cytochrome P-450 enzymes in diabetic and fasting rats. |
| 139 | 2818618 | Similarities and differences in the regulation of hepatic cytochrome P-450 enzymes by diabetes and fasting in male rats. |
| 140 | 2818618 | The effects of streptozotocin-induced diabetes and fasting on hepatic cytochrome P-450 enzymes in sexually mature male rats were studied by immunochemical techniques and enzyme assays. |
| 141 | 2818618 | In contrast, P-450 UT-A (a male specific form) decreased drastically from 295 pmol/mg in the control group to about 10% of this value in diabetic rats and to 50% in fasting rats. |
| 142 | 2818618 | Slight changes in cytochromes P-450 UT-F, P-450 UT-I and P-450 PB-C were also observed under these conditions, but the biological significance is not known. |
| 143 | 2818618 | These results suggest that different mechanisms exist for the regulation of the expression of cytochrome P-450 enzymes in diabetic and fasting rats. |
| 144 | 2818618 | Similarities and differences in the regulation of hepatic cytochrome P-450 enzymes by diabetes and fasting in male rats. |
| 145 | 2818618 | The effects of streptozotocin-induced diabetes and fasting on hepatic cytochrome P-450 enzymes in sexually mature male rats were studied by immunochemical techniques and enzyme assays. |
| 146 | 2818618 | In contrast, P-450 UT-A (a male specific form) decreased drastically from 295 pmol/mg in the control group to about 10% of this value in diabetic rats and to 50% in fasting rats. |
| 147 | 2818618 | Slight changes in cytochromes P-450 UT-F, P-450 UT-I and P-450 PB-C were also observed under these conditions, but the biological significance is not known. |
| 148 | 2818618 | These results suggest that different mechanisms exist for the regulation of the expression of cytochrome P-450 enzymes in diabetic and fasting rats. |
| 149 | 2818618 | Similarities and differences in the regulation of hepatic cytochrome P-450 enzymes by diabetes and fasting in male rats. |
| 150 | 2818618 | The effects of streptozotocin-induced diabetes and fasting on hepatic cytochrome P-450 enzymes in sexually mature male rats were studied by immunochemical techniques and enzyme assays. |
| 151 | 2818618 | In contrast, P-450 UT-A (a male specific form) decreased drastically from 295 pmol/mg in the control group to about 10% of this value in diabetic rats and to 50% in fasting rats. |
| 152 | 2818618 | Slight changes in cytochromes P-450 UT-F, P-450 UT-I and P-450 PB-C were also observed under these conditions, but the biological significance is not known. |
| 153 | 2818618 | These results suggest that different mechanisms exist for the regulation of the expression of cytochrome P-450 enzymes in diabetic and fasting rats. |
| 154 | 2818618 | Similarities and differences in the regulation of hepatic cytochrome P-450 enzymes by diabetes and fasting in male rats. |
| 155 | 2818618 | The effects of streptozotocin-induced diabetes and fasting on hepatic cytochrome P-450 enzymes in sexually mature male rats were studied by immunochemical techniques and enzyme assays. |
| 156 | 2818618 | In contrast, P-450 UT-A (a male specific form) decreased drastically from 295 pmol/mg in the control group to about 10% of this value in diabetic rats and to 50% in fasting rats. |
| 157 | 2818618 | Slight changes in cytochromes P-450 UT-F, P-450 UT-I and P-450 PB-C were also observed under these conditions, but the biological significance is not known. |
| 158 | 2818618 | These results suggest that different mechanisms exist for the regulation of the expression of cytochrome P-450 enzymes in diabetic and fasting rats. |
| 159 | 2888626 | The inhibition of imipramine metabolism by anti-cytochrome P-450 reductase antibodies led to the conclusion that cytochrome P-450-dependent monooxygenases are not involved in the N-oxidation of imipramine. |
| 160 | 2890479 | Total cytochrome P-450 concentrations were reduced in both STZ and WKY, whereas styrene oxide hydrolase and benzphetamine N-demethylase activities were normal in STZ and reduced in WKY. 3. |
| 161 | 2903001 | Cytochrome P-450 concentrations were similar in male and female carrier (db/+) and diabetic (db/db) mice. |
| 162 | 2943107 | The present study investigated the time course of the effect of STZ on hepatic drug metabolism, protein and cytochrome P-450 content and serum glucose and triglyceride concentration. |
| 163 | 2943107 | Liver protein was increased at 1 and 72 h but cytochrome P-450 was unaffected. |
| 164 | 2943107 | The present study investigated the time course of the effect of STZ on hepatic drug metabolism, protein and cytochrome P-450 content and serum glucose and triglyceride concentration. |
| 165 | 2943107 | Liver protein was increased at 1 and 72 h but cytochrome P-450 was unaffected. |
| 166 | 2958098 | Owing to the previously reported phosphorylation of a purified cytochrome P-450 isozyme, it is postulated that the cytochrome P-450 dependent aldrin epoxidase may be regulated by a glucagon induced phosphorylation process. |
| 167 | 2966085 | Composition changes in hepatic microsomal cytochrome P-450 during onset of streptozocin-induced diabetes and during insulin treatment. |
| 168 | 2966085 | The results suggest there are at least three types of responses by constituents of the cytochrome P-450 population to diabetes: no change in the microsomal content, a rapid increase when insulin level declines and restoration when insulin is supplied, and a rapid decline when insulin level declines and a restoration by insulin treatment. |
| 169 | 2966085 | Composition changes in hepatic microsomal cytochrome P-450 during onset of streptozocin-induced diabetes and during insulin treatment. |
| 170 | 2966085 | The results suggest there are at least three types of responses by constituents of the cytochrome P-450 population to diabetes: no change in the microsomal content, a rapid increase when insulin level declines and restoration when insulin is supplied, and a rapid decline when insulin level declines and a restoration by insulin treatment. |
| 171 | 2975197 | STZ-treated animals exhibited higher pentoxyresorufin O-dealkylase, ethoxy-resorufin O-deethylase, ethoxycoumarin O-deethylase, aniline p-hydroxylase and NADPH-cytochrome c reductase activities; similarly, increases were seen in cytochrome P-450 and b5 levels. |
| 172 | 2975197 | It is concluded that diabetes may modulate the metabolic activation of some chemical carcinogens, presumably by changing the ratio of the various cytochrome P-450 isoenzymes. |
| 173 | 2975197 | STZ-treated animals exhibited higher pentoxyresorufin O-dealkylase, ethoxy-resorufin O-deethylase, ethoxycoumarin O-deethylase, aniline p-hydroxylase and NADPH-cytochrome c reductase activities; similarly, increases were seen in cytochrome P-450 and b5 levels. |
| 174 | 2975197 | It is concluded that diabetes may modulate the metabolic activation of some chemical carcinogens, presumably by changing the ratio of the various cytochrome P-450 isoenzymes. |
| 175 | 2982381 | Spin state studies on cytochrome P-450 in liver microsomes from obese and diabetic animals. |
| 176 | 2982381 | The spin state of liver microsomal cytochrome P-450 from obese mice and streptozotocin-diabetic mice and rats has been studied both by the temperature and the type I substrates-induced spectral changes. |
| 177 | 2982381 | The high spin cytochrome P-450 is significantly decreased in these animals. |
| 178 | 2982381 | Moreover absolute spectra indicate that low spin cytochrome P-450 is stabilized in streptozotocin induced-diabetic animals. |
| 179 | 2982381 | Thus the physiopathological state may modify the in vivo spin state of cytochrome P-450 and modifications of the microsomal fatty acid composition might contribute to these changes. |
| 180 | 2982381 | Spin state studies on cytochrome P-450 in liver microsomes from obese and diabetic animals. |
| 181 | 2982381 | The spin state of liver microsomal cytochrome P-450 from obese mice and streptozotocin-diabetic mice and rats has been studied both by the temperature and the type I substrates-induced spectral changes. |
| 182 | 2982381 | The high spin cytochrome P-450 is significantly decreased in these animals. |
| 183 | 2982381 | Moreover absolute spectra indicate that low spin cytochrome P-450 is stabilized in streptozotocin induced-diabetic animals. |
| 184 | 2982381 | Thus the physiopathological state may modify the in vivo spin state of cytochrome P-450 and modifications of the microsomal fatty acid composition might contribute to these changes. |
| 185 | 2982381 | Spin state studies on cytochrome P-450 in liver microsomes from obese and diabetic animals. |
| 186 | 2982381 | The spin state of liver microsomal cytochrome P-450 from obese mice and streptozotocin-diabetic mice and rats has been studied both by the temperature and the type I substrates-induced spectral changes. |
| 187 | 2982381 | The high spin cytochrome P-450 is significantly decreased in these animals. |
| 188 | 2982381 | Moreover absolute spectra indicate that low spin cytochrome P-450 is stabilized in streptozotocin induced-diabetic animals. |
| 189 | 2982381 | Thus the physiopathological state may modify the in vivo spin state of cytochrome P-450 and modifications of the microsomal fatty acid composition might contribute to these changes. |
| 190 | 2982381 | Spin state studies on cytochrome P-450 in liver microsomes from obese and diabetic animals. |
| 191 | 2982381 | The spin state of liver microsomal cytochrome P-450 from obese mice and streptozotocin-diabetic mice and rats has been studied both by the temperature and the type I substrates-induced spectral changes. |
| 192 | 2982381 | The high spin cytochrome P-450 is significantly decreased in these animals. |
| 193 | 2982381 | Moreover absolute spectra indicate that low spin cytochrome P-450 is stabilized in streptozotocin induced-diabetic animals. |
| 194 | 2982381 | Thus the physiopathological state may modify the in vivo spin state of cytochrome P-450 and modifications of the microsomal fatty acid composition might contribute to these changes. |
| 195 | 2982381 | Spin state studies on cytochrome P-450 in liver microsomes from obese and diabetic animals. |
| 196 | 2982381 | The spin state of liver microsomal cytochrome P-450 from obese mice and streptozotocin-diabetic mice and rats has been studied both by the temperature and the type I substrates-induced spectral changes. |
| 197 | 2982381 | The high spin cytochrome P-450 is significantly decreased in these animals. |
| 198 | 2982381 | Moreover absolute spectra indicate that low spin cytochrome P-450 is stabilized in streptozotocin induced-diabetic animals. |
| 199 | 2982381 | Thus the physiopathological state may modify the in vivo spin state of cytochrome P-450 and modifications of the microsomal fatty acid composition might contribute to these changes. |
| 200 | 2998479 | Isolated hepatocytes from rats with experimental diabetes exhibit increased content of cytochrome P-450 and cyclic AMP and normal activities of the regulatory enzymes delta-aminolevulinic acid synthase and ferrochelatase. |
| 201 | 2998479 | The inducing effect exerted by phenobarbital on cytochrome P-450, delta-aminolevulinic acid synthase and ferrochelatase biosynthesis and cyclic AMP content in diabetic hepatic cells is markedly greater than that observed in normal hepatocytes. |
| 202 | 2998479 | Isolated hepatocytes from rats with experimental diabetes exhibit increased content of cytochrome P-450 and cyclic AMP and normal activities of the regulatory enzymes delta-aminolevulinic acid synthase and ferrochelatase. |
| 203 | 2998479 | The inducing effect exerted by phenobarbital on cytochrome P-450, delta-aminolevulinic acid synthase and ferrochelatase biosynthesis and cyclic AMP content in diabetic hepatic cells is markedly greater than that observed in normal hepatocytes. |
| 204 | 3040322 | The mixed function oxidase system was assayed by determination of the cytochrome P-450 content and NADPH cytochrome c reductase in liver. |
| 205 | 3040322 | Carbohydrate metabolism was evaluated by determining blood glucose, enzymes associated with glucose phosphorylation in the liver (glucokinase, hexokinase), glucose storage as glycogen and enzymatic delivery, glucose-6-phosphatase, and peripheral tissue by determining phosphorylating enzyme (hexokinase) and a key glycolytic enzyme (pyruvate kinase) and glycogen content in muscles. |
| 206 | 3041683 | These findings indicate that the amount of cytochrome P-450 isozyme involved in the oxidation of 3-methyl group may be regulated by insulin. 5. |
| 207 | 3048268 | Cytochrome P-450 alterations in the BB/Wor spontaneously diabetic rat. |
| 208 | 3048268 | The hepatic content of two individual cytochrome P-450 enzymes was analyzed in spontaneously diabetic (BB/Wor) male rats. |
| 209 | 3048268 | These results confirm that the changes in some individual forms of cytochrome P-450 after chemical (streptozotocin) induction of diabetes are also seen in the spontaneously diabetic animal. |
| 210 | 3048268 | The earlier observed alterations in cytochrome P-450 are therefore due to the state of diabetes and not to inductive or depressive effects of streptozotocin. |
| 211 | 3048268 | Cytochrome P-450 alterations in the BB/Wor spontaneously diabetic rat. |
| 212 | 3048268 | The hepatic content of two individual cytochrome P-450 enzymes was analyzed in spontaneously diabetic (BB/Wor) male rats. |
| 213 | 3048268 | These results confirm that the changes in some individual forms of cytochrome P-450 after chemical (streptozotocin) induction of diabetes are also seen in the spontaneously diabetic animal. |
| 214 | 3048268 | The earlier observed alterations in cytochrome P-450 are therefore due to the state of diabetes and not to inductive or depressive effects of streptozotocin. |
| 215 | 3048268 | Cytochrome P-450 alterations in the BB/Wor spontaneously diabetic rat. |
| 216 | 3048268 | The hepatic content of two individual cytochrome P-450 enzymes was analyzed in spontaneously diabetic (BB/Wor) male rats. |
| 217 | 3048268 | These results confirm that the changes in some individual forms of cytochrome P-450 after chemical (streptozotocin) induction of diabetes are also seen in the spontaneously diabetic animal. |
| 218 | 3048268 | The earlier observed alterations in cytochrome P-450 are therefore due to the state of diabetes and not to inductive or depressive effects of streptozotocin. |
| 219 | 3048268 | Cytochrome P-450 alterations in the BB/Wor spontaneously diabetic rat. |
| 220 | 3048268 | The hepatic content of two individual cytochrome P-450 enzymes was analyzed in spontaneously diabetic (BB/Wor) male rats. |
| 221 | 3048268 | These results confirm that the changes in some individual forms of cytochrome P-450 after chemical (streptozotocin) induction of diabetes are also seen in the spontaneously diabetic animal. |
| 222 | 3048268 | The earlier observed alterations in cytochrome P-450 are therefore due to the state of diabetes and not to inductive or depressive effects of streptozotocin. |
| 223 | 3113478 | The residual catalytic activity resistant to antibody inhibition may be a reflection of the inaccessibility of a certain amount of cytochrome P-450j due to interference by NADPH-cytochrome P-450 reductase based on results obtained with the reconstituted system. |
| 224 | 3124229 | The effect of diabetes on the activity of hepatic cholesterol 7 alpha-hydroxylase (CH-7 alpha) was studied in reconstituted systems using partially purified cytochrome P-450 (P-450) from control and diabetic rat livers. |
| 225 | 3141600 | Metabolic changes in lipids, ascorbic acid, and hepatic microsomal cytochrome P-450 by feeding polychlorinated biphenyls (PCB) were investigated in streptozotocin-induced diabetic rats. |
| 226 | 3141600 | Liver microsomal cytochrome P-450 and b5 were both increased by dietary PCB in group P. |
| 227 | 3141600 | Metabolic changes in lipids, ascorbic acid, and hepatic microsomal cytochrome P-450 by feeding polychlorinated biphenyls (PCB) were investigated in streptozotocin-induced diabetic rats. |
| 228 | 3141600 | Liver microsomal cytochrome P-450 and b5 were both increased by dietary PCB in group P. |
| 229 | 3300683 | Similar procedures were used to analyze the distribution of cytochrome P-450 molecules along intracellular membranes; however, special labeling techniques were necessary for this quantification in the electron microscope. |
| 230 | 3300683 | Immunoenzyme cytochemically stained secretions can also be studied morphometrically, and microdensitometry and microfluorometry can also be used to quantify immunocytochemical reactions, as is shown in the analysis of the intralobular distribution of NADPH-cytochrome P-450 reductase in the rat liver. |
| 231 | 3300683 | Similar procedures were used to analyze the distribution of cytochrome P-450 molecules along intracellular membranes; however, special labeling techniques were necessary for this quantification in the electron microscope. |
| 232 | 3300683 | Immunoenzyme cytochemically stained secretions can also be studied morphometrically, and microdensitometry and microfluorometry can also be used to quantify immunocytochemical reactions, as is shown in the analysis of the intralobular distribution of NADPH-cytochrome P-450 reductase in the rat liver. |
| 233 | 3308889 | Responses to insulin by two forms of rat hepatic microsomal cytochrome P-450 that undergo major (RLM6) and minor (RLM5b) elevations in diabetes. |
| 234 | 3308889 | Total cytochrome P-450 levels rise in diabetic rats. |
| 235 | 3308889 | Two specific forms of cytochrome P-450 that are elevated have been isolated from liver microsomes of streptozotocin-induced idabetic male rats. |
| 236 | 3308889 | One enzyme, termed RLM6, metabolizes aniline and acetol, but not testosterone, in a reconstituted system with NADPH-cytochrome P-450 reductase. |
| 237 | 3308889 | Polyclonal antibodies to RLM6 recognized most other forms of cytochrome P-450 in Western blots, but could be made monospecific by adsorption to cross-reacting proteins coupled to Sepharose 4B. |
| 238 | 3308889 | The other form of cytochrome P-450, RLM5b, does not metabolize aniline and only poorly metabolizes acetol and testosterone. |
| 239 | 3308889 | Responses to insulin by two forms of rat hepatic microsomal cytochrome P-450 that undergo major (RLM6) and minor (RLM5b) elevations in diabetes. |
| 240 | 3308889 | Total cytochrome P-450 levels rise in diabetic rats. |
| 241 | 3308889 | Two specific forms of cytochrome P-450 that are elevated have been isolated from liver microsomes of streptozotocin-induced idabetic male rats. |
| 242 | 3308889 | One enzyme, termed RLM6, metabolizes aniline and acetol, but not testosterone, in a reconstituted system with NADPH-cytochrome P-450 reductase. |
| 243 | 3308889 | Polyclonal antibodies to RLM6 recognized most other forms of cytochrome P-450 in Western blots, but could be made monospecific by adsorption to cross-reacting proteins coupled to Sepharose 4B. |
| 244 | 3308889 | The other form of cytochrome P-450, RLM5b, does not metabolize aniline and only poorly metabolizes acetol and testosterone. |
| 245 | 3308889 | Responses to insulin by two forms of rat hepatic microsomal cytochrome P-450 that undergo major (RLM6) and minor (RLM5b) elevations in diabetes. |
| 246 | 3308889 | Total cytochrome P-450 levels rise in diabetic rats. |
| 247 | 3308889 | Two specific forms of cytochrome P-450 that are elevated have been isolated from liver microsomes of streptozotocin-induced idabetic male rats. |
| 248 | 3308889 | One enzyme, termed RLM6, metabolizes aniline and acetol, but not testosterone, in a reconstituted system with NADPH-cytochrome P-450 reductase. |
| 249 | 3308889 | Polyclonal antibodies to RLM6 recognized most other forms of cytochrome P-450 in Western blots, but could be made monospecific by adsorption to cross-reacting proteins coupled to Sepharose 4B. |
| 250 | 3308889 | The other form of cytochrome P-450, RLM5b, does not metabolize aniline and only poorly metabolizes acetol and testosterone. |
| 251 | 3308889 | Responses to insulin by two forms of rat hepatic microsomal cytochrome P-450 that undergo major (RLM6) and minor (RLM5b) elevations in diabetes. |
| 252 | 3308889 | Total cytochrome P-450 levels rise in diabetic rats. |
| 253 | 3308889 | Two specific forms of cytochrome P-450 that are elevated have been isolated from liver microsomes of streptozotocin-induced idabetic male rats. |
| 254 | 3308889 | One enzyme, termed RLM6, metabolizes aniline and acetol, but not testosterone, in a reconstituted system with NADPH-cytochrome P-450 reductase. |
| 255 | 3308889 | Polyclonal antibodies to RLM6 recognized most other forms of cytochrome P-450 in Western blots, but could be made monospecific by adsorption to cross-reacting proteins coupled to Sepharose 4B. |
| 256 | 3308889 | The other form of cytochrome P-450, RLM5b, does not metabolize aniline and only poorly metabolizes acetol and testosterone. |
| 257 | 3308889 | Responses to insulin by two forms of rat hepatic microsomal cytochrome P-450 that undergo major (RLM6) and minor (RLM5b) elevations in diabetes. |
| 258 | 3308889 | Total cytochrome P-450 levels rise in diabetic rats. |
| 259 | 3308889 | Two specific forms of cytochrome P-450 that are elevated have been isolated from liver microsomes of streptozotocin-induced idabetic male rats. |
| 260 | 3308889 | One enzyme, termed RLM6, metabolizes aniline and acetol, but not testosterone, in a reconstituted system with NADPH-cytochrome P-450 reductase. |
| 261 | 3308889 | Polyclonal antibodies to RLM6 recognized most other forms of cytochrome P-450 in Western blots, but could be made monospecific by adsorption to cross-reacting proteins coupled to Sepharose 4B. |
| 262 | 3308889 | The other form of cytochrome P-450, RLM5b, does not metabolize aniline and only poorly metabolizes acetol and testosterone. |
| 263 | 3308889 | Responses to insulin by two forms of rat hepatic microsomal cytochrome P-450 that undergo major (RLM6) and minor (RLM5b) elevations in diabetes. |
| 264 | 3308889 | Total cytochrome P-450 levels rise in diabetic rats. |
| 265 | 3308889 | Two specific forms of cytochrome P-450 that are elevated have been isolated from liver microsomes of streptozotocin-induced idabetic male rats. |
| 266 | 3308889 | One enzyme, termed RLM6, metabolizes aniline and acetol, but not testosterone, in a reconstituted system with NADPH-cytochrome P-450 reductase. |
| 267 | 3308889 | Polyclonal antibodies to RLM6 recognized most other forms of cytochrome P-450 in Western blots, but could be made monospecific by adsorption to cross-reacting proteins coupled to Sepharose 4B. |
| 268 | 3308889 | The other form of cytochrome P-450, RLM5b, does not metabolize aniline and only poorly metabolizes acetol and testosterone. |
| 269 | 3311048 | The absence of any significant changes in cytochrome P-450 content after 1/2, 1 and 2 hr of insulin treatment indicates that the increase in steroid metabolizing enzyme activities is not due to an increase in de-novo enzyme synthesis. |
| 270 | 3358267 | Bromobenzene (500 microliters/kg, ip) elicited opposing responses in diabetic and normal rats in N-demethylase activity, in UDP-glucuronosyltransferase activity toward 1-naphthol, estrone, and testosterone, and in glutathione S-transferase activity toward 1-chloro-2,4-dinitrobenzene. |
| 271 | 3358267 | Total cytochrome P450 concentrations were reduced by both induction of diabetes and hepatotoxicant challenge. |
| 272 | 3365247 | Induction of renal cytochrome P-450 in hepatic microsomes of diabetic rats. |
| 273 | 3365247 | We purified two forms of cytochrome P-450 which was induced in hepatic microsomes of diabetic male rates treated with streptozotocin. |
| 274 | 3365247 | The other form, designated P450 DM-2, had a minimum molecular weight 53000 and a CO-reduced absorption maximum at 452 nm. |
| 275 | 3365247 | The P450 DM-2 efficiently catalyzed the omega- and (omega-1)-hydroxylation of lauric acid, but was not efficient in metabolizing aminopyrine, 7-ethoxycoumarin, aniline, N-nitrosodimethylamine, or testosterone. |
| 276 | 3365247 | The NH2-terminal sequence of P450 DM-2 was identical to that of P450 K-5, the major renal cytochrome P-450. |
| 277 | 3365247 | P450 DM-2 and P450 K-5 are closely related forms. |
| 278 | 3365247 | Induction of renal cytochrome P-450 in hepatic microsomes of diabetic rats. |
| 279 | 3365247 | We purified two forms of cytochrome P-450 which was induced in hepatic microsomes of diabetic male rates treated with streptozotocin. |
| 280 | 3365247 | The other form, designated P450 DM-2, had a minimum molecular weight 53000 and a CO-reduced absorption maximum at 452 nm. |
| 281 | 3365247 | The P450 DM-2 efficiently catalyzed the omega- and (omega-1)-hydroxylation of lauric acid, but was not efficient in metabolizing aminopyrine, 7-ethoxycoumarin, aniline, N-nitrosodimethylamine, or testosterone. |
| 282 | 3365247 | The NH2-terminal sequence of P450 DM-2 was identical to that of P450 K-5, the major renal cytochrome P-450. |
| 283 | 3365247 | P450 DM-2 and P450 K-5 are closely related forms. |
| 284 | 3365247 | Induction of renal cytochrome P-450 in hepatic microsomes of diabetic rats. |
| 285 | 3365247 | We purified two forms of cytochrome P-450 which was induced in hepatic microsomes of diabetic male rates treated with streptozotocin. |
| 286 | 3365247 | The other form, designated P450 DM-2, had a minimum molecular weight 53000 and a CO-reduced absorption maximum at 452 nm. |
| 287 | 3365247 | The P450 DM-2 efficiently catalyzed the omega- and (omega-1)-hydroxylation of lauric acid, but was not efficient in metabolizing aminopyrine, 7-ethoxycoumarin, aniline, N-nitrosodimethylamine, or testosterone. |
| 288 | 3365247 | The NH2-terminal sequence of P450 DM-2 was identical to that of P450 K-5, the major renal cytochrome P-450. |
| 289 | 3365247 | P450 DM-2 and P450 K-5 are closely related forms. |
| 290 | 3365247 | Induction of renal cytochrome P-450 in hepatic microsomes of diabetic rats. |
| 291 | 3365247 | We purified two forms of cytochrome P-450 which was induced in hepatic microsomes of diabetic male rates treated with streptozotocin. |
| 292 | 3365247 | The other form, designated P450 DM-2, had a minimum molecular weight 53000 and a CO-reduced absorption maximum at 452 nm. |
| 293 | 3365247 | The P450 DM-2 efficiently catalyzed the omega- and (omega-1)-hydroxylation of lauric acid, but was not efficient in metabolizing aminopyrine, 7-ethoxycoumarin, aniline, N-nitrosodimethylamine, or testosterone. |
| 294 | 3365247 | The NH2-terminal sequence of P450 DM-2 was identical to that of P450 K-5, the major renal cytochrome P-450. |
| 295 | 3365247 | P450 DM-2 and P450 K-5 are closely related forms. |
| 296 | 3365247 | Induction of renal cytochrome P-450 in hepatic microsomes of diabetic rats. |
| 297 | 3365247 | We purified two forms of cytochrome P-450 which was induced in hepatic microsomes of diabetic male rates treated with streptozotocin. |
| 298 | 3365247 | The other form, designated P450 DM-2, had a minimum molecular weight 53000 and a CO-reduced absorption maximum at 452 nm. |
| 299 | 3365247 | The P450 DM-2 efficiently catalyzed the omega- and (omega-1)-hydroxylation of lauric acid, but was not efficient in metabolizing aminopyrine, 7-ethoxycoumarin, aniline, N-nitrosodimethylamine, or testosterone. |
| 300 | 3365247 | The NH2-terminal sequence of P450 DM-2 was identical to that of P450 K-5, the major renal cytochrome P-450. |
| 301 | 3365247 | P450 DM-2 and P450 K-5 are closely related forms. |
| 302 | 3365247 | Induction of renal cytochrome P-450 in hepatic microsomes of diabetic rats. |
| 303 | 3365247 | We purified two forms of cytochrome P-450 which was induced in hepatic microsomes of diabetic male rates treated with streptozotocin. |
| 304 | 3365247 | The other form, designated P450 DM-2, had a minimum molecular weight 53000 and a CO-reduced absorption maximum at 452 nm. |
| 305 | 3365247 | The P450 DM-2 efficiently catalyzed the omega- and (omega-1)-hydroxylation of lauric acid, but was not efficient in metabolizing aminopyrine, 7-ethoxycoumarin, aniline, N-nitrosodimethylamine, or testosterone. |
| 306 | 3365247 | The NH2-terminal sequence of P450 DM-2 was identical to that of P450 K-5, the major renal cytochrome P-450. |
| 307 | 3365247 | P450 DM-2 and P450 K-5 are closely related forms. |
| 308 | 3382419 | Purification and characterization of diabetes-inducible cytochrome P-450. |
| 309 | 3382419 | A diabetes-inducible form of cytochrome P-450, termed P-450DM, was purified to electrophoretical homogeneity (MW 51,000) by high-performance liquid chromatography from liver microsomes of diabetic rats induced with streptozotocin. |
| 310 | 3382419 | Purification and characterization of diabetes-inducible cytochrome P-450. |
| 311 | 3382419 | A diabetes-inducible form of cytochrome P-450, termed P-450DM, was purified to electrophoretical homogeneity (MW 51,000) by high-performance liquid chromatography from liver microsomes of diabetic rats induced with streptozotocin. |
| 312 | 3386237 | Mitochondrial cytochrome P-450 concentrations were not affected by diabetes but steroid 11 beta-hydroxylase activity was greater in the diabetics than in controls after both 1 and 2 months. |
| 313 | 3386237 | Microsomal cytochrome P-450 concentrations were unaffected by diabetes but 21-hydroxylase activity was significantly lower in adrenal microsomes from diabetics than from controls. |
| 314 | 3386237 | Mitochondrial cytochrome P-450 concentrations were not affected by diabetes but steroid 11 beta-hydroxylase activity was greater in the diabetics than in controls after both 1 and 2 months. |
| 315 | 3386237 | Microsomal cytochrome P-450 concentrations were unaffected by diabetes but 21-hydroxylase activity was significantly lower in adrenal microsomes from diabetics than from controls. |
| 316 | 3548715 | Decrease in the levels of a constitutive cytochrome P-450 (RLM5) in hepatic microsomes of diabetic rats. |
| 317 | 3548715 | Cytochrome P-450 dependent hydroxylation of testosterone has been measured in hepatic microsomes of control, diabetic and insulin-treated diabetic rats. |
| 318 | 3548715 | These results provide evidence that specific constitutive cytochrome P-450 enzymes are altered in the diabetic state and that these changes are not permanent since they can be overcome, at least partially, by insulin replacement therapy. |
| 319 | 3548715 | Decrease in the levels of a constitutive cytochrome P-450 (RLM5) in hepatic microsomes of diabetic rats. |
| 320 | 3548715 | Cytochrome P-450 dependent hydroxylation of testosterone has been measured in hepatic microsomes of control, diabetic and insulin-treated diabetic rats. |
| 321 | 3548715 | These results provide evidence that specific constitutive cytochrome P-450 enzymes are altered in the diabetic state and that these changes are not permanent since they can be overcome, at least partially, by insulin replacement therapy. |
| 322 | 3548715 | Decrease in the levels of a constitutive cytochrome P-450 (RLM5) in hepatic microsomes of diabetic rats. |
| 323 | 3548715 | Cytochrome P-450 dependent hydroxylation of testosterone has been measured in hepatic microsomes of control, diabetic and insulin-treated diabetic rats. |
| 324 | 3548715 | These results provide evidence that specific constitutive cytochrome P-450 enzymes are altered in the diabetic state and that these changes are not permanent since they can be overcome, at least partially, by insulin replacement therapy. |
| 325 | 3770136 | Immunoquantitation of some cytochrome P-450 isozymes in liver microsomes from streptozotocin-diabetic rats. |
| 326 | 3770136 | Streptozotocin-diabetes in rats leads to a decrease of cytochrome P-450 UT-A (the major form in control rats) and an increase of cytochrome P-450 PB-B (the major one induced by phenobarbital treatment) in liver microsomes. |
| 327 | 3770136 | The increased benzphetamine-N-demethylase activity can be related to the induction of cytochrome P-450 PB-B. |
| 328 | 3770136 | Immunoquantitation of some cytochrome P-450 isozymes in liver microsomes from streptozotocin-diabetic rats. |
| 329 | 3770136 | Streptozotocin-diabetes in rats leads to a decrease of cytochrome P-450 UT-A (the major form in control rats) and an increase of cytochrome P-450 PB-B (the major one induced by phenobarbital treatment) in liver microsomes. |
| 330 | 3770136 | The increased benzphetamine-N-demethylase activity can be related to the induction of cytochrome P-450 PB-B. |
| 331 | 3770136 | Immunoquantitation of some cytochrome P-450 isozymes in liver microsomes from streptozotocin-diabetic rats. |
| 332 | 3770136 | Streptozotocin-diabetes in rats leads to a decrease of cytochrome P-450 UT-A (the major form in control rats) and an increase of cytochrome P-450 PB-B (the major one induced by phenobarbital treatment) in liver microsomes. |
| 333 | 3770136 | The increased benzphetamine-N-demethylase activity can be related to the induction of cytochrome P-450 PB-B. |
| 334 | 3896629 | The sodium dodecylsulfate electrophoretic profile of liver microsomal proteins from each group of rats exhibited distinct increases as well as decreases in the cytochrome P-450 region. |
| 335 | 3896629 | Stimulation of testosterone metabolism by insulin may be associated with a higher synthesis of certain cytochrome P-450 isozymes. |
| 336 | 3896629 | The sodium dodecylsulfate electrophoretic profile of liver microsomal proteins from each group of rats exhibited distinct increases as well as decreases in the cytochrome P-450 region. |
| 337 | 3896629 | Stimulation of testosterone metabolism by insulin may be associated with a higher synthesis of certain cytochrome P-450 isozymes. |
| 338 | 4002660 | Alloxan diabetes was accompanied by an increase in ascorbate-NADPH-dependent lipid peroxidation with a simultaneous decrease in content of cytochrome P-450 and in the rate aniline hydroxylation in rat liver microsomal fraction. |
| 339 | 4002660 | Activation of lipid peroxidation, which led to impairment of the endoplasmic reticulum integrity as well as to destruction of cytochrome P-450, may be important in pathogenesis of alloxan diabetes. |
| 340 | 4002660 | Alloxan diabetes was accompanied by an increase in ascorbate-NADPH-dependent lipid peroxidation with a simultaneous decrease in content of cytochrome P-450 and in the rate aniline hydroxylation in rat liver microsomal fraction. |
| 341 | 4002660 | Activation of lipid peroxidation, which led to impairment of the endoplasmic reticulum integrity as well as to destruction of cytochrome P-450, may be important in pathogenesis of alloxan diabetes. |
| 342 | 4025003 | The major lipid predictors of coronary events, plasma high density lipoprotein cholesterol (HDL-C) and the HDL-C/total cholesterol (T-C) ratio, and blood glucose (BG) in 12 subjects with non-insulin-dependent diabetes mellitus were related to hepatic lipids, proteins and microsomal enzyme activity assessed by liver cytochrome P-450 (P-450). |
| 343 | 4025003 | Non-insulin-dependent diabetics had low HDL-C/T-C ratio, liver phospholipid (PL) and P-450 and high serum and liver triglyceride (TG) concentrations. |
| 344 | 4025003 | The major lipid predictors of coronary events, plasma high density lipoprotein cholesterol (HDL-C) and the HDL-C/total cholesterol (T-C) ratio, and blood glucose (BG) in 12 subjects with non-insulin-dependent diabetes mellitus were related to hepatic lipids, proteins and microsomal enzyme activity assessed by liver cytochrome P-450 (P-450). |
| 345 | 4025003 | Non-insulin-dependent diabetics had low HDL-C/T-C ratio, liver phospholipid (PL) and P-450 and high serum and liver triglyceride (TG) concentrations. |
| 346 | 4027353 | The effect of different hyperglucagonemic states on monooxygenase activities and isozymic pattern of cytochrome P-450 in mouse. |
| 347 | 4027353 | By conjunction of monooxygenase assays and immunoquantitation of specific isozymes of cytochrome P-450, the actual inducing ability of glucagon has been shown and it might explain some of the modifications of the drug metabolizing system in diabetic mice. |
| 348 | 4027353 | The isozymic pattern of cytochrome P-450 of liver microsomes from diabetic mice appears very different from that produced by classical inducers. |
| 349 | 4027353 | The effect of different hyperglucagonemic states on monooxygenase activities and isozymic pattern of cytochrome P-450 in mouse. |
| 350 | 4027353 | By conjunction of monooxygenase assays and immunoquantitation of specific isozymes of cytochrome P-450, the actual inducing ability of glucagon has been shown and it might explain some of the modifications of the drug metabolizing system in diabetic mice. |
| 351 | 4027353 | The isozymic pattern of cytochrome P-450 of liver microsomes from diabetic mice appears very different from that produced by classical inducers. |
| 352 | 4027353 | The effect of different hyperglucagonemic states on monooxygenase activities and isozymic pattern of cytochrome P-450 in mouse. |
| 353 | 4027353 | By conjunction of monooxygenase assays and immunoquantitation of specific isozymes of cytochrome P-450, the actual inducing ability of glucagon has been shown and it might explain some of the modifications of the drug metabolizing system in diabetic mice. |
| 354 | 4027353 | The isozymic pattern of cytochrome P-450 of liver microsomes from diabetic mice appears very different from that produced by classical inducers. |
| 355 | 5150143 | Effect of adrenalectomy or alloxan diabetes on the substrate interaction with cytochrome P-450 in the oxidation of drugs by liver microsomes. |
| 356 | 5312937 | The substrate interaction with cytochrome P-450 in drug oxidation. |
| 357 | 6109605 | Cytochrome P-450 content was increased in hepatocytes and microsomes of these animals. |
| 358 | 6109605 | Treatment of diabetic male rats with insulin returned drug disposition and cytochrome P-450 in hepatocytes to control levels. |
| 359 | 6109605 | In females, production of oxidized metabolites in hepatocytes as well as mono-oxygenase activities in microsomes were increased by diabetes, whereas cytochrome P-450 levels were not significantly altered in hepatocytes or microsomes. |
| 360 | 6109605 | Cytochrome P-450 content was increased in hepatocytes and microsomes of these animals. |
| 361 | 6109605 | Treatment of diabetic male rats with insulin returned drug disposition and cytochrome P-450 in hepatocytes to control levels. |
| 362 | 6109605 | In females, production of oxidized metabolites in hepatocytes as well as mono-oxygenase activities in microsomes were increased by diabetes, whereas cytochrome P-450 levels were not significantly altered in hepatocytes or microsomes. |
| 363 | 6109605 | Cytochrome P-450 content was increased in hepatocytes and microsomes of these animals. |
| 364 | 6109605 | Treatment of diabetic male rats with insulin returned drug disposition and cytochrome P-450 in hepatocytes to control levels. |
| 365 | 6109605 | In females, production of oxidized metabolites in hepatocytes as well as mono-oxygenase activities in microsomes were increased by diabetes, whereas cytochrome P-450 levels were not significantly altered in hepatocytes or microsomes. |
| 366 | 6201195 | Study of benzphetamine-N-demethylase in streptozotocin-diabetic mice and rats: evidence for the induction of catalytically and immunologically specific forms of cytochrome P450. |
| 367 | 6201195 | Phenobarbital treatment and streptozotocin-diabetes both increase, in mouse and rat microsomes, a benzphetamine-N-demethylase activity which can be inhibited by a specific antibody raised against purified rat phenobarbital-induced cytochrome P-450. |
| 368 | 6201195 | However, similar studies performed on cytochrome P-450 A and B fractions separated by DEAE-cellulose chromatography, clearly proved that streptozotocin-diabetes promotes in mice the synthesis of two new species of cytochrome P-450 and that the streptozotocin diabetes-induced forms are different in mouse and rat. |
| 369 | 6201195 | Study of benzphetamine-N-demethylase in streptozotocin-diabetic mice and rats: evidence for the induction of catalytically and immunologically specific forms of cytochrome P450. |
| 370 | 6201195 | Phenobarbital treatment and streptozotocin-diabetes both increase, in mouse and rat microsomes, a benzphetamine-N-demethylase activity which can be inhibited by a specific antibody raised against purified rat phenobarbital-induced cytochrome P-450. |
| 371 | 6201195 | However, similar studies performed on cytochrome P-450 A and B fractions separated by DEAE-cellulose chromatography, clearly proved that streptozotocin-diabetes promotes in mice the synthesis of two new species of cytochrome P-450 and that the streptozotocin diabetes-induced forms are different in mouse and rat. |
| 372 | 6201195 | Study of benzphetamine-N-demethylase in streptozotocin-diabetic mice and rats: evidence for the induction of catalytically and immunologically specific forms of cytochrome P450. |
| 373 | 6201195 | Phenobarbital treatment and streptozotocin-diabetes both increase, in mouse and rat microsomes, a benzphetamine-N-demethylase activity which can be inhibited by a specific antibody raised against purified rat phenobarbital-induced cytochrome P-450. |
| 374 | 6201195 | However, similar studies performed on cytochrome P-450 A and B fractions separated by DEAE-cellulose chromatography, clearly proved that streptozotocin-diabetes promotes in mice the synthesis of two new species of cytochrome P-450 and that the streptozotocin diabetes-induced forms are different in mouse and rat. |
| 375 | 6217856 | This azoreductase activity was inhibited by cyanide and cytochrome b5 antibody, but was resistant to carbon monoxide and SKF-525A (beta-diethylaminoethyl-diphenylpropylacetate). 2. |
| 376 | 6217856 | Azoreductase activity, NADPH-cytochrome P-450 reductase, cytochromes P-450 and b5 were measured in liver microsomes prepared from fasted animals and from animals treated with 20-methylcholanthrene, phenobarbital, streptozotocin or 3-aminotriazole plus allyl-isopropylacetamide. |
| 377 | 6217856 | No direct correlation could be established between the variations of azoreductase activity and those of cytochromes P-450 and b5, and of NADPH-cytochrome P-450 reductase in these experimental situations. |
| 378 | 6217856 | This azoreductase activity was inhibited by cyanide and cytochrome b5 antibody, but was resistant to carbon monoxide and SKF-525A (beta-diethylaminoethyl-diphenylpropylacetate). 2. |
| 379 | 6217856 | Azoreductase activity, NADPH-cytochrome P-450 reductase, cytochromes P-450 and b5 were measured in liver microsomes prepared from fasted animals and from animals treated with 20-methylcholanthrene, phenobarbital, streptozotocin or 3-aminotriazole plus allyl-isopropylacetamide. |
| 380 | 6217856 | No direct correlation could be established between the variations of azoreductase activity and those of cytochromes P-450 and b5, and of NADPH-cytochrome P-450 reductase in these experimental situations. |
| 381 | 6305526 | The result suggest that diabetes causes an alteration of the composition of cytochrome P-450 isozymes; the forms efficient in metabolizing NDMA are increased while certain other forms of cytochrome P-450 are decreased. |
| 382 | 6347206 | From electrophoresis of hepatic microsomal proteins we determined that spontaneous diabetes of short duration does alter the protein distribution in the cytochrome P-450 region. |
| 383 | 6365718 | The associations between liver histological changes and hepatic cytochrome P-450 content (P-450) and the activities of aryl hydrocarbon hydroxylase (AHH) and 7-ethoxycoumarin O-de-ethylase (ECD) have been investigated in 30 diabetics undergoing diagnostic liver biopsy. |
| 384 | 6365718 | There were more than 10-fold interindividual variations in P-450 contents and AHH and ECD activities in the diabetics. |
| 385 | 6365718 | P-450 content decreased with increasing severity of liver histological changes, whereas AHH and ECD activities were significantly reduced only in biopsies with severe histological changes. |
| 386 | 6365718 | However, despite differential effects of liver disorders on P-450 and AHH and ECD activities there were highly significant correlations between these three parameters with each other. |
| 387 | 6365718 | The associations between liver histological changes and hepatic cytochrome P-450 content (P-450) and the activities of aryl hydrocarbon hydroxylase (AHH) and 7-ethoxycoumarin O-de-ethylase (ECD) have been investigated in 30 diabetics undergoing diagnostic liver biopsy. |
| 388 | 6365718 | There were more than 10-fold interindividual variations in P-450 contents and AHH and ECD activities in the diabetics. |
| 389 | 6365718 | P-450 content decreased with increasing severity of liver histological changes, whereas AHH and ECD activities were significantly reduced only in biopsies with severe histological changes. |
| 390 | 6365718 | However, despite differential effects of liver disorders on P-450 and AHH and ECD activities there were highly significant correlations between these three parameters with each other. |
| 391 | 6365718 | The associations between liver histological changes and hepatic cytochrome P-450 content (P-450) and the activities of aryl hydrocarbon hydroxylase (AHH) and 7-ethoxycoumarin O-de-ethylase (ECD) have been investigated in 30 diabetics undergoing diagnostic liver biopsy. |
| 392 | 6365718 | There were more than 10-fold interindividual variations in P-450 contents and AHH and ECD activities in the diabetics. |
| 393 | 6365718 | P-450 content decreased with increasing severity of liver histological changes, whereas AHH and ECD activities were significantly reduced only in biopsies with severe histological changes. |
| 394 | 6365718 | However, despite differential effects of liver disorders on P-450 and AHH and ECD activities there were highly significant correlations between these three parameters with each other. |
| 395 | 6365718 | The associations between liver histological changes and hepatic cytochrome P-450 content (P-450) and the activities of aryl hydrocarbon hydroxylase (AHH) and 7-ethoxycoumarin O-de-ethylase (ECD) have been investigated in 30 diabetics undergoing diagnostic liver biopsy. |
| 396 | 6365718 | There were more than 10-fold interindividual variations in P-450 contents and AHH and ECD activities in the diabetics. |
| 397 | 6365718 | P-450 content decreased with increasing severity of liver histological changes, whereas AHH and ECD activities were significantly reduced only in biopsies with severe histological changes. |
| 398 | 6365718 | However, despite differential effects of liver disorders on P-450 and AHH and ECD activities there were highly significant correlations between these three parameters with each other. |
| 399 | 6379147 | Hepatic microsomal cytochrome P-450 content and drug metabolizing activity in obese, diabetic C57BL/KsJ mice homozygous for the diabetes gene mutation (db/db) have been compared with levels found in livers of 1) lean, nondiabetic control mice with the same C57BL/KsJ genetic background and 2) lean C57BL/6J animals made diabetic by streptozotocin treatment. |
| 400 | 6379147 | No changes in specific enzyme content or activity were seen in young db/db mice, but microsomal protein and total hepatic cytochrome P-450 content and meperidine demethylation and pentobarbital hydroxylation activity were markedly increased compared to controls. |
| 401 | 6379147 | In hyperglycemic, hypoinsulinemic mice with streptozotocin-induced diabetes mellitus, the amount of microsomal protein did not change, but hepatic cytochrome P-450 content and enzyme activity were significantly increased whether expressed per milligram of microsomal protein or as totals per liver. |
| 402 | 6379147 | These differences in hepatic microsomal enzymes between hyperinsulinemic and hypoinsulinemic mice with diabetes mellitus suggest that both hyperglycemia and insulin separately and significantly influence cytochrome P-450 turnover and mixed function oxidase activity. |
| 403 | 6379147 | Hepatic microsomal cytochrome P-450 content and drug metabolizing activity in obese, diabetic C57BL/KsJ mice homozygous for the diabetes gene mutation (db/db) have been compared with levels found in livers of 1) lean, nondiabetic control mice with the same C57BL/KsJ genetic background and 2) lean C57BL/6J animals made diabetic by streptozotocin treatment. |
| 404 | 6379147 | No changes in specific enzyme content or activity were seen in young db/db mice, but microsomal protein and total hepatic cytochrome P-450 content and meperidine demethylation and pentobarbital hydroxylation activity were markedly increased compared to controls. |
| 405 | 6379147 | In hyperglycemic, hypoinsulinemic mice with streptozotocin-induced diabetes mellitus, the amount of microsomal protein did not change, but hepatic cytochrome P-450 content and enzyme activity were significantly increased whether expressed per milligram of microsomal protein or as totals per liver. |
| 406 | 6379147 | These differences in hepatic microsomal enzymes between hyperinsulinemic and hypoinsulinemic mice with diabetes mellitus suggest that both hyperglycemia and insulin separately and significantly influence cytochrome P-450 turnover and mixed function oxidase activity. |
| 407 | 6379147 | Hepatic microsomal cytochrome P-450 content and drug metabolizing activity in obese, diabetic C57BL/KsJ mice homozygous for the diabetes gene mutation (db/db) have been compared with levels found in livers of 1) lean, nondiabetic control mice with the same C57BL/KsJ genetic background and 2) lean C57BL/6J animals made diabetic by streptozotocin treatment. |
| 408 | 6379147 | No changes in specific enzyme content or activity were seen in young db/db mice, but microsomal protein and total hepatic cytochrome P-450 content and meperidine demethylation and pentobarbital hydroxylation activity were markedly increased compared to controls. |
| 409 | 6379147 | In hyperglycemic, hypoinsulinemic mice with streptozotocin-induced diabetes mellitus, the amount of microsomal protein did not change, but hepatic cytochrome P-450 content and enzyme activity were significantly increased whether expressed per milligram of microsomal protein or as totals per liver. |
| 410 | 6379147 | These differences in hepatic microsomal enzymes between hyperinsulinemic and hypoinsulinemic mice with diabetes mellitus suggest that both hyperglycemia and insulin separately and significantly influence cytochrome P-450 turnover and mixed function oxidase activity. |
| 411 | 6379147 | Hepatic microsomal cytochrome P-450 content and drug metabolizing activity in obese, diabetic C57BL/KsJ mice homozygous for the diabetes gene mutation (db/db) have been compared with levels found in livers of 1) lean, nondiabetic control mice with the same C57BL/KsJ genetic background and 2) lean C57BL/6J animals made diabetic by streptozotocin treatment. |
| 412 | 6379147 | No changes in specific enzyme content or activity were seen in young db/db mice, but microsomal protein and total hepatic cytochrome P-450 content and meperidine demethylation and pentobarbital hydroxylation activity were markedly increased compared to controls. |
| 413 | 6379147 | In hyperglycemic, hypoinsulinemic mice with streptozotocin-induced diabetes mellitus, the amount of microsomal protein did not change, but hepatic cytochrome P-450 content and enzyme activity were significantly increased whether expressed per milligram of microsomal protein or as totals per liver. |
| 414 | 6379147 | These differences in hepatic microsomal enzymes between hyperinsulinemic and hypoinsulinemic mice with diabetes mellitus suggest that both hyperglycemia and insulin separately and significantly influence cytochrome P-450 turnover and mixed function oxidase activity. |
| 415 | 6414061 | Catalytic activities of cytochrome P-450 from female rat liver: correlation with sex differences in drug metabolism in diabetic liver. |
| 416 | 6414061 | Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of detergent solubilized cytochrome P-450 fractions from normal and diabetic female rat liver microsomes revealed the induction of a 52,000 molecular weight microsomal hemeprotein in diabetic liver. |
| 417 | 6414061 | Catalytic activities of cytochrome P-450 from female rat liver: correlation with sex differences in drug metabolism in diabetic liver. |
| 418 | 6414061 | Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of detergent solubilized cytochrome P-450 fractions from normal and diabetic female rat liver microsomes revealed the induction of a 52,000 molecular weight microsomal hemeprotein in diabetic liver. |
| 419 | 6529530 | The effect of fatty degeneration of liver parenchyma on drug metabolism was investigated in 21 obese non-insulin-dependent diabetic subjects by measuring plasma antipyrine kinetics, hepatic cytochrome P-450, liver size and the extent of fatty infiltration. |
| 420 | 6529530 | The hepatic drug metabolising capacity, as measured by total antipyrine clearance and the estimated total amount of cytochrome P-450, was at the same level as in non-diabetic control subjects with normal livers. |
| 421 | 6529530 | Relative antipyrine clearance (per unit weight of liver) and cytochrome P-450 concentrations were significantly lower in the diabetics than in controls. |
| 422 | 6529530 | The effect of fatty degeneration of liver parenchyma on drug metabolism was investigated in 21 obese non-insulin-dependent diabetic subjects by measuring plasma antipyrine kinetics, hepatic cytochrome P-450, liver size and the extent of fatty infiltration. |
| 423 | 6529530 | The hepatic drug metabolising capacity, as measured by total antipyrine clearance and the estimated total amount of cytochrome P-450, was at the same level as in non-diabetic control subjects with normal livers. |
| 424 | 6529530 | Relative antipyrine clearance (per unit weight of liver) and cytochrome P-450 concentrations were significantly lower in the diabetics than in controls. |
| 425 | 6529530 | The effect of fatty degeneration of liver parenchyma on drug metabolism was investigated in 21 obese non-insulin-dependent diabetic subjects by measuring plasma antipyrine kinetics, hepatic cytochrome P-450, liver size and the extent of fatty infiltration. |
| 426 | 6529530 | The hepatic drug metabolising capacity, as measured by total antipyrine clearance and the estimated total amount of cytochrome P-450, was at the same level as in non-diabetic control subjects with normal livers. |
| 427 | 6529530 | Relative antipyrine clearance (per unit weight of liver) and cytochrome P-450 concentrations were significantly lower in the diabetics than in controls. |
| 428 | 6606590 | The basal levels of the key enzymes involved in heme synthesis, ALA-S and ALA-dehydratase (ALA-D), were decreased about 36% and 54%, respectively, 44-46 days after diabetes induction. |
| 429 | 6606590 | The activity of benzo(a)pyrene hydroxylase in diabetic rats was also increased in proportion to the microsomal content of cytochrome P-450. |
| 430 | 6606590 | However, a similar stimulatory response in ALA-S activity to CoCl2 administration was observed only in control or insulin-treated diabetic rats. |
| 431 | 6617929 | The relationship between blood lactate levels, liver histology and microsomal enzyme activity (cytochrome P-450 content) was assessed in 32 non-insulin-dependent diabetics (NIDD) undergoing diagnostic liver biopsy. |
| 432 | 6617929 | P-450 was significantly correlated with lactate (rs -0.79), pyruvate (rs -0.65) and serum insulin (rs -0.53). |
| 433 | 6617929 | The relationship between blood lactate levels, liver histology and microsomal enzyme activity (cytochrome P-450 content) was assessed in 32 non-insulin-dependent diabetics (NIDD) undergoing diagnostic liver biopsy. |
| 434 | 6617929 | P-450 was significantly correlated with lactate (rs -0.79), pyruvate (rs -0.65) and serum insulin (rs -0.53). |
| 435 | 6651874 | The in vitro enzymatic activities associated with cytochrome P-450-dependent metabolism and glutathione S-transferase conjugation activity were markedly altered in hyperthyroid rats. |
| 436 | 6651874 | Cytochrome P-450 levels, aminopyrine N-demethylase activity, glutathione levels and glutathione S-transferase activity were all significantly lower in hyperthyroid rats. |
| 437 | 6651874 | Maximal changes in both the cytochrome P-450 system and in the glutathione detoxification system were required before halothane demonstrated its hepatotoxic effects. |
| 438 | 6651874 | The in vitro enzymatic activities associated with cytochrome P-450-dependent metabolism and glutathione S-transferase conjugation activity were markedly altered in hyperthyroid rats. |
| 439 | 6651874 | Cytochrome P-450 levels, aminopyrine N-demethylase activity, glutathione levels and glutathione S-transferase activity were all significantly lower in hyperthyroid rats. |
| 440 | 6651874 | Maximal changes in both the cytochrome P-450 system and in the glutathione detoxification system were required before halothane demonstrated its hepatotoxic effects. |
| 441 | 6688350 | Microsomal content of heme and cytochrome P-450, and the activities of tryptophan pyrrolase and the drug-metabolizing enzymes benzo[a]pyrene (BP) hydroxylase and aniline hydroxylase, were increased in the livers of diabetic rats. |
| 442 | 6688350 | Cobalt chloride produced a marked increase in MHO with a concomitant decrease in microsomal content of cytochrome P-450 and its associated BP hydroxylase activity in normal as well as chronically diabetic rats. |
| 443 | 6688350 | Microsomal content of heme and cytochrome P-450, and the activities of tryptophan pyrrolase and the drug-metabolizing enzymes benzo[a]pyrene (BP) hydroxylase and aniline hydroxylase, were increased in the livers of diabetic rats. |
| 444 | 6688350 | Cobalt chloride produced a marked increase in MHO with a concomitant decrease in microsomal content of cytochrome P-450 and its associated BP hydroxylase activity in normal as well as chronically diabetic rats. |
| 445 | 6703708 | Several lines of observations suggest that this is due to the induction of specific cytochrome P-450 isozymes. |
| 446 | 6752493 | Absorbed organotin compounds rapidly undergo dealkylation by the microsomal mono-oxygenase system dependent on cytochrome P-450 in the liver, brain or other organs, and the compounds and their metabolites distribute to the whole body, ultimately being excreted into urine, bile and faeces. |
| 447 | 6768119 | Alterations in hepatic microsomal cytochrome P-450 hemeproteins in diabetic rats. |
| 448 | 6768119 | These results support the concept that the substrate specific changes in drug metabolism observed in diabetic rats may be related to specific alterations in the hepatic cytochrome P-450 hemeprotein population. |
| 449 | 6768119 | Alterations in hepatic microsomal cytochrome P-450 hemeproteins in diabetic rats. |
| 450 | 6768119 | These results support the concept that the substrate specific changes in drug metabolism observed in diabetic rats may be related to specific alterations in the hepatic cytochrome P-450 hemeprotein population. |
| 451 | 6782003 | Cytochrome P450 mediated drug metabolism in the streptozotocin diabetic rat. |
| 452 | 6812187 | Drug metabolism in a reconstituted system by diabetes-dependent hepatic cytochrome P-450. |
| 453 | 6812187 | Previous studies have shown that diabetes induces a unique 52,000 molecular weight cytochrome P-450 in rat hepatic microsomes. |
| 454 | 6812187 | Drug metabolism in a reconstituted system by diabetes-dependent hepatic cytochrome P-450. |
| 455 | 6812187 | Previous studies have shown that diabetes induces a unique 52,000 molecular weight cytochrome P-450 in rat hepatic microsomes. |
| 456 | 6873879 | Effect of adrenalectomy on the cytochrome P-450 population of diabetic rat liver. |
| 457 | 6975948 | Hepatic cytochrome P-450 content was also determined. |
| 458 | 6975948 | The diabetic state increased hepatic AHH and ECD activities in the control female rats, while in the adrenalectomized female rats the activities of both enzymes were decreased compared to the control diabetic rats. |
| 459 | 6975948 | STZ-induced diabetes produced a decrease in pulmonary AHH and ECD activities and increased intestinal AHH and ECD activities in both sexes. |
| 460 | 6975948 | The diabetic state in the adrenalectomized rats resulted in further reduction in pulmonary AHH and ECD activities in both sexes, but failed to increase the intestinal AHH activity only in the female rat. |
| 461 | 6975948 | Hepatic cytochrome P-450 contents were increased in the female but not male adrenalectomized rats when treated with STZ. |
| 462 | 6975948 | The effects of STZ-induced diabetes in adrenalectomized rats on AHH, ECD and hepatic cytochrome P-450 content in liver, lung and intestine depended upon sex of animal, substrate and tissue. |
| 463 | 6975948 | Hepatic cytochrome P-450 content was also determined. |
| 464 | 6975948 | The diabetic state increased hepatic AHH and ECD activities in the control female rats, while in the adrenalectomized female rats the activities of both enzymes were decreased compared to the control diabetic rats. |
| 465 | 6975948 | STZ-induced diabetes produced a decrease in pulmonary AHH and ECD activities and increased intestinal AHH and ECD activities in both sexes. |
| 466 | 6975948 | The diabetic state in the adrenalectomized rats resulted in further reduction in pulmonary AHH and ECD activities in both sexes, but failed to increase the intestinal AHH activity only in the female rat. |
| 467 | 6975948 | Hepatic cytochrome P-450 contents were increased in the female but not male adrenalectomized rats when treated with STZ. |
| 468 | 6975948 | The effects of STZ-induced diabetes in adrenalectomized rats on AHH, ECD and hepatic cytochrome P-450 content in liver, lung and intestine depended upon sex of animal, substrate and tissue. |
| 469 | 6975948 | Hepatic cytochrome P-450 content was also determined. |
| 470 | 6975948 | The diabetic state increased hepatic AHH and ECD activities in the control female rats, while in the adrenalectomized female rats the activities of both enzymes were decreased compared to the control diabetic rats. |
| 471 | 6975948 | STZ-induced diabetes produced a decrease in pulmonary AHH and ECD activities and increased intestinal AHH and ECD activities in both sexes. |
| 472 | 6975948 | The diabetic state in the adrenalectomized rats resulted in further reduction in pulmonary AHH and ECD activities in both sexes, but failed to increase the intestinal AHH activity only in the female rat. |
| 473 | 6975948 | Hepatic cytochrome P-450 contents were increased in the female but not male adrenalectomized rats when treated with STZ. |
| 474 | 6975948 | The effects of STZ-induced diabetes in adrenalectomized rats on AHH, ECD and hepatic cytochrome P-450 content in liver, lung and intestine depended upon sex of animal, substrate and tissue. |
| 475 | 7150359 | Effect of diabetes on rat liver cytochrome P-450. |
| 476 | 7150359 | Evidence for a unique diabetes-dependent rat liver cytochrome P-450. |
| 477 | 7150359 | Effect of diabetes on rat liver cytochrome P-450. |
| 478 | 7150359 | Evidence for a unique diabetes-dependent rat liver cytochrome P-450. |
| 479 | 7397002 | Liver microsomal cytochrome P-450 and related monooxygenase activities in genetically hyperglycemic (ob/ob and db/db) and lean streptozotocin-treated mice. |
| 480 | 7439538 | Hepatic cytochrome P-450 (P-450), determined from the biopsy samples, was used as an in vitro parameter, since it is a direct measure of microsomal drug-metabolizing enzyme activity. |
| 481 | 7514568 | The similarity of sequence and cofactor binding sites has suggested that the NOS genes may also be related to cytochrome P450 reductase, as well as to plant and bacterial oxidoreductases. |
| 482 | 7514568 | Identification of the human gene for endothelial NOS (NOS3) was confirmed by nucleotide sequence analysis of the first coding exon, which was found to be identical to its cognate cDNA. |
| 483 | 7562487 | These increases were consistent with significant induction of hepatic cytochrome P450 (1.14 +/- 0.45 vs. 0.54 +/- 0.10 nmol/mg protein) and an elevated hepatic free CoA content (313.4 +/- 48.5 vs. 172.9 +/- 38.6 nmol/g) relative to control (P < or = .05). |
| 484 | 7562487 | In hepatocytes from type II diabetic rats there were significant reductions (P < or = .05) in the rate constants for ibuprofenyl-CoA formation (1.02 +/- 0.12 vs. 1.22 +/- 0.12 hr-1), R-ibuprofen elimination (0.21 +/- 0.06 vs. 0.34 +/- 0.10 hr-1) and S-ibuprofen elimination (0.41 +/- 0.07 vs. 0.73 +/- 0.11 hr-1) but no change in hepatic content of cytochrome P450 or CoA relative to control. |
| 485 | 7562487 | These increases were consistent with significant induction of hepatic cytochrome P450 (1.14 +/- 0.45 vs. 0.54 +/- 0.10 nmol/mg protein) and an elevated hepatic free CoA content (313.4 +/- 48.5 vs. 172.9 +/- 38.6 nmol/g) relative to control (P < or = .05). |
| 486 | 7562487 | In hepatocytes from type II diabetic rats there were significant reductions (P < or = .05) in the rate constants for ibuprofenyl-CoA formation (1.02 +/- 0.12 vs. 1.22 +/- 0.12 hr-1), R-ibuprofen elimination (0.21 +/- 0.06 vs. 0.34 +/- 0.10 hr-1) and S-ibuprofen elimination (0.41 +/- 0.07 vs. 0.73 +/- 0.11 hr-1) but no change in hepatic content of cytochrome P450 or CoA relative to control. |
| 487 | 7620514 | Bradykinin stimulates phospholipases to release arachidonic acid (AA) which can be metabolized by cyclooxygenase, lipoxygenase and cytochrome P450 (P450) to yield vasoactive products that may contribute to the effect of the peptide. |
| 488 | 7700245 | Insulin down-regulates cytochrome P450 2B and 2E expression at the post-transcriptional level in the rat hepatoma cell line. |
| 489 | 7700245 | The aim of our work was to study the effects of insulin on P450 2B and 2E expression in differentiated Fao hepatoma cells. |
| 490 | 7700245 | Exposure of the cells to 0.1 microM insulin caused 60% and 80% decreases in the steady state levels of P450 2B and 2E proteins, respectively, within 24 hr. |
| 491 | 7700245 | Indeed, 5-6 hr of insulin treatment produced 80 and 50% decreases in P450 2B and 2E mRNA levels, respectively. |
| 492 | 7700245 | From our results, it can be concluded that insulin down-regulates the expression of P450 2B by shortening the half-life of its mRNA (half-lives of 6.9 hr without insulin and 3.6 hr with insulin), whereas it down-regulates the expression of P450 2E both by weak repression of the transcription rate (-30%) and, in particular, by acceleration of its mRNA turnover (half-lives of 8.5 hr without insulin and 3.3 hr with insulin). |
| 493 | 7700245 | Insulin down-regulates cytochrome P450 2B and 2E expression at the post-transcriptional level in the rat hepatoma cell line. |
| 494 | 7700245 | The aim of our work was to study the effects of insulin on P450 2B and 2E expression in differentiated Fao hepatoma cells. |
| 495 | 7700245 | Exposure of the cells to 0.1 microM insulin caused 60% and 80% decreases in the steady state levels of P450 2B and 2E proteins, respectively, within 24 hr. |
| 496 | 7700245 | Indeed, 5-6 hr of insulin treatment produced 80 and 50% decreases in P450 2B and 2E mRNA levels, respectively. |
| 497 | 7700245 | From our results, it can be concluded that insulin down-regulates the expression of P450 2B by shortening the half-life of its mRNA (half-lives of 6.9 hr without insulin and 3.6 hr with insulin), whereas it down-regulates the expression of P450 2E both by weak repression of the transcription rate (-30%) and, in particular, by acceleration of its mRNA turnover (half-lives of 8.5 hr without insulin and 3.3 hr with insulin). |
| 498 | 7700245 | Insulin down-regulates cytochrome P450 2B and 2E expression at the post-transcriptional level in the rat hepatoma cell line. |
| 499 | 7700245 | The aim of our work was to study the effects of insulin on P450 2B and 2E expression in differentiated Fao hepatoma cells. |
| 500 | 7700245 | Exposure of the cells to 0.1 microM insulin caused 60% and 80% decreases in the steady state levels of P450 2B and 2E proteins, respectively, within 24 hr. |
| 501 | 7700245 | Indeed, 5-6 hr of insulin treatment produced 80 and 50% decreases in P450 2B and 2E mRNA levels, respectively. |
| 502 | 7700245 | From our results, it can be concluded that insulin down-regulates the expression of P450 2B by shortening the half-life of its mRNA (half-lives of 6.9 hr without insulin and 3.6 hr with insulin), whereas it down-regulates the expression of P450 2E both by weak repression of the transcription rate (-30%) and, in particular, by acceleration of its mRNA turnover (half-lives of 8.5 hr without insulin and 3.3 hr with insulin). |
| 503 | 7700245 | Insulin down-regulates cytochrome P450 2B and 2E expression at the post-transcriptional level in the rat hepatoma cell line. |
| 504 | 7700245 | The aim of our work was to study the effects of insulin on P450 2B and 2E expression in differentiated Fao hepatoma cells. |
| 505 | 7700245 | Exposure of the cells to 0.1 microM insulin caused 60% and 80% decreases in the steady state levels of P450 2B and 2E proteins, respectively, within 24 hr. |
| 506 | 7700245 | Indeed, 5-6 hr of insulin treatment produced 80 and 50% decreases in P450 2B and 2E mRNA levels, respectively. |
| 507 | 7700245 | From our results, it can be concluded that insulin down-regulates the expression of P450 2B by shortening the half-life of its mRNA (half-lives of 6.9 hr without insulin and 3.6 hr with insulin), whereas it down-regulates the expression of P450 2E both by weak repression of the transcription rate (-30%) and, in particular, by acceleration of its mRNA turnover (half-lives of 8.5 hr without insulin and 3.3 hr with insulin). |
| 508 | 7700245 | Insulin down-regulates cytochrome P450 2B and 2E expression at the post-transcriptional level in the rat hepatoma cell line. |
| 509 | 7700245 | The aim of our work was to study the effects of insulin on P450 2B and 2E expression in differentiated Fao hepatoma cells. |
| 510 | 7700245 | Exposure of the cells to 0.1 microM insulin caused 60% and 80% decreases in the steady state levels of P450 2B and 2E proteins, respectively, within 24 hr. |
| 511 | 7700245 | Indeed, 5-6 hr of insulin treatment produced 80 and 50% decreases in P450 2B and 2E mRNA levels, respectively. |
| 512 | 7700245 | From our results, it can be concluded that insulin down-regulates the expression of P450 2B by shortening the half-life of its mRNA (half-lives of 6.9 hr without insulin and 3.6 hr with insulin), whereas it down-regulates the expression of P450 2E both by weak repression of the transcription rate (-30%) and, in particular, by acceleration of its mRNA turnover (half-lives of 8.5 hr without insulin and 3.3 hr with insulin). |
| 513 | 7713353 | It reduced the cytochrome P-450 content by 30%, this effect being reversed by insulin therapy. 3. |
| 514 | 7713353 | Diabetes determined a lower UDPGT substrate efficiency not reversed by insulin therapy. |
| 515 | 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. |
| 516 | 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. |
| 517 | 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. |
| 518 | 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. |
| 519 | 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. |
| 520 | 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. |
| 521 | 7749391 | Vascular-derived kinins induce vasodilatation through the release of endothelial compounds (prostacyclin, EDRFs and cytochrome P-450). |
| 522 | 7840166 | Differential short- and long-term effects of insulin on ANG II action in human adrenal glomerulosa cells. |
| 523 | 7840166 | In the present studies, we have examined the acute and chronic effects of insulin on angiotensin II (ANG II)-induced aldosterone synthesis in cultured normal and adenomatous human adrenal glomerulosa cells. |
| 524 | 7840166 | Short-term insulin treatment (1.5 h) resulted in inhibition of ANG II-induced aldosterone synthesis. |
| 525 | 7840166 | The 12-lipoxygenase pathway of arachidonate metabolism has been shown to play a key role in ANG II-induced aldosterone synthesis. |
| 526 | 7840166 | The acute inhibitory effects of insulin were in part mediated by inhibition of the 12-lipoxygenase pathway. |
| 527 | 7840166 | The chronic stimulatory effect of insulin seemed to be due at least in part to the upregulation of cytochrome P-450 side-chain cleavage enzyme levels. |
| 528 | 7840166 | These findings suggest that insulin has a differential temporal effect on ANG II action and therefore may be an important regulator of ANG II-induced aldosterone synthesis in the adrenal. |
| 529 | 7880321 | Cytochrome P450 changes in rats with streptozocin-induced diabetes. |
| 530 | 7880321 | The induction and/or suppression of hepatic cytochrome P450 isozymes seen in diabetes seem to contribute to this alteration. |
| 531 | 7880321 | Analysis of cytochrome P450 isozymes in diabetic rats is helpful in elucidating the impaired metabolism of some endogenous substrates catalyzed by the cytochrome P450, such as steroid hormones and fatty acids, in diabetes. |
| 532 | 7880321 | Cytochrome P450 changes in rats with streptozocin-induced diabetes. |
| 533 | 7880321 | The induction and/or suppression of hepatic cytochrome P450 isozymes seen in diabetes seem to contribute to this alteration. |
| 534 | 7880321 | Analysis of cytochrome P450 isozymes in diabetic rats is helpful in elucidating the impaired metabolism of some endogenous substrates catalyzed by the cytochrome P450, such as steroid hormones and fatty acids, in diabetes. |
| 535 | 7880321 | Cytochrome P450 changes in rats with streptozocin-induced diabetes. |
| 536 | 7880321 | The induction and/or suppression of hepatic cytochrome P450 isozymes seen in diabetes seem to contribute to this alteration. |
| 537 | 7880321 | Analysis of cytochrome P450 isozymes in diabetic rats is helpful in elucidating the impaired metabolism of some endogenous substrates catalyzed by the cytochrome P450, such as steroid hormones and fatty acids, in diabetes. |
| 538 | 7891359 | These data indicate that ketones are associated with oxidative hemoglobin damage in cats, and suggest that ketone metabolism, ie by cytochrome P450 2E1, may be a potential source of in vivo oxygen radical generation in animals with ketosis. |
| 539 | 7922169 | New information has also become available about the renal biology of cytochrome P-450 metabolites of arachidonic acid as well as about nonenzymatically generated biologically potent eicosanoids, the F2-isoprostanes. |
| 540 | 8067257 | Chemical diabetes produced in male rats by treatment with alloxan (45 mg/kg) decreased aminopyrine N-demethylase activity but not hepatic microsomal protein, cytochrome P-450 and cytochrome b5 contents. |
| 541 | 8071947 | Modulation of the rat hepatic cytochrome P450 composition by long-term streptozotocin-induced insulin-dependent diabetes. |
| 542 | 8071947 | The effects of long-term insulin-dependent diabetes on the enzymatic activities of hepatic cytochrome P450 isozymes were determined in rats rendered diabetic by the administration of streptozotocin and killed 4, 8, and 12 weeks following treatment. |
| 543 | 8071947 | It is concluded that the duration of diabetes modulates the hepatic cytochrome P450 profile, with the effect being isoenzyme specific. |
| 544 | 8071947 | Modulation of the rat hepatic cytochrome P450 composition by long-term streptozotocin-induced insulin-dependent diabetes. |
| 545 | 8071947 | The effects of long-term insulin-dependent diabetes on the enzymatic activities of hepatic cytochrome P450 isozymes were determined in rats rendered diabetic by the administration of streptozotocin and killed 4, 8, and 12 weeks following treatment. |
| 546 | 8071947 | It is concluded that the duration of diabetes modulates the hepatic cytochrome P450 profile, with the effect being isoenzyme specific. |
| 547 | 8071947 | Modulation of the rat hepatic cytochrome P450 composition by long-term streptozotocin-induced insulin-dependent diabetes. |
| 548 | 8071947 | The effects of long-term insulin-dependent diabetes on the enzymatic activities of hepatic cytochrome P450 isozymes were determined in rats rendered diabetic by the administration of streptozotocin and killed 4, 8, and 12 weeks following treatment. |
| 549 | 8071947 | It is concluded that the duration of diabetes modulates the hepatic cytochrome P450 profile, with the effect being isoenzyme specific. |
| 550 | 8111071 | The insulin-mimetic effects of vanadate in preventing the increase in the level and activity of several P450 proteins in streptozotocin-diabetic rats were examined, in order to extend knowledge of the insulin-like actions of vanadate from glucose metabolism to P450-dependent metabolism. |
| 551 | 8111071 | In summary, vanadate appears to exert insulin-mimetic actions on the P450III and P450I family proteins that have a key role in cytochrome P450-dependent metabolism. |
| 552 | 8111071 | The insulin-mimetic effects of vanadate in preventing the increase in the level and activity of several P450 proteins in streptozotocin-diabetic rats were examined, in order to extend knowledge of the insulin-like actions of vanadate from glucose metabolism to P450-dependent metabolism. |
| 553 | 8111071 | In summary, vanadate appears to exert insulin-mimetic actions on the P450III and P450I family proteins that have a key role in cytochrome P450-dependent metabolism. |
| 554 | 8274152 | Diabetes produced by streptozotocin induced CYP4A2 and P450 K-2 (similar form with CYP2C23) but not P450 K-4 (similar form with CYP4A8) and induced lauric acid hydroxylation activity. |
| 555 | 8274152 | Treatment of diabetic rats with thyroid hormone (T3) as well as with insulin reversed the increase in the levels of CYP4A2 and P450 K-2. |
| 556 | 8274152 | Thyroidectomy also induced CYP4A2 and P450 K-2 in the rat kidney. |
| 557 | 8274152 | These findings suggest that expression of CYP4A2 and P450 K-2 in rat kidney is suppressively regulated by thyroid hormone and the decrease in thyroid hormone level in the diabetic state affects the levels of CYP4A2 and P450 K-2. |
| 558 | 8274152 | Diabetes produced by streptozotocin induced CYP4A2 and P450 K-2 (similar form with CYP2C23) but not P450 K-4 (similar form with CYP4A8) and induced lauric acid hydroxylation activity. |
| 559 | 8274152 | Treatment of diabetic rats with thyroid hormone (T3) as well as with insulin reversed the increase in the levels of CYP4A2 and P450 K-2. |
| 560 | 8274152 | Thyroidectomy also induced CYP4A2 and P450 K-2 in the rat kidney. |
| 561 | 8274152 | These findings suggest that expression of CYP4A2 and P450 K-2 in rat kidney is suppressively regulated by thyroid hormone and the decrease in thyroid hormone level in the diabetic state affects the levels of CYP4A2 and P450 K-2. |
| 562 | 8274152 | Diabetes produced by streptozotocin induced CYP4A2 and P450 K-2 (similar form with CYP2C23) but not P450 K-4 (similar form with CYP4A8) and induced lauric acid hydroxylation activity. |
| 563 | 8274152 | Treatment of diabetic rats with thyroid hormone (T3) as well as with insulin reversed the increase in the levels of CYP4A2 and P450 K-2. |
| 564 | 8274152 | Thyroidectomy also induced CYP4A2 and P450 K-2 in the rat kidney. |
| 565 | 8274152 | These findings suggest that expression of CYP4A2 and P450 K-2 in rat kidney is suppressively regulated by thyroid hormone and the decrease in thyroid hormone level in the diabetic state affects the levels of CYP4A2 and P450 K-2. |
| 566 | 8274152 | Diabetes produced by streptozotocin induced CYP4A2 and P450 K-2 (similar form with CYP2C23) but not P450 K-4 (similar form with CYP4A8) and induced lauric acid hydroxylation activity. |
| 567 | 8274152 | Treatment of diabetic rats with thyroid hormone (T3) as well as with insulin reversed the increase in the levels of CYP4A2 and P450 K-2. |
| 568 | 8274152 | Thyroidectomy also induced CYP4A2 and P450 K-2 in the rat kidney. |
| 569 | 8274152 | These findings suggest that expression of CYP4A2 and P450 K-2 in rat kidney is suppressively regulated by thyroid hormone and the decrease in thyroid hormone level in the diabetic state affects the levels of CYP4A2 and P450 K-2. |
| 570 | 8294080 | These isoforms are regulated by Ca(2+)-calmodulin with NADPH, FAD/FMN and tetrahydrobiopterin as co-factors and reveal a high degree of homology with the amino-acid sequence of cytochrome P450 reductase within the C-terminal domain. |
| 571 | 8363636 | Changes in amounts of cytochrome P450 isozymes and levels of catalytic activities in hepatic and renal microsomes of rats with streptozocin-induced diabetes. |
| 572 | 8363636 | We studied changes in cytochrome P450 isozymes in both hepatic and renal microsomes of rats with diabetes caused by streptozocin, and compared the results with changes in catalytic activities in the microsomes. |
| 573 | 8363636 | In hepatic microsomes of diabetic rats, the amount of cytochrome P450 2E1, an acetone-inducible isozyme, was two and a half times that of control rats, and that of P450 4A2, a major renal isozyme, was three times that in the controls. |
| 574 | 8363636 | The induction and suppression of cytochrome P450 isozymes in diabetic rats were consistent with the changes in the catalytic activities. |
| 575 | 8363636 | Changes in amounts of cytochrome P450 isozymes and levels of catalytic activities in hepatic and renal microsomes of rats with streptozocin-induced diabetes. |
| 576 | 8363636 | We studied changes in cytochrome P450 isozymes in both hepatic and renal microsomes of rats with diabetes caused by streptozocin, and compared the results with changes in catalytic activities in the microsomes. |
| 577 | 8363636 | In hepatic microsomes of diabetic rats, the amount of cytochrome P450 2E1, an acetone-inducible isozyme, was two and a half times that of control rats, and that of P450 4A2, a major renal isozyme, was three times that in the controls. |
| 578 | 8363636 | The induction and suppression of cytochrome P450 isozymes in diabetic rats were consistent with the changes in the catalytic activities. |
| 579 | 8363636 | Changes in amounts of cytochrome P450 isozymes and levels of catalytic activities in hepatic and renal microsomes of rats with streptozocin-induced diabetes. |
| 580 | 8363636 | We studied changes in cytochrome P450 isozymes in both hepatic and renal microsomes of rats with diabetes caused by streptozocin, and compared the results with changes in catalytic activities in the microsomes. |
| 581 | 8363636 | In hepatic microsomes of diabetic rats, the amount of cytochrome P450 2E1, an acetone-inducible isozyme, was two and a half times that of control rats, and that of P450 4A2, a major renal isozyme, was three times that in the controls. |
| 582 | 8363636 | The induction and suppression of cytochrome P450 isozymes in diabetic rats were consistent with the changes in the catalytic activities. |
| 583 | 8363636 | Changes in amounts of cytochrome P450 isozymes and levels of catalytic activities in hepatic and renal microsomes of rats with streptozocin-induced diabetes. |
| 584 | 8363636 | We studied changes in cytochrome P450 isozymes in both hepatic and renal microsomes of rats with diabetes caused by streptozocin, and compared the results with changes in catalytic activities in the microsomes. |
| 585 | 8363636 | In hepatic microsomes of diabetic rats, the amount of cytochrome P450 2E1, an acetone-inducible isozyme, was two and a half times that of control rats, and that of P450 4A2, a major renal isozyme, was three times that in the controls. |
| 586 | 8363636 | The induction and suppression of cytochrome P450 isozymes in diabetic rats were consistent with the changes in the catalytic activities. |
| 587 | 8435090 | Sex differences in the diabetes-induced modulation of rat hepatic cytochrome P450 proteins. |
| 588 | 8435090 | Sex differences in the diabetes-induced changes in hepatic cytochrome P450 proteins were investigated in rats treated with streptozotocin. |
| 589 | 8435090 | Changes in specific cytochrome P450 proteins were monitored using diagnostic substrates and immunologically utilizing specific polyclonal antibodies. |
| 590 | 8435090 | When expressed in terms of nmoles of total cytochrome P450, ethoxyresorufin O-deethylase activity was increased by treatment with streptozotocin, the extent of induction being the same in the two sexes. |
| 591 | 8435090 | These findings indicate that sex-specific changes in certain cytochrome P450 proteins exist in response to insulin-dependent diabetes but these cannot, however, be ascribed to sex differences in the severity of diabetes induced by streptozotocin since the degrees of hyperketonaemia and hyperglycaemia were the same in the two sexes. |
| 592 | 8435090 | Sex differences in the diabetes-induced modulation of rat hepatic cytochrome P450 proteins. |
| 593 | 8435090 | Sex differences in the diabetes-induced changes in hepatic cytochrome P450 proteins were investigated in rats treated with streptozotocin. |
| 594 | 8435090 | Changes in specific cytochrome P450 proteins were monitored using diagnostic substrates and immunologically utilizing specific polyclonal antibodies. |
| 595 | 8435090 | When expressed in terms of nmoles of total cytochrome P450, ethoxyresorufin O-deethylase activity was increased by treatment with streptozotocin, the extent of induction being the same in the two sexes. |
| 596 | 8435090 | These findings indicate that sex-specific changes in certain cytochrome P450 proteins exist in response to insulin-dependent diabetes but these cannot, however, be ascribed to sex differences in the severity of diabetes induced by streptozotocin since the degrees of hyperketonaemia and hyperglycaemia were the same in the two sexes. |
| 597 | 8435090 | Sex differences in the diabetes-induced modulation of rat hepatic cytochrome P450 proteins. |
| 598 | 8435090 | Sex differences in the diabetes-induced changes in hepatic cytochrome P450 proteins were investigated in rats treated with streptozotocin. |
| 599 | 8435090 | Changes in specific cytochrome P450 proteins were monitored using diagnostic substrates and immunologically utilizing specific polyclonal antibodies. |
| 600 | 8435090 | When expressed in terms of nmoles of total cytochrome P450, ethoxyresorufin O-deethylase activity was increased by treatment with streptozotocin, the extent of induction being the same in the two sexes. |
| 601 | 8435090 | These findings indicate that sex-specific changes in certain cytochrome P450 proteins exist in response to insulin-dependent diabetes but these cannot, however, be ascribed to sex differences in the severity of diabetes induced by streptozotocin since the degrees of hyperketonaemia and hyperglycaemia were the same in the two sexes. |
| 602 | 8435090 | Sex differences in the diabetes-induced modulation of rat hepatic cytochrome P450 proteins. |
| 603 | 8435090 | Sex differences in the diabetes-induced changes in hepatic cytochrome P450 proteins were investigated in rats treated with streptozotocin. |
| 604 | 8435090 | Changes in specific cytochrome P450 proteins were monitored using diagnostic substrates and immunologically utilizing specific polyclonal antibodies. |
| 605 | 8435090 | When expressed in terms of nmoles of total cytochrome P450, ethoxyresorufin O-deethylase activity was increased by treatment with streptozotocin, the extent of induction being the same in the two sexes. |
| 606 | 8435090 | These findings indicate that sex-specific changes in certain cytochrome P450 proteins exist in response to insulin-dependent diabetes but these cannot, however, be ascribed to sex differences in the severity of diabetes induced by streptozotocin since the degrees of hyperketonaemia and hyperglycaemia were the same in the two sexes. |
| 607 | 8435090 | Sex differences in the diabetes-induced modulation of rat hepatic cytochrome P450 proteins. |
| 608 | 8435090 | Sex differences in the diabetes-induced changes in hepatic cytochrome P450 proteins were investigated in rats treated with streptozotocin. |
| 609 | 8435090 | Changes in specific cytochrome P450 proteins were monitored using diagnostic substrates and immunologically utilizing specific polyclonal antibodies. |
| 610 | 8435090 | When expressed in terms of nmoles of total cytochrome P450, ethoxyresorufin O-deethylase activity was increased by treatment with streptozotocin, the extent of induction being the same in the two sexes. |
| 611 | 8435090 | These findings indicate that sex-specific changes in certain cytochrome P450 proteins exist in response to insulin-dependent diabetes but these cannot, however, be ascribed to sex differences in the severity of diabetes induced by streptozotocin since the degrees of hyperketonaemia and hyperglycaemia were the same in the two sexes. |
| 612 | 8443210 | Cytochrome P-450 in liver microsomes of streptozotocin-induced diabetic rats: purification and characterization. |
| 613 | 8443210 | Two diabetes-inducible forms of cytochrome P-450, named P-450ST-1 and -ST-2, were purified from the liver microsomes of streptozotocin-diabetic male rats by sodium cholate solubilization, octylamino-Sepharose 4B chromatography and high-performance liquid chromatography with DEAE-5PW and hydroxyapatite columns. |
| 614 | 8443210 | The catalytic activities, molecular weights, NH2-terminal sequences and/or immunochemical properties of P-450ST-1 and -ST-2 did not agree with those of the other cytochrome P-450 forms purified from diabetic rats previously. |
| 615 | 8443210 | Cytochrome P-450 in liver microsomes of streptozotocin-induced diabetic rats: purification and characterization. |
| 616 | 8443210 | Two diabetes-inducible forms of cytochrome P-450, named P-450ST-1 and -ST-2, were purified from the liver microsomes of streptozotocin-diabetic male rats by sodium cholate solubilization, octylamino-Sepharose 4B chromatography and high-performance liquid chromatography with DEAE-5PW and hydroxyapatite columns. |
| 617 | 8443210 | The catalytic activities, molecular weights, NH2-terminal sequences and/or immunochemical properties of P-450ST-1 and -ST-2 did not agree with those of the other cytochrome P-450 forms purified from diabetic rats previously. |
| 618 | 8443210 | Cytochrome P-450 in liver microsomes of streptozotocin-induced diabetic rats: purification and characterization. |
| 619 | 8443210 | Two diabetes-inducible forms of cytochrome P-450, named P-450ST-1 and -ST-2, were purified from the liver microsomes of streptozotocin-diabetic male rats by sodium cholate solubilization, octylamino-Sepharose 4B chromatography and high-performance liquid chromatography with DEAE-5PW and hydroxyapatite columns. |
| 620 | 8443210 | The catalytic activities, molecular weights, NH2-terminal sequences and/or immunochemical properties of P-450ST-1 and -ST-2 did not agree with those of the other cytochrome P-450 forms purified from diabetic rats previously. |
| 621 | 8482528 | Only streptozotocin liver microsomes exhibited changes in the cytochrome P-450 normal spectral characteristics. 3. |
| 622 | 8482528 | Results suggest that diabetogenic agents modify sex related isoenzymes of cytochrome P-450 differently and selectively reduce the synthesis of certain UDP-glucuronyltransferase forms. |
| 623 | 8482528 | Only streptozotocin liver microsomes exhibited changes in the cytochrome P-450 normal spectral characteristics. 3. |
| 624 | 8482528 | Results suggest that diabetogenic agents modify sex related isoenzymes of cytochrome P-450 differently and selectively reduce the synthesis of certain UDP-glucuronyltransferase forms. |
| 625 | 8529805 | In addition, the finding that the mitogen-activated protein kinase (MAP kinase) pathway was tyrosine phosphorylated, and presumably activated, in endothelial cells after an increase in [Ca2+]i has wideranging implications for these cells. |
| 626 | 8529805 | Indeed, MAP kinase recognizes many different substrates in the cell, including growth factor receptors, microtubule-associated proteins, specific serine-threonine protein kinases, phospholipase A2, and transcription factors. |
| 627 | 8529805 | Indeed, this mediator, which seems to be an endothelium-derived, cytochrome P450-derived metabolite of arachidonic acid, would now appear to represent a substantial constitutive component of the vasodilator response to bradykinin. |
| 628 | 8553687 | Extrahepatic expression of P450 proteins in insulin-dependent diabetes mellitus. |
| 629 | 8553687 | It is concluded that streptozotocin-induced insulin-dependent diabetes modulates extrahepatic P450 proteins, the effect being both tissue- and isoform-specific. |
| 630 | 8553687 | Extrahepatic expression of P450 proteins in insulin-dependent diabetes mellitus. |
| 631 | 8553687 | It is concluded that streptozotocin-induced insulin-dependent diabetes modulates extrahepatic P450 proteins, the effect being both tissue- and isoform-specific. |
| 632 | 8626872 | Growth hormone treatment increases cytochrome P450-mediated antipyrine clearance in man. |
| 633 | 8626872 | We used the antipyrine clearance test (APC) to examine the effect of growth hormone (GH) therapy on hepatic cytochrome P450 (CYP) enzyme activity. |
| 634 | 8626872 | Growth hormone treatment increases cytochrome P450-mediated antipyrine clearance in man. |
| 635 | 8626872 | We used the antipyrine clearance test (APC) to examine the effect of growth hormone (GH) therapy on hepatic cytochrome P450 (CYP) enzyme activity. |
| 636 | 8793056 | In this study we examined whether or not diabetes alters levels of P450 side-chain cleavage enzyme (P450scc), 3 beta-hydroxysteroid dehydrogenase (3 beta-HSD), or the cholesterol transport proteins, steroidogenic acute regulatory (StAR) protein and sterol carrier protein-2 (SCP2), leading to lower progesterone levels and pregnancy loss. |
| 637 | 8793056 | Rats (Day 3 pregnant) received an injection of streptozotocin (STZ, 60 mg/kg; i.v.) to induce a diabetic state; P450scc, 3 beta-HSD, and SCP2 were examined by Western and Northern blot analysis in ovarian tissue 12 days after injection of STZ (diabetic rats, n = 12) or vehicle (nondiabetic rats, n = 12). |
| 638 | 8793056 | Ovarian StAR mRNA levels were increased slightly in the diabetic animals, and ovarian P450scc and 3 beta-HSD mRNA levels were increased 3-fold in the diabetic animals that aborted relative to the nondiabetic animals and the +Ft diabetic animals. |
| 639 | 8793056 | Results of this study confirm that SCPx mRNA levels are elevated following diabetes onset and that StAR, P450scc, and 3 beta-HSD mRNA levels do not correspond with the reduced steroid hormone profile associated with diabetes. |
| 640 | 8825678 | Induction and suppression of renal and hepatic cytochrome P450-dependent monooxygenases by acute and chronic streptozotocin diabetes in hamsters. |
| 641 | 8825678 | Total cytochrome P450 content and NADPH-cytochrome P450 reductase activity in kidney and liver microsomes of the diabetic hamsters were similar to the controls. |
| 642 | 8825678 | Induction and suppression of renal and hepatic cytochrome P450-dependent monooxygenases by acute and chronic streptozotocin diabetes in hamsters. |
| 643 | 8825678 | Total cytochrome P450 content and NADPH-cytochrome P450 reductase activity in kidney and liver microsomes of the diabetic hamsters were similar to the controls. |
| 644 | 8826976 | High D-glucose and 3-OMG increased superoxide anion (O2-) formation (133 and 293%, respectively), which was insensitive to inhibitors of cyclooxygenase (5,8,11,14-eicosatetraynoic acid [ETYA], indomethacin), lipoxygenase (ETYA, gossypol, nordihydroguaiaretic acid [NDGA]), cytochrome P450 (NDGA, econazole, miconazole), and nitric oxide (NO) synthase (L-omega N-nitroarginine), while it was diminished by desferal, a metal chelator. |
| 645 | 8937480 | Effect of bitter melon (Momordica charantia) fruit juice on the hepatic cytochrome P450-dependent monooxygenases and glutathione S-transferases in streptozotocin-induced diabetic rats. |
| 646 | 8937480 | In the present study, we have investigated the effects of oral feeding of karela fruit juice on the hepatic cytochrome P450 (CYP) and glutathione S-transferase (GST) drug-metabolizing enzymes in the streptozotocin (STZ)-induced diabetic rat. |
| 647 | 8937480 | Western immunoblot analysis of CYP and GST isozymes exhibited a differential response during diabetes. |
| 648 | 8937480 | The expression of CYP1A1, 2B1, 2E1, 3A4, and 4A2 in diabetes, while a decrease in GST mu was observed. |
| 649 | 8937480 | Our results suggest that the changes in hepatic phase I and phase II drug-metabolizing enzyme activities in the STZ-induced diabetic animals may be associated with the altered expression of different CYP and GST isozymes. |
| 650 | 8937480 | Effect of bitter melon (Momordica charantia) fruit juice on the hepatic cytochrome P450-dependent monooxygenases and glutathione S-transferases in streptozotocin-induced diabetic rats. |
| 651 | 8937480 | In the present study, we have investigated the effects of oral feeding of karela fruit juice on the hepatic cytochrome P450 (CYP) and glutathione S-transferase (GST) drug-metabolizing enzymes in the streptozotocin (STZ)-induced diabetic rat. |
| 652 | 8937480 | Western immunoblot analysis of CYP and GST isozymes exhibited a differential response during diabetes. |
| 653 | 8937480 | The expression of CYP1A1, 2B1, 2E1, 3A4, and 4A2 in diabetes, while a decrease in GST mu was observed. |
| 654 | 8937480 | Our results suggest that the changes in hepatic phase I and phase II drug-metabolizing enzyme activities in the STZ-induced diabetic animals may be associated with the altered expression of different CYP and GST isozymes. |
| 655 | 9001594 | Effect of vitamin C supplementation on hepatic cytochrome P450 mixed-function oxidase activity in streptozotocin-diabetic rats. |
| 656 | 9001594 | The effect of vitamin C supplementation on hepatic cytochrome P450 expression was investigated in streptozotocin (STZ) diabetic male Wistar Albino rats. |
| 657 | 9001594 | Effect of vitamin C supplementation on hepatic cytochrome P450 mixed-function oxidase activity in streptozotocin-diabetic rats. |
| 658 | 9001594 | The effect of vitamin C supplementation on hepatic cytochrome P450 expression was investigated in streptozotocin (STZ) diabetic male Wistar Albino rats. |
| 659 | 9016816 | CYP2B, CYP4A, and CYP2E1 mRNA levels are elevated in response to pathophysiological conditions, such as diabetes, high-fat diet, and fasting, in which lipids and ketone bodies are increased. |
| 660 | 9016816 | In order to avoid confounding hormonal effects, we utilized primary rat hepatocytes to examine whether ketone bodies or fatty acids altered CYP2B, CYP4A, or CYP2E1 expression. |
| 661 | 9016816 | Ketone bodies increased CYP2B mRNA and protein levels, but failed to alter CYP4A or CYP2E1 expression. |
| 662 | 9016816 | Straight-chain saturated fatty acids, C8 to C16, increased levels of CYP2B and CYP4A mRNA, but not CYP2E1 mRNA. |
| 663 | 9016816 | Addition of glycerol, which suppresses fatty acid synthesis by inhibiting conversion of lactate to pyruvate, decreased basal expression of CYP2B and CYP4A but did not alter CYP2E1 expression. |
| 664 | 9016816 | These results provide evidence that intracellular levels of fatty acids and ketone bodies regulate the expression of CYP2B but not CYP2E1. |
| 665 | 9016816 | CYP2B, CYP4A, and CYP2E1 mRNA levels are elevated in response to pathophysiological conditions, such as diabetes, high-fat diet, and fasting, in which lipids and ketone bodies are increased. |
| 666 | 9016816 | In order to avoid confounding hormonal effects, we utilized primary rat hepatocytes to examine whether ketone bodies or fatty acids altered CYP2B, CYP4A, or CYP2E1 expression. |
| 667 | 9016816 | Ketone bodies increased CYP2B mRNA and protein levels, but failed to alter CYP4A or CYP2E1 expression. |
| 668 | 9016816 | Straight-chain saturated fatty acids, C8 to C16, increased levels of CYP2B and CYP4A mRNA, but not CYP2E1 mRNA. |
| 669 | 9016816 | Addition of glycerol, which suppresses fatty acid synthesis by inhibiting conversion of lactate to pyruvate, decreased basal expression of CYP2B and CYP4A but did not alter CYP2E1 expression. |
| 670 | 9016816 | These results provide evidence that intracellular levels of fatty acids and ketone bodies regulate the expression of CYP2B but not CYP2E1. |
| 671 | 9016816 | CYP2B, CYP4A, and CYP2E1 mRNA levels are elevated in response to pathophysiological conditions, such as diabetes, high-fat diet, and fasting, in which lipids and ketone bodies are increased. |
| 672 | 9016816 | In order to avoid confounding hormonal effects, we utilized primary rat hepatocytes to examine whether ketone bodies or fatty acids altered CYP2B, CYP4A, or CYP2E1 expression. |
| 673 | 9016816 | Ketone bodies increased CYP2B mRNA and protein levels, but failed to alter CYP4A or CYP2E1 expression. |
| 674 | 9016816 | Straight-chain saturated fatty acids, C8 to C16, increased levels of CYP2B and CYP4A mRNA, but not CYP2E1 mRNA. |
| 675 | 9016816 | Addition of glycerol, which suppresses fatty acid synthesis by inhibiting conversion of lactate to pyruvate, decreased basal expression of CYP2B and CYP4A but did not alter CYP2E1 expression. |
| 676 | 9016816 | These results provide evidence that intracellular levels of fatty acids and ketone bodies regulate the expression of CYP2B but not CYP2E1. |
| 677 | 9016816 | CYP2B, CYP4A, and CYP2E1 mRNA levels are elevated in response to pathophysiological conditions, such as diabetes, high-fat diet, and fasting, in which lipids and ketone bodies are increased. |
| 678 | 9016816 | In order to avoid confounding hormonal effects, we utilized primary rat hepatocytes to examine whether ketone bodies or fatty acids altered CYP2B, CYP4A, or CYP2E1 expression. |
| 679 | 9016816 | Ketone bodies increased CYP2B mRNA and protein levels, but failed to alter CYP4A or CYP2E1 expression. |
| 680 | 9016816 | Straight-chain saturated fatty acids, C8 to C16, increased levels of CYP2B and CYP4A mRNA, but not CYP2E1 mRNA. |
| 681 | 9016816 | Addition of glycerol, which suppresses fatty acid synthesis by inhibiting conversion of lactate to pyruvate, decreased basal expression of CYP2B and CYP4A but did not alter CYP2E1 expression. |
| 682 | 9016816 | These results provide evidence that intracellular levels of fatty acids and ketone bodies regulate the expression of CYP2B but not CYP2E1. |
| 683 | 9016816 | CYP2B, CYP4A, and CYP2E1 mRNA levels are elevated in response to pathophysiological conditions, such as diabetes, high-fat diet, and fasting, in which lipids and ketone bodies are increased. |
| 684 | 9016816 | In order to avoid confounding hormonal effects, we utilized primary rat hepatocytes to examine whether ketone bodies or fatty acids altered CYP2B, CYP4A, or CYP2E1 expression. |
| 685 | 9016816 | Ketone bodies increased CYP2B mRNA and protein levels, but failed to alter CYP4A or CYP2E1 expression. |
| 686 | 9016816 | Straight-chain saturated fatty acids, C8 to C16, increased levels of CYP2B and CYP4A mRNA, but not CYP2E1 mRNA. |
| 687 | 9016816 | Addition of glycerol, which suppresses fatty acid synthesis by inhibiting conversion of lactate to pyruvate, decreased basal expression of CYP2B and CYP4A but did not alter CYP2E1 expression. |
| 688 | 9016816 | These results provide evidence that intracellular levels of fatty acids and ketone bodies regulate the expression of CYP2B but not CYP2E1. |
| 689 | 9016816 | CYP2B, CYP4A, and CYP2E1 mRNA levels are elevated in response to pathophysiological conditions, such as diabetes, high-fat diet, and fasting, in which lipids and ketone bodies are increased. |
| 690 | 9016816 | In order to avoid confounding hormonal effects, we utilized primary rat hepatocytes to examine whether ketone bodies or fatty acids altered CYP2B, CYP4A, or CYP2E1 expression. |
| 691 | 9016816 | Ketone bodies increased CYP2B mRNA and protein levels, but failed to alter CYP4A or CYP2E1 expression. |
| 692 | 9016816 | Straight-chain saturated fatty acids, C8 to C16, increased levels of CYP2B and CYP4A mRNA, but not CYP2E1 mRNA. |
| 693 | 9016816 | Addition of glycerol, which suppresses fatty acid synthesis by inhibiting conversion of lactate to pyruvate, decreased basal expression of CYP2B and CYP4A but did not alter CYP2E1 expression. |
| 694 | 9016816 | These results provide evidence that intracellular levels of fatty acids and ketone bodies regulate the expression of CYP2B but not CYP2E1. |
| 695 | 9039952 | For example, diabetes, which disrupts glucose and ketone homeostasis, insulin sensitivity, gonadal and neuroendocrine hormone balance, protein kinase C isoform expression, and P450 metabolism, also disturbs hepatic sulfotransferase gene expression. |
| 696 | 9061564 | Levels of DM and its primary metabolite dextrorphan (DX) were utilized to guide DM therapy and exhibited patterns reflective of the extensive and poor metabolizer phenotypes for CYP2D6, the cytochrome P450 isoform responsible for DM metabolism. |
| 697 | 9061564 | In the patient who appeared to represent the extensive metabolizer (EM) phenotype, treatment with the non-specific cytochrome P450 inhibitor cimetidine was required to reduce biotransformation of DM to DX and, thus, to increase DM plasma concentrations. |
| 698 | 9061564 | These cases demonstrate the importance of CYP2D6 phenotype in providing safe and effective DM therapy to patients with NKH. |
| 699 | 9061564 | Levels of DM and its primary metabolite dextrorphan (DX) were utilized to guide DM therapy and exhibited patterns reflective of the extensive and poor metabolizer phenotypes for CYP2D6, the cytochrome P450 isoform responsible for DM metabolism. |
| 700 | 9061564 | In the patient who appeared to represent the extensive metabolizer (EM) phenotype, treatment with the non-specific cytochrome P450 inhibitor cimetidine was required to reduce biotransformation of DM to DX and, thus, to increase DM plasma concentrations. |
| 701 | 9061564 | These cases demonstrate the importance of CYP2D6 phenotype in providing safe and effective DM therapy to patients with NKH. |
| 702 | 9114822 | The MEOS was purified and reconstituted using 2E1, phospholipids, and cytochrome P-450 reductase and shown to oxidize ethanol to acetaldehyde, mainly as a monooxygenase and secondarily via hydroxyl radicals, with transcriptional and posttranscriptional regulation. |
| 703 | 9200662 | The crucial role of glucocorticoids in obesity and insulin resistance and the actions of the OB protein leptin on the hypothalamic-pituitary-adrenal (HPA) axis suggest that there is an important interaction of leptin with the glucocorticoid system. |
| 704 | 9200662 | The accumulation of P450 17alpha mRNA following incubation with ACTH (10 nmol/l) and leptin (10-1,000 ng/ml) was analyzed by Northern blot. |
| 705 | 9200662 | Addition of OB protein (10-1,000 ng/ml) led to a dose-dependent reduction of ACTH-stimulated cytochrome P450 17alpha mRNA accumulation (from 80 to 45%), suggesting that leptin regulates adrenal steroidogenesis at the transcriptional level. |
| 706 | 9200662 | The crucial role of glucocorticoids in obesity and insulin resistance and the actions of the OB protein leptin on the hypothalamic-pituitary-adrenal (HPA) axis suggest that there is an important interaction of leptin with the glucocorticoid system. |
| 707 | 9200662 | The accumulation of P450 17alpha mRNA following incubation with ACTH (10 nmol/l) and leptin (10-1,000 ng/ml) was analyzed by Northern blot. |
| 708 | 9200662 | Addition of OB protein (10-1,000 ng/ml) led to a dose-dependent reduction of ACTH-stimulated cytochrome P450 17alpha mRNA accumulation (from 80 to 45%), suggesting that leptin regulates adrenal steroidogenesis at the transcriptional level. |
| 709 | 9363841 | Induction of cytochrome P450 2E1 (CYP2E1) has been shown to occur through two distinct mechanisms. |
| 710 | 9363841 | During the course of our previous study which demonstrated hyperoxia-induced specific pretranslational induction of CYP1A1/2 in the liver and CYP1A1 in the lung, we observed a progressive increase of hepatic CYP2E1 mRNA in animals of the hyperoxia group. |
| 711 | 9402951 | Insulin effects on CYP2E1, 2B, 3A, and 4A expression in primary cultured rat hepatocytes. |
| 712 | 9402951 | Although hyperketonemia and/or altered growth hormone secretion caused by diabetes have been implicated in enhanced CYP2E1, 2B, 3A and 4A expression, the effect of insulin on hepatic P450 expression, in the absence of associated metabolic/hormonal alterations, remains unknown. |
| 713 | 9402951 | Dispos., 23:681, 1995) to express stable and inducible CYP2E1 mRNA and protein levels, and provide an excellent system for mechanistic examination of the effect of insulin on CYP2E1, 2B, 3A and 4A expression. |
| 714 | 9402951 | Maintaining primary rat hepatocytes in culture in the absence of insulin for 48, 72, or 96 h increased CYP2E1 mRNA levels 5-, 11-, and 4-fold, respectively, relative to cells maintained in the presence of the standard concentration of 1 microM insulin. |
| 715 | 9402951 | In contrast, CYP2B mRNA levels increased only approximately 2-fold in the absence of insulin, when compared with the presence of 1 microM insulin. |
| 716 | 9402951 | CYP2E1 and 2B protein levels were increased 6.7- and 3.8-fold, respectively, in cells cultured for 96 h in the absence of insulin as compared with those cultured in medium containing 1 microM insulin. |
| 717 | 9402951 | Concentration-response studies revealed that decreasing the concentration of insulin below 10 nM (i.e. 1 nM, 0.1 nM, no insulin) increased CYP2E1 mRNA levels 4-, 7-, and 11-fold, respectively. |
| 718 | 9402951 | As CYP3A and 4A expression is also elevated in diabetic rats, the effects of insulin on these P450s was also examined. |
| 719 | 9402951 | CYP3A mRNA levels were unaltered and CYP4A mRNA levels were decreased marginally (approximately 50%) by the absence of insulin relative to levels in cells cultured in the presence of 1 microM insulin over 96 h in culture. |
| 720 | 9402951 | The results of this study provide evidence that insulin itself, in the absence of other diabetes-induced metabolic or hormonal alterations, affects CYP2E1 and 2B, but not CYP3A or 4A, expression in primary cultured rat hepatocytes. |
| 721 | 9402951 | Furthermore, CYP2E1 expression is differentially regulated by insulin relative to CYP2B, 3A or 4A. |
| 722 | 9402951 | This study also demonstrates that decreasing the concentration of insulin in the culture medium provides a method by which CYP2E1 levels can be increased in primary cultured hepatocytes to facilitate mechanistic studies on the regulation of CYP2E1 expression. |
| 723 | 9402951 | Insulin effects on CYP2E1, 2B, 3A, and 4A expression in primary cultured rat hepatocytes. |
| 724 | 9402951 | Although hyperketonemia and/or altered growth hormone secretion caused by diabetes have been implicated in enhanced CYP2E1, 2B, 3A and 4A expression, the effect of insulin on hepatic P450 expression, in the absence of associated metabolic/hormonal alterations, remains unknown. |
| 725 | 9402951 | Dispos., 23:681, 1995) to express stable and inducible CYP2E1 mRNA and protein levels, and provide an excellent system for mechanistic examination of the effect of insulin on CYP2E1, 2B, 3A and 4A expression. |
| 726 | 9402951 | Maintaining primary rat hepatocytes in culture in the absence of insulin for 48, 72, or 96 h increased CYP2E1 mRNA levels 5-, 11-, and 4-fold, respectively, relative to cells maintained in the presence of the standard concentration of 1 microM insulin. |
| 727 | 9402951 | In contrast, CYP2B mRNA levels increased only approximately 2-fold in the absence of insulin, when compared with the presence of 1 microM insulin. |
| 728 | 9402951 | CYP2E1 and 2B protein levels were increased 6.7- and 3.8-fold, respectively, in cells cultured for 96 h in the absence of insulin as compared with those cultured in medium containing 1 microM insulin. |
| 729 | 9402951 | Concentration-response studies revealed that decreasing the concentration of insulin below 10 nM (i.e. 1 nM, 0.1 nM, no insulin) increased CYP2E1 mRNA levels 4-, 7-, and 11-fold, respectively. |
| 730 | 9402951 | As CYP3A and 4A expression is also elevated in diabetic rats, the effects of insulin on these P450s was also examined. |
| 731 | 9402951 | CYP3A mRNA levels were unaltered and CYP4A mRNA levels were decreased marginally (approximately 50%) by the absence of insulin relative to levels in cells cultured in the presence of 1 microM insulin over 96 h in culture. |
| 732 | 9402951 | The results of this study provide evidence that insulin itself, in the absence of other diabetes-induced metabolic or hormonal alterations, affects CYP2E1 and 2B, but not CYP3A or 4A, expression in primary cultured rat hepatocytes. |
| 733 | 9402951 | Furthermore, CYP2E1 expression is differentially regulated by insulin relative to CYP2B, 3A or 4A. |
| 734 | 9402951 | This study also demonstrates that decreasing the concentration of insulin in the culture medium provides a method by which CYP2E1 levels can be increased in primary cultured hepatocytes to facilitate mechanistic studies on the regulation of CYP2E1 expression. |
| 735 | 9402951 | Insulin effects on CYP2E1, 2B, 3A, and 4A expression in primary cultured rat hepatocytes. |
| 736 | 9402951 | Although hyperketonemia and/or altered growth hormone secretion caused by diabetes have been implicated in enhanced CYP2E1, 2B, 3A and 4A expression, the effect of insulin on hepatic P450 expression, in the absence of associated metabolic/hormonal alterations, remains unknown. |
| 737 | 9402951 | Dispos., 23:681, 1995) to express stable and inducible CYP2E1 mRNA and protein levels, and provide an excellent system for mechanistic examination of the effect of insulin on CYP2E1, 2B, 3A and 4A expression. |
| 738 | 9402951 | Maintaining primary rat hepatocytes in culture in the absence of insulin for 48, 72, or 96 h increased CYP2E1 mRNA levels 5-, 11-, and 4-fold, respectively, relative to cells maintained in the presence of the standard concentration of 1 microM insulin. |
| 739 | 9402951 | In contrast, CYP2B mRNA levels increased only approximately 2-fold in the absence of insulin, when compared with the presence of 1 microM insulin. |
| 740 | 9402951 | CYP2E1 and 2B protein levels were increased 6.7- and 3.8-fold, respectively, in cells cultured for 96 h in the absence of insulin as compared with those cultured in medium containing 1 microM insulin. |
| 741 | 9402951 | Concentration-response studies revealed that decreasing the concentration of insulin below 10 nM (i.e. 1 nM, 0.1 nM, no insulin) increased CYP2E1 mRNA levels 4-, 7-, and 11-fold, respectively. |
| 742 | 9402951 | As CYP3A and 4A expression is also elevated in diabetic rats, the effects of insulin on these P450s was also examined. |
| 743 | 9402951 | CYP3A mRNA levels were unaltered and CYP4A mRNA levels were decreased marginally (approximately 50%) by the absence of insulin relative to levels in cells cultured in the presence of 1 microM insulin over 96 h in culture. |
| 744 | 9402951 | The results of this study provide evidence that insulin itself, in the absence of other diabetes-induced metabolic or hormonal alterations, affects CYP2E1 and 2B, but not CYP3A or 4A, expression in primary cultured rat hepatocytes. |
| 745 | 9402951 | Furthermore, CYP2E1 expression is differentially regulated by insulin relative to CYP2B, 3A or 4A. |
| 746 | 9402951 | This study also demonstrates that decreasing the concentration of insulin in the culture medium provides a method by which CYP2E1 levels can be increased in primary cultured hepatocytes to facilitate mechanistic studies on the regulation of CYP2E1 expression. |
| 747 | 9402951 | Insulin effects on CYP2E1, 2B, 3A, and 4A expression in primary cultured rat hepatocytes. |
| 748 | 9402951 | Although hyperketonemia and/or altered growth hormone secretion caused by diabetes have been implicated in enhanced CYP2E1, 2B, 3A and 4A expression, the effect of insulin on hepatic P450 expression, in the absence of associated metabolic/hormonal alterations, remains unknown. |
| 749 | 9402951 | Dispos., 23:681, 1995) to express stable and inducible CYP2E1 mRNA and protein levels, and provide an excellent system for mechanistic examination of the effect of insulin on CYP2E1, 2B, 3A and 4A expression. |
| 750 | 9402951 | Maintaining primary rat hepatocytes in culture in the absence of insulin for 48, 72, or 96 h increased CYP2E1 mRNA levels 5-, 11-, and 4-fold, respectively, relative to cells maintained in the presence of the standard concentration of 1 microM insulin. |
| 751 | 9402951 | In contrast, CYP2B mRNA levels increased only approximately 2-fold in the absence of insulin, when compared with the presence of 1 microM insulin. |
| 752 | 9402951 | CYP2E1 and 2B protein levels were increased 6.7- and 3.8-fold, respectively, in cells cultured for 96 h in the absence of insulin as compared with those cultured in medium containing 1 microM insulin. |
| 753 | 9402951 | Concentration-response studies revealed that decreasing the concentration of insulin below 10 nM (i.e. 1 nM, 0.1 nM, no insulin) increased CYP2E1 mRNA levels 4-, 7-, and 11-fold, respectively. |
| 754 | 9402951 | As CYP3A and 4A expression is also elevated in diabetic rats, the effects of insulin on these P450s was also examined. |
| 755 | 9402951 | CYP3A mRNA levels were unaltered and CYP4A mRNA levels were decreased marginally (approximately 50%) by the absence of insulin relative to levels in cells cultured in the presence of 1 microM insulin over 96 h in culture. |
| 756 | 9402951 | The results of this study provide evidence that insulin itself, in the absence of other diabetes-induced metabolic or hormonal alterations, affects CYP2E1 and 2B, but not CYP3A or 4A, expression in primary cultured rat hepatocytes. |
| 757 | 9402951 | Furthermore, CYP2E1 expression is differentially regulated by insulin relative to CYP2B, 3A or 4A. |
| 758 | 9402951 | This study also demonstrates that decreasing the concentration of insulin in the culture medium provides a method by which CYP2E1 levels can be increased in primary cultured hepatocytes to facilitate mechanistic studies on the regulation of CYP2E1 expression. |
| 759 | 9449216 | Estrogen biosynthesis is a critical factor during pregnancy and is carried out in the placenta via aromatase (cytochrome P450 19A1), which catalyzes the conversion of C-19 androgens to C-18 estrogens. |
| 760 | 9449216 | Previous studies have shown that hormones such as insulin-like growth factors and insulin regulate aromatase activity when studied in vitro. |
| 761 | 9449216 | To this end, we measured the production of 19-hydroxyandrostenedione, 19-oxoadrostenedione and estrone in 30 placental tissues from diabetic patients, using [7-3H]androst-4-ene-3,17-dione as a model substrate for aromatase (P450 19A1). |
| 762 | 9449216 | Additionally, NADPH P450-reductase levels were measured in these same tissues to determine whether alterations in this enzyme necessary for aromatase activity could be affected by diabetes. |
| 763 | 9449216 | Estrogen biosynthesis is a critical factor during pregnancy and is carried out in the placenta via aromatase (cytochrome P450 19A1), which catalyzes the conversion of C-19 androgens to C-18 estrogens. |
| 764 | 9449216 | Previous studies have shown that hormones such as insulin-like growth factors and insulin regulate aromatase activity when studied in vitro. |
| 765 | 9449216 | To this end, we measured the production of 19-hydroxyandrostenedione, 19-oxoadrostenedione and estrone in 30 placental tissues from diabetic patients, using [7-3H]androst-4-ene-3,17-dione as a model substrate for aromatase (P450 19A1). |
| 766 | 9449216 | Additionally, NADPH P450-reductase levels were measured in these same tissues to determine whether alterations in this enzyme necessary for aromatase activity could be affected by diabetes. |
| 767 | 9449216 | Estrogen biosynthesis is a critical factor during pregnancy and is carried out in the placenta via aromatase (cytochrome P450 19A1), which catalyzes the conversion of C-19 androgens to C-18 estrogens. |
| 768 | 9449216 | Previous studies have shown that hormones such as insulin-like growth factors and insulin regulate aromatase activity when studied in vitro. |
| 769 | 9449216 | To this end, we measured the production of 19-hydroxyandrostenedione, 19-oxoadrostenedione and estrone in 30 placental tissues from diabetic patients, using [7-3H]androst-4-ene-3,17-dione as a model substrate for aromatase (P450 19A1). |
| 770 | 9449216 | Additionally, NADPH P450-reductase levels were measured in these same tissues to determine whether alterations in this enzyme necessary for aromatase activity could be affected by diabetes. |
| 771 | 9464448 | Although the identity of endothelium-derived hyperpolarizing factor (EDHF) remains to be established, cytochrome P450 (CYP)-dependent metabolites of arachidonic acid (AA), namely, the epoxides, fulfill several of the criteria required for consideration as putative mediators of endothelium-dependent hyperpolarization. |
| 772 | 9466088 | SSRIs have fewer drug interactions than older antidepressants, and even the SSRI inhibition of hepatic cytochrome P450 enzymes has proven only very infrequently to be of clinical importance. |
| 773 | 9467831 | Cytochrome P450-dependent oxidation and glutathione conjugation of xenobiotics in alloxan-induced diabetic rat. |
| 774 | 9467831 | The status of cytochrome P450-dependent oxidative biotransformation of aminopyrine and benzo(a)pyrene (Phase I reaction) and glutathione S-transferase (GST) catalyzed conjugation with 1-chloro-2,4-dinitrobenzene (CDNB) (Phase II reaction) was evaluated in diabetic rats sacrificed 3 weeks after alloxan treatment (2 doses of 75 mg/kg at an interval of 48 h, i.p.). |
| 775 | 9467831 | Cytochrome P450-dependent oxidation and glutathione conjugation of xenobiotics in alloxan-induced diabetic rat. |
| 776 | 9467831 | The status of cytochrome P450-dependent oxidative biotransformation of aminopyrine and benzo(a)pyrene (Phase I reaction) and glutathione S-transferase (GST) catalyzed conjugation with 1-chloro-2,4-dinitrobenzene (CDNB) (Phase II reaction) was evaluated in diabetic rats sacrificed 3 weeks after alloxan treatment (2 doses of 75 mg/kg at an interval of 48 h, i.p.). |
| 777 | 9519715 | Reduced glutathione, inhibitors of cytochrome P-450, and monoaminooxidases A and B blocked this Ca2+ mobilization. |
| 778 | 9519715 | It is concluded that the mechanism of RX871024-induced Ca2+ mobilization from intracellular stores involves changes in the oxidation/reduction state of the pancreatic beta-cell and may be controlled by cytochrome P-450. |
| 779 | 9519715 | Reduced glutathione, inhibitors of cytochrome P-450, and monoaminooxidases A and B blocked this Ca2+ mobilization. |
| 780 | 9519715 | It is concluded that the mechanism of RX871024-induced Ca2+ mobilization from intracellular stores involves changes in the oxidation/reduction state of the pancreatic beta-cell and may be controlled by cytochrome P-450. |
| 781 | 9531526 | Effects of gestational and overt diabetes on human placental cytochromes P450 and glutathione S-transferase. |
| 782 | 9531526 | Animal and in vivo studies have observed that the presence of diabetes alters the expression of hepatic metabolizing enzymes (cytochrome P450 and glutathione S-transferase); however, it is unknown whether similar alterations occur in the human placenta. |
| 783 | 9531526 | To evaluate whether diabetes has any effect of placental xenobiotic metabolizing activity, the catalytic activities of 7-ethoxyresorufin O-deethylation (EROD, CYP1A1), chlorzoxazone 6-hydroxylation (CYP2E1), dextromethorphan N-demethylation (CYP3A4), dextromethorphan O-demethylation (CYP2D6), and 1-chloro-2, 4-dinitrobenzene (CDNB) conjugation with glutathione (glutathione S-transferase, GST) from placentas of diet (class A1) and insulin-dependent (class A2) gestational diabetics and overt diabetics were compared with matched controls. |
| 784 | 9531526 | In contrast to that observed with CYP1A1, a small but statistically significant reduction in GST activity was noted in overt diabetics as compared with their matched controls and gestational diabetics. |
| 785 | 9531526 | GST protein was detectable in all tissues studied, but no CYP protein could be detected in any of the tissues. |
| 786 | 9531526 | Effects of gestational and overt diabetes on human placental cytochromes P450 and glutathione S-transferase. |
| 787 | 9531526 | Animal and in vivo studies have observed that the presence of diabetes alters the expression of hepatic metabolizing enzymes (cytochrome P450 and glutathione S-transferase); however, it is unknown whether similar alterations occur in the human placenta. |
| 788 | 9531526 | To evaluate whether diabetes has any effect of placental xenobiotic metabolizing activity, the catalytic activities of 7-ethoxyresorufin O-deethylation (EROD, CYP1A1), chlorzoxazone 6-hydroxylation (CYP2E1), dextromethorphan N-demethylation (CYP3A4), dextromethorphan O-demethylation (CYP2D6), and 1-chloro-2, 4-dinitrobenzene (CDNB) conjugation with glutathione (glutathione S-transferase, GST) from placentas of diet (class A1) and insulin-dependent (class A2) gestational diabetics and overt diabetics were compared with matched controls. |
| 789 | 9531526 | In contrast to that observed with CYP1A1, a small but statistically significant reduction in GST activity was noted in overt diabetics as compared with their matched controls and gestational diabetics. |
| 790 | 9531526 | GST protein was detectable in all tissues studied, but no CYP protein could be detected in any of the tissues. |
| 791 | 9569450 | It is suggested that an isozyme of cytochrome P450 that appears in diabetic rats might be responsible for altered toxicity of cadmium. |
| 792 | 9620105 | It induces cytochrome P450 isoenzyme 3A4, although few drug interactions have been identified to date. |
| 793 | 9652687 | The catalytic region of HIV-1 protease, to which protease inhibitors bind, has approximately 60% homology to regions within two proteins that regulate lipid metabolism: cytoplasmic retinoic-acid binding protein type 1 (CRABP-1) and low density lipoprotein-receptor-related protein (LRP). |
| 794 | 9652687 | We hypothesise that protease inhibitors inhibit CRABP-1-modified, and cytochrome P450 3A-mediated synthesis of cis-9-retinoic acid, a key activator of the retinoid X receptor; and peroxisome proliferator activated receptor type gamma (PPAR-gamma) heterodimer, an adipocyte receptor that regulates peripheral adipocyte differentiation and apoptosis. |
| 795 | 9652687 | Protease-inhibitor binding to LRP would impair hepatic chylomicron uptake and triglyceride clearance by the endothelial LRP-lipoprotein lipase complex. |
| 796 | 9731699 | IRE-ABP (insulin response element-A binding protein), an SRY-like protein, inhibits C/EBPalpha (CCAAT/enhancer-binding protein alpha)-stimulated expression of the sex-specific cytochrome P450 2C12 gene. |
| 797 | 9731699 | In primary hepatocytes, overexpression of an insulin response element-A binding protein (IRE-ABP), a member of the SRY family of high-mobility group (HMG) proteins, inhibits CCAAT/enhancer-binding protein alpha (C/EBPalpha)-mediated activation of the female-specific cytochrome P450 2C12 (CYP2C12) gene, but not the male-specific cytochrome P450 2C11 (CYP2C11) gene. |
| 798 | 9731699 | Taken together, our findings suggest that SRY-like proteins can bind to a subset of sequences recognized by the C/EBP family of DNA-binding proteins and modulate gene transcription in a context-specific manner. |
| 799 | 9731699 | IRE-ABP (insulin response element-A binding protein), an SRY-like protein, inhibits C/EBPalpha (CCAAT/enhancer-binding protein alpha)-stimulated expression of the sex-specific cytochrome P450 2C12 gene. |
| 800 | 9731699 | In primary hepatocytes, overexpression of an insulin response element-A binding protein (IRE-ABP), a member of the SRY family of high-mobility group (HMG) proteins, inhibits CCAAT/enhancer-binding protein alpha (C/EBPalpha)-mediated activation of the female-specific cytochrome P450 2C12 (CYP2C12) gene, but not the male-specific cytochrome P450 2C11 (CYP2C11) gene. |
| 801 | 9731699 | Taken together, our findings suggest that SRY-like proteins can bind to a subset of sequences recognized by the C/EBP family of DNA-binding proteins and modulate gene transcription in a context-specific manner. |
| 802 | 9743237 | Exposure to XO/HX also affected other signal transduction mechanisms involved in endothelial Ca2+ signaling, such as microsomal cytochrome P450 epoxygenase and membrane hyperpolarization to Ca2+ store depletion with thapsigargin (+103% and +48%, respectively) and tyrosine kinase activity (+97%). |
| 803 | 9794154 | Cytochrome P450 2E1 activity in diabetic and obese patients as assessed by chlorzoxazone hydroxylation. |
| 804 | 9794154 | Cytochrome P450 2E1 (CYP2E1) is a phase I detoxification enzyme, which is induced by chronic alcohol consumption. |
| 805 | 9794154 | Even though the glucidic parameters were highly disturbed (mean fasting glycemia > 7.9 mmol/L, post prandial glycemia > 12.2 mmol/L and fructosamine > 326 mumol/L), CYP2E1 activity was not enhanced either in insulin-dependent diabetics (IDDs, n = 7) nor in non-obese non-insulin-dependent diabetics (NIDDs, n = 15) when compared to controls (n = 42) (0.21 +/- 0.03, 0.33 +/- 0.03 and 0.30 +/- 0.02, respectively, mean +/- SEM). |
| 806 | 9794154 | In obese patients, with (n = 13) or without (n = 17) NIDD mellitus, CYP2E1 activity was increased by a mean of 40% when compared to controls. |
| 807 | 9794154 | Cytochrome P450 2E1 activity in diabetic and obese patients as assessed by chlorzoxazone hydroxylation. |
| 808 | 9794154 | Cytochrome P450 2E1 (CYP2E1) is a phase I detoxification enzyme, which is induced by chronic alcohol consumption. |
| 809 | 9794154 | Even though the glucidic parameters were highly disturbed (mean fasting glycemia > 7.9 mmol/L, post prandial glycemia > 12.2 mmol/L and fructosamine > 326 mumol/L), CYP2E1 activity was not enhanced either in insulin-dependent diabetics (IDDs, n = 7) nor in non-obese non-insulin-dependent diabetics (NIDDs, n = 15) when compared to controls (n = 42) (0.21 +/- 0.03, 0.33 +/- 0.03 and 0.30 +/- 0.02, respectively, mean +/- SEM). |
| 810 | 9794154 | In obese patients, with (n = 13) or without (n = 17) NIDD mellitus, CYP2E1 activity was increased by a mean of 40% when compared to controls. |
| 811 | 9827545 | Genotyping of human cytochrome P450 2A6 (CYP2A6), a nicotine C-oxidase. |
| 812 | 9827545 | Cytochrome P450 2A6 (CYP2A6) is a polymorphic enzyme responsible for the oxidation of certain precarcinogens and drugs and is the major nicotine C-oxidase. |
| 813 | 9827545 | Genotyping of human cytochrome P450 2A6 (CYP2A6), a nicotine C-oxidase. |
| 814 | 9827545 | Cytochrome P450 2A6 (CYP2A6) is a polymorphic enzyme responsible for the oxidation of certain precarcinogens and drugs and is the major nicotine C-oxidase. |
| 815 | 9888542 | OB protein leptin inhibits the secretion of cortisol in primary cultures of bovine adrenocortical cells and down-regulates 17alpha-hydroxylase cytochrome P450 mRNA expression. |
| 816 | 9888542 | To analyze if leptin regulates other major enzymes involved in adrenal steroidogenesis we tested its effect on mRNA expression for two further key enzymes, C21-hydroxylase (P450C21) and side-chain cleavage enzyme (P450SCC). |
| 817 | 9888542 | Addition of leptin led to a reduction of ACTH-stimulated mRNA accumulation of 73% for P450C21 and of 45% for P450SCC. |
| 818 | 9890957 | An effect mediated via Ca2+-independent phospholipase A2 and protein kinase C-dependent phosphorylation of the alpha-subunit. |
| 819 | 9890957 | This effect, like that of glucose, was blocked by nordihydroguaiaretic acid, a selective inhibitor of the lipooxygenase metabolic pathway, but not by inhibitors of the cyclooxygenase or cytochrome P450-monooxygenase pathways. |
| 820 | 9893876 | However, barbiturates as well as phenytoin do not influence the metabolism of sevoflurane because these agents do not induce the major hepatic defluorinating enzyme cytochrome P450 2E1. |
| 821 | 9893876 | Obesity, untreated diabetes mellitus and alcohol abuse increase the hepatic content and activity of cytochrome P450 2E1 and therefore enhanced anaesthetic defluorination is to be suspected. |
| 822 | 9893876 | However, barbiturates as well as phenytoin do not influence the metabolism of sevoflurane because these agents do not induce the major hepatic defluorinating enzyme cytochrome P450 2E1. |
| 823 | 9893876 | Obesity, untreated diabetes mellitus and alcohol abuse increase the hepatic content and activity of cytochrome P450 2E1 and therefore enhanced anaesthetic defluorination is to be suspected. |
| 824 | 10049703 | Hepatic levels of the cytochrome P450 (CYP) proteins 2E1 and 4A are often increased in obesity, diabetes and fasting. |
| 825 | 10049703 | In order to more fully characterize the regulation of CYP2E1 and CYP4A in obesity and obesity-related (type II) diabetes, we analyzed the hepatic expression of CYP2E1 and CYP4A in ob/ob mice which are leptin deficient, and fa/fa Zucker rats which have defective leptin receptor function. |
| 826 | 10049703 | Further, they implicate leptin receptor signaling as a factor that may modulate expression of CYP gene products involved in fatty acid oxidation. |
| 827 | 10094576 | Characterization of cytochrome P450 and glutathione S-transferase activity and expression in male and female ob/ob mice. |
| 828 | 10215695 | Insulin differentially affects xenobiotic-enhanced, cytochrome P-450 (CYP)2E1, CYP2B, CYP3A, and CYP4A expression in primary cultured rat hepatocytes. |
| 829 | 10215695 | Uncontrolled diabetes results in enhanced expression of cytochrome P-450 (CYP)2E1, CYP2B, CYP3A, and CYP4A. |
| 830 | 10215695 | Because of the simultaneous and confounding metabolic and hormonal changes that occur in vivo as a consequence of diabetes, primary cultured rat hepatocytes provide an excellent model system for examination of the effects of insulin on P-450 expression and on xenobiotic-mediated P-450 expression. |
| 831 | 10215695 | In the present study, we examined the effects of insulin on pyridine-, phenobarbital-, and ciprofibrate-mediated expression of CYP2E1, CYP2B, CYP3A, and CYP4A in primary cultured rat hepatocytes. |
| 832 | 10215695 | Pyridine addition to primary rat hepatocytes cultured in the presence of 1 nM insulin or in the absence of insulin resulted in a 3.5-fold and 3-fold enhancement in CYP2E1 protein expression, respectively, in the absence of any pyridine-mediated increase in mRNA expression. |
| 833 | 10215695 | Thus, the fold-induction of CYP2E1 protein in response to pyridine was 1.5- to 1.8-fold greater in either the absence of insulin or in the presence of 1 nM insulin, respectively, than that monitored in the presence of 1 microM insulin. |
| 834 | 10215695 | To examine whether insulin effects on xenobiotic-mediated CYP2E1 expression were selective, insulin effects on xenobiotic-mediated expression of transcriptionally regulated CYP2B, CYP3A, and CYP4A were examined. |
| 835 | 10215695 | Pyridine- or phenobarbital-mediated induction of CYP2B mRNA and protein expression in hepatocytes was suppressed by as much as 80% at lower insulin levels (0 and 1 nM), relative to the level monitored in the presence of 1 microM insulin. |
| 836 | 10215695 | Omitting insulin from the medium resulted in a 50% decrease in CYP3A mRNA levels in response to phenobarbital treatment and a 30% decrease in CYP4A mRNA levels in response to ciprofibrate treatment, relative to the level obtained in response to these treatments in the presence of 1 microM insulin. |
| 837 | 10215695 | The results of this study demonstrate that decreasing the insulin level in the primary hepatocyte culture medium enhanced xenobiotic-mediated CYP2E1 expression, whereas lower insulin levels suppressed xenobiotic-mediated CYP2B, CYP3A, and CYP4A expression in this cell culture system. |
| 838 | 10215695 | Insulin differentially affects xenobiotic-enhanced, cytochrome P-450 (CYP)2E1, CYP2B, CYP3A, and CYP4A expression in primary cultured rat hepatocytes. |
| 839 | 10215695 | Uncontrolled diabetes results in enhanced expression of cytochrome P-450 (CYP)2E1, CYP2B, CYP3A, and CYP4A. |
| 840 | 10215695 | Because of the simultaneous and confounding metabolic and hormonal changes that occur in vivo as a consequence of diabetes, primary cultured rat hepatocytes provide an excellent model system for examination of the effects of insulin on P-450 expression and on xenobiotic-mediated P-450 expression. |
| 841 | 10215695 | In the present study, we examined the effects of insulin on pyridine-, phenobarbital-, and ciprofibrate-mediated expression of CYP2E1, CYP2B, CYP3A, and CYP4A in primary cultured rat hepatocytes. |
| 842 | 10215695 | Pyridine addition to primary rat hepatocytes cultured in the presence of 1 nM insulin or in the absence of insulin resulted in a 3.5-fold and 3-fold enhancement in CYP2E1 protein expression, respectively, in the absence of any pyridine-mediated increase in mRNA expression. |
| 843 | 10215695 | Thus, the fold-induction of CYP2E1 protein in response to pyridine was 1.5- to 1.8-fold greater in either the absence of insulin or in the presence of 1 nM insulin, respectively, than that monitored in the presence of 1 microM insulin. |
| 844 | 10215695 | To examine whether insulin effects on xenobiotic-mediated CYP2E1 expression were selective, insulin effects on xenobiotic-mediated expression of transcriptionally regulated CYP2B, CYP3A, and CYP4A were examined. |
| 845 | 10215695 | Pyridine- or phenobarbital-mediated induction of CYP2B mRNA and protein expression in hepatocytes was suppressed by as much as 80% at lower insulin levels (0 and 1 nM), relative to the level monitored in the presence of 1 microM insulin. |
| 846 | 10215695 | Omitting insulin from the medium resulted in a 50% decrease in CYP3A mRNA levels in response to phenobarbital treatment and a 30% decrease in CYP4A mRNA levels in response to ciprofibrate treatment, relative to the level obtained in response to these treatments in the presence of 1 microM insulin. |
| 847 | 10215695 | The results of this study demonstrate that decreasing the insulin level in the primary hepatocyte culture medium enhanced xenobiotic-mediated CYP2E1 expression, whereas lower insulin levels suppressed xenobiotic-mediated CYP2B, CYP3A, and CYP4A expression in this cell culture system. |
| 848 | 10215695 | Insulin differentially affects xenobiotic-enhanced, cytochrome P-450 (CYP)2E1, CYP2B, CYP3A, and CYP4A expression in primary cultured rat hepatocytes. |
| 849 | 10215695 | Uncontrolled diabetes results in enhanced expression of cytochrome P-450 (CYP)2E1, CYP2B, CYP3A, and CYP4A. |
| 850 | 10215695 | Because of the simultaneous and confounding metabolic and hormonal changes that occur in vivo as a consequence of diabetes, primary cultured rat hepatocytes provide an excellent model system for examination of the effects of insulin on P-450 expression and on xenobiotic-mediated P-450 expression. |
| 851 | 10215695 | In the present study, we examined the effects of insulin on pyridine-, phenobarbital-, and ciprofibrate-mediated expression of CYP2E1, CYP2B, CYP3A, and CYP4A in primary cultured rat hepatocytes. |
| 852 | 10215695 | Pyridine addition to primary rat hepatocytes cultured in the presence of 1 nM insulin or in the absence of insulin resulted in a 3.5-fold and 3-fold enhancement in CYP2E1 protein expression, respectively, in the absence of any pyridine-mediated increase in mRNA expression. |
| 853 | 10215695 | Thus, the fold-induction of CYP2E1 protein in response to pyridine was 1.5- to 1.8-fold greater in either the absence of insulin or in the presence of 1 nM insulin, respectively, than that monitored in the presence of 1 microM insulin. |
| 854 | 10215695 | To examine whether insulin effects on xenobiotic-mediated CYP2E1 expression were selective, insulin effects on xenobiotic-mediated expression of transcriptionally regulated CYP2B, CYP3A, and CYP4A were examined. |
| 855 | 10215695 | Pyridine- or phenobarbital-mediated induction of CYP2B mRNA and protein expression in hepatocytes was suppressed by as much as 80% at lower insulin levels (0 and 1 nM), relative to the level monitored in the presence of 1 microM insulin. |
| 856 | 10215695 | Omitting insulin from the medium resulted in a 50% decrease in CYP3A mRNA levels in response to phenobarbital treatment and a 30% decrease in CYP4A mRNA levels in response to ciprofibrate treatment, relative to the level obtained in response to these treatments in the presence of 1 microM insulin. |
| 857 | 10215695 | The results of this study demonstrate that decreasing the insulin level in the primary hepatocyte culture medium enhanced xenobiotic-mediated CYP2E1 expression, whereas lower insulin levels suppressed xenobiotic-mediated CYP2B, CYP3A, and CYP4A expression in this cell culture system. |
| 858 | 10215695 | Insulin differentially affects xenobiotic-enhanced, cytochrome P-450 (CYP)2E1, CYP2B, CYP3A, and CYP4A expression in primary cultured rat hepatocytes. |
| 859 | 10215695 | Uncontrolled diabetes results in enhanced expression of cytochrome P-450 (CYP)2E1, CYP2B, CYP3A, and CYP4A. |
| 860 | 10215695 | Because of the simultaneous and confounding metabolic and hormonal changes that occur in vivo as a consequence of diabetes, primary cultured rat hepatocytes provide an excellent model system for examination of the effects of insulin on P-450 expression and on xenobiotic-mediated P-450 expression. |
| 861 | 10215695 | In the present study, we examined the effects of insulin on pyridine-, phenobarbital-, and ciprofibrate-mediated expression of CYP2E1, CYP2B, CYP3A, and CYP4A in primary cultured rat hepatocytes. |
| 862 | 10215695 | Pyridine addition to primary rat hepatocytes cultured in the presence of 1 nM insulin or in the absence of insulin resulted in a 3.5-fold and 3-fold enhancement in CYP2E1 protein expression, respectively, in the absence of any pyridine-mediated increase in mRNA expression. |
| 863 | 10215695 | Thus, the fold-induction of CYP2E1 protein in response to pyridine was 1.5- to 1.8-fold greater in either the absence of insulin or in the presence of 1 nM insulin, respectively, than that monitored in the presence of 1 microM insulin. |
| 864 | 10215695 | To examine whether insulin effects on xenobiotic-mediated CYP2E1 expression were selective, insulin effects on xenobiotic-mediated expression of transcriptionally regulated CYP2B, CYP3A, and CYP4A were examined. |
| 865 | 10215695 | Pyridine- or phenobarbital-mediated induction of CYP2B mRNA and protein expression in hepatocytes was suppressed by as much as 80% at lower insulin levels (0 and 1 nM), relative to the level monitored in the presence of 1 microM insulin. |
| 866 | 10215695 | Omitting insulin from the medium resulted in a 50% decrease in CYP3A mRNA levels in response to phenobarbital treatment and a 30% decrease in CYP4A mRNA levels in response to ciprofibrate treatment, relative to the level obtained in response to these treatments in the presence of 1 microM insulin. |
| 867 | 10215695 | The results of this study demonstrate that decreasing the insulin level in the primary hepatocyte culture medium enhanced xenobiotic-mediated CYP2E1 expression, whereas lower insulin levels suppressed xenobiotic-mediated CYP2B, CYP3A, and CYP4A expression in this cell culture system. |
| 868 | 10215695 | Insulin differentially affects xenobiotic-enhanced, cytochrome P-450 (CYP)2E1, CYP2B, CYP3A, and CYP4A expression in primary cultured rat hepatocytes. |
| 869 | 10215695 | Uncontrolled diabetes results in enhanced expression of cytochrome P-450 (CYP)2E1, CYP2B, CYP3A, and CYP4A. |
| 870 | 10215695 | Because of the simultaneous and confounding metabolic and hormonal changes that occur in vivo as a consequence of diabetes, primary cultured rat hepatocytes provide an excellent model system for examination of the effects of insulin on P-450 expression and on xenobiotic-mediated P-450 expression. |
| 871 | 10215695 | In the present study, we examined the effects of insulin on pyridine-, phenobarbital-, and ciprofibrate-mediated expression of CYP2E1, CYP2B, CYP3A, and CYP4A in primary cultured rat hepatocytes. |
| 872 | 10215695 | Pyridine addition to primary rat hepatocytes cultured in the presence of 1 nM insulin or in the absence of insulin resulted in a 3.5-fold and 3-fold enhancement in CYP2E1 protein expression, respectively, in the absence of any pyridine-mediated increase in mRNA expression. |
| 873 | 10215695 | Thus, the fold-induction of CYP2E1 protein in response to pyridine was 1.5- to 1.8-fold greater in either the absence of insulin or in the presence of 1 nM insulin, respectively, than that monitored in the presence of 1 microM insulin. |
| 874 | 10215695 | To examine whether insulin effects on xenobiotic-mediated CYP2E1 expression were selective, insulin effects on xenobiotic-mediated expression of transcriptionally regulated CYP2B, CYP3A, and CYP4A were examined. |
| 875 | 10215695 | Pyridine- or phenobarbital-mediated induction of CYP2B mRNA and protein expression in hepatocytes was suppressed by as much as 80% at lower insulin levels (0 and 1 nM), relative to the level monitored in the presence of 1 microM insulin. |
| 876 | 10215695 | Omitting insulin from the medium resulted in a 50% decrease in CYP3A mRNA levels in response to phenobarbital treatment and a 30% decrease in CYP4A mRNA levels in response to ciprofibrate treatment, relative to the level obtained in response to these treatments in the presence of 1 microM insulin. |
| 877 | 10215695 | The results of this study demonstrate that decreasing the insulin level in the primary hepatocyte culture medium enhanced xenobiotic-mediated CYP2E1 expression, whereas lower insulin levels suppressed xenobiotic-mediated CYP2B, CYP3A, and CYP4A expression in this cell culture system. |
| 878 | 10215695 | Insulin differentially affects xenobiotic-enhanced, cytochrome P-450 (CYP)2E1, CYP2B, CYP3A, and CYP4A expression in primary cultured rat hepatocytes. |
| 879 | 10215695 | Uncontrolled diabetes results in enhanced expression of cytochrome P-450 (CYP)2E1, CYP2B, CYP3A, and CYP4A. |
| 880 | 10215695 | Because of the simultaneous and confounding metabolic and hormonal changes that occur in vivo as a consequence of diabetes, primary cultured rat hepatocytes provide an excellent model system for examination of the effects of insulin on P-450 expression and on xenobiotic-mediated P-450 expression. |
| 881 | 10215695 | In the present study, we examined the effects of insulin on pyridine-, phenobarbital-, and ciprofibrate-mediated expression of CYP2E1, CYP2B, CYP3A, and CYP4A in primary cultured rat hepatocytes. |
| 882 | 10215695 | Pyridine addition to primary rat hepatocytes cultured in the presence of 1 nM insulin or in the absence of insulin resulted in a 3.5-fold and 3-fold enhancement in CYP2E1 protein expression, respectively, in the absence of any pyridine-mediated increase in mRNA expression. |
| 883 | 10215695 | Thus, the fold-induction of CYP2E1 protein in response to pyridine was 1.5- to 1.8-fold greater in either the absence of insulin or in the presence of 1 nM insulin, respectively, than that monitored in the presence of 1 microM insulin. |
| 884 | 10215695 | To examine whether insulin effects on xenobiotic-mediated CYP2E1 expression were selective, insulin effects on xenobiotic-mediated expression of transcriptionally regulated CYP2B, CYP3A, and CYP4A were examined. |
| 885 | 10215695 | Pyridine- or phenobarbital-mediated induction of CYP2B mRNA and protein expression in hepatocytes was suppressed by as much as 80% at lower insulin levels (0 and 1 nM), relative to the level monitored in the presence of 1 microM insulin. |
| 886 | 10215695 | Omitting insulin from the medium resulted in a 50% decrease in CYP3A mRNA levels in response to phenobarbital treatment and a 30% decrease in CYP4A mRNA levels in response to ciprofibrate treatment, relative to the level obtained in response to these treatments in the presence of 1 microM insulin. |
| 887 | 10215695 | The results of this study demonstrate that decreasing the insulin level in the primary hepatocyte culture medium enhanced xenobiotic-mediated CYP2E1 expression, whereas lower insulin levels suppressed xenobiotic-mediated CYP2B, CYP3A, and CYP4A expression in this cell culture system. |
| 888 | 10215695 | Insulin differentially affects xenobiotic-enhanced, cytochrome P-450 (CYP)2E1, CYP2B, CYP3A, and CYP4A expression in primary cultured rat hepatocytes. |
| 889 | 10215695 | Uncontrolled diabetes results in enhanced expression of cytochrome P-450 (CYP)2E1, CYP2B, CYP3A, and CYP4A. |
| 890 | 10215695 | Because of the simultaneous and confounding metabolic and hormonal changes that occur in vivo as a consequence of diabetes, primary cultured rat hepatocytes provide an excellent model system for examination of the effects of insulin on P-450 expression and on xenobiotic-mediated P-450 expression. |
| 891 | 10215695 | In the present study, we examined the effects of insulin on pyridine-, phenobarbital-, and ciprofibrate-mediated expression of CYP2E1, CYP2B, CYP3A, and CYP4A in primary cultured rat hepatocytes. |
| 892 | 10215695 | Pyridine addition to primary rat hepatocytes cultured in the presence of 1 nM insulin or in the absence of insulin resulted in a 3.5-fold and 3-fold enhancement in CYP2E1 protein expression, respectively, in the absence of any pyridine-mediated increase in mRNA expression. |
| 893 | 10215695 | Thus, the fold-induction of CYP2E1 protein in response to pyridine was 1.5- to 1.8-fold greater in either the absence of insulin or in the presence of 1 nM insulin, respectively, than that monitored in the presence of 1 microM insulin. |
| 894 | 10215695 | To examine whether insulin effects on xenobiotic-mediated CYP2E1 expression were selective, insulin effects on xenobiotic-mediated expression of transcriptionally regulated CYP2B, CYP3A, and CYP4A were examined. |
| 895 | 10215695 | Pyridine- or phenobarbital-mediated induction of CYP2B mRNA and protein expression in hepatocytes was suppressed by as much as 80% at lower insulin levels (0 and 1 nM), relative to the level monitored in the presence of 1 microM insulin. |
| 896 | 10215695 | Omitting insulin from the medium resulted in a 50% decrease in CYP3A mRNA levels in response to phenobarbital treatment and a 30% decrease in CYP4A mRNA levels in response to ciprofibrate treatment, relative to the level obtained in response to these treatments in the presence of 1 microM insulin. |
| 897 | 10215695 | The results of this study demonstrate that decreasing the insulin level in the primary hepatocyte culture medium enhanced xenobiotic-mediated CYP2E1 expression, whereas lower insulin levels suppressed xenobiotic-mediated CYP2B, CYP3A, and CYP4A expression in this cell culture system. |
| 898 | 10376448 | Autoantibodies to adrenal cytochrome P450 antigens in isolated Addison's disease and autoimmune polyendocrine syndrome type II. |
| 899 | 10376448 | Adrenal P450 enzymes 21-hydroxylase (21OH), 17alpha-hydroxylase (17OH) and side chain cleavage enzyme (SCC) represent major target antigens in adrenal autoimmunity. |
| 900 | 10376448 | Autoantibodies to adrenal cytochrome P450 antigens in isolated Addison's disease and autoimmune polyendocrine syndrome type II. |
| 901 | 10376448 | Adrenal P450 enzymes 21-hydroxylase (21OH), 17alpha-hydroxylase (17OH) and side chain cleavage enzyme (SCC) represent major target antigens in adrenal autoimmunity. |
| 902 | 10393316 | The P450s of the CYP7 and CYP8 families, except for CYP8A (prostacyclin synthase), catalyze the oxygenation of sterols from an alpha surface in the middle of the steroid skeleton. |
| 903 | 10393316 | These facts suggest that CYP8B is a P450 closely linked to those of the CYP7 family. |
| 904 | 10393316 | The P450s of the CYP7 and CYP8 families, except for CYP8A (prostacyclin synthase), catalyze the oxygenation of sterols from an alpha surface in the middle of the steroid skeleton. |
| 905 | 10393316 | These facts suggest that CYP8B is a P450 closely linked to those of the CYP7 family. |
| 906 | 10415922 | There are at least three modes of action of RX871024 in beta-cells: (1) RX871024 blocks the ATP-dependent, Ca(2+)-activated, and delayed rectifier K+ channel activity; (2) RX871024 causes mobilization of Ca2+ from thapsigargin-sensitive intracellular stores, the effect probably controlled by cytochrome P450; and (3) the stimulatory activity of RX871024 on insulin release involves interaction of the compound with the exocytotic machinery, unrelated to the changes in membrane potential and cytoplasmic-free Ca2+ concentration, whereas protein phosphorylation plays an important role in this process. |
| 907 | 10447556 | Benzene is a ubiquitous environmental pollutant primarily metabolized by a cytochrome P-450 (CYP-450) isoenzyme, CYP-450 IIE1. |
| 908 | 10456185 | We have found evidence that a polymorphism in the regulatory region of CYP11a (encoding P450 cholesterol side chain cleavage, also an important enzyme in the steroidogenic pathway) is associated with and linked to PCOS. |
| 909 | 10475154 | Pathohistological examination revealed a pheochromocytoma with positive immunostaining for interleukin-6 (IL-6) and negative immunostaining for ACTH, vasoactive intestinal polypeptide (VIP) and cytochrome P450, and with no signs of malignancy. |
| 910 | 10496299 | Troglitazone may enhance the activities of cytochrome P450 (CYP) 3A and/or transporter(s) thereby reducing the plasma concentrations of terfenadine, cyclosporin, atorvastatin and fexofenadine. |
| 911 | 10497147 | Troglitazone increases cytochrome P-450 3A protein and activity in primary cultures of human hepatocytes. |
| 912 | 10497147 | TRO is known to increase the activity of cytochrome P-450 (CYP) 3A in vivo. |
| 913 | 10497147 | We have investigated the effect of TRO on CYP3A protein content and the activity of CYP3A (as measured by the formation of 6beta-hydroxytestosterone formation) in primary cultures of human hepatocytes in comparison with rifampicin (RIF). |
| 914 | 10497147 | Troglitazone increases cytochrome P-450 3A protein and activity in primary cultures of human hepatocytes. |
| 915 | 10497147 | TRO is known to increase the activity of cytochrome P-450 (CYP) 3A in vivo. |
| 916 | 10497147 | We have investigated the effect of TRO on CYP3A protein content and the activity of CYP3A (as measured by the formation of 6beta-hydroxytestosterone formation) in primary cultures of human hepatocytes in comparison with rifampicin (RIF). |
| 917 | 10510156 | Characterization of the cytochrome P450 enzymes involved in the in vitro metabolism of rosiglitazone. |
| 918 | 10711628 | We studied the long-term effects of streptozotocin-induced diabetes on tissue-specific cytochrome P450 (CYP) and glutathione-dependent (GSH-dependent) xenobiotic metabolism in rats. |
| 919 | 10711628 | During diabetes an increased expression of CYP1A1, CYP2E1, and CYP4A1 isoenzymes was also seen by Western blot analysis. |
| 920 | 10711628 | A marked decrease (65%) in hepatic GSH content and glutathione S-transferase (GST) activity and an increase (about two-fold) in brain GSH and GST activity was observed in diabetic rats. |
| 921 | 10711628 | Karela-juice feeding, in general, reversed the effect of chronic diabetes on the modulation of both P450-dependent monooxygenase activities and GSH-dependent oxidative stress related LPO and GST activities. |
| 922 | 10711628 | We studied the long-term effects of streptozotocin-induced diabetes on tissue-specific cytochrome P450 (CYP) and glutathione-dependent (GSH-dependent) xenobiotic metabolism in rats. |
| 923 | 10711628 | During diabetes an increased expression of CYP1A1, CYP2E1, and CYP4A1 isoenzymes was also seen by Western blot analysis. |
| 924 | 10711628 | A marked decrease (65%) in hepatic GSH content and glutathione S-transferase (GST) activity and an increase (about two-fold) in brain GSH and GST activity was observed in diabetic rats. |
| 925 | 10711628 | Karela-juice feeding, in general, reversed the effect of chronic diabetes on the modulation of both P450-dependent monooxygenase activities and GSH-dependent oxidative stress related LPO and GST activities. |
| 926 | 10731667 | Insulin is a dominant suppressor of sterol 12 alpha-hydroxylase P450 (CYP8B) expression in rat liver: possible role of insulin in circadian rhythm of CYP8B. |
| 927 | 10731667 | The rhythm of CYP8B was the inverse of the circadian variation of serum insulin level and was similar to the circadian rhythm of glucose 6-phosphatase. |
| 928 | 10748653 | Carr suggests that such drugs should have this lipid-increasing effect because of their inhibition of low density lipoprotein-receptor-related protein, cytoplasmic retinoic-acid binding protein type 1 and P450 3A cytochrome. |
| 929 | 10748653 | According to another hypothesis Tumor necrosis factor-alpha, through inhibition of lipoprotein-lipase, would determine high fat-storage in the adipose tissue. |
| 930 | 10752642 | Effect of troglitazone on cytochrome P450 enzymes in primary cultures of human and rat hepatocytes. |
| 931 | 10752642 | Primary cultures of human hepatocytes were used to investigate the induction potential of troglitazone with respect to CYP3A4, CYP2B6 and CYP1A1/2. |
| 932 | 10752642 | Troglitazone increased CYP2B6 immunoreactive protein but did not significantly effect CYP1A1/2 activity, immunoreactive protein or mRNA. 3. |
| 933 | 10752642 | Troglitazone produced significant increases in CYP3A message, protein and activity in primary rat hepatocytes, a slight increase in CYP2B1/2 activity and no change in CYP1A1/2 message or activity. 4. |
| 934 | 10752642 | These results provide evidence that troglitazone can induce CYP3A and CYP2B enzymes while apparently not altering CYP1A. |
| 935 | 10752642 | Effect of troglitazone on cytochrome P450 enzymes in primary cultures of human and rat hepatocytes. |
| 936 | 10752642 | Primary cultures of human hepatocytes were used to investigate the induction potential of troglitazone with respect to CYP3A4, CYP2B6 and CYP1A1/2. |
| 937 | 10752642 | Troglitazone increased CYP2B6 immunoreactive protein but did not significantly effect CYP1A1/2 activity, immunoreactive protein or mRNA. 3. |
| 938 | 10752642 | Troglitazone produced significant increases in CYP3A message, protein and activity in primary rat hepatocytes, a slight increase in CYP2B1/2 activity and no change in CYP1A1/2 message or activity. 4. |
| 939 | 10752642 | These results provide evidence that troglitazone can induce CYP3A and CYP2B enzymes while apparently not altering CYP1A. |
| 940 | 10752642 | Effect of troglitazone on cytochrome P450 enzymes in primary cultures of human and rat hepatocytes. |
| 941 | 10752642 | Primary cultures of human hepatocytes were used to investigate the induction potential of troglitazone with respect to CYP3A4, CYP2B6 and CYP1A1/2. |
| 942 | 10752642 | Troglitazone increased CYP2B6 immunoreactive protein but did not significantly effect CYP1A1/2 activity, immunoreactive protein or mRNA. 3. |
| 943 | 10752642 | Troglitazone produced significant increases in CYP3A message, protein and activity in primary rat hepatocytes, a slight increase in CYP2B1/2 activity and no change in CYP1A1/2 message or activity. 4. |
| 944 | 10752642 | These results provide evidence that troglitazone can induce CYP3A and CYP2B enzymes while apparently not altering CYP1A. |
| 945 | 10752642 | Effect of troglitazone on cytochrome P450 enzymes in primary cultures of human and rat hepatocytes. |
| 946 | 10752642 | Primary cultures of human hepatocytes were used to investigate the induction potential of troglitazone with respect to CYP3A4, CYP2B6 and CYP1A1/2. |
| 947 | 10752642 | Troglitazone increased CYP2B6 immunoreactive protein but did not significantly effect CYP1A1/2 activity, immunoreactive protein or mRNA. 3. |
| 948 | 10752642 | Troglitazone produced significant increases in CYP3A message, protein and activity in primary rat hepatocytes, a slight increase in CYP2B1/2 activity and no change in CYP1A1/2 message or activity. 4. |
| 949 | 10752642 | These results provide evidence that troglitazone can induce CYP3A and CYP2B enzymes while apparently not altering CYP1A. |
| 950 | 10812837 | Polymorphism and the induction/inhibition of drug-metabolizing enzymes, such as cytochrome P450, aldehyde dehydrogenase (ALDH), glutathione S-transferase (GST), N-acetyltransferase (NAT), and NAD(P)H-quinone oxidoreductase (NQO1), were reviewed in relation to susceptibility to disease and to inter-individual difference in biological monitorings. |
| 951 | 10812837 | Investigation of such situations has generated data implicating GSTT1, GSTM1, NAT2, and NQO1 polymorphisms in biological monitoring of some chemicals; the ALDH2 polymorphism is the likely link between the genotype and the metabolism of low molecular aliphatic aldehydes. |
| 952 | 10814527 | Insulin sensitizer, troglitazone, directly inhibits aromatase activity in human ovarian granulosa cells. |
| 953 | 10814527 | Ovarian granulosa cells synthesize estrogens from androgens, which are catalyzed by aromatase cytochrome P450 (P450arom). |
| 954 | 10814527 | Troglitazone (Tro), one of the insulin-sensitizing compounds, thiazolidinediones (TZDs), is a ligand for peroxisome proliferator activated receptor gamma (PPARgamma) and is effective in the treatment of both non-insulin-dependent diabetes mellitus (NIDDM) as well as polycystic ovary syndrome (PCOS). |
| 955 | 10814527 | These results suggest that Tro directly inhibit the aromatase activity in human granulosa cells probably via nuclear receptor system PPARgamma:RXR heterodimer. |
| 956 | 10838356 | Effects of gestational and overt diabetes on placental cytochromes P450 and glutathione S-transferase. |
| 957 | 10838356 | Objective: Animal and in vivo human studies have observed that diabetes alters the expression of hepatic metabolizing cytochrome P450 (CYP) and glutathione S-transferase (GST) enzymes. |
| 958 | 10838356 | Our objective was to compare placental xenobiotic metabolizing activity in diabetics to matched non-diabetic controls to determine if the presence of diabetes alters placental xenobiotic metabolizing activity.Methods: The catalytic activities of 7-ethoxyresorufin-O-deethylation [EROD] (CYP1A1), chlorzoxazone 6-hydroxylation (CYP2E1), dextromethorphan N-demethylation (CYP3A4), dextromethorphan O-demethylation (CYP2D6), and 1-chloro-2,4-dinitrobenzene (CDNB) conjugation with glutathione (GST) from placentas of diet controlled (class A1) and insulin-dependent (class A2) gestational diabetics and overt diabetics were compared to matched controls.Results: No differences in EROD activity were observed among overt or gestational diabetics and their respectively matched controls. |
| 959 | 10838356 | Effects of gestational and overt diabetes on placental cytochromes P450 and glutathione S-transferase. |
| 960 | 10838356 | Objective: Animal and in vivo human studies have observed that diabetes alters the expression of hepatic metabolizing cytochrome P450 (CYP) and glutathione S-transferase (GST) enzymes. |
| 961 | 10838356 | Our objective was to compare placental xenobiotic metabolizing activity in diabetics to matched non-diabetic controls to determine if the presence of diabetes alters placental xenobiotic metabolizing activity.Methods: The catalytic activities of 7-ethoxyresorufin-O-deethylation [EROD] (CYP1A1), chlorzoxazone 6-hydroxylation (CYP2E1), dextromethorphan N-demethylation (CYP3A4), dextromethorphan O-demethylation (CYP2D6), and 1-chloro-2,4-dinitrobenzene (CDNB) conjugation with glutathione (GST) from placentas of diet controlled (class A1) and insulin-dependent (class A2) gestational diabetics and overt diabetics were compared to matched controls.Results: No differences in EROD activity were observed among overt or gestational diabetics and their respectively matched controls. |
| 962 | 11000659 | Modulation of cytochrome P-450 dependent monooxygenases in streptozotocin-induced diabetic hamster: I. |
| 963 | 11000659 | Effects of propofol on defluorination and cytochrome P-450 activities. |
| 964 | 11000659 | Modulation of cytochrome P-450 dependent monooxygenases in streptozotocin-induced diabetic hamster: I. |
| 965 | 11000659 | Effects of propofol on defluorination and cytochrome P-450 activities. |
| 966 | 11000668 | Modulation of cytochrome P450-dependent monooxygenases in streptozotocin-induced diabetic hamster: II. |
| 967 | 11000668 | Reverse role of insulin in P450 activity and defluorination. |
| 968 | 11000668 | Modulation of cytochrome P450-dependent monooxygenases in streptozotocin-induced diabetic hamster: II. |
| 969 | 11000668 | Reverse role of insulin in P450 activity and defluorination. |
| 970 | 11159615 | No evidence exists that pioglitazone induces hepatic cytochrome P450 isoform CYP3A4. |
| 971 | 11195057 | Cytochrome P450 metabolites of arachidonic acid in the control of renal function. |
| 972 | 11195057 | Recent studies indicate that arachidonic acid is primarily metabolized by cytochrome P450 enzymes of the 4A and 2C families in the kidney to 20-hydroxyeicosatetraenoic acid (HETE), epoxyeicosatrienoic acids (EETs) and dihydroxyeicosatrienoic acids. |
| 973 | 11195057 | There, they regulate sodium/potassium-ATPase activity and serve as second messengers for the natriuretic effects of dopamine, parathyroid hormone and angiotensin II. 20-HETE is also produced in the thick ascending loop of Henle. |
| 974 | 11195057 | The renal production of cytochrome P450 metabolites of arachidonic acid is altered in hypertension, diabetes, toxemia of pregnancy, and hepatorenal syndrome. |
| 975 | 11195057 | Given the importance of cytochrome P450 metabolites of arachidonic acid in the control of renal function, it is likely that changes in this system contribute to the abnormalities in renal function that are associated with many of these conditions. |
| 976 | 11195057 | Cytochrome P450 metabolites of arachidonic acid in the control of renal function. |
| 977 | 11195057 | Recent studies indicate that arachidonic acid is primarily metabolized by cytochrome P450 enzymes of the 4A and 2C families in the kidney to 20-hydroxyeicosatetraenoic acid (HETE), epoxyeicosatrienoic acids (EETs) and dihydroxyeicosatrienoic acids. |
| 978 | 11195057 | There, they regulate sodium/potassium-ATPase activity and serve as second messengers for the natriuretic effects of dopamine, parathyroid hormone and angiotensin II. 20-HETE is also produced in the thick ascending loop of Henle. |
| 979 | 11195057 | The renal production of cytochrome P450 metabolites of arachidonic acid is altered in hypertension, diabetes, toxemia of pregnancy, and hepatorenal syndrome. |
| 980 | 11195057 | Given the importance of cytochrome P450 metabolites of arachidonic acid in the control of renal function, it is likely that changes in this system contribute to the abnormalities in renal function that are associated with many of these conditions. |
| 981 | 11195057 | Cytochrome P450 metabolites of arachidonic acid in the control of renal function. |
| 982 | 11195057 | Recent studies indicate that arachidonic acid is primarily metabolized by cytochrome P450 enzymes of the 4A and 2C families in the kidney to 20-hydroxyeicosatetraenoic acid (HETE), epoxyeicosatrienoic acids (EETs) and dihydroxyeicosatrienoic acids. |
| 983 | 11195057 | There, they regulate sodium/potassium-ATPase activity and serve as second messengers for the natriuretic effects of dopamine, parathyroid hormone and angiotensin II. 20-HETE is also produced in the thick ascending loop of Henle. |
| 984 | 11195057 | The renal production of cytochrome P450 metabolites of arachidonic acid is altered in hypertension, diabetes, toxemia of pregnancy, and hepatorenal syndrome. |
| 985 | 11195057 | Given the importance of cytochrome P450 metabolites of arachidonic acid in the control of renal function, it is likely that changes in this system contribute to the abnormalities in renal function that are associated with many of these conditions. |
| 986 | 11195057 | Cytochrome P450 metabolites of arachidonic acid in the control of renal function. |
| 987 | 11195057 | Recent studies indicate that arachidonic acid is primarily metabolized by cytochrome P450 enzymes of the 4A and 2C families in the kidney to 20-hydroxyeicosatetraenoic acid (HETE), epoxyeicosatrienoic acids (EETs) and dihydroxyeicosatrienoic acids. |
| 988 | 11195057 | There, they regulate sodium/potassium-ATPase activity and serve as second messengers for the natriuretic effects of dopamine, parathyroid hormone and angiotensin II. 20-HETE is also produced in the thick ascending loop of Henle. |
| 989 | 11195057 | The renal production of cytochrome P450 metabolites of arachidonic acid is altered in hypertension, diabetes, toxemia of pregnancy, and hepatorenal syndrome. |
| 990 | 11195057 | Given the importance of cytochrome P450 metabolites of arachidonic acid in the control of renal function, it is likely that changes in this system contribute to the abnormalities in renal function that are associated with many of these conditions. |
| 991 | 11196419 | There is a progressive and concurrent increase of ACTH1-39 and cortisol (F) in the circulation of fetal sheep during the last 15-20 days of pregnancy (term, day 145-150) associated with increased expression of hypothalamic CRH pituitary POMC and adrenal ACTH receptor and steroidogenic enzymes, particularly P450 C17. |
| 992 | 11220287 | To date, rosiglitazone has been shown to have no reported cases of idiosyncratic drug reactions leading to jaundice or liver failure and no clinically significant drug interactions with cytochrome P450 3A4-metabolized drugs such as nifedipine. |
| 993 | 11223374 | In patients with the rare, recessively inherited type 1 APS (APS-1), characterized by the triad of chronic mucocutaneous moniliasis, hypoparathyroidism, and Addison's disease, primary amenorrhea (elevated pituitary gonadotropins) or oligomenorrhea and infertility are constant features. |
| 994 | 11223374 | These autoantibodies react with 3 P450 enzymes involved with steroidogenesis, namely, 21-hydroxylase (adrenal specific), 17 alpha-hydroxylase, and the side chain cleavage enzyme. |
| 995 | 11259542 | Regulation of hepatic cytochrome P450 2C11 via cAMP: implications for down-regulation in diabetes, fasting, and inflammation. |
| 996 | 11259542 | The effect of glucagon and its second messenger cAMP on cytochrome P450 2C11 (CYP2C11) expression was investigated in primary hepatocytes cultured on Matrigel. |
| 997 | 11259542 | These results suggest a role for glucagon in the down-regulation of CYP2C11 in diabetic rats, and provide a possible explanation for the known sensitivity of this cytochrome P450 to suppression in various stress and disease models. |
| 998 | 11259542 | Regulation of hepatic cytochrome P450 2C11 via cAMP: implications for down-regulation in diabetes, fasting, and inflammation. |
| 999 | 11259542 | The effect of glucagon and its second messenger cAMP on cytochrome P450 2C11 (CYP2C11) expression was investigated in primary hepatocytes cultured on Matrigel. |
| 1000 | 11259542 | These results suggest a role for glucagon in the down-regulation of CYP2C11 in diabetic rats, and provide a possible explanation for the known sensitivity of this cytochrome P450 to suppression in various stress and disease models. |
| 1001 | 11259542 | Regulation of hepatic cytochrome P450 2C11 via cAMP: implications for down-regulation in diabetes, fasting, and inflammation. |
| 1002 | 11259542 | The effect of glucagon and its second messenger cAMP on cytochrome P450 2C11 (CYP2C11) expression was investigated in primary hepatocytes cultured on Matrigel. |
| 1003 | 11259542 | These results suggest a role for glucagon in the down-regulation of CYP2C11 in diabetic rats, and provide a possible explanation for the known sensitivity of this cytochrome P450 to suppression in various stress and disease models. |
| 1004 | 11281188 | Both troglitazone and simvastatin are metabolized by cytochrome P-450 3A4. |
| 1005 | 11286146 | Inhibitors of cytochrome P-450 isoenzymes 3A4 and 2C19 should be used cautiously in patients taking cilostazol, and this drug is contraindicated in patients with congestive heart failure. |
| 1006 | 11449877 | There is a potential for interactions between nateglinide and medications affected by the cytochrome P-450 isoenzyme system. |
| 1007 | 11454726 | When male Sprague-Dawley rats (250-275 g) were maintained on diet restriction (DR, 35% of ad libitum fed rats, 21 days) the total hepatic microsomal cytochrome P450 (CYP450) was increased 2-fold along with a 4.6-fold increase in CYP2E1 protein, which corresponded with a 3-fold increase in CYP2E1 activity as measured by chlorzoxazone hydroxylation. |
| 1008 | 11454726 | CCl(4) (4 ml/kg i.p.), a known substrate of CYP2E1, caused lower liver injury and higher animal survival confirming inhibition of CYP2E1 by DAS pretreatment. |
| 1009 | 11465407 | Since limited information is available about alterations of cytochrome P450 levels in diabetic animals other than rat, expression of P450s in the liver and kidney of the streptozotocin (STZ)-induced diabetic mouse was investigated. 2. |
| 1010 | 11465407 | The results indicate that mouse P450s respond to insulin-dependent diabetes mellitus differently from those of the rat, and suggest that the expression of P450s in diabetes is not generally the same across animal species. |
| 1011 | 11465407 | Since limited information is available about alterations of cytochrome P450 levels in diabetic animals other than rat, expression of P450s in the liver and kidney of the streptozotocin (STZ)-induced diabetic mouse was investigated. 2. |
| 1012 | 11465407 | The results indicate that mouse P450s respond to insulin-dependent diabetes mellitus differently from those of the rat, and suggest that the expression of P450s in diabetes is not generally the same across animal species. |
| 1013 | 11469724 | Hepatic cytochrome P450 regulation in disease states. |
| 1014 | 11469724 | Hepatic cytochrome P450 (P450) enzyme activities and gene expression can be profoundly altered in disease states. |
| 1015 | 11469724 | Hepatic cytochrome P450 regulation in disease states. |
| 1016 | 11469724 | Hepatic cytochrome P450 (P450) enzyme activities and gene expression can be profoundly altered in disease states. |
| 1017 | 11499333 | Oral terbinafine, unlike itraconazole (a potent cytochrome P-450 [CYP] 3A4 inhibitor), has a relatively low potential for drug-drug interactions, making terbinafine a useful agent for the treatment of tinea infections in immunocompromised patients (e.g., those who are HIV positive and those with diabetes), who are likely to be receiving concomitant medications. |
| 1018 | 11594240 | It is metabolised by the hepatic cytochrome P450 enzyme system. |
| 1019 | 11735645 | It should be mentioned that troglitazone, unlike pioglitazone and rosiglitazone, induces the cytochrome P450 isoform 3A4, which is partly responsible for its metabolism, and may be prone to drug interactions. |
| 1020 | 11773611 | Recent studies have indicated that arachidonic acid is primarily metabolized by cytochrome P-450 (CYP) enzymes in the brain, lung, kidney, and peripheral vasculature to 20-hydroxyeicosatetraenoic acid (20-HETE) and epoxyeicosatrienoic acids (EETs) and that these compounds play critical roles in the regulation of renal, pulmonary, and cardiac function and vascular tone. |
| 1021 | 11811373 | Among the vasorelaxants are nitric oxide (NO), prostacyclin, various endothelium-derived hyperpolarizing factors (EDHFs, such as cytochrome P-450 monooxygenase metabolites of arachidonic acid like epoxyeicosatrienoic acids, and endocannabinoids), and C-type natriuretic peptide. |
| 1022 | 11826398 | Insulin signaling in the transcriptional and posttranscriptional regulation of CYP2E1 expression. |
| 1023 | 11826398 | Diabetes has been reported to increase the expression of cytochrome P450 (CYP) 2E1 messenger RNA (mRNA) and protein several-fold, and enhanced expression has been associated with elevated ketone bodies. |
| 1024 | 11826398 | Primary cultured rat hepatocytes were used to explore ketone body and insulin regulation of CYP2E1 expression. |
| 1025 | 11826398 | Insulin produced a concentration-dependent decrease in CYP2E1 mRNA levels, and insulin receptor immunoprecipitation showed a correspondence between receptor phosphorylation and the decrease in CYP2E1 mRNA levels at physiologic levels of insulin. |
| 1026 | 11826398 | The phosphatidylinositol 3-kinase (PI3-kinase) inhibitors wortmannin or LY294002 and rapamycin, an inhibitor of p70 S6 kinase phosphorylation, ameliorated the insulin-mediated decrease in CYP2E1 mRNA levels. |
| 1027 | 11826398 | Geldanamycin, which inhibits Src kinase, also abrogated the insulin-mediated decrease in CYP2E1 mRNA levels. |
| 1028 | 11826398 | In contrast, the protein kinase C (PKC) inhibitor bisindolylmaleimide, the mitogen-activated protein kinase kinase (MEK) inhibitor PD98059, and the p38 mitogen-activated protein (MAP) kinase inhibitor SB202190 did not affect the insulin-mediated decrease in CYP2E1. |
| 1029 | 11826398 | CYP2E1 mRNA half-life decreased from approximately 48 hours in the absence of insulin to approximately 15 hours at 10 nmol/L insulin, and this decrease was prevented by wortmannin. |
| 1030 | 11826398 | The half-life of CYP2B mRNA was increased by insulin, whereas that of CYP3A was unaffected. |
| 1031 | 11826398 | Analysis of CYP2E1 gene transcription using heterogeneous nuclear RNA (hnRNA) showed that insulin suppressed CYP2E1 transcription. |
| 1032 | 11826398 | In conclusion, these data show involvement of transcriptional and posttranscriptional mechanisms in the insulin-mediated regulation of CYP2E1 and implicate PI3-kinase, p70 S6 kinase, and Src kinase in mediating these effects. |
| 1033 | 11826398 | Insulin signaling in the transcriptional and posttranscriptional regulation of CYP2E1 expression. |
| 1034 | 11826398 | Diabetes has been reported to increase the expression of cytochrome P450 (CYP) 2E1 messenger RNA (mRNA) and protein several-fold, and enhanced expression has been associated with elevated ketone bodies. |
| 1035 | 11826398 | Primary cultured rat hepatocytes were used to explore ketone body and insulin regulation of CYP2E1 expression. |
| 1036 | 11826398 | Insulin produced a concentration-dependent decrease in CYP2E1 mRNA levels, and insulin receptor immunoprecipitation showed a correspondence between receptor phosphorylation and the decrease in CYP2E1 mRNA levels at physiologic levels of insulin. |
| 1037 | 11826398 | The phosphatidylinositol 3-kinase (PI3-kinase) inhibitors wortmannin or LY294002 and rapamycin, an inhibitor of p70 S6 kinase phosphorylation, ameliorated the insulin-mediated decrease in CYP2E1 mRNA levels. |
| 1038 | 11826398 | Geldanamycin, which inhibits Src kinase, also abrogated the insulin-mediated decrease in CYP2E1 mRNA levels. |
| 1039 | 11826398 | In contrast, the protein kinase C (PKC) inhibitor bisindolylmaleimide, the mitogen-activated protein kinase kinase (MEK) inhibitor PD98059, and the p38 mitogen-activated protein (MAP) kinase inhibitor SB202190 did not affect the insulin-mediated decrease in CYP2E1. |
| 1040 | 11826398 | CYP2E1 mRNA half-life decreased from approximately 48 hours in the absence of insulin to approximately 15 hours at 10 nmol/L insulin, and this decrease was prevented by wortmannin. |
| 1041 | 11826398 | The half-life of CYP2B mRNA was increased by insulin, whereas that of CYP3A was unaffected. |
| 1042 | 11826398 | Analysis of CYP2E1 gene transcription using heterogeneous nuclear RNA (hnRNA) showed that insulin suppressed CYP2E1 transcription. |
| 1043 | 11826398 | In conclusion, these data show involvement of transcriptional and posttranscriptional mechanisms in the insulin-mediated regulation of CYP2E1 and implicate PI3-kinase, p70 S6 kinase, and Src kinase in mediating these effects. |
| 1044 | 11856910 | Three major candidates are the epoxyeicosatrienoic acids, cytochrome P450 metabolites of arachidonic acid, potassium ion and hydrogen peroxide. |
| 1045 | 11985890 | Polycyclic aromatic hydrocarbons (PAHs) and N-nitrosamines (NNA) are mainly activated by cytochrome P450s, and their associated enzyme activities such as aryl hydrocarbon (benzo(a)pyrene) hydroxylase (AHH), N-nitrosdimethylamine N-demethylase I (NDMA-dI), NADPH-cytochrome C reductase, and detoxified by glutathione S-transferase (GST) and glutathione (GSH). |
| 1046 | 11985890 | Alloxan treatment increased the hepatic activity of cytochrome P450, NADPH-cytochrome C reductase, AHH, NDMA-dI, GST and GSH by 112, 122, 82, 99, 64 and 26%, respectively. |
| 1047 | 12044959 | The mechanism of dissociation of cortisol and DHEA synthesis in aging depends on another regulator of 17,20-lyase of cytochrome P450c17 such as cytochrome P450 reductase. |
| 1048 | 12044959 | We demonstrated significant decrease in cytochrome P450 reductase activity in bovine aged adrenal glands. |
| 1049 | 12044959 | We clarified the conversion of DHEA to estrone by cytochrome P450 aromatase in primary cultured human osteoblasts. |
| 1050 | 12044959 | The mechanism of dissociation of cortisol and DHEA synthesis in aging depends on another regulator of 17,20-lyase of cytochrome P450c17 such as cytochrome P450 reductase. |
| 1051 | 12044959 | We demonstrated significant decrease in cytochrome P450 reductase activity in bovine aged adrenal glands. |
| 1052 | 12044959 | We clarified the conversion of DHEA to estrone by cytochrome P450 aromatase in primary cultured human osteoblasts. |
| 1053 | 12044959 | The mechanism of dissociation of cortisol and DHEA synthesis in aging depends on another regulator of 17,20-lyase of cytochrome P450c17 such as cytochrome P450 reductase. |
| 1054 | 12044959 | We demonstrated significant decrease in cytochrome P450 reductase activity in bovine aged adrenal glands. |
| 1055 | 12044959 | We clarified the conversion of DHEA to estrone by cytochrome P450 aromatase in primary cultured human osteoblasts. |
| 1056 | 12062933 | We studied the effects of TRZ on the hepatotoxicity of carbon tetrachloride (CCl(4)) and acetaminophen (APAP) in rats, both of which exert their toxic effects through bioactivation associated with cytochrome P450 3A (CYP3A) and 2E1 (CYP2E1). |
| 1057 | 12062933 | Three weeks later, the rats were either sacrificed for an in vitro metabolism study or challenged with 0.50 g/kg CCl(4) p.o. or 0.75 g/kg APAP i.p.TRZ at 100 and 500 mg/kg/rat increased the CYP3A level as well as the testosterone 6beta-hydroxylation activities in liver microsomes, but did not affect CYP2E1. |
| 1058 | 12062933 | TRZ also enhanced APAP hepatotoxicity, as evidenced by significantly increased levels of alanine aminotransferase, aspartate aminotransferase and alpha-glutathione S-transferase in the plasma of rats, and by significantly low hepatic glutathione concentration. |
| 1059 | 12130701 | Effect of hyperinsulinemia and type 2 diabetes-like hyperglycemia on expression of hepatic cytochrome p450 and glutathione s-transferase isoforms in a New Zealand obese-derived mouse backcross population. |
| 1060 | 12130701 | In subgroups of a New Zealand obese mouse-derived backcross population with defined aberrations of glucose homeostasis, a comprehensive study of the hepatic expression of cytochrome P450 and glutathione S-transferase was performed. |
| 1061 | 12130701 | Three patterns of alterations in response to insulin resistance (normoglycemia/hyperinsulinemia) or diabetes (hyperglycemia/hypoinsulinemia) were observed: mRNA levels of Cyp2b9, Cyp3a16, Cyp4a14, and Gstt2 as assessed by Northern- and dot-blot analysis were increased markedly in liver from diabetic mice with no or only a slight increase in insulin resistant mice. |
| 1062 | 12130701 | Furthermore, expression of Cyp1a2, Cyp7b1, Gstm3, and Gstm6 was reduced in both diabetic and insulin resistant mice. |
| 1063 | 12130701 | Effect of hyperinsulinemia and type 2 diabetes-like hyperglycemia on expression of hepatic cytochrome p450 and glutathione s-transferase isoforms in a New Zealand obese-derived mouse backcross population. |
| 1064 | 12130701 | In subgroups of a New Zealand obese mouse-derived backcross population with defined aberrations of glucose homeostasis, a comprehensive study of the hepatic expression of cytochrome P450 and glutathione S-transferase was performed. |
| 1065 | 12130701 | Three patterns of alterations in response to insulin resistance (normoglycemia/hyperinsulinemia) or diabetes (hyperglycemia/hypoinsulinemia) were observed: mRNA levels of Cyp2b9, Cyp3a16, Cyp4a14, and Gstt2 as assessed by Northern- and dot-blot analysis were increased markedly in liver from diabetic mice with no or only a slight increase in insulin resistant mice. |
| 1066 | 12130701 | Furthermore, expression of Cyp1a2, Cyp7b1, Gstm3, and Gstm6 was reduced in both diabetic and insulin resistant mice. |
| 1067 | 12180353 | Cilostazol undergoes intensive and finally complete hepatic metabolism via the cytochrome P450 systems. |
| 1068 | 12242686 | CYP2B expression tended to decrease and CYP2E1 and 4A expression tended to increase in SZ-injected hamsters, although the results were not significant. |
| 1069 | 12399156 | The activities examined were cytochrome P450 (CYP) isoform activities (CYP2A6, CYP2D6, CYP2C19, CYP1A2, CYP2E1, CYP3A4 and CYP2C9) and phase 2 conjugation enzyme activities (phenol sulfotransferase (PST) and glucuronyl transferase (UGT)). |
| 1070 | 12399156 | However, when three enzyme activities ((CYP3A4 x UGT)/PST) were taken into account, a correlation was made (r(2)=0.53). |
| 1071 | 12399156 | Based on the correlation, we hypothesize that TRO and TRO sulfate are direct acting toxicants, whereas CYP3A4 oxidation and glucuronidation are detoxification pathways. |
| 1072 | 12399157 | The cytochrome P450 (CYP) inhibitors furafylline (CYP1A1/2), omeprazole (CYP2C19), ketoconazole (CYP3A4), and sulfaphenazole (CYP2C9) had no inhibitory effect on the TGZ metabolism suggesting that several P450s may play a role in the TGZ metabolic pathway. |
| 1073 | 12405866 | All HIV protease inhibitors are metabolised by and inhibit cytochrome P450 (CYP) 3A4. |
| 1074 | 12410059 | In patients with chronic renal failure, co-administration of colchicine with simvastatin may accelerate the onset of myopathy because CYP3A4 (part of cytochrome P450) is crucial in the breakdown of both drugs. |
| 1075 | 12410060 | Regarding the mechanism of severe weight gain in these two patients, we speculate a drug-drug interaction involving inhibition of the cytochrome P450 enzyme 2D6 (CYP4502D6) by paroxetine. |
| 1076 | 12534643 | Diabetes mellitus increases the in vivo activity of cytochrome P450 2E1 in humans. |
| 1077 | 12569201 | On activation by these compounds, PXR coordinately induces a network of transporters, cytochrome P450 enzymes, and other genes that effectively clear xenobiotics from the liver and intestine. |
| 1078 | 12569201 | To address this issue, we noted that there is substantial overlap in the substrate specificities of PXR and its critical CYP3A target gene. |
| 1079 | 12569201 | This prompted us to ask whether endogenous CYP3A substrates also serve as PXR ligands. |
| 1080 | 12569201 | We demonstrate that 5beta-cholestane-3alpha,7alpha,12alpha-triol (triol), a cholesterol-derived CYP3A substrate, is a potent PXR agonist that effectively induces cyp3a expression in mice. |
| 1081 | 12569201 | We now demonstrate that triol fails to activate human PXR or induce the CYP3A-salvage pathway. |
| 1082 | 12569201 | This explains why humans are more susceptible to sterol accumulation and suggests that synthetic ligands for human PXR could be used to treat cerebrotendinous xanthomatosis and other disorders of cholesterol excess. |
| 1083 | 12570747 | Arachidonic acid can be metabolized by cytochrome p450 (CYP450) enzymes to 5,6-, 8,9-, 11,12-, and 14,15-epoxyeicosatrienoic acids (EETs), their corresponding dihydroxyeicosa-trienoic acids (DHETs), and 20-hydroxyeicosatetraenoic acid (20-HETE). |
| 1084 | 12596357 | Numerous variants of cytochrome P450 enzymes and the pregnane X receptor, recently associated with protein expression and altered catalytic activities, may prove to be of use in the future in drug candidate profiling. |
| 1085 | 12615243 | To facilitate clinical studies investigating the dependence of NA elimination on the genotype of cytochrome P450 isoenzymes, we developed a rapid HPLC method for determination of NA in human plasma samples. |
| 1086 | 12681244 | Renal vascular effects of cyclooxygenase and cytochrome P450 metabolites of arachidonic acid have been extensively studied, with major advances having been made. |
| 1087 | 12681244 | More recently, studies indicate that arachidonic acid metabolites of the lipoxygenase and cytochrome P450 pathway, such as hydroxyeicosatetraenoic acids and epoxyeicosatrienoic acids, play novel roles in glomerular mesangial and epithelial cells that are relevant to the pathogenesis of kidney disease associated with diabetes and hypertension. |
| 1088 | 12681244 | Renal vascular effects of cyclooxygenase and cytochrome P450 metabolites of arachidonic acid have been extensively studied, with major advances having been made. |
| 1089 | 12681244 | More recently, studies indicate that arachidonic acid metabolites of the lipoxygenase and cytochrome P450 pathway, such as hydroxyeicosatetraenoic acids and epoxyeicosatrienoic acids, play novel roles in glomerular mesangial and epithelial cells that are relevant to the pathogenesis of kidney disease associated with diabetes and hypertension. |
| 1090 | 12727972 | We have synthesized the human N-terminal POMC fragment 1-28-POMC with the disulfide bridges in the correct position between cysteine residues 2-24 and 8-20 and studied the activity of these peptides in adrenocortical tumor cells in vitro. 1-28-POMC stimulated cell proliferation in human NCI-h295 and mouse Y-1 adrenal cancer cell lines and also in primary cultures of bovine adrenocortical cells in a concentration-dependent manner. 1-28-POMC led to rapid activation of the MAPKs extracellular signal-regulated kinases-1 and -2, but not c-Jun N-terminal kinase and p38, pathways. |
| 1091 | 12727972 | However, protein levels of important regulators of steroidogenesis [steroidogenic factor-1, DAX-1 (dosage-sensitive sex reversal-adrenal hypoplasia congenita critical region on the X-chromosome 1), steroidogenic acute regulatory protein, and cytochrome P450 side-chain cleavage enzyme] remained unaffected by 1-28-POMC treatment. |
| 1092 | 12743630 | It is not metabolized by the common cytochrome P-450 3A4 enzyme, possibly reducing the risk for drug interactions. |
| 1093 | 12926555 | The specific activity of cytochrome P-450 was significantly reduced by 69.3% (p < 0.05) in diabetic animals in comparison to the controls. |
| 1094 | 12931254 | According to the results of pharmacokinetic studies, pitavastatin showed favorable and promising safety profile; it was only slightly metabolized by the cytochrome P450 (CYP) system, its lactone form had no inhibitory effects on the CYP3A4-mediated metabolism of concomitantly administered drugs; P-glycoprotein-mediated transport did not play a major role in its disposition, and pitavastatin did not inhibit P-glycoprotein activity. |
| 1095 | 12963435 | Association of troglitazone-induced liver injury with mutation of the cytochrome P450 2C19 gene. |
| 1096 | 12963435 | We examined, retrospectively, the frequency of the polymorphisms of the cytochrome P450 (CYP) 2C19 and 2D6 genes in eight patients with type 2 diabetes who had troglitazone-induced liver injury and 31 subjects who tolerated troglitazone well. |
| 1097 | 12963435 | Association of troglitazone-induced liver injury with mutation of the cytochrome P450 2C19 gene. |
| 1098 | 12963435 | We examined, retrospectively, the frequency of the polymorphisms of the cytochrome P450 (CYP) 2C19 and 2D6 genes in eight patients with type 2 diabetes who had troglitazone-induced liver injury and 31 subjects who tolerated troglitazone well. |
| 1099 | 14575518 | The oxidative enzymes, cytochrome P450 (CYP) 3A4 and CYP3A5, and the drug efflux pump P-glycoprotein (P-gp) in enterocytes regulate this process. |
| 1100 | 14575518 | Most substrates for the P-gp pump are also substrates for the CYP3A enzymes. |
| 1101 | 14575518 | An efficient barrier to xenobiotic absorption is formed by the CYP enzymes and P-gp, and by the two systems working synergistically. |
| 1102 | 14575518 | Genetic polymorphisms have been reported for the genes associated with the expression of the CYP3A enzymes and P-gp. |
| 1103 | 14575518 | Genetic polymorphism of the multiple drug resistance gene-1 (MDR1, also known as ABCB1) [3435C/T] and the CYP3A5 genes (CYP3A5*1, CYP3AP1*1) have the greatest potential to influence the pharmacokinetics of immunosuppressants. |
| 1104 | 14575518 | The presence of the CYP3A5*1 allele is necessary for the production of a fully catalytic CYP3A5 protein, and also influences the ratio of CYP3A4 : CYP3A5 as well as the overall CYP3A catalytic activity. |
| 1105 | 14575518 | The CYP3A4 : CYP3A5 ratio may, in turn, influence the pattern of drug metabolites formed. |
| 1106 | 14575523 | Cytochrome P450 2J2 polymorphism in healthy Caucasians and those with diabetes mellitus. |
| 1107 | 14599559 | Hepatocyte nuclear factor 1 alpha (HNF1alpha) is a liver enriched homeodomain-containing transcription factor that has been shown to transactivate the promoters of several cytochrome P450 (CYP) genes, including CYP2E1, CYP1A2, CYP7A1, and CYP27, in vitro. |
| 1108 | 14599559 | Analysis of CYP gene expression revealed marked reductions in expression of Cyp1a2, Cyp2c29 and Cyp2e1, and a moderate reduction of Cyp3a11. |
| 1109 | 14599559 | There are also significant changes in the expression of genes encoding CYPs involved in fatty acid and bile acid metabolism characterized by a reduction in the expression of Cyp7b1, and Cyp27 as well as elevations in Cyp4a1/3, Cyp7a1, Cyp8b1, and Cyp39a1 expression. |
| 1110 | 14672050 | Host defense to mycobacterial infection is largely mediated by cellular immunity, and Th1-related cytokines, such as IFN-gamma and IL-12, play a central role in this response. |
| 1111 | 14672050 | Our study observed similar findings and furthermore indicated that IFN-gamma and IL-12 production by BCG-stimulated PBMC was lower in poorly-controlled DM patients than that in well-controlled DM patients and healthy subjects. |
| 1112 | 14672050 | Interestingly, levels of IFN-gamma and IL-12 in serum, lung, liver and spleen after infection were significantly reduced in DM mice when compared with those in control mice. |
| 1113 | 14672050 | RFP induces cytochrome P-450 in liver, accelerates the metabolism of some concomitant drug agents, and reduces blood concentration them remarkably. |
| 1114 | 14693714 | Elevated mitochondrial cytochrome P450 2E1 and glutathione S-transferase A4-4 in streptozotocin-induced diabetic rats: tissue-specific variations and roles in oxidative stress. |
| 1115 | 14693714 | We show a five- to eightfold increase of cytochrome P450 2E1 (CYP2E1) and glutathione S-transferase (GST) A4-4 levels in mitochondria from STZ-treated rat tissues compared with those in nondiabetic rat tissues, suggesting possible roles in the disease process. |
| 1116 | 14693714 | Transient transfection of COS cells with CYP2E1 cDNA caused a similar accumulation of CYP2E1 and GST A4-4 in mitochondria and increased production of mitochondrial ROS. |
| 1117 | 14693714 | Elevated mitochondrial cytochrome P450 2E1 and glutathione S-transferase A4-4 in streptozotocin-induced diabetic rats: tissue-specific variations and roles in oxidative stress. |
| 1118 | 14693714 | We show a five- to eightfold increase of cytochrome P450 2E1 (CYP2E1) and glutathione S-transferase (GST) A4-4 levels in mitochondria from STZ-treated rat tissues compared with those in nondiabetic rat tissues, suggesting possible roles in the disease process. |
| 1119 | 14693714 | Transient transfection of COS cells with CYP2E1 cDNA caused a similar accumulation of CYP2E1 and GST A4-4 in mitochondria and increased production of mitochondrial ROS. |
| 1120 | 14708419 | Biochemically, oxidative stress and lipid peroxidation and their ensuing damage are implicated in the pathogenesis of NASH and alcoholic steatohepatitis (probably resulting from free fatty acids in the mitochondria, and induction of the cytochrome P450 isoform CYP2E1 in hepatocytes and Kupffer's cells). |
| 1121 | 14715828 | We present the fourth case of an adult man (29 yr old) affected by aromatase deficiency resulting from a novel homozygous inactivating mutation of the CYP19 (P450(arom)) gene. |
| 1122 | 14727985 | Simvastatin and lovastatin are significantly metabolized by cytochrome P450 enzymes (CYP3A4) and are therefore not recommended for coadministration with protease inhibitors. |
| 1123 | 14748619 | Nateglinide is extensively metabolised, primarily by cytochrome P450 2C9, and eliminated primarily by the kidney. |
| 1124 | 14764761 | The prevalence of autoantibodies against nine intracellular enzyme autoantigens, namely 21-hydroxylase, side-chain cleavage enzyme (SCC), 17 alpha-hydroxylase, glutamic acid decarboxylase 65, aromatic L-amino acid decarboxylase, tyrosine phosphatase-like protein IA-2, tryptophan hydroxylase (TPH), tyrosine hydroxylase, cytochrome P450 1A2, and against the extracellular calcium-sensing receptor, was assessed in 90 patients with autoimmune polyendocrine syndrome type I. |
| 1125 | 14764761 | Autoantibodies against tyrosine phosphatase-like protein IA-2 were associated with insulin-dependent diabetes mellitus with an OR of 14.9, but with low sensitivity. |
| 1126 | 14965324 | Our initial studies on renal cyclooxygenase (COX)-2 expression and activity addressed the critical role of angiotensin II (Ang II) in increasing tumor necrosis factor alpha (TNF) that eventuated in expression of COX-2 in the medullary thick ascending limb (mTAL) of the nephron. |
| 1127 | 14965324 | COX-2 supplanted the dominant oxygenase, the cytochrome P450 (CYP) enzyme, omega-hydroxylase, that synthesized 20-hydroxyeicosatetraenoic acid (20-HETE). |
| 1128 | 15056802 | Regulation of CYP2E1 by ethanol and palmitic acid and CYP4A11 by clofibrate in primary cultures of human hepatocytes. |
| 1129 | 15056802 | CYP2E1 and CYP4A11 are cytochrome P450 enzymes that are regulated by physiological conditions including diabetes and fasting. |
| 1130 | 15056802 | Here, we used primary cultures of human hepatocytes to determine if certain xenochemicals could regulate CYP2E1 and CYP4A11. |
| 1131 | 15056802 | Ethanol significantly (p < 0.05) increased expression of CYP2E1 mRNA by 216 +/- 32% of control, but did not alter CYP4A11 mRNA accumulation (145 +/- 22% of control). |
| 1132 | 15056802 | In contrast, hepatocytes exposed to ethanol exhibited only a slight elevation in CYP2E1 protein (122 +/- 13% of control) and a negligible effect on CYP4A11 protein. |
| 1133 | 15056802 | Clofibrate significantly (p < 0.05) enhanced both CYP4A11 mRNA and protein by 239 +/- 30% and 154 +/- 10% of control, respectively, but did not increase CYP2E1. |
| 1134 | 15056802 | Because rodent CYP4A is reportedly regulated by fatty acids through peroxisome proliferator activated receptor alpha (PPARalpha) and CYP2E1 is induced by high fat diets, we examined the effects of a medium chain fatty acid, palmitate on CYP2E1 mRNA content. |
| 1135 | 15056802 | Collectively, results presented here identify agents that enhance CYP2E1 and CYP4A11 at the transcription level and suggest that fatty acids may represent a similar mode of regulation for these P450 enzymes. |
| 1136 | 15056802 | The lack of induction of CYP2E1 protein by ethanol in human hepatocytes indicates that for certain P450 enzymes, isolated hepatocytes may not be an adequate tool for predicting in vivo responses. |
| 1137 | 15056802 | Regulation of CYP2E1 by ethanol and palmitic acid and CYP4A11 by clofibrate in primary cultures of human hepatocytes. |
| 1138 | 15056802 | CYP2E1 and CYP4A11 are cytochrome P450 enzymes that are regulated by physiological conditions including diabetes and fasting. |
| 1139 | 15056802 | Here, we used primary cultures of human hepatocytes to determine if certain xenochemicals could regulate CYP2E1 and CYP4A11. |
| 1140 | 15056802 | Ethanol significantly (p < 0.05) increased expression of CYP2E1 mRNA by 216 +/- 32% of control, but did not alter CYP4A11 mRNA accumulation (145 +/- 22% of control). |
| 1141 | 15056802 | In contrast, hepatocytes exposed to ethanol exhibited only a slight elevation in CYP2E1 protein (122 +/- 13% of control) and a negligible effect on CYP4A11 protein. |
| 1142 | 15056802 | Clofibrate significantly (p < 0.05) enhanced both CYP4A11 mRNA and protein by 239 +/- 30% and 154 +/- 10% of control, respectively, but did not increase CYP2E1. |
| 1143 | 15056802 | Because rodent CYP4A is reportedly regulated by fatty acids through peroxisome proliferator activated receptor alpha (PPARalpha) and CYP2E1 is induced by high fat diets, we examined the effects of a medium chain fatty acid, palmitate on CYP2E1 mRNA content. |
| 1144 | 15056802 | Collectively, results presented here identify agents that enhance CYP2E1 and CYP4A11 at the transcription level and suggest that fatty acids may represent a similar mode of regulation for these P450 enzymes. |
| 1145 | 15056802 | The lack of induction of CYP2E1 protein by ethanol in human hepatocytes indicates that for certain P450 enzymes, isolated hepatocytes may not be an adequate tool for predicting in vivo responses. |
| 1146 | 15056802 | Regulation of CYP2E1 by ethanol and palmitic acid and CYP4A11 by clofibrate in primary cultures of human hepatocytes. |
| 1147 | 15056802 | CYP2E1 and CYP4A11 are cytochrome P450 enzymes that are regulated by physiological conditions including diabetes and fasting. |
| 1148 | 15056802 | Here, we used primary cultures of human hepatocytes to determine if certain xenochemicals could regulate CYP2E1 and CYP4A11. |
| 1149 | 15056802 | Ethanol significantly (p < 0.05) increased expression of CYP2E1 mRNA by 216 +/- 32% of control, but did not alter CYP4A11 mRNA accumulation (145 +/- 22% of control). |
| 1150 | 15056802 | In contrast, hepatocytes exposed to ethanol exhibited only a slight elevation in CYP2E1 protein (122 +/- 13% of control) and a negligible effect on CYP4A11 protein. |
| 1151 | 15056802 | Clofibrate significantly (p < 0.05) enhanced both CYP4A11 mRNA and protein by 239 +/- 30% and 154 +/- 10% of control, respectively, but did not increase CYP2E1. |
| 1152 | 15056802 | Because rodent CYP4A is reportedly regulated by fatty acids through peroxisome proliferator activated receptor alpha (PPARalpha) and CYP2E1 is induced by high fat diets, we examined the effects of a medium chain fatty acid, palmitate on CYP2E1 mRNA content. |
| 1153 | 15056802 | Collectively, results presented here identify agents that enhance CYP2E1 and CYP4A11 at the transcription level and suggest that fatty acids may represent a similar mode of regulation for these P450 enzymes. |
| 1154 | 15056802 | The lack of induction of CYP2E1 protein by ethanol in human hepatocytes indicates that for certain P450 enzymes, isolated hepatocytes may not be an adequate tool for predicting in vivo responses. |
| 1155 | 15063342 | Rosiglitazone is extensively metabolized by cytochrome P450 2C8 and so may have some utility as an in vivo probe for this enzyme. |
| 1156 | 15080500 | For the purpose of the clinical trial of the complexes in the future, we examined the toxic effects of these three Zn(II) complexes in regard of the LD50 values and hepatic cytochrome P450 levels. |
| 1157 | 15080500 | No changes of both CYP1A1 and CYP2E1 levels in the liver of KK-Ay mice treated with the three Zn(II) complexes were observed. |
| 1158 | 15090158 | A high throughput screening assay to screen for CYP2E1 metabolism and inhibition using a fluorogenic vivid p450 substrate. |
| 1159 | 15090158 | The application of isozyme-specific high-throughput screening (HTS) assays for characterizing the interactions of potential drug candidates with major human drug-metabolizing cytochrome p450 enzymes (p450s) is newly becoming an essential part of this process. |
| 1160 | 15090158 | Fluorescence-based HTS assays have been successfully employed for in vitro assessment of drug-drug interactions and enzyme inhibition with several p450 isoforms, including CYP3A4, CYP2D6, CYP2C9, and CYP2C19. |
| 1161 | 15090158 | A high throughput screening assay to screen for CYP2E1 metabolism and inhibition using a fluorogenic vivid p450 substrate. |
| 1162 | 15090158 | The application of isozyme-specific high-throughput screening (HTS) assays for characterizing the interactions of potential drug candidates with major human drug-metabolizing cytochrome p450 enzymes (p450s) is newly becoming an essential part of this process. |
| 1163 | 15090158 | Fluorescence-based HTS assays have been successfully employed for in vitro assessment of drug-drug interactions and enzyme inhibition with several p450 isoforms, including CYP3A4, CYP2D6, CYP2C9, and CYP2C19. |
| 1164 | 15090158 | A high throughput screening assay to screen for CYP2E1 metabolism and inhibition using a fluorogenic vivid p450 substrate. |
| 1165 | 15090158 | The application of isozyme-specific high-throughput screening (HTS) assays for characterizing the interactions of potential drug candidates with major human drug-metabolizing cytochrome p450 enzymes (p450s) is newly becoming an essential part of this process. |
| 1166 | 15090158 | Fluorescence-based HTS assays have been successfully employed for in vitro assessment of drug-drug interactions and enzyme inhibition with several p450 isoforms, including CYP3A4, CYP2D6, CYP2C9, and CYP2C19. |
| 1167 | 15099124 | Repaglinide is metabolised by the cytochrome P450 (CYP) 3A4 enzyme system and therefore has the potential to interact with other CYP3A4 substrates when administered concurrently. |
| 1168 | 15119115 | This condition comes from the progressive accumulation of the free fatty acids in mitochondria and from the induction of cytochrome P450, CYP 2E1 isoform in hepatocytes and Kupffer cells. |
| 1169 | 15123006 | Traditionally, attention to the problem of AED-induced bone loss has been focused on those drugs that induce the hepatic cytochrome P450 enzyme system, thereby increasing the metabolism of vitamin D. |
| 1170 | 15150316 | In this study, we identified the expression of cytochromes P450 in rat white adipose tissues and investigated the effects of typical lipophilic cytochrome P450 inducers, namely phenobarbital, dexamethasone, and beta-naphthoflavone. |
| 1171 | 15150316 | Phenobarbital and dexamethasone also induced both the mRNA and protein of CYP2Bs and CYP3As, respectively, in adipose tissue, although significant interindividual differences were observed. |
| 1172 | 15150316 | These results suggest that the mechanisms by which cytochrome P450 genes are regulated in the liver are also functional in rat adipose tissues. |
| 1173 | 15150316 | In this study, we identified the expression of cytochromes P450 in rat white adipose tissues and investigated the effects of typical lipophilic cytochrome P450 inducers, namely phenobarbital, dexamethasone, and beta-naphthoflavone. |
| 1174 | 15150316 | Phenobarbital and dexamethasone also induced both the mRNA and protein of CYP2Bs and CYP3As, respectively, in adipose tissue, although significant interindividual differences were observed. |
| 1175 | 15150316 | These results suggest that the mechanisms by which cytochrome P450 genes are regulated in the liver are also functional in rat adipose tissues. |
| 1176 | 15150316 | In this study, we identified the expression of cytochromes P450 in rat white adipose tissues and investigated the effects of typical lipophilic cytochrome P450 inducers, namely phenobarbital, dexamethasone, and beta-naphthoflavone. |
| 1177 | 15150316 | Phenobarbital and dexamethasone also induced both the mRNA and protein of CYP2Bs and CYP3As, respectively, in adipose tissue, although significant interindividual differences were observed. |
| 1178 | 15150316 | These results suggest that the mechanisms by which cytochrome P450 genes are regulated in the liver are also functional in rat adipose tissues. |
| 1179 | 15242186 | In this paper, we present the effects of two organic fractions and two aqueous extracts from the leaves of S. sonchifolius on rat hepatocyte viability, on oxidative damage induced by tert-butyl hydroperoxide (t-BH) and allyl alcohol (AA), and on glucose metabolism and their insulin-like effect on the expression of cytochrome P450 (CYP) mRNA. |
| 1180 | 15242186 | Moreover, the effects of the organic fractions (200 and 250 microg/ml) and to a lesser extent, the tea infusion (500 microg/ml) on rat CYP2B and CYP2E mRNA expression, were comparable to those observed with insulin. |
| 1181 | 15242186 | In this paper, we present the effects of two organic fractions and two aqueous extracts from the leaves of S. sonchifolius on rat hepatocyte viability, on oxidative damage induced by tert-butyl hydroperoxide (t-BH) and allyl alcohol (AA), and on glucose metabolism and their insulin-like effect on the expression of cytochrome P450 (CYP) mRNA. |
| 1182 | 15242186 | Moreover, the effects of the organic fractions (200 and 250 microg/ml) and to a lesser extent, the tea infusion (500 microg/ml) on rat CYP2B and CYP2E mRNA expression, were comparable to those observed with insulin. |
| 1183 | 15242818 | These compounds require bioactivation by cytochrome P450 2E1 (CYP2E1) for exertion of their toxic effects. |
| 1184 | 15242818 | Two mammalian insulin secreting pancreatic beta-cell lines BRIN BD11h2E1 and INS-1h2E1, which express human full length CYP2E1 cDNA, were used to elucidate the role of CYP2E1-mediated nitrosamine bioactivation in pancreatic beta-cell dysfunction and destruction. |
| 1185 | 15379059 | [Cytochrome P450 activity and its alteration in different diseases]. |
| 1186 | 15379059 | Cytochrome P450 (CYP) enzymes participate in the metabolism of a variety of naturally occurring and foreign compounds by reactions requiring NADPH and O2. |
| 1187 | 15379059 | [Cytochrome P450 activity and its alteration in different diseases]. |
| 1188 | 15379059 | Cytochrome P450 (CYP) enzymes participate in the metabolism of a variety of naturally occurring and foreign compounds by reactions requiring NADPH and O2. |
| 1189 | 15462162 | Supportive care with broad-spectrum antibiotics, granulocyte colony-stimulating factor, repeated blood transfusions, and albumin supplement was given. |
| 1190 | 15462162 | Coadministration of Cantharanthus roseus and cisapride was noted, and these two drugs are both substrates of cytochrome P450 3A4 enzymes (CYP 3A4). |
| 1191 | 15462162 | Because the vinca alkaloids are extensively metabolized by the liver cytochrome P450 enzymes, poor hepatic function and drug-herb interaction might predispose the patient to develop the bone marrow toxicity. |
| 1192 | 15462162 | Supportive care with broad-spectrum antibiotics, granulocyte colony-stimulating factor, repeated blood transfusions, and albumin supplement was given. |
| 1193 | 15462162 | Coadministration of Cantharanthus roseus and cisapride was noted, and these two drugs are both substrates of cytochrome P450 3A4 enzymes (CYP 3A4). |
| 1194 | 15462162 | Because the vinca alkaloids are extensively metabolized by the liver cytochrome P450 enzymes, poor hepatic function and drug-herb interaction might predispose the patient to develop the bone marrow toxicity. |
| 1195 | 15539809 | The conversion of DHEA to estrone by cytochrome P450 aromatase in primary cultured human osteoblasts was clarified. |
| 1196 | 15543094 | The elevated levels of immunoglobulins, about 20% more muscle in the pulmonary arteries, increased airway smooth muscle cells, and increased fetal hemoglobin and erythropoietin are evidence of chronic hypoxia before death. |
| 1197 | 15543094 | These proinflammatory cytokines down-regulate gene expression of major cytochrome P-450 and/or other enzymes with the specific effects on mRNA levels, protein expression, and enzyme activity, thus affecting metabolism of several endogenous lipophilic substances, such as steroids, lipid-soluble vitamins, prostaglandins, leukotrienes, thromboxanes, and exogenous substances. |
| 1198 | 15543094 | PEPCK deficit found in SIDS infants (caused also by vitamin A deficiency) and eventually enhanced by PACAP lipolysis of adipocyte triglycerides resulted in an increased FA level in blood because of their impaired reesterification to triacylglycerol in adipocytes. |
| 1199 | 15543094 | Pulmonary edema and petechial hemorrhages often present in SIDS victims may be the result of the vascular leak syndrome caused by IL-2 and IFN-alpha. |
| 1200 | 15543094 | Chronic hypoxia with the release of proinflammatory mediators IL-1alpha, IL-1beta and IL-6, and overloading of the cardiovascular and respiratory systems due to the narrowing airways and small pulmonary arteries of these children could also contribute to the development of these abnormalities. |
| 1201 | 15543094 | Moreover, chronic hypoxia of SIDS infants induced also production of hypoxia-inducible factor 1alpha (HIF-1alpha), which stimulated synthesis and release of different growth factors by vascular endothelial cells and intensified subclinical inflammatory reactions in the central nervous system, perhaps potentiated also by PACAP and VIP gene mutations. |
| 1202 | 15554233 | Oxidation of ethanol via alcohol dehydrogenase (ADH) explains various metabolic effects of ethanol but does not account for the tolerance. |
| 1203 | 15554233 | This fact, as well as the discovery of the proliferation of the smooth endoplasmic reticulum (SER) after chronic alcohol consumption, suggested the existence of an additional pathway which was then described by Lieber and DeCarli, namely the microsomal ethanol oxidizing system (MEOS), involving cytochrome P450. |
| 1204 | 15554233 | After chronic ethanol consumption, the activity of the MEOS increases, with an associated rise in cytochrome P450, especially CYP2E1, most conclusively shown in alcohol dehydrogenase negative deer mice. |
| 1205 | 15554233 | CYP1A2 and CYP3A4, two other perivenular P450s, also sustain the metabolism of ethanol, thereby contributing to MEOS activity and possibly liver injury. |
| 1206 | 15554233 | Oxidation of ethanol via alcohol dehydrogenase (ADH) explains various metabolic effects of ethanol but does not account for the tolerance. |
| 1207 | 15554233 | This fact, as well as the discovery of the proliferation of the smooth endoplasmic reticulum (SER) after chronic alcohol consumption, suggested the existence of an additional pathway which was then described by Lieber and DeCarli, namely the microsomal ethanol oxidizing system (MEOS), involving cytochrome P450. |
| 1208 | 15554233 | After chronic ethanol consumption, the activity of the MEOS increases, with an associated rise in cytochrome P450, especially CYP2E1, most conclusively shown in alcohol dehydrogenase negative deer mice. |
| 1209 | 15554233 | CYP1A2 and CYP3A4, two other perivenular P450s, also sustain the metabolism of ethanol, thereby contributing to MEOS activity and possibly liver injury. |
| 1210 | 15554233 | Oxidation of ethanol via alcohol dehydrogenase (ADH) explains various metabolic effects of ethanol but does not account for the tolerance. |
| 1211 | 15554233 | This fact, as well as the discovery of the proliferation of the smooth endoplasmic reticulum (SER) after chronic alcohol consumption, suggested the existence of an additional pathway which was then described by Lieber and DeCarli, namely the microsomal ethanol oxidizing system (MEOS), involving cytochrome P450. |
| 1212 | 15554233 | After chronic ethanol consumption, the activity of the MEOS increases, with an associated rise in cytochrome P450, especially CYP2E1, most conclusively shown in alcohol dehydrogenase negative deer mice. |
| 1213 | 15554233 | CYP1A2 and CYP3A4, two other perivenular P450s, also sustain the metabolism of ethanol, thereby contributing to MEOS activity and possibly liver injury. |
| 1214 | 15571475 | The risk is increased by certain concomitant drugs, including gemfibrozil and potent inhibitors of cytochrome P450 3A4. |
| 1215 | 15592575 | Olmesartan is not metabolized by the cytochrome P-450 and has a dual route of elimination, by kidneys and liver. |
| 1216 | 15617513 | Regulatory sequence responsible for insulin destabilization of cytochrome P450 2B1 (CYP2B1) mRNA. |
| 1217 | 15617513 | Diabetes has been reported to increase CYP2E1 (cytochrome P450) and CYP2B1 expression at both the mRNA and protein levels in rat livers. |
| 1218 | 15617513 | We first identified a 16-mer sequence that we later showed to be the actual functional target of insulin on the rat CYP2E1 mRNA. |
| 1219 | 15617513 | This sequence has a hairpin loop structure, shows 80% sequence identity with a structure previously identified on CYP2E1 and is also responsible for the post-transcriptional effects of insulin on this mRNA. |
| 1220 | 15617513 | Regulatory sequence responsible for insulin destabilization of cytochrome P450 2B1 (CYP2B1) mRNA. |
| 1221 | 15617513 | Diabetes has been reported to increase CYP2E1 (cytochrome P450) and CYP2B1 expression at both the mRNA and protein levels in rat livers. |
| 1222 | 15617513 | We first identified a 16-mer sequence that we later showed to be the actual functional target of insulin on the rat CYP2E1 mRNA. |
| 1223 | 15617513 | This sequence has a hairpin loop structure, shows 80% sequence identity with a structure previously identified on CYP2E1 and is also responsible for the post-transcriptional effects of insulin on this mRNA. |
| 1224 | 15689053 | Experimental data indicate that potential DDI between policosanol and drugs metabolized through the cytochrome P450 hepatic system are not expected, but pharmacodynamic DDI cannot be excluded. |
| 1225 | 15708677 | In vitro metabolism of a new oxazolidinedione hypoglycemic agent utilizing liver microsomes and recombinant human cytochrome P450 enzymes. |
| 1226 | 15708677 | PPARgamma agonists have proven useful in the treatment of type 2 diabetes, which is characterized by hyperglycemia, insulin resistance and/or abnormal insulin secretion. |
| 1227 | 15708677 | The metabolism of this oxazolidinedione (OZD) was investigated in male rat, dog, monkey and human liver microsomes, and recombinant human cytochrome P450 enzymes (CYP1A2, CYP2A6, CYP2B6, CYP2C8, CYP2C9, CYP2C19, CYP2D6, CYP2E1 and CYP3A4) in the presence of NADPH. |
| 1228 | 15708677 | Further, CYP2C8 and CYP2C19 did not display different regioselectivity for hydroxylation on the cyclohexane ring with both of them giving rise to C-3 and C-4 hydroxy metabolites, but they did display different stereoselectivity with CYP2C8 preferring cyclohexane hydroxylation in equatorial positions and CYP2C19 in axial positions. |
| 1229 | 15708677 | In vitro metabolism of a new oxazolidinedione hypoglycemic agent utilizing liver microsomes and recombinant human cytochrome P450 enzymes. |
| 1230 | 15708677 | PPARgamma agonists have proven useful in the treatment of type 2 diabetes, which is characterized by hyperglycemia, insulin resistance and/or abnormal insulin secretion. |
| 1231 | 15708677 | The metabolism of this oxazolidinedione (OZD) was investigated in male rat, dog, monkey and human liver microsomes, and recombinant human cytochrome P450 enzymes (CYP1A2, CYP2A6, CYP2B6, CYP2C8, CYP2C9, CYP2C19, CYP2D6, CYP2E1 and CYP3A4) in the presence of NADPH. |
| 1232 | 15708677 | Further, CYP2C8 and CYP2C19 did not display different regioselectivity for hydroxylation on the cyclohexane ring with both of them giving rise to C-3 and C-4 hydroxy metabolites, but they did display different stereoselectivity with CYP2C8 preferring cyclohexane hydroxylation in equatorial positions and CYP2C19 in axial positions. |
| 1233 | 15808883 | There was also no difference in liver thiobarbituric acid reactive substances (TBARS) and cytochrome P450 values between AF, BuF and vehicle-treated control rats. |
| 1234 | 15821098 | Cytochrome P450 (CYP) genes were also significantly reduced in 12 week old diabetic liver of ZDF rats. |
| 1235 | 15822183 | Cytochrome P450-catalyzed metabolism of arachidonic acid is an important pathway for the formation of paracrine and autocrine mediators of numerous biological effects. |
| 1236 | 15822183 | Members of the cytochrome P450 4A and 4F families are the major omega-hydroxylases, and the substrate selectivity and regulation of these enzymes has been the subject of numerous studies. |
| 1237 | 15822183 | Cytochrome P450-catalyzed metabolism of arachidonic acid is an important pathway for the formation of paracrine and autocrine mediators of numerous biological effects. |
| 1238 | 15822183 | Members of the cytochrome P450 4A and 4F families are the major omega-hydroxylases, and the substrate selectivity and regulation of these enzymes has been the subject of numerous studies. |
| 1239 | 15854203 | Metabolism of pitavastatin by the cytochrome P450 (CYP) system is minimal, principally through CYP 2C9, with little involvement of the CYP 3A4 isoenzyme, potentially reducing the risk of drug-drug interactions between pitavastatin and other drugs known to inhibit CYP enzymes. |
| 1240 | 15906000 | The effects of diabetes on cytochrome P450 (CYP)-dependent drug metabolizing enzymes are yet to be clarified. |
| 1241 | 15963007 | Relevant pharmacological agents are those that are widely coadministered in diabetic patients (e.g. lipid-lowering agents, antihypertensive agents); those that have a narrow efficacy/toxicity ratio (e.g. digoxin, warfarin); or those that are known to induce (rifampicin [rifampin]) or inhibit (fluconazole) the cytochrome P450 (CYP) system. |
| 1242 | 15964029 | Effect of insulin-mimetic vanadyl sulfate on cytochrome P450 2E1-dependent p-nitrophenol hydroxylation in the liver microsomes of streptozotocin-induced type 1 diabetic rats. |
| 1243 | 15964029 | We have examined the age-dependent changes of CYP2E1 in the liver microsomes of type 1 diabetic STZ rats, the effects of VOSO4 on the contents of total P450 and CYP2E1, and the activities of CYP2E1 in terms of p-nitrophenol hydroxylation. |
| 1244 | 15964029 | The contents of P450 and CYP2E1 and CYP2E1 activity were enhanced with the development of diabetes. |
| 1245 | 15964029 | When the hyperglycemia of STZ rats was improved by daily intraperitoneal injections of VOSO4 for 10 days at the doses of 7 mg/kg body weight for 5 days, 5 mg/kg for the following 3 days, and then 2.5 mg/kg for 2 days, the P450 and CYP2E1 levels and CYP2E1 activity were lowered than those in the untreated STZ rats. |
| 1246 | 15964029 | Effect of insulin-mimetic vanadyl sulfate on cytochrome P450 2E1-dependent p-nitrophenol hydroxylation in the liver microsomes of streptozotocin-induced type 1 diabetic rats. |
| 1247 | 15964029 | We have examined the age-dependent changes of CYP2E1 in the liver microsomes of type 1 diabetic STZ rats, the effects of VOSO4 on the contents of total P450 and CYP2E1, and the activities of CYP2E1 in terms of p-nitrophenol hydroxylation. |
| 1248 | 15964029 | The contents of P450 and CYP2E1 and CYP2E1 activity were enhanced with the development of diabetes. |
| 1249 | 15964029 | When the hyperglycemia of STZ rats was improved by daily intraperitoneal injections of VOSO4 for 10 days at the doses of 7 mg/kg body weight for 5 days, 5 mg/kg for the following 3 days, and then 2.5 mg/kg for 2 days, the P450 and CYP2E1 levels and CYP2E1 activity were lowered than those in the untreated STZ rats. |
| 1250 | 15964029 | Effect of insulin-mimetic vanadyl sulfate on cytochrome P450 2E1-dependent p-nitrophenol hydroxylation in the liver microsomes of streptozotocin-induced type 1 diabetic rats. |
| 1251 | 15964029 | We have examined the age-dependent changes of CYP2E1 in the liver microsomes of type 1 diabetic STZ rats, the effects of VOSO4 on the contents of total P450 and CYP2E1, and the activities of CYP2E1 in terms of p-nitrophenol hydroxylation. |
| 1252 | 15964029 | The contents of P450 and CYP2E1 and CYP2E1 activity were enhanced with the development of diabetes. |
| 1253 | 15964029 | When the hyperglycemia of STZ rats was improved by daily intraperitoneal injections of VOSO4 for 10 days at the doses of 7 mg/kg body weight for 5 days, 5 mg/kg for the following 3 days, and then 2.5 mg/kg for 2 days, the P450 and CYP2E1 levels and CYP2E1 activity were lowered than those in the untreated STZ rats. |
| 1254 | 15964029 | Effect of insulin-mimetic vanadyl sulfate on cytochrome P450 2E1-dependent p-nitrophenol hydroxylation in the liver microsomes of streptozotocin-induced type 1 diabetic rats. |
| 1255 | 15964029 | We have examined the age-dependent changes of CYP2E1 in the liver microsomes of type 1 diabetic STZ rats, the effects of VOSO4 on the contents of total P450 and CYP2E1, and the activities of CYP2E1 in terms of p-nitrophenol hydroxylation. |
| 1256 | 15964029 | The contents of P450 and CYP2E1 and CYP2E1 activity were enhanced with the development of diabetes. |
| 1257 | 15964029 | When the hyperglycemia of STZ rats was improved by daily intraperitoneal injections of VOSO4 for 10 days at the doses of 7 mg/kg body weight for 5 days, 5 mg/kg for the following 3 days, and then 2.5 mg/kg for 2 days, the P450 and CYP2E1 levels and CYP2E1 activity were lowered than those in the untreated STZ rats. |
| 1258 | 16014574 | Cytochrome P-450-dependent metabolism of arachidonic acid in the kidney of rats with diabetes insipidus. |
| 1259 | 16014574 | This study compared the renal metabolism of arachidonic acid in Brattleboro (BB) (vasopressin deficient) and Long-Evans (LE) control rats and the effects of a cytochrome P-450 (CYP) inhibitor 1-aminobenzotriazole (ABT) on renal function in these animals. |
| 1260 | 16029066 | The major metabolic pathway for losartan is by the cytochrome P450 (CYP) 3A4, 2C9 and 2C10 isoenzymes. |
| 1261 | 16038570 | Tacrolimus is primarily metabolised by cytochrome P450 (CYP) 3A enzymes in the gut wall and liver. |
| 1262 | 16043020 | The major pathway for the metabolism of gammaT is the cytochrome P450 dependent oxidation to its water-soluble metabolite gamma-CEHC, which is excreted in urine. |
| 1263 | 16054976 | Chronic ethanol consumption may promote carcinogenesis by (1) production of acetaldehyde, which is a weak mutagen and carcinogen; (2) induction of cytochrome P450 2E1 and associated oxidative stress and conversion of procarcinogens to carcinogens; (3) depletion of S-adenosylmethionine and, consequently, induction of global DNA hypomethylation; (4) induction of increased production of inhibitory guanine nucleotide regulatory proteins and components of extracellular signal-regulated kinase-mitogen-activated protein kinase signaling; (5) accumulation of iron and associated oxidative stress; (6) inactivation of the tumor suppressor gene BRCA1 and increased estrogen responsiveness (primarily in breast); and (7) impairment of retinoic acid metabolism. |
| 1264 | 16054976 | Nicotine may promote carcinogenesis through activation of extracellular signal-regulated kinase/cyclooxygenase-2/vascular endothelial growth factor signaling pathway. |
| 1265 | 16054982 | Alcohol and its metabolites (acetaldehyde and fatty acid ethyl esters) can alter metabolic pathways involved in the inflammatory response and carcinogenesis, and they are mediated by one or more of the following mechanisms: (1) premature activation of zymogens; (2) induction of the inflammatory response through activation of nuclear transcription factors, including nuclear factor-kappa and activation protein 1; (3) increased production of reactive oxygen species, resulting in oxidative DNA damage and altered effect of dietary antioxidants; (4) activation of pancreatic stellate cells, which leads to fibrosis; (5) gene mutation in enzymes related to cytochrome P450, glutathione S-transferase, aldehyde dehydrogenase, cationic trypsinogen, and pancreatic secretory trypsin inhibitor; (6) synergistic effects of ethanol and tobacco carcinogen on NNK [nitrosamine 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone] metabolism; and (7) dysregulation of proliferation and apoptosis. |
| 1266 | 16151981 | On the contrary, in large preovulatory follicles inhibition of testosterone secretion is due to their action on 17-beta-HSD while stimulatory or inhibitory action on estradiol secretion is the result of their action on P450 aromatase activity. |
| 1267 | 16170675 | Raised levels of tissue plasminogen activator and plasminogen activator inhibitor-1 have been found in these patients, and there are reports about hypertension associated with antiretroviral therapy. |
| 1268 | 16170675 | Some HMG-CoA reductase inhibitors, however, share common hepatic metabolization pathways with protease inhibitors (cytochrome P450 3A4 system), thereby potentially leading to additional liver and muscle toxicity. |
| 1269 | 16175602 | Obese WAT showed increased TNFalpha and leptin expression and reciprocally reduced adiponectin expression. |
| 1270 | 16175602 | The expression of lipogenic transcription factors (SREBP-1c, PPARgamma, LXRalpha) was increased, whereas that of a lipolytic nuclear factor PPARalpha was reduced in SH. |
| 1271 | 16175602 | SH was associated with reduced cytochrome P450 (Cyp)2e1 but increased Cyp4a. |
| 1272 | 16175602 | In conclusion, forced overfeeding with a high-fat diet in mice induces obesity, insulin resistance, and SH in the absence of TNF signaling or Cyp2e1 induction. |
| 1273 | 16192107 | It is metabolized mainly by cytochrome P450 (CYP) 2 D 6 and, to a minor extent, by CYP1A2. |
| 1274 | 16255658 | Duloxetine would not be expected to cause clinically significant inhibition of the metabolic clearance of drugs metabolised by P450 (CYP)3A, (CYP)1A2, (CYP)2C9, or (CYP)2C19, but would be expected to cause some inhibition of CYP 2D6. |
| 1275 | 16285069 | These adverse effects have not been observed in clinical trials, but they have not been specifically assessed in humans. (9) Animal studies raised the possibility of fetal toxicity and teratogenicity. (10) The aripiprazole dose must be either halved or doubled during co-administration with inhibitors or inducers of cytochrome P450 isoenzymes CYP 3A4 and CYP 2D6. (11) In practice, there are too many unanswered questions to recommend aripiprazole for patients with schizophrenia. |
| 1276 | 16312011 | Diclofenac was reported to be metabolized via the hepatic microsomal cytochrome P450 (CYP) 2C11 in male rats. |
| 1277 | 16325295 | Glimepiride, a sulfonylurea hypoglycemic agent, is metabolized by cytochrome P450 2C9 (CYP2C9) which is known to have genetic polymorphisms. |
| 1278 | 16337197 | Ethanol increases mitochondrial cytochrome P450 2E1 in mouse liver and rat hepatocytes. |
| 1279 | 16337197 | Enhanced hepatic levels of cytochrome P450 2E1 (CYP2E1) may play a key role in the pathogenesis of some liver diseases because CYP2E1 represents a significant source of reactive oxygen species. |
| 1280 | 16337197 | In contrast, in leptin-deficient obese mice, ethanol administration did not increase mitochondrial CYP2E1, nor it depleted mitochondrial glutathione, suggesting that leptin deficiency hampers mitochondrial targeting of CYP2E1. |
| 1281 | 16337197 | Ethanol increases mitochondrial cytochrome P450 2E1 in mouse liver and rat hepatocytes. |
| 1282 | 16337197 | Enhanced hepatic levels of cytochrome P450 2E1 (CYP2E1) may play a key role in the pathogenesis of some liver diseases because CYP2E1 represents a significant source of reactive oxygen species. |
| 1283 | 16337197 | In contrast, in leptin-deficient obese mice, ethanol administration did not increase mitochondrial CYP2E1, nor it depleted mitochondrial glutathione, suggesting that leptin deficiency hampers mitochondrial targeting of CYP2E1. |
| 1284 | 16372821 | Effect of genetic polymorphisms in cytochrome p450 (CYP) 2C9 and CYP2C8 on the pharmacokinetics of oral antidiabetic drugs: clinical relevance. |
| 1285 | 16372821 | The polymorphic enzyme cytochrome P450 (CYP) 2C9 is the main enzyme catalysing the biotransformation of sulphonylureas. |
| 1286 | 16372821 | CYP2C8 and CYP3A4 are the main enzymes catalysing biotransformation of the thiazolidinediones troglitazone and pioglitazone, whereas rosiglitazone is metabolised by CYP2C9 and CYP2C8. |
| 1287 | 16372821 | Effect of genetic polymorphisms in cytochrome p450 (CYP) 2C9 and CYP2C8 on the pharmacokinetics of oral antidiabetic drugs: clinical relevance. |
| 1288 | 16372821 | The polymorphic enzyme cytochrome P450 (CYP) 2C9 is the main enzyme catalysing the biotransformation of sulphonylureas. |
| 1289 | 16372821 | CYP2C8 and CYP3A4 are the main enzymes catalysing biotransformation of the thiazolidinediones troglitazone and pioglitazone, whereas rosiglitazone is metabolised by CYP2C9 and CYP2C8. |
| 1290 | 16375696 | Cytochrome P450 (CYP) is a group of enzymes that metabolize drugs to a more water-soluble form, rendering them available for renal excretion. |
| 1291 | 16375696 | Nearly 50% of all medications currently on the market are metabolized by the enzyme CYP3A4, while metabolism of another 35-40% occurs through enzymes CYP1A2, CYP2C19, CYP2D6, CYP3A5 CYP3A6, and CYP3A7. |
| 1292 | 16397976 | Animal studies suggest a possible risk of haemangiosarcoma, although no human cases have yet been described. (10) Pregabalin, like gabapentin, is eliminated unchanged in urine, implying a limited risk of interactions involving cytochrome P450, and suggesting that the dose should be reduced in patients with even moderate renal failure (creatinine clearance below 60 ml/min). (11) In practice, pregabalin offers nothing new for patients with partial epilepsy, for whom several other antiepileptics are available. |
| 1293 | 16415108 | Cytochrome P450 epoxygenases provide a novel mechanism for penile erection. |
| 1294 | 16415108 | Immunoblotting results showed that protein expressions of epoxygenases from cytochrome P450 (CYP)2B, 2C and 2J subfamilies, as well as NADPH CYP reductase were present in rat corpora cavernosa, which was confirmed by immunohistochemical analysis. |
| 1295 | 16415108 | Cytochrome P450 epoxygenases provide a novel mechanism for penile erection. |
| 1296 | 16415108 | Immunoblotting results showed that protein expressions of epoxygenases from cytochrome P450 (CYP)2B, 2C and 2J subfamilies, as well as NADPH CYP reductase were present in rat corpora cavernosa, which was confirmed by immunohistochemical analysis. |
| 1297 | 16488120 | Flavin-containing monooxygenase and cytochrome P450 activities in experimental diabetes. |
| 1298 | 16488120 | Microsomal monooxygenases - cytochrome P450 (CYP, EC 1.14.14.1) and flavin-containing monooxygenase (FMO, EC 1.14.13.8) - have profound roles in drug metabolism. |
| 1299 | 16488120 | While the induction of some metabolic enzymes such as hepatic FMO and intestinal CYP1A, CYP2B is recognized in experimental diabetes, the effect of insulin treatment on FMO and intestinal CYP3A in diabetic animals has not been reported before. |
| 1300 | 16488120 | Hepatic FMO1 activity increased in diabetic rats, but it was restored to control value on insulin treatment. |
| 1301 | 16488120 | Insulin itself had no effect on FMO1 activity in non-diabetic animals. |
| 1302 | 16488120 | A remarkable increase of total CYP content was accompanied by a reduced CYP3A specific enzyme activity in the small intestine of diabetic animals. |
| 1303 | 16488120 | Both, hepatic FMO1 and intestinal CYP3A activity correlated with average blood glucose concentration in untreated diabetic rats. |
| 1304 | 16488120 | These results indicate that insulin is involved in the regulation of hepatic FMO1 and intestinal CYP3A in rats. |
| 1305 | 16488120 | The marked reduction of intestinal CYP3A capacity suggests that diabetes exerts a substantial effect on the activity of most determining intestinal CYP enzyme. |
| 1306 | 16488120 | Flavin-containing monooxygenase and cytochrome P450 activities in experimental diabetes. |
| 1307 | 16488120 | Microsomal monooxygenases - cytochrome P450 (CYP, EC 1.14.14.1) and flavin-containing monooxygenase (FMO, EC 1.14.13.8) - have profound roles in drug metabolism. |
| 1308 | 16488120 | While the induction of some metabolic enzymes such as hepatic FMO and intestinal CYP1A, CYP2B is recognized in experimental diabetes, the effect of insulin treatment on FMO and intestinal CYP3A in diabetic animals has not been reported before. |
| 1309 | 16488120 | Hepatic FMO1 activity increased in diabetic rats, but it was restored to control value on insulin treatment. |
| 1310 | 16488120 | Insulin itself had no effect on FMO1 activity in non-diabetic animals. |
| 1311 | 16488120 | A remarkable increase of total CYP content was accompanied by a reduced CYP3A specific enzyme activity in the small intestine of diabetic animals. |
| 1312 | 16488120 | Both, hepatic FMO1 and intestinal CYP3A activity correlated with average blood glucose concentration in untreated diabetic rats. |
| 1313 | 16488120 | These results indicate that insulin is involved in the regulation of hepatic FMO1 and intestinal CYP3A in rats. |
| 1314 | 16488120 | The marked reduction of intestinal CYP3A capacity suggests that diabetes exerts a substantial effect on the activity of most determining intestinal CYP enzyme. |
| 1315 | 16488120 | Flavin-containing monooxygenase and cytochrome P450 activities in experimental diabetes. |
| 1316 | 16488120 | Microsomal monooxygenases - cytochrome P450 (CYP, EC 1.14.14.1) and flavin-containing monooxygenase (FMO, EC 1.14.13.8) - have profound roles in drug metabolism. |
| 1317 | 16488120 | While the induction of some metabolic enzymes such as hepatic FMO and intestinal CYP1A, CYP2B is recognized in experimental diabetes, the effect of insulin treatment on FMO and intestinal CYP3A in diabetic animals has not been reported before. |
| 1318 | 16488120 | Hepatic FMO1 activity increased in diabetic rats, but it was restored to control value on insulin treatment. |
| 1319 | 16488120 | Insulin itself had no effect on FMO1 activity in non-diabetic animals. |
| 1320 | 16488120 | A remarkable increase of total CYP content was accompanied by a reduced CYP3A specific enzyme activity in the small intestine of diabetic animals. |
| 1321 | 16488120 | Both, hepatic FMO1 and intestinal CYP3A activity correlated with average blood glucose concentration in untreated diabetic rats. |
| 1322 | 16488120 | These results indicate that insulin is involved in the regulation of hepatic FMO1 and intestinal CYP3A in rats. |
| 1323 | 16488120 | The marked reduction of intestinal CYP3A capacity suggests that diabetes exerts a substantial effect on the activity of most determining intestinal CYP enzyme. |
| 1324 | 16557553 | Liver-specific loss of beta-catenin blocks glutamine synthesis pathway activity and cytochrome p450 expression in mice. |
| 1325 | 16557553 | There is accumulating evidence that Wnt/beta-catenin signaling is involved in the regulation of liver development and physiology. |
| 1326 | 16557553 | The presence of genetic alterations resulting in constitutive beta-catenin stabilization in human and murine liver tumors also implicates this pathway in hepatocyte proliferation. |
| 1327 | 16557553 | In the present study, we generated hepatocyte-specific beta-catenin knockout mice to explore the role of beta-catenin in liver function. |
| 1328 | 16557553 | Conditional knockout mice were born at the expected Mendelian ratio and developed normally to adulthood, indicating beta-catenin is dispensable for essential liver function under normal breeding conditions. |
| 1329 | 16557553 | Furthermore, the expression of two cytochrome P450 enzymes, CYP1A2 and CYP2E1, was almost completely abolished in livers from hepatocyte-specific beta-catenin knockout mice. |
| 1330 | 16557553 | Consequently, these mice were resistant to acetaminophen challenge, confirming the requirement of these cytochrome P450 enzymes for metabolism of xenobiotic substances. |
| 1331 | 16557553 | In conclusion, in addition to regulating hepatocyte proliferation, beta-catenin may also control multiple aspects of normal liver function. |
| 1332 | 16557553 | Liver-specific loss of beta-catenin blocks glutamine synthesis pathway activity and cytochrome p450 expression in mice. |
| 1333 | 16557553 | There is accumulating evidence that Wnt/beta-catenin signaling is involved in the regulation of liver development and physiology. |
| 1334 | 16557553 | The presence of genetic alterations resulting in constitutive beta-catenin stabilization in human and murine liver tumors also implicates this pathway in hepatocyte proliferation. |
| 1335 | 16557553 | In the present study, we generated hepatocyte-specific beta-catenin knockout mice to explore the role of beta-catenin in liver function. |
| 1336 | 16557553 | Conditional knockout mice were born at the expected Mendelian ratio and developed normally to adulthood, indicating beta-catenin is dispensable for essential liver function under normal breeding conditions. |
| 1337 | 16557553 | Furthermore, the expression of two cytochrome P450 enzymes, CYP1A2 and CYP2E1, was almost completely abolished in livers from hepatocyte-specific beta-catenin knockout mice. |
| 1338 | 16557553 | Consequently, these mice were resistant to acetaminophen challenge, confirming the requirement of these cytochrome P450 enzymes for metabolism of xenobiotic substances. |
| 1339 | 16557553 | In conclusion, in addition to regulating hepatocyte proliferation, beta-catenin may also control multiple aspects of normal liver function. |
| 1340 | 16557553 | Liver-specific loss of beta-catenin blocks glutamine synthesis pathway activity and cytochrome p450 expression in mice. |
| 1341 | 16557553 | There is accumulating evidence that Wnt/beta-catenin signaling is involved in the regulation of liver development and physiology. |
| 1342 | 16557553 | The presence of genetic alterations resulting in constitutive beta-catenin stabilization in human and murine liver tumors also implicates this pathway in hepatocyte proliferation. |
| 1343 | 16557553 | In the present study, we generated hepatocyte-specific beta-catenin knockout mice to explore the role of beta-catenin in liver function. |
| 1344 | 16557553 | Conditional knockout mice were born at the expected Mendelian ratio and developed normally to adulthood, indicating beta-catenin is dispensable for essential liver function under normal breeding conditions. |
| 1345 | 16557553 | Furthermore, the expression of two cytochrome P450 enzymes, CYP1A2 and CYP2E1, was almost completely abolished in livers from hepatocyte-specific beta-catenin knockout mice. |
| 1346 | 16557553 | Consequently, these mice were resistant to acetaminophen challenge, confirming the requirement of these cytochrome P450 enzymes for metabolism of xenobiotic substances. |
| 1347 | 16557553 | In conclusion, in addition to regulating hepatocyte proliferation, beta-catenin may also control multiple aspects of normal liver function. |
| 1348 | 16581331 | Patients who received a lipid-lowering medication with a concomitant cytochrome P450 3A4 (CYP3A4) inhibitor had a 6-fold increased rate of muscle disorders, including rhabdomyolysis. |
| 1349 | 16606331 | Ethanol-induced cytochrome P-450 2E1 produces various reactive oxygen species, leading to the formation of lipid peroxides such as 4-hydroxy-nonenal. |
| 1350 | 16640453 | Ranolazine is extensively metabolised by cytochrome P450 (CYP) 3A enzymes and, to a lesser extent, by CYP2D6, with approximately 5% excreted renally unchanged. |
| 1351 | 16679742 | The nuclear receptor constitutive androstane receptor (CAR), a key transcription factor for the expression of cytochrome P450 (CYP) 2B genes, resides in the cytoplasm under untreated conditions and translocates into the nucleus upon xenobiotic exposure. |
| 1352 | 16679742 | CAR forms a multiprotein complex including heat shock protein 90 in the cytoplasm as the glucocorticoid receptor, and it is likely that protein phosphatase 2A plays a critical role in the first step of CAR nuclear translocation. |
| 1353 | 16679742 | In obese mice fed a high-fat diet, however, hepatic CYP3A levels are drastically decreased without any significant changes in the expression of nuclear receptors including the pregnane X receptor and hepatocyte nuclear factor-4, which are known to be key transcription factors in the expression of CYP3A genes. |
| 1354 | 16713008 | Metabolism of arachidonic acid by cytochrome P450 to the vasoconstrictor 20-HETE is thought to be involved in the pathogenesis of hypertension, but the relationship of 20-HETE with insulin resistance is not clearly understood. |
| 1355 | 16764555 | Three major enzymatic pathways, COX (cyclo-oxygenase), CYP450 (cytochrome P450) and LOX (lipoxygenase), are responsible for the metabolism of arachidonic acid metabolites to bioactive eicosanoids. |
| 1356 | 16788382 | Genetic variations in cytochrome P450 2C9 (CYP2C9) are known to contribute to interindividual and interethnic variability in response to clinical drugs such as warfarin. |
| 1357 | 16820274 | Tissue-specific effect of ascorbic acid supplementation on the expression of cytochrome P450 2E1 and oxidative stress in streptozotocin-induced diabetic rats. |
| 1358 | 16820274 | An increased cytochrome P450 2E1 (CYP2E1) expression level with a concomitant increase in the production of reactive oxygen species were found in all the tissues of STZ-induced diabetic rats tested compared with an untreated control, suggesting the possible diabetes-induced tissue injury. |
| 1359 | 16820274 | Tissue-specific effect of ascorbic acid supplementation on the expression of cytochrome P450 2E1 and oxidative stress in streptozotocin-induced diabetic rats. |
| 1360 | 16820274 | An increased cytochrome P450 2E1 (CYP2E1) expression level with a concomitant increase in the production of reactive oxygen species were found in all the tissues of STZ-induced diabetic rats tested compared with an untreated control, suggesting the possible diabetes-induced tissue injury. |
| 1361 | 16861398 | To test the hypothesis that protein kinase C (PKC)beta-induced reactive oxygen species (ROS) underlie the vascular dysfunction in diabetes, we examined the effects of (S)-13[(dimethylamino)-methyl]-10,11-14,15-tetrahydro-4,9:16,21-dimetheno-1H,13H-dibenzo[e,k]pyrrolo[3,4-h][1,4,13]oxadi-azacyclohexadecene-1,3(2H)-dione (LY333531; LY), a specific PKCbeta inhibitor, on arachidonic acid (AA)-mediated dilation in small coronary arteries from streptozotocin-induced diabetic rats. |
| 1362 | 16861398 | In controls, AA-mediated vasodilation was inhibited by miconazole (an inhibitor of cytochrome P450 epoxygenase) and by iberiotoxin (IBTX, an inhibitor of the large conductance Ca(2+)-activated K(+) channel), but miconazole and IBTX had no effects in diabetic vessels. |
| 1363 | 16880618 | Our results demonstrate that db/db mice and Zucker fatty rats exhibit different expression profiles of P450s and nuclear receptors despite their similar characteristics for obesity and diabetes resulting from a defect in the leptin signaling pathway. |
| 1364 | 16921779 | Although the N-terminal heme domain functionally resembles cytochromes P450, no structural similarities exist between cytochrome P450 and nitric oxide synthases heme domains. |
| 1365 | 16972209 | For prevention, predisposing risk factors like electrolyte disturbances, pre-existing cardiac diseases, co-medication with QT prolonging drugs and medication with potential cytochrome P450 interaction have to be taken into consideration. |
| 1366 | 17015271 | Differential regulation of hepatic cytochrome P450 monooxygenases in streptozotocin-induced diabetic rats. |
| 1367 | 17015271 | The present investigation was carried out to study the expression of major cytochrome P450 (CYP) isozymes in streptozotocin-induced diabetes with concomitant insulin therapy. |
| 1368 | 17015271 | Uncontrolled hyperglycemia in the early phase of diabetes resulted in differential regulation of cytochrome P450 isozymes. |
| 1369 | 17015271 | CYP1B1, CYP1A2, heme oxygenase (HO)-2 proteins and CYP1A2-dependent 7-ethoxyresorufin O-deethylase (EROD) activity were upregulated in the hepatic microsomes of diabetic rats. |
| 1370 | 17015271 | Insulin therapy ameliorated EROD activity and the expression of CYP1A2, CYP1B1 and HO-2 proteins. |
| 1371 | 17015271 | Insulin therapy resulted in complete amelioration of CYP2E1 whereas CYP2B1 protein was partially ameliorated. |
| 1372 | 17015271 | These results demonstrate widespread alterations in the expression of CYP isozymes in diabetic rats that are ameliorated by insulin therapy. |
| 1373 | 17015271 | Differential regulation of hepatic cytochrome P450 monooxygenases in streptozotocin-induced diabetic rats. |
| 1374 | 17015271 | The present investigation was carried out to study the expression of major cytochrome P450 (CYP) isozymes in streptozotocin-induced diabetes with concomitant insulin therapy. |
| 1375 | 17015271 | Uncontrolled hyperglycemia in the early phase of diabetes resulted in differential regulation of cytochrome P450 isozymes. |
| 1376 | 17015271 | CYP1B1, CYP1A2, heme oxygenase (HO)-2 proteins and CYP1A2-dependent 7-ethoxyresorufin O-deethylase (EROD) activity were upregulated in the hepatic microsomes of diabetic rats. |
| 1377 | 17015271 | Insulin therapy ameliorated EROD activity and the expression of CYP1A2, CYP1B1 and HO-2 proteins. |
| 1378 | 17015271 | Insulin therapy resulted in complete amelioration of CYP2E1 whereas CYP2B1 protein was partially ameliorated. |
| 1379 | 17015271 | These results demonstrate widespread alterations in the expression of CYP isozymes in diabetic rats that are ameliorated by insulin therapy. |
| 1380 | 17015271 | Differential regulation of hepatic cytochrome P450 monooxygenases in streptozotocin-induced diabetic rats. |
| 1381 | 17015271 | The present investigation was carried out to study the expression of major cytochrome P450 (CYP) isozymes in streptozotocin-induced diabetes with concomitant insulin therapy. |
| 1382 | 17015271 | Uncontrolled hyperglycemia in the early phase of diabetes resulted in differential regulation of cytochrome P450 isozymes. |
| 1383 | 17015271 | CYP1B1, CYP1A2, heme oxygenase (HO)-2 proteins and CYP1A2-dependent 7-ethoxyresorufin O-deethylase (EROD) activity were upregulated in the hepatic microsomes of diabetic rats. |
| 1384 | 17015271 | Insulin therapy ameliorated EROD activity and the expression of CYP1A2, CYP1B1 and HO-2 proteins. |
| 1385 | 17015271 | Insulin therapy resulted in complete amelioration of CYP2E1 whereas CYP2B1 protein was partially ameliorated. |
| 1386 | 17015271 | These results demonstrate widespread alterations in the expression of CYP isozymes in diabetic rats that are ameliorated by insulin therapy. |
| 1387 | 17017939 | There are pharmacological interactions between these drugs and other medications metabolized by the cytochrome P450 (P3A4 isoform), such as the azole antifungals, erythromycin and the HIV protease inhibitors. |
| 1388 | 17027963 | Collectively, these data suggest that bradykinin-induced, EDHF-dependent relaxation in small mesenteric arteries from db/db mice is mediated via cytochrome P450 product that activates the large conductance calcium-activated potassium (BK(Ca) or Slo) channel, whereas the acetylcholine-induced, EDHF-mediated relaxation involves neither cytochrome P450 product nor hydrogen peroxide. |
| 1389 | 17034659 | Biochemical parameters such as cellular reduced glutathione content, content of cytochromes P450 and b5, and the expression of glutathione-S-transferase alpha (subunits Ya and Yc2) were not affected by the induced diabetes. |
| 1390 | 17097148 | Our laboratory has reported that insulin and growth factors regulate drug metabolizing enzyme gene and protein expression, including cytochromes P450 (CYP), glutathione S-transferases (GST) and microsomal epoxide hydrolase (mEH), through receptors which are members of the large receptor tyrosine kinase (RTK) family, and by downstream effectors such as phosphatidylinositol 3-kinase, mitogen activated protein kinase (MAPK), Akt/protein kinase B (PKB), mammalian target of rapamycin (mTOR), and the p70 ribosomal protein S6 kinase (p70S6 kinase). |
| 1391 | 17121211 | In these trials, duloxetine increased blood pressure in a dose-dependent manner. (7) Duloxetine is metabolized by cytochrome P450 isoenzymes CYP 1A2 and CYP 2D6, creating an important risk of interactions with other drugs. (8) In practice, duloxetine currently has no place in the treatment of depression or diabetic neuropathy. |
| 1392 | 17126841 | Synergistic effect of cytochrome P450 epoxygenase CYP2J2*7 polymorphism with smoking on the onset of premature myocardial infarction. |
| 1393 | 17150260 | Epoxyeicosatrienoic acids (EETs), derived from arachidonic acid by cytochrome P450 epoxygenases, are potent vasodilators that function as endothelium-derived hyperpolarizing factors in some vascular beds. |
| 1394 | 17159333 | In the diabetic group, the AA-induced sustained relaxation was completely inhibited by indomethacin [cyclooxygenase (COX) inhibitor], SKF525A [cytochrome P450 (CYP450) inhibitor], or clotrimazole (epoxygenase inhibitor), but not by furegrelate [thromboxane A(2) (TXA(2))-synthase inhibitor], SQ29548 (TXA(2)-receptor antagonist), or baicalein [lipoxygenase (LOX) inhibitor]. |
| 1395 | 17184944 | The Drosophila wing somatic mutation and recombination test (SMART) was applied in the standard version with basal biotransformation activity as well as in a variant version with increased cytochrome P450-dependent bioactivation capacity. |
| 1396 | 17201456 | Because they are metabolised via cytochrome P450 (CYP), glitazones are exposed to numerous pharmacokinetic interactions. |
| 1397 | 17201456 | CYP2C8 and CYP3A4 are the main isoenzymes catalysing biotransformation of pioglitazone (as with troglitazone), whereas rosiglitazone is metabolised by CYP2C9 and CYP2C8. |
| 1398 | 17220565 | Clinical laboratory tests immediately before the transplantation and cytochrome P450 3A5 genotype were not related to the high blood concentrations of sirolimus after the loading dose. |
| 1399 | 17253883 | Because glinides are metabolised via cytochrome P450 (CYP) 3A4 isoenzyme, they are indeed exposed to pharmacokinetic interactions. |
| 1400 | 17253883 | In addition to CYP3A4, repaglinide is metabolised via CYP2C8, while nateglinide metabolism also involves CYP2C9. |
| 1401 | 17266202 | In silico prediction of cytochrome P450 2D6 and 3A4 inhibition using Gaussian kernel weighted k-nearest neighbor and extended connectivity fingerprints, including structural fragment analysis of inhibitors versus noninhibitors. |
| 1402 | 17266202 | Inhibition of cytochrome P450 (CYP) enzymes is unwanted because of the risk of severe side effects due to drug-drug interactions. |
| 1403 | 17266202 | We present two in silico Gaussian kernel weighted k-nearest neighbor models based on extended connectivity fingerprints that classify CYP2D6 and CYP3A4 inhibition. |
| 1404 | 17266202 | Data used for modeling consisted of diverse sets of 1153 and 1382 drug candidates tested for CYP2D6 and CYP3A4 inhibition in human liver microsomes. |
| 1405 | 17266202 | CYP2D6 and CYP3A4 inhibition were additionally classified for an external test set on 14 drugs, and multidimensional scaling plots showed that the drugs in the external test set were in the periphery of the training sets. |
| 1406 | 17266202 | Furthermore, fragment analyses were performed and structural fragments frequent in CYP2D6 and CYP3A4 inhibitors and noninhibitors are presented. |
| 1407 | 17266202 | In silico prediction of cytochrome P450 2D6 and 3A4 inhibition using Gaussian kernel weighted k-nearest neighbor and extended connectivity fingerprints, including structural fragment analysis of inhibitors versus noninhibitors. |
| 1408 | 17266202 | Inhibition of cytochrome P450 (CYP) enzymes is unwanted because of the risk of severe side effects due to drug-drug interactions. |
| 1409 | 17266202 | We present two in silico Gaussian kernel weighted k-nearest neighbor models based on extended connectivity fingerprints that classify CYP2D6 and CYP3A4 inhibition. |
| 1410 | 17266202 | Data used for modeling consisted of diverse sets of 1153 and 1382 drug candidates tested for CYP2D6 and CYP3A4 inhibition in human liver microsomes. |
| 1411 | 17266202 | CYP2D6 and CYP3A4 inhibition were additionally classified for an external test set on 14 drugs, and multidimensional scaling plots showed that the drugs in the external test set were in the periphery of the training sets. |
| 1412 | 17266202 | Furthermore, fragment analyses were performed and structural fragments frequent in CYP2D6 and CYP3A4 inhibitors and noninhibitors are presented. |
| 1413 | 17266616 | Pharmacological agents such as potassium channel openers or cytochrome P450 metabolites have been used to either protect or recover EDHF-dependent mechanisms. |
| 1414 | 17297925 | Recombinant antibody piezoimmunosensors for the detection of cytochrome P450 1B1. |
| 1415 | 17297925 | The phase I enzyme known as cytochrome P450 1B1 (CYP1B1) is involved in the metabolism of many endogenous and exogenous compounds, including carcinogens. |
| 1416 | 17297925 | Three anti-CYP1B1 scFvs (designated B-66, D-23, and L-21) were biotinylated and used to capture and specifically detect CYP1B1 from samples in solution. |
| 1417 | 17297925 | Recombinant antibody piezoimmunosensors for the detection of cytochrome P450 1B1. |
| 1418 | 17297925 | The phase I enzyme known as cytochrome P450 1B1 (CYP1B1) is involved in the metabolism of many endogenous and exogenous compounds, including carcinogens. |
| 1419 | 17297925 | Three anti-CYP1B1 scFvs (designated B-66, D-23, and L-21) were biotinylated and used to capture and specifically detect CYP1B1 from samples in solution. |
| 1420 | 17362773 | Current treatment strategies to overcome acute intoxications focus on the induction of hepatic cytochrome P450 enzymes to accelerate tacrolimus degradation. |
| 1421 | 17395703 | The cytochrome P450 25-hydroxyvitamin D3-1alpha-hydroxylase (CYP27b1) plays a pivotal role in vitamin D physiology by catalyzing synthesis of active 1,25-dihydroxyvitamin D3 [1,25(OH)2D3]. |
| 1422 | 17395703 | In common with other P450s, CYP27b1 is known to exhibit alternative splicing. |
| 1423 | 17395703 | The cytochrome P450 25-hydroxyvitamin D3-1alpha-hydroxylase (CYP27b1) plays a pivotal role in vitamin D physiology by catalyzing synthesis of active 1,25-dihydroxyvitamin D3 [1,25(OH)2D3]. |
| 1424 | 17395703 | In common with other P450s, CYP27b1 is known to exhibit alternative splicing. |
| 1425 | 17442507 | Hepatic drug-metabolizing enzyme activity was also estimated by measuring the systemic clearance of antipyrine, and the expression of hepatic cytochrome P450 (CYP) 3A2 and CYP1A2, which is closely related to the metabolism from DZN to DZN-oxon, a strong inhibitor of both ChE and AChE. |
| 1426 | 17457372 | Major candidate molecules/mediators of EDHF signalling are K+, electrical coupling through gap junctions, cytochrome P450 metabolites, and endothelial small- and intermediate Ca2+-activated K+ channels (SK(Ca) and IK(Ca)). |
| 1427 | 17462606 | The aim of this investigation was to determine the kinetics for the metabolism of glyburide by cytochrome P450 (CYP) isozymes of human and baboon placental and hepatic microsomes. |
| 1428 | 17487428 | Inhibition of cytochrome P450 reversed the PARP inhibitory action of vitamin D and 7-dehydrocholesterol, indicating that conversion to 1alpha,25-dihydroxyvitamin D3 mediates their PARP inhibitory action. |
| 1429 | 17597710 | Cytochrome P450 2C9 *2 and *3 polymorphisms and the dose and effect of sulfonylurea in type II diabetes mellitus. |
| 1430 | 17597710 | Sulfonylurea hypoglycemics are mainly metabolized by the cytochrome P450 2C9 (CYP2C9) enzyme. |
| 1431 | 17597710 | Cytochrome P450 2C9 *2 and *3 polymorphisms and the dose and effect of sulfonylurea in type II diabetes mellitus. |
| 1432 | 17597710 | Sulfonylurea hypoglycemics are mainly metabolized by the cytochrome P450 2C9 (CYP2C9) enzyme. |
| 1433 | 17612649 | Vascular dysfunction in type 2 diabetic TallyHo mice: role for an increase in the contribution of PGH2/TxA2 receptor activation and cytochrome p450 products. |
| 1434 | 17612649 | Nomega-nitro-L-arginine methyl ester markedly increased the ACh-induced contractions in TH mice, whereas SQ29548, a thromboxane receptor antagonist, and cytochrome P450 (CYP) inhibitors 17-octadecynoic acid and sulfaphenazole, the latter being specific for CYP2C6 and 2C9, decreased and (or) normalized the contractile response to ACh in TH mice. |
| 1435 | 17612649 | The present study indicates that enhanced contribution of prostaglandin H2/thromboxane A2 receptor and CYP, likely CYP2C6 and 2C9, play a critical role in the pathogenesis of increased EDCF in the aortae of type 2 diabetic TH mice. |
| 1436 | 17612649 | Vascular dysfunction in type 2 diabetic TallyHo mice: role for an increase in the contribution of PGH2/TxA2 receptor activation and cytochrome p450 products. |
| 1437 | 17612649 | Nomega-nitro-L-arginine methyl ester markedly increased the ACh-induced contractions in TH mice, whereas SQ29548, a thromboxane receptor antagonist, and cytochrome P450 (CYP) inhibitors 17-octadecynoic acid and sulfaphenazole, the latter being specific for CYP2C6 and 2C9, decreased and (or) normalized the contractile response to ACh in TH mice. |
| 1438 | 17612649 | The present study indicates that enhanced contribution of prostaglandin H2/thromboxane A2 receptor and CYP, likely CYP2C6 and 2C9, play a critical role in the pathogenesis of increased EDCF in the aortae of type 2 diabetic TH mice. |
| 1439 | 17855173 | Role of cytochrome P450 metabolites of arachidonic acid in regulation of corporal smooth muscle tone in diabetic and older rats. |
| 1440 | 17855173 | This study examined the role of cytochrome P450 (CYP) metabolites of arachidonic acid (AA) to rat corporal smooth muscle tone. 11, 12-Epoxyeicosatrienoic acid (EET) (10(-11)-10(-6 )M) produced dose-dependent relaxation of rat (control; 10 weeks old) corpus cavernosum with a pD(2) value of 8.8+/-0.2 and a maximal relaxation of 80+/-9%, whereas 20-hydroxyeicosatetraenoic (20-HETE) did not have an effect. |
| 1441 | 17855173 | Role of cytochrome P450 metabolites of arachidonic acid in regulation of corporal smooth muscle tone in diabetic and older rats. |
| 1442 | 17855173 | This study examined the role of cytochrome P450 (CYP) metabolites of arachidonic acid (AA) to rat corporal smooth muscle tone. 11, 12-Epoxyeicosatrienoic acid (EET) (10(-11)-10(-6 )M) produced dose-dependent relaxation of rat (control; 10 weeks old) corpus cavernosum with a pD(2) value of 8.8+/-0.2 and a maximal relaxation of 80+/-9%, whereas 20-hydroxyeicosatetraenoic (20-HETE) did not have an effect. |
| 1443 | 17873277 | Class A scavenger receptor-mediated macrophage adhesion requires coupling of calcium-independent phospholipase A(2) and 12/15-lipoxygenase to Rac and Cdc42 activation. |
| 1444 | 17873277 | SR-A-dependent macrophage adhesion was abolished by selectively inhibiting calcium-independent PLA(2) (iPLA(2)) activity and absent in macrophages isolated from iPLA(2) beta(-/-) mice. |
| 1445 | 17873277 | Our results further demonstrate that 12/15-lipoxygenase (12/15-LOX)-derived, but not cyclooxygenase- or cytochrome P450-dependent epoxygenase-derived AA metabolites, are specifically required for SR-A-dependent adhesion. |
| 1446 | 17873277 | Because of their role in regulating actin polymerization and cell adhesion, Rac and Cdc42 activation were also examined and shown to be increased via an iPLA(2)- and LOX-dependent pathway. |
| 1447 | 17873277 | Together, our results identify a novel role for iPLA(2)-catalyzed AA release and its metabolism by 12/15-LOX in coupling SR-A-mediated macrophage adhesion to Rac and Cdc42 activation. |
| 1448 | 17912464 | Evaluation of genotype distributions by the chi-square test revealed that the 13989-->G (Ile118Val) polymorphism of the cytochrome P450, subfamily IIIA, polypeptide 4 gene (CYP3A4) was significantly (false discovery rate, 0.000009) associated with the prevalence of type 2 diabetes mellitus. |
| 1449 | 17963417 | Most studies involving cytochrome P450 (CYP) genes had small sample sizes (21 studies <50 subjects) and were among healthy volunteers. |
| 1450 | 17963417 | Polymorphisms in genes encoding the inwardly rectifying potassium channel Kir6.2 (KCNJ11) and the insulin receptor substrate-1 (IRS1) were reported to be associated with an increased risk of (secondary) failure to respond to sulfonylurea therapy. |
| 1451 | 17963417 | A significant decrease in fasting plasma glucose and hemoglobin A(1c) (HbA(1c)) in response to rosiglitazone was seen in subjects carrying the Pro12Ala polymorphism of the peroxisome proliferator-activated receptor-gamma (PPARG) gene. |
| 1452 | 17974492 | Several probable sources of free radical generation have been suggested in diabetes, including cytochrome P450 (CYP) monooxygenase-dependent pathways. |
| 1453 | 18158829 | Levels of cytochrome P450 2E1 mRNA, as measured by reverse transcription-polymerase chain reaction, were lower in the livers of the DGTS-treated rats than those of the control group. |
| 1454 | 18277067 | PPAR-alpha agonist fenofibrate induces renal CYP enzymes and reduces blood pressure and glomerular hypertrophy in Zucker diabetic fatty rats. |
| 1455 | 18277067 | We have previously shown that fenofibrate, a peroxisome proliferator-activated receptor-alpha activator, increases renal cytochrome P450 (CYP)-derived eicosanoids and improves endothelial function in pre-diabetic obese rats. |
| 1456 | 18277067 | Western blot and fluorescent immunostaining revealed that the over-expression of collagen type IV and alpha-smooth muscle actin was significantly attenuated in the kidney of fenofibrate-treated ZDF (F-ZDF) rats. |
| 1457 | 18277067 | Taken together, our results demonstrate that fenofibrate may lower blood pressure and attenuate glomerular hypertrophy and collagen accumulation through the downregulation of cyclin D1 and upregulation of CYP monooxygenases in the late stage of type-2 diabetes. |
| 1458 | 18326808 | Diabetic rats were treated for 3 wk with fenofibrate to increase expression of cytochrome P-450 (CYP4A) in an attempt to find an intervention that would restore release of 20-HETE from the diabetic rat kidney. |
| 1459 | 18326808 | We conclude that oxidative stress, increased aldose reductase activity, or increased COX activity does not contribute to the renal deficit of 20-HETE in diabetes, which may be directly related to insulin deficiency. |
| 1460 | 18329630 | Herbal antidiabetic preparations are often used as an add-on therapy in diabetes and such herbal preparations often contains quercetin that can inhibit cytochrome P450 (CYP) 3A4. |
| 1461 | 18427905 | Assessment of a new chemical entity for cytochrome P450 (CYP) enzyme induction at an early stage in discovery is crucial to prevent potential drug-drug interactions. |
| 1462 | 18427905 | CYP3A, the most abundant CYP isoform in the liver, metabolizes approximately 50% of drugs currently on the market and is also a highly inducible enzyme. |
| 1463 | 18460640 | Growth hormone (GH) controls the physiology and pathophysiology of the liver, and its signals are conducted by two members of the family of signal transducers and activators of transcription, STAT5A and STAT5B. |
| 1464 | 18460640 | Mice in which the Stat5a/b locus has been inactivated specifically in hepatocytes display GH resistance, the sex-specific expression of genes associated with liver metabolism and the cytochrome P-450 system is lost, and they develop hepatosteatosis. |
| 1465 | 18460640 | Evidence is accumulating that in the absence of STAT5A/B GH aberrantly activates STAT1 and STAT3 and their downstream target genes and thereby offers a partial explanation of some of the physiological alterations observed in Stat5a/b-null mice and human patients. |
| 1466 | 18460640 | We hypothesize that phenotypic changes observed in the absence of STAT5A/B are due to two distinct molecular consequences: first, the failure of STAT5A/B target genes to be activated by GH and second, the rerouting of GH signaling to other members of the STAT family. |
| 1467 | 18460640 | Rerouting of GH signaling to STAT1 and STAT3 might partially compensate for the loss of STAT5A/B, but it certainly activates biological programs distinct from STAT5A/B. |
| 1468 | 18476487 | The expression and in vivo induction of the P450 isoforms CYP2B, CYP2E, CYP3A and CYP4A in liver and lymphocyte samples is determined using Western blot analysis. |
| 1469 | 18523913 | The key enzyme of estrogen biosynthesis, aromatase cytochrome P450, is encoded by CYP19. |
| 1470 | 18581075 | Thereby, aspirin and clopidogrel resistance have been considered a multifactorial phenomenon underlying factors ranging from nonadherence of patients to antiplatelet therapy to demographic characteristics (age, diabetes, renal failure, etc.), acute coronary syndromes as well as genetic polymorphisms involving platelet glycoproteins and cytochrome P450 isoenzymes. |
| 1471 | 18602936 | The xenobiotic-metabolizing cytochrome P450 (CYP) 2A5 enzyme has been shown to be induced by fasting and by glucagon and cyclic AMP (cAMP), which mediate numerous fasting responses. |
| 1472 | 18602936 | Chromatin immunoprecipitation assays showed that PGC-1alpha binds, together with HNF-4alpha, to the same region at the Cyp2a5 proximal promoter. |
| 1473 | 18602936 | In conclusion, PGC-1alpha mediates the expression of Cyp2a5 induced by cAMP in mouse hepatocytes through coactivation of transcription factor HNF-4alpha. |
| 1474 | 18611061 | It acts at the point of activation of the renin-angiotensin-aldosterone system, or renin system, inhibiting the conversion of angiotensinogen to angiotensin I by renin and thereby reducing the formation of angiotensin II by angiotensin-converting enzyme (ACE) and ACE-independent pathways. |
| 1475 | 18611061 | Once absorbed, aliskiren is eliminated through the hepatobiliary route as unchanged drug and, to a lesser extent, through oxidative metabolism by cytochrome P450 (CYP) 3A4. |
| 1476 | 18611061 | Similar reductions in PRA are observed when aliskiren is administered in combination with agents that alone increase PRA, including diuretics (hydrochlorothiazide, furosemide [frusemide]), ACE inhibitors (ramipril) and angiotensin receptor blockers (valsartan), despite greater increases in the plasma renin concentration. |
| 1477 | 18620046 | No xanthine oxidase, cytochrome P450s, the Fenton reaction, or macrophage activation were required for the production of radical adducts. |
| 1478 | 18789379 | The activity of hepatic drug-metabolizing enzymes and expression of hepatic cytochrome P450 (CYP) 1A2, CYP3A2 and CYP2D1, which oxidize DZN to DZN-oxon, a potent ChE inhibitor, were measured before DZN injection. |
| 1479 | 19022234 | By co-treatment with specific inhibitors for cytochrome P450 (CYP) 2C and CYP3A - the major phase I enzymes involved in liver xenobiotic metabolism - we could confirm the prominent role of CYP3A in the bioactivation of troglitazone as well as the role of CYP3A and CYP2C in the activation of diclofenac. |
| 1480 | 19095443 | Optimization of the amino acid residue of a series of anthranilimide-based glycogen phosphorylase inhibitors is described leading to the identification of serine and threonine ether analogs. t-Butylthreonine analog 20 displayed potent in vitro inhibition of GPa, low potential for P450 inhibition, and excellent pharmacokinetic properties. |
| 1481 | 19129086 | Influence of SLCO1B1 and CYP2C8 gene polymorphisms on rosiglitazone pharmacokinetics in healthy volunteers. |
| 1482 | 19129086 | We sought to determine the joint effects of polymorphisms in the SLCO1B1 drug transporter gene and the cytochrome P450 ( CYP ) 2C8-metabolising enzyme gene on rosiglitazone pharmacokinetics in healthy volunteers. |
| 1483 | 19129086 | We concluded that polymorphisms in the CYP2C8 drug-metabolising enzyme gene, but not the SLCO1B1 drug transporter gene, significantly influence rosiglitazone disposition in humans. |
| 1484 | 19208908 | Mechanisms of podocyte injury in diabetes: role of cytochrome P450 and NADPH oxidases. |
| 1485 | 19249953 | A cardiology consultation performed on the day of admission determined that a markedly elevated creatine kinase-myocardial band isoenzyme level and borderline-high troponin I level were diagnostic of rhabdomyolysis secondary to statin use. |
| 1486 | 19249953 | Studies must be performed to further evaluate the in vivo effect of sitagliptin on the cytochrome P450 3A4 enzyme system and to elucidate other mechanisms that may potentiate such a drug-drug interaction. |
| 1487 | 19264869 | P450 oxidoreductase expressed in rat chondrocytes modulates chondrogenesis via cholesterol- and Indian Hedgehog-dependent mechanisms. |
| 1488 | 19264869 | Cytochrome P450 oxidoreductase (POR) is the electron donor for microsomal cytochrome P450 enzymes and other non-P450 enzymes. |
| 1489 | 19264869 | Because cholesterol is required for normal activity of the hedgehog proteins, we evaluated the effects of POR siRNAs on the expression of Indian hedgehog (Ihh), an important regulator of chondrogenesis. |
| 1490 | 19264869 | POR siRNA-transfected chondrocytes exhibited reduced Ihh expression, with such effect being neutralized by cholesterol. |
| 1491 | 19264869 | Lastly, recombinant human/mouse Ihh prevented the POR siRNA-mediated effects on chondrocyte proliferation, differentiation, and apoptosis. |
| 1492 | 19264869 | Our findings suggest that the bone malformations associated with defective POR activity are due to reduced cholesterol synthesis and, in turn, reduced Ihh expression in chondrocytes. |
| 1493 | 19264869 | P450 oxidoreductase expressed in rat chondrocytes modulates chondrogenesis via cholesterol- and Indian Hedgehog-dependent mechanisms. |
| 1494 | 19264869 | Cytochrome P450 oxidoreductase (POR) is the electron donor for microsomal cytochrome P450 enzymes and other non-P450 enzymes. |
| 1495 | 19264869 | Because cholesterol is required for normal activity of the hedgehog proteins, we evaluated the effects of POR siRNAs on the expression of Indian hedgehog (Ihh), an important regulator of chondrogenesis. |
| 1496 | 19264869 | POR siRNA-transfected chondrocytes exhibited reduced Ihh expression, with such effect being neutralized by cholesterol. |
| 1497 | 19264869 | Lastly, recombinant human/mouse Ihh prevented the POR siRNA-mediated effects on chondrocyte proliferation, differentiation, and apoptosis. |
| 1498 | 19264869 | Our findings suggest that the bone malformations associated with defective POR activity are due to reduced cholesterol synthesis and, in turn, reduced Ihh expression in chondrocytes. |
| 1499 | 19275551 | Role of NF-kappaB in the regulation of cytochrome P450 enzymes. |
| 1500 | 19275551 | Nuclear factor kappa B (NF-kappaB) is an important transcription factor that regulates a wide spectrum of genes including cytochrome P450 (CYP), the most important family of drug metabolizing enzymes. |
| 1501 | 19275551 | Therefore, in this review, we addressed the potential role of NF-kappaB in CYP regulation. |
| 1502 | 19275551 | We proposed three mechanisms by which NF-kappaB can regulate CYP expression and activity. |
| 1503 | 19275551 | First, NF-kappaB can directly regulate the expression of CYP1A1, CYP2B1/2, CYP2C11, CYP2D5, CYP2E1, CYP3A7, and CYP27B1 through binding to the promoter region of these genes. |
| 1504 | 19275551 | Second, NF-kappaB indirectly regulates the transcription of CYP genes through mutual repression with some nuclear receptors that are involved in CYP regulation such as AhR, CAR, GR, PXR, RXR, PPAR, FXR, and LXR. |
| 1505 | 19275551 | Finally, NF-kappaB can regulate CYP activity at post-transcriptional level by inducing heme oxygenase or by affecting the CYP protein stability. |
| 1506 | 19275551 | Therefore, we propose that NF-kappaB could be one of the links between inflammation, oxidative stress, and CYP regulation in these diseases. |
| 1507 | 19275551 | In conclusion, NF-kappaB plays a crucial role in the regulation of CYP through several mechanisms and this role can explain the altered CYP regulation in many conditions. |
| 1508 | 19275551 | Role of NF-kappaB in the regulation of cytochrome P450 enzymes. |
| 1509 | 19275551 | Nuclear factor kappa B (NF-kappaB) is an important transcription factor that regulates a wide spectrum of genes including cytochrome P450 (CYP), the most important family of drug metabolizing enzymes. |
| 1510 | 19275551 | Therefore, in this review, we addressed the potential role of NF-kappaB in CYP regulation. |
| 1511 | 19275551 | We proposed three mechanisms by which NF-kappaB can regulate CYP expression and activity. |
| 1512 | 19275551 | First, NF-kappaB can directly regulate the expression of CYP1A1, CYP2B1/2, CYP2C11, CYP2D5, CYP2E1, CYP3A7, and CYP27B1 through binding to the promoter region of these genes. |
| 1513 | 19275551 | Second, NF-kappaB indirectly regulates the transcription of CYP genes through mutual repression with some nuclear receptors that are involved in CYP regulation such as AhR, CAR, GR, PXR, RXR, PPAR, FXR, and LXR. |
| 1514 | 19275551 | Finally, NF-kappaB can regulate CYP activity at post-transcriptional level by inducing heme oxygenase or by affecting the CYP protein stability. |
| 1515 | 19275551 | Therefore, we propose that NF-kappaB could be one of the links between inflammation, oxidative stress, and CYP regulation in these diseases. |
| 1516 | 19275551 | In conclusion, NF-kappaB plays a crucial role in the regulation of CYP through several mechanisms and this role can explain the altered CYP regulation in many conditions. |
| 1517 | 19302554 | Cytochrome P450 metabolites of arachidonic acid play a role in the enhanced cardiac dysfunction in diabetic rats following ischaemic reperfusion injury. |
| 1518 | 19302554 | 1 This study examined the contribution of cytochrome P450 metabolites of arachidonic acid in mediating ischaemia/reperfusion (I/R)-induced cardiac dysfunction in normal and diabetic rats. 2 We first compared the metabolism of arachidonic acid in microsomes prepared from the hearts of control rats and rats treated with streptozotocin (55 mg kg(-1)) to induce diabetes. |
| 1519 | 19302554 | Cytochrome P450 metabolites of arachidonic acid play a role in the enhanced cardiac dysfunction in diabetic rats following ischaemic reperfusion injury. |
| 1520 | 19302554 | 1 This study examined the contribution of cytochrome P450 metabolites of arachidonic acid in mediating ischaemia/reperfusion (I/R)-induced cardiac dysfunction in normal and diabetic rats. 2 We first compared the metabolism of arachidonic acid in microsomes prepared from the hearts of control rats and rats treated with streptozotocin (55 mg kg(-1)) to induce diabetes. |
| 1521 | 19406192 | Effect of taurine supplementation on cytochrome P450 2E1 and oxidative stress in the liver and kidneys of rats with streptozotocin-induced diabetes. |
| 1522 | 19427425 | In conclusion, our findings support the hypothesis that clopidogrel nonresponsiveness is primarily the result of genetic mechanisms and factors that may influence activity of the cytochrome P-450 system. |
| 1523 | 19596526 | We analyzed the expression of glutathione S-transferases (GST) and cytochrome P450 enzymes (CYP) in 23 HCA, 20 HCC, and 22 focal nodular hyperplasias (FNH) using immunohistochemistry. |
| 1524 | 19596526 | The liver tissue revealed consistent specific staining for GST alpha, CYP1A1, 1A2, 2E1, and 3A4. |
| 1525 | 19596526 | Therefore, reduced expression of GST alpha and CYP3A4 may indicate specific metabolic defects in the tumor tissue characterizing subgroups of HCA and HCC. |
| 1526 | 19665535 | Actions of ethnobotanically selected Cree anti-diabetic plants on human cytochrome P450 isoforms and flavin-containing monooxygenase 3. |
| 1527 | 19706858 | Association of cytochrome P450 2C19 genotype with the antiplatelet effect and clinical efficacy of clopidogrel therapy. |
| 1528 | 19728747 | The majority of currently used immunosuppressant drugs in organ transplantation are metabolized by cytochrome P450 (CYP) or uridine diphosphate-glucuronosyltransferases and are substrates of the multidrug resistance (MDR)-1 transporter P-glycoprotein, the MDR-associated protein 2 or the canalicular multispecific organic anion transporter, which predisposes these immunosuppressant compounds to specific interactions with commonly prescribed drugs. |
| 1529 | 19787562 | Inherited variations of the vitamin K epoxide reductase C1 enzyme and of the cytochrome P450 2C9 system influence the dosage as well as exogenous factors such as food and drug intake or intercurrent diseases. |
| 1530 | 19787562 | Indirect systemic and oral direct factor Xa and oral direct thrombin inhibitors are currently being developed for the prevention of embolism in patients with AF. |
| 1531 | 19787709 | Cytochrome P450 enzymes and the heart. |
| 1532 | 19787709 | The cytochrome P450 monooxygenase system (CYP) is a multigene superfamily of heme-thiolate enzymes, which are important in the metabolism of foreign and endogenous compounds. |
| 1533 | 19787709 | Cytochrome P450 enzymes and the heart. |
| 1534 | 19787709 | The cytochrome P450 monooxygenase system (CYP) is a multigene superfamily of heme-thiolate enzymes, which are important in the metabolism of foreign and endogenous compounds. |
| 1535 | 19794412 | Sulfonylureas are metabolized mainly by the cytochrome p450 2C9 (CYP2C9) enzyme. |
| 1536 | 19794412 | We found that patients with two copies of a loss-of-function allele were 3.4 times (P = 0.0009) more likely to achieve a treatment hemoglobin A(1c) (HbA(1c)) level <7% than patients with two wild-type CYP2C9 alleles. |
| 1537 | 19830825 | One of the major outcomes of recent studies include significantly improved effectiveness of cytochrome P450 directed enzyme pro-drug delivery tools when used in conjunction with P35, which may help in alleviating drug resistance in tumor cells and simultaneously prolonging the cytotoxic effects of anti-cancer drugs. |
| 1538 | 19845526 | We discuss results of randomized studies and clinical observations which have shown that pharmacokinetics of clopidogrel might vary substantially in dependence of polymorphisms of genes responsible for synthesis of P2Y12 receptors of platelets or cytochromic isoenzymes P-450 CYP of liver with participation of which formation of active metabolite of clopidogrel occurs. |
| 1539 | 19928580 | [On the possibility of patient phenotyping on the basis of cytochrome p-450 1A2 isoenzyme activity using caffeine as the test substrate]. |
| 1540 | 19928580 | Data on the drugs metabolized mainly in cytochrome P-450 1A2 isoenzyme (CYP 1A2) are analyzed. |
| 1541 | 19928580 | [On the possibility of patient phenotyping on the basis of cytochrome p-450 1A2 isoenzyme activity using caffeine as the test substrate]. |
| 1542 | 19928580 | Data on the drugs metabolized mainly in cytochrome P-450 1A2 isoenzyme (CYP 1A2) are analyzed. |
| 1543 | 19932784 | Cytochrome P450 (CYP) 2C19 polymorphism was a major determinant of the response to clopidogrel and could be responsible for a failure of dose adjustment. |
| 1544 | 19965612 | In determining mechanisms that regulate wound healing, we found that wounding induced formation of novel endogenous 14S,21S-dihydroxy-docosa-4Z,7Z,10Z,12E,16Z,19Z-hexaenoic acids (14S,21S-diHDHA);14R,21R-diHDHA; 14S,21R-diHDHA; and/or 14R,21S-diHDHA. 12-lipoxygenase and cytochrome P450 catalysis in tandem converted docosahexaenoic acid to 14S,21R-diHDHA and 14S,21S-diHDHA through the intermediacy of 14S-HDHA; P450 also converted 14R-HDHA to novel 14R,21R-diHDHA and 14R,21S-diHDHA. |
| 1545 | 20041835 | Effect of polyphenolic compounds from Solanum torvum on plasma lipid peroxidation, superoxide anion and cytochrome P450 2E1 in human liver microsomes. |
| 1546 | 20041835 | Cytochrome P450 2E1 enzymes (CYP2E1) are involved in drug metabolism in the liver and metabolism of DNA-reaction generating intra-mitochondrial ROS, which leads to micro- and macro-vascular pathology in diabetes. |
| 1547 | 20041835 | These results imply that ST is a natural source of polyphenolic antioxidants, which have cytochrome P450 2E1 enzyme inhibiting and free radical scavenging properties, as related to lipid peroxidation and superoxide anion activity. |
| 1548 | 20041835 | Effect of polyphenolic compounds from Solanum torvum on plasma lipid peroxidation, superoxide anion and cytochrome P450 2E1 in human liver microsomes. |
| 1549 | 20041835 | Cytochrome P450 2E1 enzymes (CYP2E1) are involved in drug metabolism in the liver and metabolism of DNA-reaction generating intra-mitochondrial ROS, which leads to micro- and macro-vascular pathology in diabetes. |
| 1550 | 20041835 | These results imply that ST is a natural source of polyphenolic antioxidants, which have cytochrome P450 2E1 enzyme inhibiting and free radical scavenging properties, as related to lipid peroxidation and superoxide anion activity. |
| 1551 | 20041835 | Effect of polyphenolic compounds from Solanum torvum on plasma lipid peroxidation, superoxide anion and cytochrome P450 2E1 in human liver microsomes. |
| 1552 | 20041835 | Cytochrome P450 2E1 enzymes (CYP2E1) are involved in drug metabolism in the liver and metabolism of DNA-reaction generating intra-mitochondrial ROS, which leads to micro- and macro-vascular pathology in diabetes. |
| 1553 | 20041835 | These results imply that ST is a natural source of polyphenolic antioxidants, which have cytochrome P450 2E1 enzyme inhibiting and free radical scavenging properties, as related to lipid peroxidation and superoxide anion activity. |
| 1554 | 20067334 | Obesity does not appear to have an impact on drug binding to albumin; however, data regarding alpha(1)-acid glycoprotein binding have been contradictory. |
| 1555 | 20067334 | In the obese, increases in cytochrome P450 2E1 activity and phase II conjugation activity have been observed. |
| 1556 | 20099993 | The renin-angiotensin system genes, cytokine-encoding genes, and plasminogen activator inhibitor type 1 genes have been implicated in calcineurin inhibitor-induced nephrotoxicity, as well as in development of renal failure. |
| 1557 | 20099993 | A number of genes are implicated in contributing to diabetes, and these include the vitamin D receptor gene, VDR; hepatocyte nuclear factor genes, HNF; transcription factor 7-like 2 gene, TCF7L2; angiotensin-converting enzyme gene, ACE; cytokines; peroxisome proliferator-activated receptor gamma gene, PPARG; and others. |
| 1558 | 20099993 | Studies have suggested that the VDR, PPARG, HNF1A, and adenosine 5'-triphosphate-binding cassette ABCC8 (which encodes the sulfonylurea receptor) genes are associated with calcineurin inhibitor-induced diabetes. |
| 1559 | 20099993 | The genes encoding for the angiotensin-converting enzyme, endothelial constitutive nitric oxide synthase, and cytochrome P450 3A isoenzyme have been involved in the development of hypertension and in calcineurin inhibitor-induced hypertension. |
| 1560 | 20126370 | With DHEA treatment, cytosolic malate dehydrogenase activities were significantly increased by ~5 fold and glucose 6-phosphate dehydrogenase activities were decreased by ~25% compared to carcinogen treated group. |
| 1561 | 20126370 | However, liver microsomal cytochrome P-450 content and NADPH-dependent cytochrome P-450 reductase activities were not altered with DHEA treatment. |
| 1562 | 20126370 | However, vitamin E did not alter glucose 6-phosphate dehydrogenase or malate dehydrogenase activities. |
| 1563 | 20140850 | Genetic variation in the G-50T polymorphism of the cytochrome P450 epoxygenase CYP2J2 gene and the risk of younger onset type 2 diabetes among Chinese population: potential interaction with body mass index and family history. |
| 1564 | 20163193 | Small intestinal cytochrome P450 (Cyp) 3a expression in TSOD mice was significantly lower than in TSNO mice. |
| 1565 | 20163193 | In insulin-treated mice, small intestinal Cyp3a expression was significantly lower than in control mice. |
| 1566 | 20163193 | These results suggested that the differences in changes in small intestinal Cyp3a expression between T1DM and T2DM may be due to differences in plasma insulin concentrations. |
| 1567 | 20183527 | Cytochrome P-450 2E1 (CYP2E1) is a key enzyme in the metabolic activation of a variety of toxicants including nitrosamines, benzene, vinyl chloride, and halogenated solvents such as trichloroethylene. |
| 1568 | 20217240 | Microarray analysis found expressions of genes related to thiol redox, fatty acid oxidation in peroxisome and cytochrome P450 were significantly changed, indicating system in which non-enzyme antioxidant capacity was impaired and sources from which reactive oxygen species (ROS) generated, which revealed the molecular mechanism of oxidative stress induced by high-glucose diet. |
| 1569 | 20300478 | PPAR/RXR Regulation of Fatty Acid Metabolism and Fatty Acid omega-Hydroxylase (CYP4) Isozymes: Implications for Prevention of Lipotoxicity in Fatty Liver Disease. |
| 1570 | 20300478 | How steatosis increases PPARalpha activated gene expression of fatty acid transport proteins, peroxisomal and mitochondrial fatty acid beta-oxidation and omega-oxidation of fatty acids genes regardless of whether dietary fatty acids are polyunsaturated (PUFA), monounsaturated (MUFA), or saturated (SFA) may be determined by the interplay of PPARs and HNF4alpha with the fatty acid transport proteins L-FABP and ACBP. |
| 1571 | 20300478 | In hepatic steatosis and steatohepatitis, the omega-oxidation cytochrome P450 CYP4A gene expression is increased even with reduced hepatic levels of PPARalpha. |
| 1572 | 20300478 | This strongly implies that CYP4A fatty acid omega-hydroxylase P450s may play an important role in the development of steatohepatitis. |
| 1573 | 20300478 | PPAR/RXR Regulation of Fatty Acid Metabolism and Fatty Acid omega-Hydroxylase (CYP4) Isozymes: Implications for Prevention of Lipotoxicity in Fatty Liver Disease. |
| 1574 | 20300478 | How steatosis increases PPARalpha activated gene expression of fatty acid transport proteins, peroxisomal and mitochondrial fatty acid beta-oxidation and omega-oxidation of fatty acids genes regardless of whether dietary fatty acids are polyunsaturated (PUFA), monounsaturated (MUFA), or saturated (SFA) may be determined by the interplay of PPARs and HNF4alpha with the fatty acid transport proteins L-FABP and ACBP. |
| 1575 | 20300478 | In hepatic steatosis and steatohepatitis, the omega-oxidation cytochrome P450 CYP4A gene expression is increased even with reduced hepatic levels of PPARalpha. |
| 1576 | 20300478 | This strongly implies that CYP4A fatty acid omega-hydroxylase P450s may play an important role in the development of steatohepatitis. |
| 1577 | 20373255 | AVP-923 consists of a combination of the NMDA antagonist/sigma1 receptor agonist dextromethorphan hydrobromide (DM) and the cytochrome P450 2D6 (CYP2D6) enzyme inhibitor quinidine sulfate (Q). |
| 1578 | 20410220 | Concomitant mutations in the P450 oxidoreductase and androgen receptor genes presenting with 46,XY disordered sex development and androgenization at adrenarche. |
| 1579 | 20417277 | Our recent foci have been on P450 oxidoreductase deficiency (ORD) and apparent cortisone reductase deficiency (ACRD). |
| 1580 | 20437462 | Contributions of human cytochrome P450 enzymes to glyburide metabolism. |
| 1581 | 20437462 | Therefore, there has been a continued interest in identifying human cytochrome P450 (CYP) isoforms that play a major role in the metabolism of GLB. |
| 1582 | 20437462 | The present study systematically investigated the contributions of various human CYP isoforms (CYP3A4, CYP3A5, CYP2C8, CYP2C9 and CYP2C19) to in vitro metabolism of GLB. |
| 1583 | 20437462 | GLB depletion and metabolite formation in human liver microsomes were most significantly inhibited by the CYP3A inhibitor ketoconazole compared with the inhibitors of other CYP isoforms. |
| 1584 | 20437462 | Furthermore, multiple correlation analysis between GLB depletion and individual CYP activities was performed, demonstrating a significant correlation between GLB depletion and the CYP3A probe activity in 16 individual human liver microsomal preparations, but not between GLB depletion and the CYP2C19, CYP2C8 or CYP2C9 probe activity. |
| 1585 | 20437462 | By using recombinant supersomes overexpressing individual human CYP isoforms, it was found that GLB could be depleted by all the enzymes tested; however, the intrinsic clearance (V(max)/K(m)) of CYP3A4 for GLB depletion was 4-17 times greater than that of other CYP isoforms. |
| 1586 | 20437462 | Contributions of human cytochrome P450 enzymes to glyburide metabolism. |
| 1587 | 20437462 | Therefore, there has been a continued interest in identifying human cytochrome P450 (CYP) isoforms that play a major role in the metabolism of GLB. |
| 1588 | 20437462 | The present study systematically investigated the contributions of various human CYP isoforms (CYP3A4, CYP3A5, CYP2C8, CYP2C9 and CYP2C19) to in vitro metabolism of GLB. |
| 1589 | 20437462 | GLB depletion and metabolite formation in human liver microsomes were most significantly inhibited by the CYP3A inhibitor ketoconazole compared with the inhibitors of other CYP isoforms. |
| 1590 | 20437462 | Furthermore, multiple correlation analysis between GLB depletion and individual CYP activities was performed, demonstrating a significant correlation between GLB depletion and the CYP3A probe activity in 16 individual human liver microsomal preparations, but not between GLB depletion and the CYP2C19, CYP2C8 or CYP2C9 probe activity. |
| 1591 | 20437462 | By using recombinant supersomes overexpressing individual human CYP isoforms, it was found that GLB could be depleted by all the enzymes tested; however, the intrinsic clearance (V(max)/K(m)) of CYP3A4 for GLB depletion was 4-17 times greater than that of other CYP isoforms. |
| 1592 | 20535861 | The synergistic action of unopposed oestrogen and leptin, compounded by increasing insulin, cortisol and xeno-oestrogen exposure directly initiate, promote and exacerbate obesity, type 2 diabetes, uterine overgrowth, prostatic enlargement, prostate cancer and breast cancer. |
| 1593 | 20535861 | This review, in collaboration with hundreds of evidence-based clinical researchers, correlates the significant interactions these hormones exert upon the upregulation of p450 aromatase, oestrogen, leptin and insulin receptor function; the normal status quo of their binding globulins; and how adduct formation alters DNA sequencing to ultimately produce an array of metabolic conditions ranging from menopausal symptoms and obesity to Alzheimer's disease and breast and prostate cancer. |
| 1594 | 20535861 | It reveals the way that poor diet, increased stress, unopposed endogenous oestrogens, exogenous oestrogens, pesticides, xeno-oestrogens and leptin are associated with increased aromatase activity, and how its products, increased endogenous oestrogen and lowered testosterone, are associated with obesity, type 2 diabetes, Alzheimer's disease and oestrogenic disease. |
| 1595 | 20590741 | DPP-4 inhibitors are in general not substrates for cytochrome P450 (except saxagliptin that is metabolized via CYP 3A4/A5) and do not act as inducers or inhibitors of this system. |
| 1596 | 20648053 | In the kidney, skin and immune cells, 25-OHD(3) is turned into bioactive 1,25(OH)(2)D(3) by the enzyme coded by CYP27B1 (cytochrome P450 family 27 subfamily B peptide 1) on chromosome 12q13.1-3. 1,25(OH)(2)D(3) binds to the vitamin D receptor, expressed in T cells and antigen-presenting cells. 1,25(OH)(2)D(3) has a suppressive role in the adaptive immune system, decreasing T-cell and dendritic cell maturation, proliferation and differentiation, shifting the balance between T-helper 1 (Th1) and Th2 cells in favor of Th2 cells and increasing the suppressive function of regulatory T cells. |
| 1597 | 20690781 | Possible pharmacokinetic interferences have been investigated between each of these compounds and various pharmacological agents, which were selected because there are other glucose-lowering agents (metformin, glibenclamide [glyburide], pioglitazone/rosiglitazone) that may be prescribed in combination with DPP-4 inhibitors, other drugs that are currently used in patients with T2DM (statins, antihypertensive agents), compounds that are known to interfere with the cytochrome P450 (CYP) system (ketoconazole, diltiazem, rifampicin [rifampin]) or with P-glycoprotein transport (ciclosporin), or agents with a narrow therapeutic safety window (warfarin, digoxin). |
| 1598 | 20699675 | Because pitavastatin is minimally metabolized by the cytochrome P-450 isoenzymes, it is associated with a lower frequency of drug-drug interactions, and this may be a desirable characteristic of pitavastatin. |
| 1599 | 20878594 | Evidence of cytochrome P450 (CYP)2D6 inhibition in clinical trials highlighted a concern for pharmacokinetic interaction with other drugs that are CYP2D6 substrates, as confirmed by a rise in the pharmacokinetic parameters of desipramine with concomitant administration of mirabegron. |
| 1600 | 20888103 | Fusidic acid does not inhibit the cytochrome P450 3A4 isoenzyme responsible for atorvastatin metabolism; increased atorvastatin levels due to inhibition of the glucuronidation pathway may be responsible. |
| 1601 | 20972517 | Grapefruit-induced drug interactions are unique in that the cytochrome P450 enzyme CYP3A4, which metabolises over 60% of commonly prescribed drugs as well as other drug transporter proteins such as P-glycoprotein and organic cation transporter proteins, which are all expressed in the intestines, are involved. |
| 1602 | 21093571 | In vitro modulatory effects of Andrographis paniculata, Centella asiatica and Orthosiphon stamineus on cytochrome P450 2C19 (CYP2C19). |
| 1603 | 21108610 | This is the first study performed in population from Bosnia & Herzegovina (BH), in which we analysed a significance of genetic variations in drug-metabolising enzyme, cytochrome P450 (CYP), in pathogenesis of Type 2 diabetes. |
| 1604 | 21108610 | Thus, results form this study seem to indicate no relationship between CYP2C9, CYP2C19, and CYP2D6 genotype and diabetes susceptibility in Bosnian population. |
| 1605 | 21115572 | Simvastatin and atorvastatin share many pharmacokinetic properties such as lipophilicity while pravastatin and rosuvastatin are relatively hydrophilic and are not metabolized by cytochrome P450 3A4. |
| 1606 | 21142408 | vivo by several cytochrome (CYP) P450 iso-enzymes to become active. |
| 1607 | 21170619 | Pharmacokinetic drug-drug interactions are minimized due to the lack of significant metabolism of pitavastatin by the cytochrome P450 enzyme system, although some drugs affect its uptake into hepatocytes and should be avoided. |
| 1608 | 21186373 | Seventeen Cree antidiabetic medicinal plants were studied to determine their potential to inhibit cytochrome P450 3A4 (CYP3A4) through mechanism-based inactivation (MBI). |
| 1609 | 21190981 | Pubertal presentation in seven patients with congenital adrenal hyperplasia due to P450 oxidoreductase deficiency. |
| 1610 | 21215474 | Dihydropyridine calcium channel blockers are preferable due to their least interaction with cytochrome P450 enzyme system and, therefore, minimal risk of potential disruption of immunosuppressive drug levels. |
| 1611 | 21326303 | Variants of the human CYP4A11, which belongs to the cytochrome P450, family 4, have been reported to be associated with hypertension in general populations. |
| 1612 | 21366960 | Its effect on gene expression level of the tissue—specific cytochrome P450 (CYP) was also studied. |
| 1613 | 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. |
| 1614 | 21455816 | Cytochrome P450 2E1 (CYP2E1), a microsomal enzyme involved in xenobiotic metabolism and generation of oxidative stress, has been implicated in promoting liver injury. |
| 1615 | 21488586 | Unlike the other gliptins, saxagliptin is metabolised by the cytochrome P450 isoenzyme CYP 3A4, hence a high potential for pharmacokinetic interactions. |
| 1616 | 21664213 | Increased expression of cytochrome P450 2E1 in nonalcoholic fatty liver disease: mechanisms and pathophysiological role. |
| 1617 | 21664213 | Besides the mitochondrial respiratory chain, cytochrome P450 2E1 (CYP2E1) has recently emerged as another potentially important cause of ROS overproduction. |
| 1618 | 21664213 | It is currently unknown why CYP2E1 is enhanced in these dysmetabolic diseases, although increased hepatic levels of fatty acids and insulin resistance might play a role. |
| 1619 | 21664213 | Moreover, CYP2E1-mediated overproduction of ROS could promote hepatic insulin resistance, which can further aggravate fatty liver. |
| 1620 | 21664213 | Increased expression of cytochrome P450 2E1 in nonalcoholic fatty liver disease: mechanisms and pathophysiological role. |
| 1621 | 21664213 | Besides the mitochondrial respiratory chain, cytochrome P450 2E1 (CYP2E1) has recently emerged as another potentially important cause of ROS overproduction. |
| 1622 | 21664213 | It is currently unknown why CYP2E1 is enhanced in these dysmetabolic diseases, although increased hepatic levels of fatty acids and insulin resistance might play a role. |
| 1623 | 21664213 | Moreover, CYP2E1-mediated overproduction of ROS could promote hepatic insulin resistance, which can further aggravate fatty liver. |
| 1624 | 21742052 | Cytochrome P450 epoxygenase CYP2J2 attenuates nephropathy in streptozotocin-induced diabetic mice. |
| 1625 | 21742052 | Cytochrome P450 (CYP) epoxygenases metabolize arachidonic acid into epoxyeicosatrienoic acids (EETs), which play important and diverse roles in the cardiovascular system. |
| 1626 | 21742052 | Cytochrome P450 epoxygenase CYP2J2 attenuates nephropathy in streptozotocin-induced diabetic mice. |
| 1627 | 21742052 | Cytochrome P450 (CYP) epoxygenases metabolize arachidonic acid into epoxyeicosatrienoic acids (EETs), which play important and diverse roles in the cardiovascular system. |
| 1628 | 21810031 | Cytochrome P450-mediated cardiovascular drug interactions. |
| 1629 | 21874273 | In his career this investigator has been involved in the study of many steroid disorders, the two most recent being P450 oxidoreductase deficiency and apparent cortisone reductase deficiency. |
| 1630 | 21880796 | A novel entity of clinically isolated adrenal insufficiency caused by a partially inactivating mutation of the gene encoding for P450 side chain cleavage enzyme (CYP11A1). |
| 1631 | 21964476 | DCPT toxicity is dependent upon the presence of an intact TZD ring and cytochrome P450 (CYP)-mediated biotransformation. |
| 1632 | 21983453 | High glucose impairs EDHF-mediated dilation of coronary arterioles via reduced cytochrome P450 activity. |
| 1633 | 21983453 | In cultured coronary endothelial cells, HG reduced endothelial epoxyeicosatrienoic acid (EET) production as well as cytochrome P450 epoxygenase (CYP) activity. |
| 1634 | 21983453 | High glucose impairs EDHF-mediated dilation of coronary arterioles via reduced cytochrome P450 activity. |
| 1635 | 21983453 | In cultured coronary endothelial cells, HG reduced endothelial epoxyeicosatrienoic acid (EET) production as well as cytochrome P450 epoxygenase (CYP) activity. |
| 1636 | 22101210 | The activities of both cytochrome P450 17α-hydroxylase/17,20 lyase and cytochrome P450 21-hydroxylase were significantly inhibited in COS-1 cells. |
| 1637 | 22101210 | Quantification of 11βOH-A4 showed this metabolite to be a major product of steroidogenesis in H295R cells and we confirm, for the first time, that this steroid metabolite is the product of the hydroxylation of A4 by human cytochrome P450 11β-hydroxylase. |
| 1638 | 22101210 | The activities of both cytochrome P450 17α-hydroxylase/17,20 lyase and cytochrome P450 21-hydroxylase were significantly inhibited in COS-1 cells. |
| 1639 | 22101210 | Quantification of 11βOH-A4 showed this metabolite to be a major product of steroidogenesis in H295R cells and we confirm, for the first time, that this steroid metabolite is the product of the hydroxylation of A4 by human cytochrome P450 11β-hydroxylase. |
| 1640 | 22101373 | Non-nucleoside reverse transcriptase inhibitors (NNRTIs) or protease inhibitors (PIs), the current first line regimens of HAART, are metabolized by the cytochrome P450 family (CYP3A4). |
| 1641 | 22101373 | Of interest, integrase inhibitors (INIs) - novel, potent anti-HIV drugs - are mainly metabolized by uridine diphosphate glucuronosyltransferase (UGT) 1A1 and do not induce or inhibit CYP3A4. |
| 1642 | 22119155 | Regarding clopidogrel, drug interferences, diabetes mellitus, increased platelet turnover, and polymorphisms of the cytochrome P450 family are involved. |
| 1643 | 22119155 | Similarly, genotyping patients for cytochrome P450 polymorphisms also shows predictivity, but not confirmed in all studies. |
| 1644 | 22119155 | Regarding clopidogrel, drug interferences, diabetes mellitus, increased platelet turnover, and polymorphisms of the cytochrome P450 family are involved. |
| 1645 | 22119155 | Similarly, genotyping patients for cytochrome P450 polymorphisms also shows predictivity, but not confirmed in all studies. |
| 1646 | 22155603 | After controlling for established AMD risk factors, including polymorphisms of the genes encoding complement factor H (CFH) and age-related maculopathy susceptibility 2/HtrA serine peptidase (ARMS2/HTRA1), and smoking history, we found that ultraviolet irradiance was protective for the development of neovascular AMD (p = 0.001). |
| 1647 | 22155603 | Based on the relationship between ultraviolet irradiance and vitamin D production, we employed a candidate gene approach for evaluating common variation in key vitamin D pathway genes (the genes encoding the vitamin D receptor [VDR]; cytochrome P450, family 27, subfamily B, polypeptide 1 [CYP27B1]; cytochrome P450, family 24, subfamily A, polypeptide 1 [CYP24A1]; and CYP27A1) in this same family-based cohort. |
| 1648 | 22162478 | Genotype-phenotype analysis in congenital adrenal hyperplasia due to P450 oxidoreductase deficiency. |
| 1649 | 22213318 | The roles of cytochrome P450 enzymes in prostate cancer development and treatment. |
| 1650 | 22213318 | The active form of vitamin D, 1α,25-dihydroxyvitamin D [1α,25(OH)(2)D], interacts with vitamin D receptor (VDR) and induces antiproliferative, anti-invasive, proapoptotic and pro-differentiation activities in prostate cancer cells. |
| 1651 | 22213318 | Three cytochrome P-450 (CYP) hydroxylases are responsible for vitamin D synthesis and degradation, including vitamin D-25-hydroxylase (25-OHase) in the liver, and 25(OH)D-1α-hydroxylase (1α-OHase) or CYP27B1, and 25(OH)D-24-hydroxylase (24-OHase) or CYP24A1 in the kidneys. |
| 1652 | 22213318 | However, it is now recognized that CYP27B1 and CYP24A1 are also expressed in many tissues and cells, including the prostate. |
| 1653 | 22213318 | Although at least six CYP enzymes have been identified with 25-OHase activity, the two major ones are CYP27A1 and CYP2R1, and both are expressed in the prostate, with CYP2R1 as the predominate type. |
| 1654 | 22213318 | Thus, in addition to 1α,25(OH)(2)D analogs, the presence of CYP2R1, CYP27B1 and CYP24A1 in the prostate suggests that the analogs of vitamin D and 25(OH)D, especially those that are resistant to CYP24A1 degradation, can be developed and used for the prevention and treatment of prostate cancer. |
| 1655 | 22213318 | The roles of cytochrome P450 enzymes in prostate cancer development and treatment. |
| 1656 | 22213318 | The active form of vitamin D, 1α,25-dihydroxyvitamin D [1α,25(OH)(2)D], interacts with vitamin D receptor (VDR) and induces antiproliferative, anti-invasive, proapoptotic and pro-differentiation activities in prostate cancer cells. |
| 1657 | 22213318 | Three cytochrome P-450 (CYP) hydroxylases are responsible for vitamin D synthesis and degradation, including vitamin D-25-hydroxylase (25-OHase) in the liver, and 25(OH)D-1α-hydroxylase (1α-OHase) or CYP27B1, and 25(OH)D-24-hydroxylase (24-OHase) or CYP24A1 in the kidneys. |
| 1658 | 22213318 | However, it is now recognized that CYP27B1 and CYP24A1 are also expressed in many tissues and cells, including the prostate. |
| 1659 | 22213318 | Although at least six CYP enzymes have been identified with 25-OHase activity, the two major ones are CYP27A1 and CYP2R1, and both are expressed in the prostate, with CYP2R1 as the predominate type. |
| 1660 | 22213318 | Thus, in addition to 1α,25(OH)(2)D analogs, the presence of CYP2R1, CYP27B1 and CYP24A1 in the prostate suggests that the analogs of vitamin D and 25(OH)D, especially those that are resistant to CYP24A1 degradation, can be developed and used for the prevention and treatment of prostate cancer. |
| 1661 | 22228945 | Peptone, b-galactoside, glycosylated abscisic acid, alkaloids, cellulose, polygalacto urease, polyuronoids, cytochrome P-450, and volatile oils are reported to be present in this plant. |
| 1662 | 22233684 | Aromatase up-regulation, insulin and raised intracellular oestrogens in men, induce adiposity, metabolic syndrome and prostate disease, via aberrant ER-α and GPER signalling. |
| 1663 | 22233684 | In the final stage of the steroidogenic cascade, testosterone is metabolised to oestradiol by P450 aromatase, in the cytoplasm of adipocytes, breast cells, endothelial cells and prostate cells, to increase intracellular oestradiol concentration at the expense of testosterone. |
| 1664 | 22233684 | It follows therefore, that any compound that up-regulates aromatase, or any molecule that mimics oestrogen, will not only increase the activation of the mainly proliferative, classic ER-α, oestrogen receptors to induce adipogenesis and growth disorders in oestrogen-sensitive tissues, but also activate the recently identified transmembrane G protein-coupled oestrogen receptors (GPER), and deleteriously alter important intracellular signalling sequences, that promote mitogenic growth and endothelial damage. |
| 1665 | 22233684 | This paper simplifies how stress, xeno-oestrogens, poor dietary choices and reactive toxins up-regulate aromatase to increase intracellular oestradiol production; how oestradiol in combination with leptin and insulin cause insulin resistance and leptin resistance through aberrant serine phosphorylation; how the increased oestradiol, insulin and leptin stimulate rapid, non-genomic G protein-coupled phosphorylation cascades, to increase fat deposition and create the vasoconstrictive, dyslipidemic features of metabolic syndrome; how aberrant GPER signalling induces benign prostatic hypertrophy; and how increased intracellular oestradiol stimulates mitogenic change and tumour-cell activators, to cause prostate cancer. |
| 1666 | 22233684 | In essence, the up-regulation of aromatase produces increased intracellular oestradiol, increases ER-α activation and increases GPER activation, in combination with insulin, to cause aberrant downstream transduction signaling, and thus induce metabolic syndrome and mitogenic prostate growth. |
| 1667 | 22287853 | Two-way pharmacokinetic interaction studies between saxagliptin and cytochrome P450 substrates or inhibitors: simvastatin, diltiazem extended-release, and ketoconazole. |
| 1668 | 22328106 | Recent in vitro and in vivo studies have shown a potent inhibition of cytochrome P450 CYP3A4 through human immune deficiency virus (HIV) protease inhibitors (PIs). |
| 1669 | 22342832 | Modulations of cytochrome P450 expression in diabetic mice by berberine. |
| 1670 | 22342832 | Interaction between berberine and the cytochrome P450 enzymes (CYPs) has been extensively reported, but there are only a few reports of this interaction in the diabetic state. |
| 1671 | 22342832 | In primary mouse hepatocytes, berberine suppressed the induction of Cyp1a1, Cyp1a2, Cyp2e1, Cyp3a11, Cyp4a10, and Cyp4a14 mRNA expression by their prototypical inducers in a concentration-dependent fashion. |
| 1672 | 22342832 | Consumption of berberine as an anti-hyperglycemic compound by diabetic patients might provide an extra benefit due to its potential to restore the expression of Cyp2e1, Cyp3a, and Cyp4a to normal levels. |
| 1673 | 22342832 | Modulations of cytochrome P450 expression in diabetic mice by berberine. |
| 1674 | 22342832 | Interaction between berberine and the cytochrome P450 enzymes (CYPs) has been extensively reported, but there are only a few reports of this interaction in the diabetic state. |
| 1675 | 22342832 | In primary mouse hepatocytes, berberine suppressed the induction of Cyp1a1, Cyp1a2, Cyp2e1, Cyp3a11, Cyp4a10, and Cyp4a14 mRNA expression by their prototypical inducers in a concentration-dependent fashion. |
| 1676 | 22342832 | Consumption of berberine as an anti-hyperglycemic compound by diabetic patients might provide an extra benefit due to its potential to restore the expression of Cyp2e1, Cyp3a, and Cyp4a to normal levels. |
| 1677 | 22385219 | Genomic DNA was genotyped for common cytochrome P450 (CYP) 2C19 variants using Taqman assays. |
| 1678 | 22847176 | The mRNA and/or protein expression of pregnane X receptor (PXR) and cytochrome P450 isoforms that alter inflammation and/or lipid metabolism are increased to a greater extent in mice that received FO + Indo. |
| 1679 | 22847176 | Combining FO with COXIBs may exert their beneficial effects on inflammation and lipid metabolism via PXR and cytochrome P450. |
| 1680 | 22847176 | The mRNA and/or protein expression of pregnane X receptor (PXR) and cytochrome P450 isoforms that alter inflammation and/or lipid metabolism are increased to a greater extent in mice that received FO + Indo. |
| 1681 | 22847176 | Combining FO with COXIBs may exert their beneficial effects on inflammation and lipid metabolism via PXR and cytochrome P450. |
| 1682 | 22911336 | Among these differentially expressed proteins, we focused mainly on the 18 upregulated proteins belonging to xenobiotic cytochrome P450 (CYP), drug metabolism/detoxification, oxidative stress/antioxidant response, and cell damage pathway. |
| 1683 | 22911336 | CYP2D1, CYP2C11, UDP-glucuronosyltransferase 2B (UGT2B), superoxide dismutase 2 (SOD2), 60 kDa heat shock protein (HSPD1), heat shock protein 90 (HSP90), and catalase (CAT) were confirmed by Western blot analysis. |
| 1684 | 22940046 | Cytochrome P450 2E1 (CYP2E1) plays a critical role in ROS generation and CYP2E1 is also induced by alcohol itself. |
| 1685 | 22940046 | This review summarizes the role of CYP2E1 in ALD and NAFLD. |
| 1686 | 22968487 | Delayed diagnosis of adrenal insufficiency in a patient with severe penoscrotal hypospadias due to two novel P450 side-change cleavage enzyme (CYP11A1) mutations (p.R360W; p.R405X). |
| 1687 | 22969879 | Association between cytochrome P450 promoter polymorphisms and ischemic stroke. |
| 1688 | 22969879 | The human cytochrome P450 (CYP) superfamily includes at least 57 genes that encode enzymes with diverse metabolic and biosynthetic functions. |
| 1689 | 22969879 | This study was conducted in order to investigate the associations between polymorphisms in CYP superfamily genes (CYP11B2, CYP17A1, CYP2B6, CYP2C9, CYP2E1 and CYP7A1) and ischemic stroke (IS). |
| 1690 | 22969879 | The rs1799998 SNP of CYP11B2 and rs3808607 of CYP7A1 were related to diabetes mellitus in IS (p<0.05). |
| 1691 | 22969879 | CYP11B2, CYP2E1 and CYP7A1 SNPs were associated with IS in the population studied. |
| 1692 | 22969879 | Association between cytochrome P450 promoter polymorphisms and ischemic stroke. |
| 1693 | 22969879 | The human cytochrome P450 (CYP) superfamily includes at least 57 genes that encode enzymes with diverse metabolic and biosynthetic functions. |
| 1694 | 22969879 | This study was conducted in order to investigate the associations between polymorphisms in CYP superfamily genes (CYP11B2, CYP17A1, CYP2B6, CYP2C9, CYP2E1 and CYP7A1) and ischemic stroke (IS). |
| 1695 | 22969879 | The rs1799998 SNP of CYP11B2 and rs3808607 of CYP7A1 were related to diabetes mellitus in IS (p<0.05). |
| 1696 | 22969879 | CYP11B2, CYP2E1 and CYP7A1 SNPs were associated with IS in the population studied. |
| 1697 | 22969879 | Association between cytochrome P450 promoter polymorphisms and ischemic stroke. |
| 1698 | 22969879 | The human cytochrome P450 (CYP) superfamily includes at least 57 genes that encode enzymes with diverse metabolic and biosynthetic functions. |
| 1699 | 22969879 | This study was conducted in order to investigate the associations between polymorphisms in CYP superfamily genes (CYP11B2, CYP17A1, CYP2B6, CYP2C9, CYP2E1 and CYP7A1) and ischemic stroke (IS). |
| 1700 | 22969879 | The rs1799998 SNP of CYP11B2 and rs3808607 of CYP7A1 were related to diabetes mellitus in IS (p<0.05). |
| 1701 | 22969879 | CYP11B2, CYP2E1 and CYP7A1 SNPs were associated with IS in the population studied. |
| 1702 | 23018631 | These genes belong to three major classes: genes involved in drug metabolism and transporters that influence pharmacokinetics (including the cytochrome P450 [CYP] superfamily, the organic anion transporting polypeptide [OATP] family, and the polyspecific organic cation transporter [OCT] family); genes encoding drug targets and receptors (including peroxisome proliferator-activated receptor gamma [PPARG], the adenosine triphosphate [ATP]-sensitive potassium channel [K(ATP)], and incretin receptors); and genes involved in the causal pathway of T2DM that are able to modify the effects of drugs (including adipokines, transcription factor 7-like 2 (T cell specific, HMG-box) [TCF7L2], insulin receptor substrate 1 [IRS1], nitric oxide synthase 1 (neuronal) adaptor protein [NOS1AP], and solute carrier family 30 (zinc transporter), member 8 [SLC30A8]). |
| 1703 | 23018631 | In addition to these three major classes, we also review the available evidence on novel genes (CDK5 regulatory subunit associated protein 1-like 1 [CDKAL1], insulin-like growth factor 2 mRNA binding protein 2 [IGF2BP2], potassium voltage-gated channel, KQT-like subfamily, member 1 [KCNQ1], paired box 4 [PAX4] and neuronal differentiation 1 [NEUROD1] transcription factors, ataxia telangiectasia mutated [ATM], and serine racemase [SRR]) that have recently been proposed as possible modulators of therapeutic response in subjects with T2DM. |
| 1704 | 23038007 | In contrast, cytochrome P450 family 4, subfamily a, polypeptide 8 (Cyp4a8), and monocyte to macrophage differentiation-associated (Mmd2) were down-regulated relative to controls. |
| 1705 | 23038007 | Possible biomarkers due to 2AA toxicity in the liver for future study include Abcb1a, Nhej1, Adam8, Cdkn1a, Mgmt, and Nrcam. |
| 1706 | 23044879 | Furthermore the description of nonclassical lipoid CAH and the protean manifestations of P450 oxidoreductase (POR) deficiencies has expanded the spectrum of human disease caused by disordered steroidogenesis. |
| 1707 | 23105795 | The effect of oral administration of aqueous extract of F. bengalensis bark on blood glucose, serum electrolytes, serum glycolytic enzymes, liver microsomal protein, hepatic cytochrome P-450 dependent monooxygenase enzymes and lipid peroxidation in liver and kidney of streptozotocin -induced diabetic rats was studied. |
| 1708 | 23105795 | Oral administration of Ficus bengalensis to fed, fasted and glucose loaded diabetic rats significantly [F > 0.05 (ANOVA) and P< 0.05 (DMRT)] decreased the blood glucose level at 5 hrs and restored the levels of serum electrolytes, glycolytic enzymes and hepatic cytochrome P-450 dependent enzyme systems and decreased the formation of liver and kidney lipid peroxides at the end of 12 weeks. |
| 1709 | 23105795 | The effect of oral administration of aqueous extract of F. bengalensis bark on blood glucose, serum electrolytes, serum glycolytic enzymes, liver microsomal protein, hepatic cytochrome P-450 dependent monooxygenase enzymes and lipid peroxidation in liver and kidney of streptozotocin -induced diabetic rats was studied. |
| 1710 | 23105795 | Oral administration of Ficus bengalensis to fed, fasted and glucose loaded diabetic rats significantly [F > 0.05 (ANOVA) and P< 0.05 (DMRT)] decreased the blood glucose level at 5 hrs and restored the levels of serum electrolytes, glycolytic enzymes and hepatic cytochrome P-450 dependent enzyme systems and decreased the formation of liver and kidney lipid peroxides at the end of 12 weeks. |
| 1711 | 23278282 | Concentration of tacrolimus and major metabolites in kidney transplant recipients as a function of diabetes mellitus and cytochrome P450 3A gene polymorphism. |
| 1712 | 23278282 | Disposition of tacrolimus and its major metabolites, 13-O-desmethyl tacrolimus and 15-O-desmethyl tacrolimus, was evaluated in stable kidney transplant recipients in relation to diabetes mellitus and genetic polymorphism of cytochrome P450 (CYP) 3A. 2. |
| 1713 | 23278282 | In addition, single nucleotide polymorphisms of the following genes: CYP3A4 (CYP3A4: CYP3A4*1B, -392A > G), 3A5 (CYP3A5: CYP3A5*3, 6986A > G) and P-glycoprotein (ABCB1: 3435C > T) were characterized. 3. |
| 1714 | 23278282 | Genetic polymorphism of CYP3A5 or CYP3A4 influence tacrolimus or metabolites dose-normalized concentrations but not metabolite to parent concentration ratios. |
| 1715 | 23278282 | Concentration of tacrolimus and major metabolites in kidney transplant recipients as a function of diabetes mellitus and cytochrome P450 3A gene polymorphism. |
| 1716 | 23278282 | Disposition of tacrolimus and its major metabolites, 13-O-desmethyl tacrolimus and 15-O-desmethyl tacrolimus, was evaluated in stable kidney transplant recipients in relation to diabetes mellitus and genetic polymorphism of cytochrome P450 (CYP) 3A. 2. |
| 1717 | 23278282 | In addition, single nucleotide polymorphisms of the following genes: CYP3A4 (CYP3A4: CYP3A4*1B, -392A > G), 3A5 (CYP3A5: CYP3A5*3, 6986A > G) and P-glycoprotein (ABCB1: 3435C > T) were characterized. 3. |
| 1718 | 23278282 | Genetic polymorphism of CYP3A5 or CYP3A4 influence tacrolimus or metabolites dose-normalized concentrations but not metabolite to parent concentration ratios. |
| 1719 | 23365120 | Prenatal diagnosis of congenital adrenal hyperplasia caused by P450 oxidoreductase deficiency. |
| 1720 | 23370354 | Effect of Cytochrome P450 2C8*3 on the Population Pharmacokinetics of Pioglitazone in Healthy Caucasian Volunteers. |
| 1721 | 23370354 | Pioglitazone undergoes hepatic metabolism by cytochrome P450 2C8 (CYP2C8) and interindividual variability exists in pioglitazone disposition and response. |
| 1722 | 23370354 | Effect of Cytochrome P450 2C8*3 on the Population Pharmacokinetics of Pioglitazone in Healthy Caucasian Volunteers. |
| 1723 | 23370354 | Pioglitazone undergoes hepatic metabolism by cytochrome P450 2C8 (CYP2C8) and interindividual variability exists in pioglitazone disposition and response. |
| 1724 | 23371804 | The inhibitory potentials of DA-9801, D. rhizoma extract, D. nipponica Makino extract, and dioscin, an active component of DA-9801, on eight human cytochrome P450 (CYP) enzymes and four UDP-glucuronosyltransferase (UGT) enzymes were investigated in human liver microsomes using liquid chromatography-tandem mass spectrometry. |
| 1725 | 23371804 | DA-9801 showed slight inhibition of CYP1A2, CYP2C8, UGT1A1, and UGT1A9 enzyme activities with IC(50) values of 396.4, 449.9, 226.0, and 408.8 μg/mL, respectively. |
| 1726 | 23371804 | D. rhizoma extract showed negligible inhibition of CYP and UGT activities, but D. nipponica extract slightly inhibited CYP1A2, CYP2C8, CYP2C9, UGT1A1, and UGT1A9 activities with IC(50) values of 264.2, 237.1, 206.8, 302.4, and 383.1 μg/mL, respectively. |
| 1727 | 23371804 | DA-9801 showed volume per dose index values of 0.44-0.88 L for a 200-mg dose, suggesting that they may not cause the inhibition of the metabolism of CYP1A2, CYP2C8, UGT1A1, and UGT1A9-catalyzed drugs in humans. |
| 1728 | 23436494 | Significant drug-drug interactions exist due to mifepristone's effects on a number of cytochrome P450 enzymes. |
| 1729 | 23515292 | Ample evidences demonstrate that cytochrome P450 (CYP) epoxygenases metabolize arachidonic acid into epoxyeicosatrienoic acids (EETs), which play crucial and diverse roles in cardiovascular homeostasis. |
| 1730 | 23515292 | CYP2J3 gene delivery in vivo increased EET generation, enhanced adiponectin expression and secretion and accompanied by activation of adiponectin downstream signaling, and decreased insulin resistance as determined by plasma insulin levels, insulin resistance index and glucose tolerance test, as well as phosphorylation of protein kinase B in both liver and muscle. |
| 1731 | 23515292 | These results further highlight the beneficial roles of the CYP epoxygenase 2J3 and its metabolites EETs on adiponectin expression and secretion. |
| 1732 | 23631744 | Inhibition of organic anion transporting polypeptide 1B1 by CP-778875 (IC50 = 2.14 ± 0.40 μM) could be the dominant cause of the pharmacokinetic interaction as CP-778875 did not exhibit significant inhibition of cytochrome P450 3A4/3A5, multidrug resistant protein 1 or breast cancer resistant protein, which are also involved in the hepatobiliary disposition of atorvastatin. |
| 1733 | 23633864 | Livers were collected at the end of experiment for histopathology and estimation of reduced glutathione (GSH), thiobarbituric acid reacting substances (TBARS), protein carbonyls, glutathione S-transferase (GST), glucose-6-phosphate dehydrogenase (G6PD), Na(+)/K(+) ATPase and Mg(2)+ ATPase, cytochrome P450 (CYP) and glycogen. |
| 1734 | 23633864 | There was an increase in the concentration of TBARS and protein carbonyls, and decrease in the concentration of GSH and glycogen, and the activity of GST, G6PD, Na(+)/K(+) ATPase and Mg(2)+ ATPase in diabetic livers, while treatment groups showed significant (P < 0.05) increase in the above parameters. |
| 1735 | 23671024 | Liver microsome stability and cytochrome P450 metabolic tests were performed on this series, revealing undesirable pharmacokinetic profiles for the triazole compounds. |
| 1736 | 23671024 | Based on its enzyme activity, metabolic stability, and selectivity over DPP8 and DPP9, we selected compound 21 r for further study of its in vivo effects in mice using an oral glucose tolerance test (OGTT). |
| 1737 | 23671259 | Mammalian P450 side-chain cleavage enzyme (CYP11A1) catalyzes the first step of steroidogenesis, the conversion of cholesterol to pregnenolone. |
| 1738 | 23696562 | Cytochrome P450 (CYP) epoxygenases metabolize arachidonic acid to biologically active cis-epoxyeicosatrienoic acids, which have potent vasodilatory, antiinflammatory, antiapoptotic, and antidiabetes properties. |
| 1739 | 23696562 | Here, we showed the effects of cardiac-specific overexpression of CYP epoxygenase 2J2 (CYP2J2) on diabetic cardiomyopathy and insulin resistance in high-fat (HF) diet fed, low-dose streptozotocin-treated mice. |
| 1740 | 23696562 | We conclude that cardiac-specific overexpression of CYP2J2 significantly protects against diabetic cardiomyopathy, which may be due to improved cardiac insulin resistance, glucose uptake, and reversal of cardiac hypertrophy. |
| 1741 | 23696562 | Relevant mechanisms may include up-regulation of peroxisome proliferator-activated receptor γ, activation of insulin receptor and AMP-activated protein kinase signaling pathways, and inhibition of nuclear factor of activated T cells c3 signal by enhanced atrial natriuretic peptide production. |
| 1742 | 23697979 | Recent evidence supports a role of loss-of-function (LOF) variants in the cytochrome P450 enzyme CYP2C19 as a determinant of clopidogrel response. |
| 1743 | 23719679 | Included variants are located in genes coding for drug transporters, i.e., the organic anion-transporting family and the organic cation transporter family; genes involved in metabolism, i.e., cytochrome P450 superfamily; genes coding for drug receptors; T2DM-associated genes; and genes identified by genome-wide association studies (GWASs). |
| 1744 | 23733671 | CYP1A1 gene belongs to the cytochrome P450 family and is known better as smokers' gene due to its hyperactivation as a consequence of long term smoking. |
| 1745 | 23746107 | Other mechanisms, such as regulating ion channels, modulating Akt signaling pathways, histone deacetylase inhibition, and cytochrome P450 inhibition, could be responsible for the cardioprotective effect of garlic. |
| 1746 | 23824954 | Alcohol dehydrogenase and cytochrome P450 2E1 can be induced by long-term exposure to ethanol in cultured liver HEP-G2 cells. |
| 1747 | 23824954 | It has been shown in previous studies that liver HEP-G2 cells (human hepatocellular carcinoma) lose their ability to express active alcohol dehydrogenase (ADH) and cytochrome P450 2E1 (CYP2E1). |
| 1748 | 23824954 | Therefore, we tested the effect of long-term exposure to ethanol on the expression and activity of both ADH and CYP2E1 in these cells. |
| 1749 | 23824954 | The expression of ADH and CYP2E1 was assessed at the mRNA and/or protein level using real-time PCR and Western blot analysis. |
| 1750 | 23824954 | Specific colorimetric assays were used for the measurement of ADH and CYP2E1 enzymatic activities. |
| 1751 | 23824954 | Caco-2 cells (active CYP2E1 and inactive ADH) were used as control cells. |
| 1752 | 23824954 | Significantly increased protein expression of ADH (about 2.5-fold) as well as CYP2E1 (about 1.6-fold) was found in HEP-G2 cells after long-term (12 mo) exposure to ethanol. |
| 1753 | 23824954 | The activity of ADH and CYP2E1 was also significantly increased from 12 ± 3 and 6 ± 1 nmol/h/mg of total protein to 191 ± 9 and 57 ± 9 nmol/h/mg of total protein, respectively. |
| 1754 | 23824954 | Alcohol dehydrogenase and cytochrome P450 2E1 can be induced by long-term exposure to ethanol in cultured liver HEP-G2 cells. |
| 1755 | 23824954 | It has been shown in previous studies that liver HEP-G2 cells (human hepatocellular carcinoma) lose their ability to express active alcohol dehydrogenase (ADH) and cytochrome P450 2E1 (CYP2E1). |
| 1756 | 23824954 | Therefore, we tested the effect of long-term exposure to ethanol on the expression and activity of both ADH and CYP2E1 in these cells. |
| 1757 | 23824954 | The expression of ADH and CYP2E1 was assessed at the mRNA and/or protein level using real-time PCR and Western blot analysis. |
| 1758 | 23824954 | Specific colorimetric assays were used for the measurement of ADH and CYP2E1 enzymatic activities. |
| 1759 | 23824954 | Caco-2 cells (active CYP2E1 and inactive ADH) were used as control cells. |
| 1760 | 23824954 | Significantly increased protein expression of ADH (about 2.5-fold) as well as CYP2E1 (about 1.6-fold) was found in HEP-G2 cells after long-term (12 mo) exposure to ethanol. |
| 1761 | 23824954 | The activity of ADH and CYP2E1 was also significantly increased from 12 ± 3 and 6 ± 1 nmol/h/mg of total protein to 191 ± 9 and 57 ± 9 nmol/h/mg of total protein, respectively. |
| 1762 | 23846787 | Differential expression of cytochrome P450 omega-hydroxylase isoforms and their association with clinicopathological features in pancreatic ductal adenocarcinoma. |
| 1763 | 23894862 | For example, genetic variations of several membrane transporters, including SLC2A1/2 and SLC47A1/2 genes, are implicated in the highly variable glycemic response to metformin, a first-line drug used to treat newly diagnosed T2DM. |
| 1764 | 23894862 | Furthermore, cytochrome P450 (CYP) enzymes are implicated in variation of sulphonylurea and meglitinide metabolism. |
| 1765 | 23985694 | Metoprolol is a selective β1-adrenergic receptor antagonist metabolized by hepatic cytochrome P450s (CYPs). |
| 1766 | 23987740 | Contribution of cytochrome P450 isoforms to gliquidone metabolism in rats and human. |
| 1767 | 23987740 | Cytochrome P450 (CYP450) isoforms are involved in the metabolism of a majority of drugs in clinical use and plays a significant role in reducing possible drug interactions. |
| 1768 | 23987740 | The other isoforms involved in the metabolism included CYP3A, CYP2D, CYP1A and CYP2E. 4. |
| 1769 | 23987740 | Further investigation of rat recombinant enzymes showed that CYP3A1 and CYP2C11 played a major role in gliquidone metabolism in vitro, while CYP2D1, CYP1A2 and CYP2E1 were also involved. 5. |
| 1770 | 23987740 | The other isoforms involved in this process were CYP2C9, CYP2C19 and CYP2D6. 6. |
| 1771 | 23987740 | The intrinsic clearance (Vmax/Km) of CYP3A4 during gliquidone metabolism was 3-12 times greater than that of other CYP450 isoforms including CYP2C9, CYP2D6 and CYP2C19. 7. |
| 1772 | 23987740 | Contribution of cytochrome P450 isoforms to gliquidone metabolism in rats and human. |
| 1773 | 23987740 | Cytochrome P450 (CYP450) isoforms are involved in the metabolism of a majority of drugs in clinical use and plays a significant role in reducing possible drug interactions. |
| 1774 | 23987740 | The other isoforms involved in the metabolism included CYP3A, CYP2D, CYP1A and CYP2E. 4. |
| 1775 | 23987740 | Further investigation of rat recombinant enzymes showed that CYP3A1 and CYP2C11 played a major role in gliquidone metabolism in vitro, while CYP2D1, CYP1A2 and CYP2E1 were also involved. 5. |
| 1776 | 23987740 | The other isoforms involved in this process were CYP2C9, CYP2C19 and CYP2D6. 6. |
| 1777 | 23987740 | The intrinsic clearance (Vmax/Km) of CYP3A4 during gliquidone metabolism was 3-12 times greater than that of other CYP450 isoforms including CYP2C9, CYP2D6 and CYP2C19. 7. |
| 1778 | 12642470 | These compounds, along with troglitazone, were evaluated for the ability to induce cytochrome P450 enzymes (P450) in primary human hepatocyte cultures and to inhibit P450 in human microsomes. |
| 1779 | 12642470 | Inhibition studies conducted for CYP1A2, CYP2C8, CYP2C9, CYP2C19, CYP2D6, CYP3A4, CYP2A6, and CYP2E1 showed troglitazone to be the most nonselective and potent inhibitor followed by rosiglitazone and pioglitazone. |
| 1780 | 12642470 | In vitro, the thiazolidinediones were strong inhibitors of CYP2C8, with K(i) values between 1.7 and 5.6 microM, and of CYP3A4, with K(i) values between 1.6 and 11.8 microM. |
| 1781 | 15039298 | Incorporation of an oxygen from water into troglitazone quinone by cytochrome P450 and myeloperoxidase. |
| 1782 | 15039298 | Recently, cytochrome P450 (P450) was shown to be able to catalyze the formation of TGZ quinone. |
| 1783 | 15039298 | The formation of TGZ quinone was inhibited approximately 90% by coincubation with ascorbic acid or cysteine in the MPO reaction system but only 10 to 20% in liver microsomes, which might reflect the difference in the mechanism by which TGZ quinone is formed by P450 and peroxidase. |
| 1784 | 15039298 | Incorporation of an oxygen from water into troglitazone quinone by cytochrome P450 and myeloperoxidase. |
| 1785 | 15039298 | Recently, cytochrome P450 (P450) was shown to be able to catalyze the formation of TGZ quinone. |
| 1786 | 15039298 | The formation of TGZ quinone was inhibited approximately 90% by coincubation with ascorbic acid or cysteine in the MPO reaction system but only 10 to 20% in liver microsomes, which might reflect the difference in the mechanism by which TGZ quinone is formed by P450 and peroxidase. |
| 1787 | 15039298 | Incorporation of an oxygen from water into troglitazone quinone by cytochrome P450 and myeloperoxidase. |
| 1788 | 15039298 | Recently, cytochrome P450 (P450) was shown to be able to catalyze the formation of TGZ quinone. |
| 1789 | 15039298 | The formation of TGZ quinone was inhibited approximately 90% by coincubation with ascorbic acid or cysteine in the MPO reaction system but only 10 to 20% in liver microsomes, which might reflect the difference in the mechanism by which TGZ quinone is formed by P450 and peroxidase. |
| 1790 | 15155556 | Troglitazone (TGZ), the first glitazone used for the treatment of type II diabetes mellitus and removed from the market for liver toxicity, was shown to bind covalently to microsomal protein and glutathione (GSH) following activation by cytochrome P450 (P450). |
| 1791 | 15155556 | The covalent binding of (14)C-TGZ in dexamethasone-induced rat liver microsomes was NADPH-dependent and required the active form of P450; it was completely inhibited by ketoconazole (10 microM) and GSH (4 mM). |
| 1792 | 15155556 | Troglitazone (TGZ), the first glitazone used for the treatment of type II diabetes mellitus and removed from the market for liver toxicity, was shown to bind covalently to microsomal protein and glutathione (GSH) following activation by cytochrome P450 (P450). |
| 1793 | 15155556 | The covalent binding of (14)C-TGZ in dexamethasone-induced rat liver microsomes was NADPH-dependent and required the active form of P450; it was completely inhibited by ketoconazole (10 microM) and GSH (4 mM). |
| 1794 | 17020953 | Subsequent studies revealed that activation of acetaminophen to an active metabolite is primarily carried out by CYP2E1, an ethanol-inducible cytochrome P450 that was first suggested by characterization of the microsomal ethanol oxidation system. |
| 1795 | 17062778 | Involvement of multiple cytochrome P450 and UDP-glucuronosyltransferase enzymes in the in vitro metabolism of muraglitazar. |
| 1796 | 17062778 | This study describes the identification of human cytochrome P450 (P450) and UDP-glucuronosyltransferase (UGT) enzymes involved in the in vitro metabolism of muraglitazar. [(14)C]Muraglitazar was metabolized by cDNA-expressed CYP2C8, 2C9, 2C19, 2D6, and 3A4, but to a very minimal extent by CYP1A2, 2A6, 2B6, 2C18, 2E1, and 3A5. |
| 1797 | 17062778 | A combination of intrinsic clearance (V(max)/K(m)) and relative concentrations of each P450 enzyme in the human liver was used to predict the contribution of CYP2C8, 2C9, 2C19, 2D6, and 3A4 to the formation of each primary oxidative metabolite and to the overall oxidative metabolism of muraglitazar. |
| 1798 | 17062778 | Glucuronidation of [(14)C]muraglitazar was catalyzed by cDNA-expressed UGT1A1, 1A3, and 1A9, but not by UGT1A6, 1A8, 1A10, 2B4, 2B7, and 2B15. |
| 1799 | 17062778 | In summary, muraglitazar was metabolized by multiple P450 and UGT enzymes to form multiple metabolites. |
| 1800 | 17062778 | Involvement of multiple cytochrome P450 and UDP-glucuronosyltransferase enzymes in the in vitro metabolism of muraglitazar. |
| 1801 | 17062778 | This study describes the identification of human cytochrome P450 (P450) and UDP-glucuronosyltransferase (UGT) enzymes involved in the in vitro metabolism of muraglitazar. [(14)C]Muraglitazar was metabolized by cDNA-expressed CYP2C8, 2C9, 2C19, 2D6, and 3A4, but to a very minimal extent by CYP1A2, 2A6, 2B6, 2C18, 2E1, and 3A5. |
| 1802 | 17062778 | A combination of intrinsic clearance (V(max)/K(m)) and relative concentrations of each P450 enzyme in the human liver was used to predict the contribution of CYP2C8, 2C9, 2C19, 2D6, and 3A4 to the formation of each primary oxidative metabolite and to the overall oxidative metabolism of muraglitazar. |
| 1803 | 17062778 | Glucuronidation of [(14)C]muraglitazar was catalyzed by cDNA-expressed UGT1A1, 1A3, and 1A9, but not by UGT1A6, 1A8, 1A10, 2B4, 2B7, and 2B15. |
| 1804 | 17062778 | In summary, muraglitazar was metabolized by multiple P450 and UGT enzymes to form multiple metabolites. |
| 1805 | 17062778 | Involvement of multiple cytochrome P450 and UDP-glucuronosyltransferase enzymes in the in vitro metabolism of muraglitazar. |
| 1806 | 17062778 | This study describes the identification of human cytochrome P450 (P450) and UDP-glucuronosyltransferase (UGT) enzymes involved in the in vitro metabolism of muraglitazar. [(14)C]Muraglitazar was metabolized by cDNA-expressed CYP2C8, 2C9, 2C19, 2D6, and 3A4, but to a very minimal extent by CYP1A2, 2A6, 2B6, 2C18, 2E1, and 3A5. |
| 1807 | 17062778 | A combination of intrinsic clearance (V(max)/K(m)) and relative concentrations of each P450 enzyme in the human liver was used to predict the contribution of CYP2C8, 2C9, 2C19, 2D6, and 3A4 to the formation of each primary oxidative metabolite and to the overall oxidative metabolism of muraglitazar. |
| 1808 | 17062778 | Glucuronidation of [(14)C]muraglitazar was catalyzed by cDNA-expressed UGT1A1, 1A3, and 1A9, but not by UGT1A6, 1A8, 1A10, 2B4, 2B7, and 2B15. |
| 1809 | 17062778 | In summary, muraglitazar was metabolized by multiple P450 and UGT enzymes to form multiple metabolites. |
| 1810 | 17062778 | Involvement of multiple cytochrome P450 and UDP-glucuronosyltransferase enzymes in the in vitro metabolism of muraglitazar. |
| 1811 | 17062778 | This study describes the identification of human cytochrome P450 (P450) and UDP-glucuronosyltransferase (UGT) enzymes involved in the in vitro metabolism of muraglitazar. [(14)C]Muraglitazar was metabolized by cDNA-expressed CYP2C8, 2C9, 2C19, 2D6, and 3A4, but to a very minimal extent by CYP1A2, 2A6, 2B6, 2C18, 2E1, and 3A5. |
| 1812 | 17062778 | A combination of intrinsic clearance (V(max)/K(m)) and relative concentrations of each P450 enzyme in the human liver was used to predict the contribution of CYP2C8, 2C9, 2C19, 2D6, and 3A4 to the formation of each primary oxidative metabolite and to the overall oxidative metabolism of muraglitazar. |
| 1813 | 17062778 | Glucuronidation of [(14)C]muraglitazar was catalyzed by cDNA-expressed UGT1A1, 1A3, and 1A9, but not by UGT1A6, 1A8, 1A10, 2B4, 2B7, and 2B15. |
| 1814 | 17062778 | In summary, muraglitazar was metabolized by multiple P450 and UGT enzymes to form multiple metabolites. |
| 1815 | 17591676 | Dehydroepiandrosterone induces human CYP2B6 through the constitutive androstane receptor. |
| 1816 | 17591676 | Treatment of rats with DHEA influences expression of cytochrome P450 (P450) genes, including peroxisome proliferator-activated receptor alpha (PPAR alpha)- and pregnane X receptor (PXR)-mediated induction of CYP4As and CYP3A23, and suppression of CYP2C11. |
| 1817 | 17591676 | DHEA treatment elevated the expression and activities of CYP3A4, CYP2C9, CYP2C19, and CYP2B6 in primary cultures of human hepatocytes. |
| 1818 | 17591676 | Induction of CYP3A4 in human hepatocytes was consistent with studies in rats, but induction of CYP2Cs was unexpected. |
| 1819 | 17591676 | Because CYP2B6 induction by DHEA in human hepatocytes might involve either PXR or constitutive androstane receptor (CAR) activation, we performed experiments in primary hepatocytes from CAR knockout mice and observed that CAR was required for maximal induction of Cyp2b10 by DHEA. |
| 1820 | 17591676 | The effect of DHEA on the activation of the xenosensors PPAR alpha, PXR, and CAR, and the consequent potential for adverse drug/toxicant interactions should be considered in humans treated with this nutriceutical agent. |
| 1821 | 17591676 | Dehydroepiandrosterone induces human CYP2B6 through the constitutive androstane receptor. |
| 1822 | 17591676 | Treatment of rats with DHEA influences expression of cytochrome P450 (P450) genes, including peroxisome proliferator-activated receptor alpha (PPAR alpha)- and pregnane X receptor (PXR)-mediated induction of CYP4As and CYP3A23, and suppression of CYP2C11. |
| 1823 | 17591676 | DHEA treatment elevated the expression and activities of CYP3A4, CYP2C9, CYP2C19, and CYP2B6 in primary cultures of human hepatocytes. |
| 1824 | 17591676 | Induction of CYP3A4 in human hepatocytes was consistent with studies in rats, but induction of CYP2Cs was unexpected. |
| 1825 | 17591676 | Because CYP2B6 induction by DHEA in human hepatocytes might involve either PXR or constitutive androstane receptor (CAR) activation, we performed experiments in primary hepatocytes from CAR knockout mice and observed that CAR was required for maximal induction of Cyp2b10 by DHEA. |
| 1826 | 17591676 | The effect of DHEA on the activation of the xenosensors PPAR alpha, PXR, and CAR, and the consequent potential for adverse drug/toxicant interactions should be considered in humans treated with this nutriceutical agent. |
| 1827 | 17591676 | Dehydroepiandrosterone induces human CYP2B6 through the constitutive androstane receptor. |
| 1828 | 17591676 | Treatment of rats with DHEA influences expression of cytochrome P450 (P450) genes, including peroxisome proliferator-activated receptor alpha (PPAR alpha)- and pregnane X receptor (PXR)-mediated induction of CYP4As and CYP3A23, and suppression of CYP2C11. |
| 1829 | 17591676 | DHEA treatment elevated the expression and activities of CYP3A4, CYP2C9, CYP2C19, and CYP2B6 in primary cultures of human hepatocytes. |
| 1830 | 17591676 | Induction of CYP3A4 in human hepatocytes was consistent with studies in rats, but induction of CYP2Cs was unexpected. |
| 1831 | 17591676 | Because CYP2B6 induction by DHEA in human hepatocytes might involve either PXR or constitutive androstane receptor (CAR) activation, we performed experiments in primary hepatocytes from CAR knockout mice and observed that CAR was required for maximal induction of Cyp2b10 by DHEA. |
| 1832 | 17591676 | The effect of DHEA on the activation of the xenosensors PPAR alpha, PXR, and CAR, and the consequent potential for adverse drug/toxicant interactions should be considered in humans treated with this nutriceutical agent. |
| 1833 | 17591676 | Dehydroepiandrosterone induces human CYP2B6 through the constitutive androstane receptor. |
| 1834 | 17591676 | Treatment of rats with DHEA influences expression of cytochrome P450 (P450) genes, including peroxisome proliferator-activated receptor alpha (PPAR alpha)- and pregnane X receptor (PXR)-mediated induction of CYP4As and CYP3A23, and suppression of CYP2C11. |
| 1835 | 17591676 | DHEA treatment elevated the expression and activities of CYP3A4, CYP2C9, CYP2C19, and CYP2B6 in primary cultures of human hepatocytes. |
| 1836 | 17591676 | Induction of CYP3A4 in human hepatocytes was consistent with studies in rats, but induction of CYP2Cs was unexpected. |
| 1837 | 17591676 | Because CYP2B6 induction by DHEA in human hepatocytes might involve either PXR or constitutive androstane receptor (CAR) activation, we performed experiments in primary hepatocytes from CAR knockout mice and observed that CAR was required for maximal induction of Cyp2b10 by DHEA. |
| 1838 | 17591676 | The effect of DHEA on the activation of the xenosensors PPAR alpha, PXR, and CAR, and the consequent potential for adverse drug/toxicant interactions should be considered in humans treated with this nutriceutical agent. |
| 1839 | 19074975 | Vildagliptin was extensively metabolized via at least four pathways before excretion, with the major metabolite M20.7 resulting from cyano group hydrolysis, which is not mediated by cytochrome P450 (P450) enzymes. |
| 1840 | 19996149 | The preclinical characterization of dapagliflozin, to allow compound selection and prediction of pharmacological and dispositional behavior in the clinic, involved Caco-2 cell permeability studies, cytochrome P450 (P450) inhibition and induction studies, P450 reaction phenotyping, metabolite identification in hepatocytes, and pharmacokinetics in rats, dogs, and monkeys. |
| 1841 | 20736321 | Hepatic gene expression of Cyp2b10, Cyp2c29, Cyp3a11, Cyp2e1, Cyp4a10, Nr1i2, Nr1i3, slco1a1, slco1a4, slco1b2, abcb1b, abcc2, and abcg2 was examined using the real-time polymerase chain reaction method in male db/db mice, a commonly used type II diabetes model. |
| 1842 | 20736321 | Functional analysis was conducted in hepatic microsomes for Cyp2b, Cyp2c, and Cyp3a using cytochrome P450-specific substrates. |
| 1843 | 20736321 | No expression changes were observed for Cyp2e1, Nr1i2, Nr1i3, abcc2, and abcg2. |
| 1844 | 21690265 | Reaction phenotyping studies using recombinant enzymes indicated a role of CYP3A4/3A5, CYP2D6, and UGT1A9/2B7 in the metabolism of PF-04971729. |
| 1845 | 21690265 | No competitive or time-dependent inhibition of the major human cytochrome P450 enzymes was discerned with PF-04971729. |
| 1846 | 21742899 | Expression of relevant transporters, such as Multidrug resistance protein 1 (Mdr1), and cytochrome P450 3a2 (Cyp3a2), which metabolizes LPV in rodents, was measured in maternal liver via quantitative reverse transcriptase polymerase chain reaction and Western blot analysis. |
| 1847 | 22393122 | The purpose of this study was to evaluate the contributions of impaired cytochrome P450 and breast cancer resistance protein (BCRP) activity and expression to drug pharmacokinetics under diabetic conditions. |
| 1848 | 22496391 | Characterization of the in vitro and in vivo metabolism and disposition and cytochrome P450 inhibition/induction profile of saxagliptin in human. |
| 1849 | 22496391 | Cytochrome P450 (P450) enzymes CYP3A4 and CYP3A5 metabolized saxagliptin and formed M2. |
| 1850 | 22496391 | Kinetic experiments indicated that the catalytic efficiency (V(max)/K(m)) for CYP3A4 was approximately 4-fold higher than that for CYP3A5. |
| 1851 | 22496391 | Characterization of the in vitro and in vivo metabolism and disposition and cytochrome P450 inhibition/induction profile of saxagliptin in human. |
| 1852 | 22496391 | Cytochrome P450 (P450) enzymes CYP3A4 and CYP3A5 metabolized saxagliptin and formed M2. |
| 1853 | 22496391 | Kinetic experiments indicated that the catalytic efficiency (V(max)/K(m)) for CYP3A4 was approximately 4-fold higher than that for CYP3A5. |
| 1854 | 22531045 | In vitro hepatotoxicity and cytochrome P450 induction and inhibition characteristics of carnosic acid, a dietary supplement with antiadipogenic properties. |
| 1855 | 22531045 | For this reason, hepatotoxicity and cytochrome P450 inhibition and induction studies were performed in primary human hepatocytes and microsomes. |
| 1856 | 22531045 | In human liver microsomes, carnosic acid did not exhibit significant time-dependent inhibition for any of the cytochrome P450 enzymes investigated, although it did inhibit CYP2C9- and CYP3A4-catalyzed reactions with K(i) values of 9.2 and 4.3 μM, respectively. |
| 1857 | 22531045 | Carnosic acid also induced CYP2B6 and CYP3A4 mRNA and enzyme activity in a dose-dependent manner. |
| 1858 | 22531045 | At 10 μM, carnosic acid increased CYP2B6 enzyme activity 61.6 and 49.3% in two donors compared with phenobarbital, and it increased CYP3A enzyme activity 82.6 and 142% compared with rifampicin. |
| 1859 | 22531045 | In vitro hepatotoxicity and cytochrome P450 induction and inhibition characteristics of carnosic acid, a dietary supplement with antiadipogenic properties. |
| 1860 | 22531045 | For this reason, hepatotoxicity and cytochrome P450 inhibition and induction studies were performed in primary human hepatocytes and microsomes. |
| 1861 | 22531045 | In human liver microsomes, carnosic acid did not exhibit significant time-dependent inhibition for any of the cytochrome P450 enzymes investigated, although it did inhibit CYP2C9- and CYP3A4-catalyzed reactions with K(i) values of 9.2 and 4.3 μM, respectively. |
| 1862 | 22531045 | Carnosic acid also induced CYP2B6 and CYP3A4 mRNA and enzyme activity in a dose-dependent manner. |
| 1863 | 22531045 | At 10 μM, carnosic acid increased CYP2B6 enzyme activity 61.6 and 49.3% in two donors compared with phenobarbital, and it increased CYP3A enzyme activity 82.6 and 142% compared with rifampicin. |
| 1864 | 22531045 | In vitro hepatotoxicity and cytochrome P450 induction and inhibition characteristics of carnosic acid, a dietary supplement with antiadipogenic properties. |
| 1865 | 22531045 | For this reason, hepatotoxicity and cytochrome P450 inhibition and induction studies were performed in primary human hepatocytes and microsomes. |
| 1866 | 22531045 | In human liver microsomes, carnosic acid did not exhibit significant time-dependent inhibition for any of the cytochrome P450 enzymes investigated, although it did inhibit CYP2C9- and CYP3A4-catalyzed reactions with K(i) values of 9.2 and 4.3 μM, respectively. |
| 1867 | 22531045 | Carnosic acid also induced CYP2B6 and CYP3A4 mRNA and enzyme activity in a dose-dependent manner. |
| 1868 | 22531045 | At 10 μM, carnosic acid increased CYP2B6 enzyme activity 61.6 and 49.3% in two donors compared with phenobarbital, and it increased CYP3A enzyme activity 82.6 and 142% compared with rifampicin. |
| 1869 | 22531045 | In vitro hepatotoxicity and cytochrome P450 induction and inhibition characteristics of carnosic acid, a dietary supplement with antiadipogenic properties. |
| 1870 | 22531045 | For this reason, hepatotoxicity and cytochrome P450 inhibition and induction studies were performed in primary human hepatocytes and microsomes. |
| 1871 | 22531045 | In human liver microsomes, carnosic acid did not exhibit significant time-dependent inhibition for any of the cytochrome P450 enzymes investigated, although it did inhibit CYP2C9- and CYP3A4-catalyzed reactions with K(i) values of 9.2 and 4.3 μM, respectively. |
| 1872 | 22531045 | Carnosic acid also induced CYP2B6 and CYP3A4 mRNA and enzyme activity in a dose-dependent manner. |
| 1873 | 22531045 | At 10 μM, carnosic acid increased CYP2B6 enzyme activity 61.6 and 49.3% in two donors compared with phenobarbital, and it increased CYP3A enzyme activity 82.6 and 142% compared with rifampicin. |
| 1874 | 22531045 | In vitro hepatotoxicity and cytochrome P450 induction and inhibition characteristics of carnosic acid, a dietary supplement with antiadipogenic properties. |
| 1875 | 22531045 | For this reason, hepatotoxicity and cytochrome P450 inhibition and induction studies were performed in primary human hepatocytes and microsomes. |
| 1876 | 22531045 | In human liver microsomes, carnosic acid did not exhibit significant time-dependent inhibition for any of the cytochrome P450 enzymes investigated, although it did inhibit CYP2C9- and CYP3A4-catalyzed reactions with K(i) values of 9.2 and 4.3 μM, respectively. |
| 1877 | 22531045 | Carnosic acid also induced CYP2B6 and CYP3A4 mRNA and enzyme activity in a dose-dependent manner. |
| 1878 | 22531045 | At 10 μM, carnosic acid increased CYP2B6 enzyme activity 61.6 and 49.3% in two donors compared with phenobarbital, and it increased CYP3A enzyme activity 82.6 and 142% compared with rifampicin. |
| 1879 | 22798551 | The toxicants in cigarette smoke can reach pancreatic tissue, and most of the toxicants require cytochrome P450 (P450)-mediated metabolic activation to exert their toxicity. |
| 1880 | 22798551 | Among all the human P450 enzymes, CYP2A13 is the most efficient enzyme in the metabolic activation of 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone (NNK), a major tobacco-specific toxicant and a suspected human carcinogen. |
| 1881 | 22798551 | The toxicants in cigarette smoke can reach pancreatic tissue, and most of the toxicants require cytochrome P450 (P450)-mediated metabolic activation to exert their toxicity. |
| 1882 | 22798551 | Among all the human P450 enzymes, CYP2A13 is the most efficient enzyme in the metabolic activation of 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone (NNK), a major tobacco-specific toxicant and a suspected human carcinogen. |
| 1883 | 22896728 | In vitro experiments with recombinant cytochrome P450 isoforms suggested that the formation of M5 was catalyzed both by CYP2D6 and CYP3A4. |
| 1884 | 22896728 | Molecular docking simulations showed that the 5' position of the pyrimidine moiety of PF-00734200 can access the heme iron-oxo of both CYP3A4 and CYP2D6 in an energetically favored orientation. |
| 1885 | 23418369 | We have used human liver microsomes in combination with selective cytochrome P450 inhibitors, specific substrates, and antibodies to identify CYP2E1 as the main activity producing nicotinamide N-oxide. |
| 1886 | 12435796 | Liver X receptor (LXR) alpha and LXRbeta are nuclear oxysterol receptors whose biological function has so far been elucidated only with respect to cholesterol and lipid metabolism. |
| 1887 | 12435796 | Notably, LXR agonist treatment up-regulated CYP4A10 and CYP4A14 together with cytochrome P450 reductase, indicating a possible enhancement of microsomal lipid peroxidation. |
| 1888 | 16099841 | Design of PAP-1, a selective small molecule Kv1.3 blocker, for the suppression of effector memory T cells in autoimmune diseases. |
| 1889 | 16099841 | Unfortunately, none of the existing small-molecule Kv1.3 blockers is selective, and many of them, such as correolide, 4-phenyl-4-[3-(methoxyphenyl)-3-oxo-2-azapropyl]cyclohexanone, and our own compound Psora-4 inhibit the cardiac K+ channel Kv1.5. |
| 1890 | 16099841 | By further exploring the structure-activity relationship around Psora-4 through a combination of traditional medicinal chemistry and whole-cell patch-clamp, we identified a series of new phenoxyalkoxypsoralens that exhibit 2- to 50-fold selectivity for Kv1.3 over Kv1.5, depending on their exact substitution pattern. |
| 1891 | 16099841 | The most potent and "drug-like" compound of this series, 5-(4-phenoxybutoxy)psoralen (PAP-1), blocks Kv1.3 in a use-dependent manner, with a Hill coefficient of 2 and an EC50 of 2 nM, by preferentially binding to the C-type inactivated state of the channel. |
| 1892 | 16099841 | PAP-1 is 23-fold selective over Kv1.5, 33- to 125-fold selective over other Kv1-family channels, and 500- to 7500-fold selective over Kv2.1, Kv3.1, Kv3.2, Kv4.2, HERG, calcium-activated K+ channels, Na+,Ca2+, and Cl- channels. |
| 1893 | 16099841 | PAP-1 does not exhibit cytotoxic or phototoxic effects, is negative in the Ames test, and affects cytochrome P450-dependent enzymes only at micromolar concentrations. |
| 1894 | 16099841 | PAP-1 and several of its derivatives therefore constitute excellent new tools to further explore Kv1.3 as a target for immunosuppression and could potentially be developed into orally available immunomodulators. |
| 1895 | 20631053 | Functional characterization of the semisynthetic bile acid derivative INT-767, a dual farnesoid X receptor and TGR5 agonist. |
| 1896 | 20631053 | Two dedicated receptors for bile acids (BAs) have been identified, the nuclear hormone receptor farnesoid X receptor (FXR) and the G protein-coupled receptor TGR5, which represent attractive targets for the treatment of metabolic and chronic liver diseases. |
| 1897 | 20631053 | Previous work characterized 6α-ethyl-3α,7α-dihydroxy-5β-cholan-24-oic acid (INT-747), a potent and selective FXR agonist, as well as 6α-ethyl-23(S)-methyl-3α,7α,12α-trihydroxy-5β-cholan-24-oic acid (INT-777), a potent and selective TGR5 agonist. |
| 1898 | 20631053 | INT-767 is a potent agonist for both FXR (mean EC(50), 30 nM by PerkinElmer AlphaScreen assay) and TGR5 (mean EC(50), 630 nM by time resolved-fluorescence resonance energy transfer), the first compound described so far to potently and selectively activate both BA receptors. |
| 1899 | 20631053 | INT-767 does not show cytotoxic effects in HepG2 cells, does not inhibit cytochrome P450 enzymes, is highly stable to phase I and II enzymatic modifications, and does not inhibit the human ether-a-go-go-related gene potassium channel. |
| 1900 | 20631053 | In line with its dual activity, INT-767 induces FXR-dependent lipid uptake by adipocytes, with the beneficial effect of shuttling lipids from central hepatic to peripheral fat storage, and promotes TGR5-dependent glucagon-like peptide-1 secretion by enteroendocrine cells, a validated target in the treatment of type 2 diabetes. |
| 1901 | 20631053 | Collectively, these preclinical results indicate that INT-767 is a safe and effective modulator of FXR and TGR5-dependent pathways, suggesting potential clinical applications in the treatment of liver and metabolic diseases. |