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Gene Information
Gene symbol: MMP2
Gene name: matrix metallopeptidase 2 (gelatinase A, 72kDa gelatinase, 72kDa type IV collagenase)
HGNC ID: 7166
Synonyms: TBE-1
Related Genes
Related Sentences
| # | PMID | Sentence |
| 1 | 7533311 | The mRNA levels for MMP-1 and MMP-3 decreased with age in STZ-induced diabetes. |
| 2 | 7533311 | At 24 weeks after STZ injection, mRNA levels for MMP-1 and MMP-3 fell to 40% (p < 0.01) and 20% (p < 0.01), respectively, in the glomeruli of diabetic rats when compared with control rats. |
| 3 | 7533311 | In contrast, mRNA levels for TIMP-1 increased significantly with age in the diabetic glomeruli and reached an 8-fold (p < 0.01) increased at 24 weeks after STZ injection. mRNA levels for MMP-2 were not altered in glomeruli from diabetic and control rats throughout the experimental period, whereas those for MMP-9 were not detected in glomeruli from either group of rats. |
| 4 | 7533311 | Insulin treatment partially ameliorated the decrease in mRNA levels for MMP-1 and MMP-3 and the increase in those for TIMP-1 in the glomeruli of diabetic rats. |
| 5 | 7533311 | These data indicate that abnormal gene regulation of MMPs and TIMP-1 in the glomeruli of diabetic rats may contribute to the progression of glomerular lesions and that hyperglycemia or insulin deficiency may be associated with abnormal MMPs and TIMP-1 gene regulation. |
| 6 | 8126240 | Both saliva and GCF collected from adult periodontitis, localized juvenile periodontitis and type II diabetes mellitus periodontitis patients contained species moving identically with gelatinase isolated from human neutrophils or MMP-9 (mean 98 kD), and species with mobility similar to gelatinase in fibroblast cell culture supernatants or MMP-2 (mean 76 kD). |
| 7 | 9394952 | The expression of mRNA and distribution of alpha 1(IV), alpha 3(IV) chains of type IV collagen, matrix metalloproteinase 2 (MMP-2), and tissue inhibitor of metalloproteinase 1 (TIMP-1) were examined in kidneys from streptozotocin-diabetic rats, 2.5 months after administration of the drug, an early time point when specific diabetic glomerular changes were still minimal. |
| 8 | 9394952 | Northern blot analysis, using whole kidney mRNA, revealed that diabetic rat kidneys expressed 113.5% more alpha 1(IV), 46.5% more alpha 3(IV), 54.8% less MMP-2 and 246% more TIMP-1 (in all instances: p < 0.05). |
| 9 | 9394952 | A quantitative analysis of the data indicated the following changes in glomeruli: (1) 74.6% more alpha 1(IV), (2) 103.8% more alpha 3(IV), (3) 40.7% less MMP-2 and (4) 80.9% more TIMP-1. |
| 10 | 9394952 | The expression of mRNA and distribution of alpha 1(IV), alpha 3(IV) chains of type IV collagen, matrix metalloproteinase 2 (MMP-2), and tissue inhibitor of metalloproteinase 1 (TIMP-1) were examined in kidneys from streptozotocin-diabetic rats, 2.5 months after administration of the drug, an early time point when specific diabetic glomerular changes were still minimal. |
| 11 | 9394952 | Northern blot analysis, using whole kidney mRNA, revealed that diabetic rat kidneys expressed 113.5% more alpha 1(IV), 46.5% more alpha 3(IV), 54.8% less MMP-2 and 246% more TIMP-1 (in all instances: p < 0.05). |
| 12 | 9394952 | A quantitative analysis of the data indicated the following changes in glomeruli: (1) 74.6% more alpha 1(IV), (2) 103.8% more alpha 3(IV), (3) 40.7% less MMP-2 and (4) 80.9% more TIMP-1. |
| 13 | 9394952 | The expression of mRNA and distribution of alpha 1(IV), alpha 3(IV) chains of type IV collagen, matrix metalloproteinase 2 (MMP-2), and tissue inhibitor of metalloproteinase 1 (TIMP-1) were examined in kidneys from streptozotocin-diabetic rats, 2.5 months after administration of the drug, an early time point when specific diabetic glomerular changes were still minimal. |
| 14 | 9394952 | Northern blot analysis, using whole kidney mRNA, revealed that diabetic rat kidneys expressed 113.5% more alpha 1(IV), 46.5% more alpha 3(IV), 54.8% less MMP-2 and 246% more TIMP-1 (in all instances: p < 0.05). |
| 15 | 9394952 | A quantitative analysis of the data indicated the following changes in glomeruli: (1) 74.6% more alpha 1(IV), (2) 103.8% more alpha 3(IV), (3) 40.7% less MMP-2 and (4) 80.9% more TIMP-1. |
| 16 | 9447953 | The expression of genes for MMP2 and TIMP2 in human diabetic nephropathy was investigated. |
| 17 | 9447953 | Contrary to TIMP2 which was expressed both in tubulo-interstitium and glomeruli in almost all renal biopsies, MMP2 gene down-regulation was observed in glomeruli from all NIDDM patients, irrespective of the albumin excretion rate, and of renal histology. |
| 18 | 9447953 | In conclusion, this study demonstrates that: 1) in glomeruli of NIDDM patients the MMP2 gene is down-regulated; 2) in biopsies of NIDDM patients the MMP2/TIMP2 pattern is peculiar for NIDDM; 3) the MMP2 gene down-regulation is observed in all NIDDM patients, irrespective of the level of albuminuria and of renal histology. |
| 19 | 9447953 | The expression of genes for MMP2 and TIMP2 in human diabetic nephropathy was investigated. |
| 20 | 9447953 | Contrary to TIMP2 which was expressed both in tubulo-interstitium and glomeruli in almost all renal biopsies, MMP2 gene down-regulation was observed in glomeruli from all NIDDM patients, irrespective of the albumin excretion rate, and of renal histology. |
| 21 | 9447953 | In conclusion, this study demonstrates that: 1) in glomeruli of NIDDM patients the MMP2 gene is down-regulated; 2) in biopsies of NIDDM patients the MMP2/TIMP2 pattern is peculiar for NIDDM; 3) the MMP2 gene down-regulation is observed in all NIDDM patients, irrespective of the level of albuminuria and of renal histology. |
| 22 | 9447953 | The expression of genes for MMP2 and TIMP2 in human diabetic nephropathy was investigated. |
| 23 | 9447953 | Contrary to TIMP2 which was expressed both in tubulo-interstitium and glomeruli in almost all renal biopsies, MMP2 gene down-regulation was observed in glomeruli from all NIDDM patients, irrespective of the albumin excretion rate, and of renal histology. |
| 24 | 9447953 | In conclusion, this study demonstrates that: 1) in glomeruli of NIDDM patients the MMP2 gene is down-regulated; 2) in biopsies of NIDDM patients the MMP2/TIMP2 pattern is peculiar for NIDDM; 3) the MMP2 gene down-regulation is observed in all NIDDM patients, irrespective of the level of albuminuria and of renal histology. |
| 25 | 9703333 | Competition-based reverse transcription-polymerase chain reaction revealed that nondiabetic and diabetic HRECs expressed constitutively mRNA for MMP-2, MMP-9, tissue inhibitor of metalloproteinase (TIMP)-1, TIMP-2, and fibronectin. |
| 26 | 9703333 | After exposure to 5 or 30 mmol/l glucose, no changes were detected in mRNA levels in MMP-2 or MMP-9, their inhibitors TIMP-1 and TIMP-2, or fibronectin in either nondiabetic or diabetic HREC cultures. |
| 27 | 9703333 | Competition-based reverse transcription-polymerase chain reaction revealed that nondiabetic and diabetic HRECs expressed constitutively mRNA for MMP-2, MMP-9, tissue inhibitor of metalloproteinase (TIMP)-1, TIMP-2, and fibronectin. |
| 28 | 9703333 | After exposure to 5 or 30 mmol/l glucose, no changes were detected in mRNA levels in MMP-2 or MMP-9, their inhibitors TIMP-1 and TIMP-2, or fibronectin in either nondiabetic or diabetic HREC cultures. |
| 29 | 9808089 | This study examines lines of all three glomerular cell types derived from female B6SJLF1/J mice, as well as mRNA levels for collagens alpha1(I), alpha1(IV), alpha3 (IV), alpha5 (IV), and alpha1 (VI), laminin, tenascin, matrix metalloproteinase-2 (MMP-2), and MMP-9. |
| 30 | 9808089 | MMP-2 and MMP-9 enzyme activity was measured by zymography. |
| 31 | 9808089 | However, they express only low levels of MMP-2 and no detectable MMP-9. |
| 32 | 9808089 | Stimulation with exogenous transforming growth factor-beta1 leads to a significant increase in collagen I, tissue inhibitors of metalloproteinase-1, and MMP-9 in conditioned media. |
| 33 | 9808089 | This study examines lines of all three glomerular cell types derived from female B6SJLF1/J mice, as well as mRNA levels for collagens alpha1(I), alpha1(IV), alpha3 (IV), alpha5 (IV), and alpha1 (VI), laminin, tenascin, matrix metalloproteinase-2 (MMP-2), and MMP-9. |
| 34 | 9808089 | MMP-2 and MMP-9 enzyme activity was measured by zymography. |
| 35 | 9808089 | However, they express only low levels of MMP-2 and no detectable MMP-9. |
| 36 | 9808089 | Stimulation with exogenous transforming growth factor-beta1 leads to a significant increase in collagen I, tissue inhibitors of metalloproteinase-1, and MMP-9 in conditioned media. |
| 37 | 9808089 | This study examines lines of all three glomerular cell types derived from female B6SJLF1/J mice, as well as mRNA levels for collagens alpha1(I), alpha1(IV), alpha3 (IV), alpha5 (IV), and alpha1 (VI), laminin, tenascin, matrix metalloproteinase-2 (MMP-2), and MMP-9. |
| 38 | 9808089 | MMP-2 and MMP-9 enzyme activity was measured by zymography. |
| 39 | 9808089 | However, they express only low levels of MMP-2 and no detectable MMP-9. |
| 40 | 9808089 | Stimulation with exogenous transforming growth factor-beta1 leads to a significant increase in collagen I, tissue inhibitors of metalloproteinase-1, and MMP-9 in conditioned media. |
| 41 | 9890310 | In conclusion, PPS alters extracellular matrix turnover through the induction of MMP-2 and alterations in the TIMP profile and may be useful in decreasing progressive glomerulosclerosis. |
| 42 | 10426384 | IGF-1 decreases collagen degradation in diabetic NOD mesangial cells: implications for diabetic nephropathy. |
| 43 | 10426384 | We showed that mesangial cells (MCs) from diabetic mice exhibited a stable phenotypic switch, consisting of both increased IGF-1 synthesis and proliferation (Elliot SJ, Striker LJ, Hattori M, Yang CW, He CJ, Peten EP, Striker GE: Mesangial cells from diabetic NOD mice constitutively secrete increased amounts of insulin-like growth factor-I. |
| 44 | 10426384 | Because the extracellular matrix (ECM) accumulation in diabetic glomerulosclerosis may be partly due to decreased degradation, we examined the effect of excess IGF-1 on collagen turnover and the activity of metalloproteinases (MMPs) and tissue inhibitors of metalloproteinase (TIMPs) in diabetic and nondiabetic NOD-MC. |
| 45 | 10426384 | Total collagen degradation was reduced by 58 +/- 18% in diabetic NOD-MCs, which correlated with a constitutive decrease in MMP-2 activity and mRNA levels, and nearly undetectable MMP-9 activity and mRNA. |
| 46 | 10426384 | The addition of recombinant IGF-1 to nondiabetic NOD-MC resulted in a decrease in MMP-2 and TIMP activity. |
| 47 | 10426384 | Furthermore, treatment of diabetic NOD-MC with a neutralizing antibody against IGF-1 increased the latent form, and restored the active form, of MMP-2. |
| 48 | 10426384 | In conclusion, the excessive production of IGF-1 contributes to the altered ECM turnover in diabetic NOD-MC, largely through a reduction of MMP-2 activity. |
| 49 | 10426384 | IGF-1 decreases collagen degradation in diabetic NOD mesangial cells: implications for diabetic nephropathy. |
| 50 | 10426384 | We showed that mesangial cells (MCs) from diabetic mice exhibited a stable phenotypic switch, consisting of both increased IGF-1 synthesis and proliferation (Elliot SJ, Striker LJ, Hattori M, Yang CW, He CJ, Peten EP, Striker GE: Mesangial cells from diabetic NOD mice constitutively secrete increased amounts of insulin-like growth factor-I. |
| 51 | 10426384 | Because the extracellular matrix (ECM) accumulation in diabetic glomerulosclerosis may be partly due to decreased degradation, we examined the effect of excess IGF-1 on collagen turnover and the activity of metalloproteinases (MMPs) and tissue inhibitors of metalloproteinase (TIMPs) in diabetic and nondiabetic NOD-MC. |
| 52 | 10426384 | Total collagen degradation was reduced by 58 +/- 18% in diabetic NOD-MCs, which correlated with a constitutive decrease in MMP-2 activity and mRNA levels, and nearly undetectable MMP-9 activity and mRNA. |
| 53 | 10426384 | The addition of recombinant IGF-1 to nondiabetic NOD-MC resulted in a decrease in MMP-2 and TIMP activity. |
| 54 | 10426384 | Furthermore, treatment of diabetic NOD-MC with a neutralizing antibody against IGF-1 increased the latent form, and restored the active form, of MMP-2. |
| 55 | 10426384 | In conclusion, the excessive production of IGF-1 contributes to the altered ECM turnover in diabetic NOD-MC, largely through a reduction of MMP-2 activity. |
| 56 | 10426384 | IGF-1 decreases collagen degradation in diabetic NOD mesangial cells: implications for diabetic nephropathy. |
| 57 | 10426384 | We showed that mesangial cells (MCs) from diabetic mice exhibited a stable phenotypic switch, consisting of both increased IGF-1 synthesis and proliferation (Elliot SJ, Striker LJ, Hattori M, Yang CW, He CJ, Peten EP, Striker GE: Mesangial cells from diabetic NOD mice constitutively secrete increased amounts of insulin-like growth factor-I. |
| 58 | 10426384 | Because the extracellular matrix (ECM) accumulation in diabetic glomerulosclerosis may be partly due to decreased degradation, we examined the effect of excess IGF-1 on collagen turnover and the activity of metalloproteinases (MMPs) and tissue inhibitors of metalloproteinase (TIMPs) in diabetic and nondiabetic NOD-MC. |
| 59 | 10426384 | Total collagen degradation was reduced by 58 +/- 18% in diabetic NOD-MCs, which correlated with a constitutive decrease in MMP-2 activity and mRNA levels, and nearly undetectable MMP-9 activity and mRNA. |
| 60 | 10426384 | The addition of recombinant IGF-1 to nondiabetic NOD-MC resulted in a decrease in MMP-2 and TIMP activity. |
| 61 | 10426384 | Furthermore, treatment of diabetic NOD-MC with a neutralizing antibody against IGF-1 increased the latent form, and restored the active form, of MMP-2. |
| 62 | 10426384 | In conclusion, the excessive production of IGF-1 contributes to the altered ECM turnover in diabetic NOD-MC, largely through a reduction of MMP-2 activity. |
| 63 | 10426384 | IGF-1 decreases collagen degradation in diabetic NOD mesangial cells: implications for diabetic nephropathy. |
| 64 | 10426384 | We showed that mesangial cells (MCs) from diabetic mice exhibited a stable phenotypic switch, consisting of both increased IGF-1 synthesis and proliferation (Elliot SJ, Striker LJ, Hattori M, Yang CW, He CJ, Peten EP, Striker GE: Mesangial cells from diabetic NOD mice constitutively secrete increased amounts of insulin-like growth factor-I. |
| 65 | 10426384 | Because the extracellular matrix (ECM) accumulation in diabetic glomerulosclerosis may be partly due to decreased degradation, we examined the effect of excess IGF-1 on collagen turnover and the activity of metalloproteinases (MMPs) and tissue inhibitors of metalloproteinase (TIMPs) in diabetic and nondiabetic NOD-MC. |
| 66 | 10426384 | Total collagen degradation was reduced by 58 +/- 18% in diabetic NOD-MCs, which correlated with a constitutive decrease in MMP-2 activity and mRNA levels, and nearly undetectable MMP-9 activity and mRNA. |
| 67 | 10426384 | The addition of recombinant IGF-1 to nondiabetic NOD-MC resulted in a decrease in MMP-2 and TIMP activity. |
| 68 | 10426384 | Furthermore, treatment of diabetic NOD-MC with a neutralizing antibody against IGF-1 increased the latent form, and restored the active form, of MMP-2. |
| 69 | 10426384 | In conclusion, the excessive production of IGF-1 contributes to the altered ECM turnover in diabetic NOD-MC, largely through a reduction of MMP-2 activity. |
| 70 | 10512375 | Because angiotensin II (AII) is involved in the pathogenesis of diabetic nephropathy, the present studies were performed to determine if AII mediates glucose-induced 1) inhibition of mesangial collagenase activity, 2) mesangial matrix accumulation, and 3) in-crease in transforming growth factor (TGF)-beta1 secretion in mesangial cells. |
| 71 | 10512375 | Exposure of mesangial cells to 30 mmol/l glucose (high glucose) vs. 5 mmol/glucose (normal glucose) for 5 days resulted in a significant decrease in collagenase activity (25%) that was normalized by 10(-4) mol/l losartan, a type 1 angiotensin II (AT1) receptor antagonist. |
| 72 | 10512375 | Also, AII decreased collagenase (MMP-2) levels but stimulated TGF-beta1 secretion in mesangial cells. |
| 73 | 10633003 | Gelatin zymograms indicated predominantly elevated matrix metalloproteinase-9 with smaller elevations of matrix metalloproteinase-2. |
| 74 | 11334407 | In addition to inhibiting matrix metalloproteinase-2 and matrix metalloproteinase-9 activity, recent studies suggest that tissue inhibitor of metalloproteinase (TIMP)-1 may inhibit apoptosis in various cell lines. |
| 75 | 11334407 | To address this question in pancreatic islets and beta-cells, we treated rat pancreatic islets and INS-1 cells with a high-dose combination of the cytokines interleukin (IL)-1beta, tumor necrosis factor-alpha, and interferon-gamma with or without the addition of TIMP-1 and TIMP-2 protein. |
| 76 | 11334407 | Next, we transfected the mouse TIMP-1 gene into INS-1 cells and performed Western immunoblotting to demonstrate expression of TIMP-1 protein. |
| 77 | 11334407 | We also evaluated the effect of TIMP-1 on IL-1beta-induced inhibition of glucose-stimulated insulin secretion (GSIS) in freshly isolated rat pancreatic islets. |
| 78 | 11334407 | Finally, we evaluated the effect of TIMP-1 on inducible nitric oxide synthase (iNOS) gene expression and nuclear factor (NF)-kappaB activity in INS-1 cells stimulated with high-dose cytokines. |
| 79 | 11334407 | TIMP-1 but not TIMP-2 prevented cytokine-induced apoptosis and cytokine-mediated inhibition of GSIS in rat islets and beta-cells. |
| 80 | 11334407 | TIMP-1 mediated these effects by inhibiting cytokine activation of NF-kappaB, but it did not affect nitric oxide production or iNOS gene expression. |
| 81 | 11357473 | Glycation cross-links inhibit matrix metalloproteinase-2 activation in vascular smooth muscle cells cultured on collagen lattice. |
| 82 | 11420306 | Gelatin zymography and Western blot analysis revealed that the activity and expression of 92-kDa (MMP-9) gelatinase, but not of 72 kDa (MMP-2) gelatinase, were significantly increased in vascular tissue and plasma of two distinct rodent models of DM. |
| 83 | 11420306 | Enhanced MMP-9 activity was significantly reduced by treatment with the antioxidants polyethylene glycol-superoxide dismutase and N-acetyl-L-cysteine but not by inhibitors of protein kinase C. |
| 84 | 11423724 | High glucose decreases matrix metalloproteinase-2 activity in rat mesangial cells via transforming growth factor-beta1. |
| 85 | 11423724 | The present studies were designed to investigate if the cytokine transforming growth factor-beta1 (TGF-beta1) mediates this effect of glucose. |
| 86 | 11423724 | The activity of 72 kDa type IV collagenase, also known as matrix metalloproteinase-2 (MMP-2), was assessed using three methods: (1) fluoresceinated gelatin degradation assay to detect free enzyme activity (activity which is present in excess of TIMP-inhibited activity); (2) zymography to measure total (free + TIMP-bound) enzyme activity; (3) ELISA using specific antibodies to measure MMP-2 levels. |
| 87 | 11423724 | TGF-beta1 and TIMP-2 levels were also determined by ELISA. |
| 88 | 11423724 | Incubation of primary cultures of rat mesangial cells for 5 days in 30 vs. 5 mM glucose resulted in a 3-fold increase in production of total TGF-beta1, a significant decrease in MMP-2 activity and immunoreactive MMP-2 levels, and an increase in TIMP-2 levels. |
| 89 | 11423724 | Addition of exogenous TGF-beta1 to mesangial cells incubated in 5 mM glucose replicated the high glucose effect by producing a significant decrease in MMP-2 levels with a concurrent increase in TIMP-2 levels. |
| 90 | 11423724 | Furthermore, glucose-induced inhibition of MMP-2 activity was completely blocked by neutralization of TGF-beta1 with anti-TGF-beta1 antibody. |
| 91 | 11423724 | We conclude that the decrease in MMP-2 activity induced by glucose loading is mediated via TGF-beta1. |
| 92 | 11423724 | High glucose decreases matrix metalloproteinase-2 activity in rat mesangial cells via transforming growth factor-beta1. |
| 93 | 11423724 | The present studies were designed to investigate if the cytokine transforming growth factor-beta1 (TGF-beta1) mediates this effect of glucose. |
| 94 | 11423724 | The activity of 72 kDa type IV collagenase, also known as matrix metalloproteinase-2 (MMP-2), was assessed using three methods: (1) fluoresceinated gelatin degradation assay to detect free enzyme activity (activity which is present in excess of TIMP-inhibited activity); (2) zymography to measure total (free + TIMP-bound) enzyme activity; (3) ELISA using specific antibodies to measure MMP-2 levels. |
| 95 | 11423724 | TGF-beta1 and TIMP-2 levels were also determined by ELISA. |
| 96 | 11423724 | Incubation of primary cultures of rat mesangial cells for 5 days in 30 vs. 5 mM glucose resulted in a 3-fold increase in production of total TGF-beta1, a significant decrease in MMP-2 activity and immunoreactive MMP-2 levels, and an increase in TIMP-2 levels. |
| 97 | 11423724 | Addition of exogenous TGF-beta1 to mesangial cells incubated in 5 mM glucose replicated the high glucose effect by producing a significant decrease in MMP-2 levels with a concurrent increase in TIMP-2 levels. |
| 98 | 11423724 | Furthermore, glucose-induced inhibition of MMP-2 activity was completely blocked by neutralization of TGF-beta1 with anti-TGF-beta1 antibody. |
| 99 | 11423724 | We conclude that the decrease in MMP-2 activity induced by glucose loading is mediated via TGF-beta1. |
| 100 | 11423724 | High glucose decreases matrix metalloproteinase-2 activity in rat mesangial cells via transforming growth factor-beta1. |
| 101 | 11423724 | The present studies were designed to investigate if the cytokine transforming growth factor-beta1 (TGF-beta1) mediates this effect of glucose. |
| 102 | 11423724 | The activity of 72 kDa type IV collagenase, also known as matrix metalloproteinase-2 (MMP-2), was assessed using three methods: (1) fluoresceinated gelatin degradation assay to detect free enzyme activity (activity which is present in excess of TIMP-inhibited activity); (2) zymography to measure total (free + TIMP-bound) enzyme activity; (3) ELISA using specific antibodies to measure MMP-2 levels. |
| 103 | 11423724 | TGF-beta1 and TIMP-2 levels were also determined by ELISA. |
| 104 | 11423724 | Incubation of primary cultures of rat mesangial cells for 5 days in 30 vs. 5 mM glucose resulted in a 3-fold increase in production of total TGF-beta1, a significant decrease in MMP-2 activity and immunoreactive MMP-2 levels, and an increase in TIMP-2 levels. |
| 105 | 11423724 | Addition of exogenous TGF-beta1 to mesangial cells incubated in 5 mM glucose replicated the high glucose effect by producing a significant decrease in MMP-2 levels with a concurrent increase in TIMP-2 levels. |
| 106 | 11423724 | Furthermore, glucose-induced inhibition of MMP-2 activity was completely blocked by neutralization of TGF-beta1 with anti-TGF-beta1 antibody. |
| 107 | 11423724 | We conclude that the decrease in MMP-2 activity induced by glucose loading is mediated via TGF-beta1. |
| 108 | 11423724 | High glucose decreases matrix metalloproteinase-2 activity in rat mesangial cells via transforming growth factor-beta1. |
| 109 | 11423724 | The present studies were designed to investigate if the cytokine transforming growth factor-beta1 (TGF-beta1) mediates this effect of glucose. |
| 110 | 11423724 | The activity of 72 kDa type IV collagenase, also known as matrix metalloproteinase-2 (MMP-2), was assessed using three methods: (1) fluoresceinated gelatin degradation assay to detect free enzyme activity (activity which is present in excess of TIMP-inhibited activity); (2) zymography to measure total (free + TIMP-bound) enzyme activity; (3) ELISA using specific antibodies to measure MMP-2 levels. |
| 111 | 11423724 | TGF-beta1 and TIMP-2 levels were also determined by ELISA. |
| 112 | 11423724 | Incubation of primary cultures of rat mesangial cells for 5 days in 30 vs. 5 mM glucose resulted in a 3-fold increase in production of total TGF-beta1, a significant decrease in MMP-2 activity and immunoreactive MMP-2 levels, and an increase in TIMP-2 levels. |
| 113 | 11423724 | Addition of exogenous TGF-beta1 to mesangial cells incubated in 5 mM glucose replicated the high glucose effect by producing a significant decrease in MMP-2 levels with a concurrent increase in TIMP-2 levels. |
| 114 | 11423724 | Furthermore, glucose-induced inhibition of MMP-2 activity was completely blocked by neutralization of TGF-beta1 with anti-TGF-beta1 antibody. |
| 115 | 11423724 | We conclude that the decrease in MMP-2 activity induced by glucose loading is mediated via TGF-beta1. |
| 116 | 11423724 | High glucose decreases matrix metalloproteinase-2 activity in rat mesangial cells via transforming growth factor-beta1. |
| 117 | 11423724 | The present studies were designed to investigate if the cytokine transforming growth factor-beta1 (TGF-beta1) mediates this effect of glucose. |
| 118 | 11423724 | The activity of 72 kDa type IV collagenase, also known as matrix metalloproteinase-2 (MMP-2), was assessed using three methods: (1) fluoresceinated gelatin degradation assay to detect free enzyme activity (activity which is present in excess of TIMP-inhibited activity); (2) zymography to measure total (free + TIMP-bound) enzyme activity; (3) ELISA using specific antibodies to measure MMP-2 levels. |
| 119 | 11423724 | TGF-beta1 and TIMP-2 levels were also determined by ELISA. |
| 120 | 11423724 | Incubation of primary cultures of rat mesangial cells for 5 days in 30 vs. 5 mM glucose resulted in a 3-fold increase in production of total TGF-beta1, a significant decrease in MMP-2 activity and immunoreactive MMP-2 levels, and an increase in TIMP-2 levels. |
| 121 | 11423724 | Addition of exogenous TGF-beta1 to mesangial cells incubated in 5 mM glucose replicated the high glucose effect by producing a significant decrease in MMP-2 levels with a concurrent increase in TIMP-2 levels. |
| 122 | 11423724 | Furthermore, glucose-induced inhibition of MMP-2 activity was completely blocked by neutralization of TGF-beta1 with anti-TGF-beta1 antibody. |
| 123 | 11423724 | We conclude that the decrease in MMP-2 activity induced by glucose loading is mediated via TGF-beta1. |
| 124 | 11423724 | High glucose decreases matrix metalloproteinase-2 activity in rat mesangial cells via transforming growth factor-beta1. |
| 125 | 11423724 | The present studies were designed to investigate if the cytokine transforming growth factor-beta1 (TGF-beta1) mediates this effect of glucose. |
| 126 | 11423724 | The activity of 72 kDa type IV collagenase, also known as matrix metalloproteinase-2 (MMP-2), was assessed using three methods: (1) fluoresceinated gelatin degradation assay to detect free enzyme activity (activity which is present in excess of TIMP-inhibited activity); (2) zymography to measure total (free + TIMP-bound) enzyme activity; (3) ELISA using specific antibodies to measure MMP-2 levels. |
| 127 | 11423724 | TGF-beta1 and TIMP-2 levels were also determined by ELISA. |
| 128 | 11423724 | Incubation of primary cultures of rat mesangial cells for 5 days in 30 vs. 5 mM glucose resulted in a 3-fold increase in production of total TGF-beta1, a significant decrease in MMP-2 activity and immunoreactive MMP-2 levels, and an increase in TIMP-2 levels. |
| 129 | 11423724 | Addition of exogenous TGF-beta1 to mesangial cells incubated in 5 mM glucose replicated the high glucose effect by producing a significant decrease in MMP-2 levels with a concurrent increase in TIMP-2 levels. |
| 130 | 11423724 | Furthermore, glucose-induced inhibition of MMP-2 activity was completely blocked by neutralization of TGF-beta1 with anti-TGF-beta1 antibody. |
| 131 | 11423724 | We conclude that the decrease in MMP-2 activity induced by glucose loading is mediated via TGF-beta1. |
| 132 | 11522674 | Because changes in the extracellular matrix (ECM) components are often associated with such cellular remodeling, we studied the adipocyte expression of the matrix metalloproteinases (MMPs) 2 and 9, two key enzymes involved in the modulation of ECM. |
| 133 | 11522674 | The present study provides the first evidence that human adipose tissue produces and secretes MMP-2 and -9 as shown by gelatin zymography analysis performed on media conditioned by human subcutaneous adipose tissue and human preadipocytes in primary cultures and by reverse transcriptase-polymerase chain reaction (RT-PCR) analysis on transcripts from mature human adipocytes. |
| 134 | 11522674 | Finally, preadipocyte treatment with MMP inhibitors such as batimastat and captopril, as well as neutralizing antibodies, markedly decreased adipocyte differentiation as demonstrated by the inhibition in the appearance of lipogenic (triglycerides) and lipolytic (glycerol release and hormone-sensitive lipase expression) markers. |
| 135 | 11522674 | These data suggest that MMP-2 and -9 could be important key regulators of adipocyte differentiation. |
| 136 | 11522674 | Because changes in the extracellular matrix (ECM) components are often associated with such cellular remodeling, we studied the adipocyte expression of the matrix metalloproteinases (MMPs) 2 and 9, two key enzymes involved in the modulation of ECM. |
| 137 | 11522674 | The present study provides the first evidence that human adipose tissue produces and secretes MMP-2 and -9 as shown by gelatin zymography analysis performed on media conditioned by human subcutaneous adipose tissue and human preadipocytes in primary cultures and by reverse transcriptase-polymerase chain reaction (RT-PCR) analysis on transcripts from mature human adipocytes. |
| 138 | 11522674 | Finally, preadipocyte treatment with MMP inhibitors such as batimastat and captopril, as well as neutralizing antibodies, markedly decreased adipocyte differentiation as demonstrated by the inhibition in the appearance of lipogenic (triglycerides) and lipolytic (glycerol release and hormone-sensitive lipase expression) markers. |
| 139 | 11522674 | These data suggest that MMP-2 and -9 could be important key regulators of adipocyte differentiation. |
| 140 | 11522674 | Because changes in the extracellular matrix (ECM) components are often associated with such cellular remodeling, we studied the adipocyte expression of the matrix metalloproteinases (MMPs) 2 and 9, two key enzymes involved in the modulation of ECM. |
| 141 | 11522674 | The present study provides the first evidence that human adipose tissue produces and secretes MMP-2 and -9 as shown by gelatin zymography analysis performed on media conditioned by human subcutaneous adipose tissue and human preadipocytes in primary cultures and by reverse transcriptase-polymerase chain reaction (RT-PCR) analysis on transcripts from mature human adipocytes. |
| 142 | 11522674 | Finally, preadipocyte treatment with MMP inhibitors such as batimastat and captopril, as well as neutralizing antibodies, markedly decreased adipocyte differentiation as demonstrated by the inhibition in the appearance of lipogenic (triglycerides) and lipolytic (glycerol release and hormone-sensitive lipase expression) markers. |
| 143 | 11522674 | These data suggest that MMP-2 and -9 could be important key regulators of adipocyte differentiation. |
| 144 | 11678966 | Peripheral blood level alterations of TIMP-1, MMP-2 and MMP-9 in patients with type 1 diabetes. |
| 145 | 11739475 | Hydrocortisone suppresses intranuclear activator-protein-1 (AP-1) binding activity in mononuclear cells and plasma matrix metalloproteinase 2 and 9 (MMP-2 and MMP-9). |
| 146 | 11739475 | Having demonstrated recently that hydrocortisone (HC) suppresses intranuclear and total cellular nuclear factor-kappa B (NF-kappa B) and increases inhibitor kappa B (I kappa B) in mononuclear cells (MNC), in vivo, we have now investigated the effect of hydrocortisone on the other major pro-inflammatory transcription factor, AP-1 and the two proteins, MMP-2 and MMP-9, whose transcription is modulated by it. |
| 147 | 11739475 | Plasma MMP-2 and MMP-9 were measured by ELISA. |
| 148 | 11739475 | Plasma MMP-2 concentration also decreased significantly at 1, 2, 4 and 8 h while MMP-9 decreased at 1 and 2 h. |
| 149 | 11739475 | These data demonstrate that the acute anti-inflammatory effect of HC, in vivo, is, in part, due to AP-1 suppression and a reduction in MMP-2 and MMP-9. |
| 150 | 11739475 | Hydrocortisone suppresses intranuclear activator-protein-1 (AP-1) binding activity in mononuclear cells and plasma matrix metalloproteinase 2 and 9 (MMP-2 and MMP-9). |
| 151 | 11739475 | Having demonstrated recently that hydrocortisone (HC) suppresses intranuclear and total cellular nuclear factor-kappa B (NF-kappa B) and increases inhibitor kappa B (I kappa B) in mononuclear cells (MNC), in vivo, we have now investigated the effect of hydrocortisone on the other major pro-inflammatory transcription factor, AP-1 and the two proteins, MMP-2 and MMP-9, whose transcription is modulated by it. |
| 152 | 11739475 | Plasma MMP-2 and MMP-9 were measured by ELISA. |
| 153 | 11739475 | Plasma MMP-2 concentration also decreased significantly at 1, 2, 4 and 8 h while MMP-9 decreased at 1 and 2 h. |
| 154 | 11739475 | These data demonstrate that the acute anti-inflammatory effect of HC, in vivo, is, in part, due to AP-1 suppression and a reduction in MMP-2 and MMP-9. |
| 155 | 11739475 | Hydrocortisone suppresses intranuclear activator-protein-1 (AP-1) binding activity in mononuclear cells and plasma matrix metalloproteinase 2 and 9 (MMP-2 and MMP-9). |
| 156 | 11739475 | Having demonstrated recently that hydrocortisone (HC) suppresses intranuclear and total cellular nuclear factor-kappa B (NF-kappa B) and increases inhibitor kappa B (I kappa B) in mononuclear cells (MNC), in vivo, we have now investigated the effect of hydrocortisone on the other major pro-inflammatory transcription factor, AP-1 and the two proteins, MMP-2 and MMP-9, whose transcription is modulated by it. |
| 157 | 11739475 | Plasma MMP-2 and MMP-9 were measured by ELISA. |
| 158 | 11739475 | Plasma MMP-2 concentration also decreased significantly at 1, 2, 4 and 8 h while MMP-9 decreased at 1 and 2 h. |
| 159 | 11739475 | These data demonstrate that the acute anti-inflammatory effect of HC, in vivo, is, in part, due to AP-1 suppression and a reduction in MMP-2 and MMP-9. |
| 160 | 11739475 | Hydrocortisone suppresses intranuclear activator-protein-1 (AP-1) binding activity in mononuclear cells and plasma matrix metalloproteinase 2 and 9 (MMP-2 and MMP-9). |
| 161 | 11739475 | Having demonstrated recently that hydrocortisone (HC) suppresses intranuclear and total cellular nuclear factor-kappa B (NF-kappa B) and increases inhibitor kappa B (I kappa B) in mononuclear cells (MNC), in vivo, we have now investigated the effect of hydrocortisone on the other major pro-inflammatory transcription factor, AP-1 and the two proteins, MMP-2 and MMP-9, whose transcription is modulated by it. |
| 162 | 11739475 | Plasma MMP-2 and MMP-9 were measured by ELISA. |
| 163 | 11739475 | Plasma MMP-2 concentration also decreased significantly at 1, 2, 4 and 8 h while MMP-9 decreased at 1 and 2 h. |
| 164 | 11739475 | These data demonstrate that the acute anti-inflammatory effect of HC, in vivo, is, in part, due to AP-1 suppression and a reduction in MMP-2 and MMP-9. |
| 165 | 11739475 | Hydrocortisone suppresses intranuclear activator-protein-1 (AP-1) binding activity in mononuclear cells and plasma matrix metalloproteinase 2 and 9 (MMP-2 and MMP-9). |
| 166 | 11739475 | Having demonstrated recently that hydrocortisone (HC) suppresses intranuclear and total cellular nuclear factor-kappa B (NF-kappa B) and increases inhibitor kappa B (I kappa B) in mononuclear cells (MNC), in vivo, we have now investigated the effect of hydrocortisone on the other major pro-inflammatory transcription factor, AP-1 and the two proteins, MMP-2 and MMP-9, whose transcription is modulated by it. |
| 167 | 11739475 | Plasma MMP-2 and MMP-9 were measured by ELISA. |
| 168 | 11739475 | Plasma MMP-2 concentration also decreased significantly at 1, 2, 4 and 8 h while MMP-9 decreased at 1 and 2 h. |
| 169 | 11739475 | These data demonstrate that the acute anti-inflammatory effect of HC, in vivo, is, in part, due to AP-1 suppression and a reduction in MMP-2 and MMP-9. |
| 170 | 11812761 | Matrix metalloproteinase-2 (MMP-2) and transforming growth factor-beta(1) (TGF-beta(1)) levels increased in B6 MC exposed to 25 mmol/l glucose but returned to baseline levels when the glucose concentration was reduced to 6 mmol/l. |
| 171 | 11812761 | MMP-2 and TGF-beta(1) were higher in ROP MC at baseline and increased in response to 25 mmol/l glucose, but remained elevated when glucose concentration was reduced. |
| 172 | 11812761 | Thus, 25 mmol/l glucose induced reversible changes in MMP-2, TGF-beta(1), and type I collagen in MC of sclerosis-resistant mice but not in MC from sclerosis-prone mice. |
| 173 | 11812761 | Matrix metalloproteinase-2 (MMP-2) and transforming growth factor-beta(1) (TGF-beta(1)) levels increased in B6 MC exposed to 25 mmol/l glucose but returned to baseline levels when the glucose concentration was reduced to 6 mmol/l. |
| 174 | 11812761 | MMP-2 and TGF-beta(1) were higher in ROP MC at baseline and increased in response to 25 mmol/l glucose, but remained elevated when glucose concentration was reduced. |
| 175 | 11812761 | Thus, 25 mmol/l glucose induced reversible changes in MMP-2, TGF-beta(1), and type I collagen in MC of sclerosis-resistant mice but not in MC from sclerosis-prone mice. |
| 176 | 11812761 | Matrix metalloproteinase-2 (MMP-2) and transforming growth factor-beta(1) (TGF-beta(1)) levels increased in B6 MC exposed to 25 mmol/l glucose but returned to baseline levels when the glucose concentration was reduced to 6 mmol/l. |
| 177 | 11812761 | MMP-2 and TGF-beta(1) were higher in ROP MC at baseline and increased in response to 25 mmol/l glucose, but remained elevated when glucose concentration was reduced. |
| 178 | 11812761 | Thus, 25 mmol/l glucose induced reversible changes in MMP-2, TGF-beta(1), and type I collagen in MC of sclerosis-resistant mice but not in MC from sclerosis-prone mice. |
| 179 | 12145178 | The aim of this study was to investigate the effects of glycation of mesangium matrix on MMP-2, the principal MMP secreted by mesangial cells to degrade type IV collagen. |
| 180 | 12145178 | Also examined were membrane type 1 MMP (MT1-MMP), tissue inhibitors of MMPs (TIMP)-1 and -2, and transforming growth factor-beta (TGF-beta), which together regulate MMP-2 activities in an interacting manner. |
| 181 | 12145178 | Analogous to the direct effects of high glucose concentrations, glycation of matrix increased the gene expression of MMP-2 and TIMP-1 (control 100 +/- 16.9 vs. glycated 197.3 +/- 30.6% and control 100 +/- 5.3 vs. glycated 152.1 +/- 20.1%, respectively; P < 0.05) and decreased MT1-MMP (control 100 +/- 1.17 vs. glycated 54.1 +/- 15.2%; P < 0.05). |
| 182 | 12145178 | Our results indicate that glycation of matrix affects the balance between MMP-2 and its activator and inhibitors, but this phenomenon is not due to TGF-beta. |
| 183 | 12145178 | The aim of this study was to investigate the effects of glycation of mesangium matrix on MMP-2, the principal MMP secreted by mesangial cells to degrade type IV collagen. |
| 184 | 12145178 | Also examined were membrane type 1 MMP (MT1-MMP), tissue inhibitors of MMPs (TIMP)-1 and -2, and transforming growth factor-beta (TGF-beta), which together regulate MMP-2 activities in an interacting manner. |
| 185 | 12145178 | Analogous to the direct effects of high glucose concentrations, glycation of matrix increased the gene expression of MMP-2 and TIMP-1 (control 100 +/- 16.9 vs. glycated 197.3 +/- 30.6% and control 100 +/- 5.3 vs. glycated 152.1 +/- 20.1%, respectively; P < 0.05) and decreased MT1-MMP (control 100 +/- 1.17 vs. glycated 54.1 +/- 15.2%; P < 0.05). |
| 186 | 12145178 | Our results indicate that glycation of matrix affects the balance between MMP-2 and its activator and inhibitors, but this phenomenon is not due to TGF-beta. |
| 187 | 12145178 | The aim of this study was to investigate the effects of glycation of mesangium matrix on MMP-2, the principal MMP secreted by mesangial cells to degrade type IV collagen. |
| 188 | 12145178 | Also examined were membrane type 1 MMP (MT1-MMP), tissue inhibitors of MMPs (TIMP)-1 and -2, and transforming growth factor-beta (TGF-beta), which together regulate MMP-2 activities in an interacting manner. |
| 189 | 12145178 | Analogous to the direct effects of high glucose concentrations, glycation of matrix increased the gene expression of MMP-2 and TIMP-1 (control 100 +/- 16.9 vs. glycated 197.3 +/- 30.6% and control 100 +/- 5.3 vs. glycated 152.1 +/- 20.1%, respectively; P < 0.05) and decreased MT1-MMP (control 100 +/- 1.17 vs. glycated 54.1 +/- 15.2%; P < 0.05). |
| 190 | 12145178 | Our results indicate that glycation of matrix affects the balance between MMP-2 and its activator and inhibitors, but this phenomenon is not due to TGF-beta. |
| 191 | 12145178 | The aim of this study was to investigate the effects of glycation of mesangium matrix on MMP-2, the principal MMP secreted by mesangial cells to degrade type IV collagen. |
| 192 | 12145178 | Also examined were membrane type 1 MMP (MT1-MMP), tissue inhibitors of MMPs (TIMP)-1 and -2, and transforming growth factor-beta (TGF-beta), which together regulate MMP-2 activities in an interacting manner. |
| 193 | 12145178 | Analogous to the direct effects of high glucose concentrations, glycation of matrix increased the gene expression of MMP-2 and TIMP-1 (control 100 +/- 16.9 vs. glycated 197.3 +/- 30.6% and control 100 +/- 5.3 vs. glycated 152.1 +/- 20.1%, respectively; P < 0.05) and decreased MT1-MMP (control 100 +/- 1.17 vs. glycated 54.1 +/- 15.2%; P < 0.05). |
| 194 | 12145178 | Our results indicate that glycation of matrix affects the balance between MMP-2 and its activator and inhibitors, but this phenomenon is not due to TGF-beta. |
| 195 | 12164930 | These differences may be contributing to the impaired healing of the diabetes mouse; however, they differ from the human data presented here, which show elevated matrix metalloproteinase 2 and reduced matrix metalloproteinase 9 in human diabetic chronic wound fluid compared to acute wound fluid. |
| 196 | 12477147 | While neutral endopeptidase (NEP) and matrix metalloproteinase-2 (MMP-2) are able to process big ET-1, inhibitors of NEP (thiorphan) and MMP (batimistat) did not affect ECE-1 activity. |
| 197 | 12477147 | In conclusion, the enzymatic pathway essential for generating vascular ET-1 is activated in the vasculature of both AA and CA diabetic patients and this activation is highly specific for ECE-1. |
| 198 | 12620921 | Finally, tissue inhibitor of metalloproteinase-2, the specific inhibitor of MMP-2, was upregulated in high glucose and could contribute to matrix accumulation. |
| 199 | 12626433 | Pure human neutrophil gelatinase B was found to destroy insulin by cleavage at 10 sites. |
| 200 | 12626433 | High expression levels of gelatinase B are maintained in the immediate proximity of insulin-secreting beta cells. |
| 201 | 12626433 | Consequently, diabetes may be worsened by enzymatic degradation of insulin by gelatinase B and by the consequent enhancement of the autoimmune process. |
| 202 | 12801609 | Our results clearly indicate that high glucose (25 mM) induced endothelial cell expression and activity of the collagenase, MMP-1 and the gelatinase, MMP-2, whilst reducing expression of the stromelysin, MMP-3 (P<0.05). |
| 203 | 12801609 | The increased MMP-1, MMP-2 and MMP-9 activities induced by high glucose exposure could promote matrix degradation thereby accelerating atherogenesis and potentially reducing plaque stability in diabetes. |
| 204 | 12801609 | Our results clearly indicate that high glucose (25 mM) induced endothelial cell expression and activity of the collagenase, MMP-1 and the gelatinase, MMP-2, whilst reducing expression of the stromelysin, MMP-3 (P<0.05). |
| 205 | 12801609 | The increased MMP-1, MMP-2 and MMP-9 activities induced by high glucose exposure could promote matrix degradation thereby accelerating atherogenesis and potentially reducing plaque stability in diabetes. |
| 206 | 12805564 | After 3 days of ischemia, MMP-2 activity and MMP-3 and MMP-13 protein levels were increased in untreated and aminoguanidine-treated diabetic mice when compared with controls (P < 0.05). |
| 207 | 12845621 | These include increased synthesis of type IV collagen following hyperglycaemia-induced alteration of the pattern of podocyte-integrin expression, decreased expression of matrix metalloproteinases (MMP-2 and 3), and increased expression of tissue inhibitor of metalloproteinase (TIMP). |
| 208 | 12845621 | Other factors which may contribute to renal matrix accumulation include vascular endothelial growth factor (VEGF), since treatment with anti-VEGF antibodies attenuates glomerular basement membrane thickening, platelet-derived growth factor (PDGF) (B chain) and its receptor, which appear to be highly expressed in mesangial and visceral epithelial cells and might play a role in the development of diabetic nephropathy. |
| 209 | 12921671 | [Expression and significance of transforming growth factor-beta1, matrix metalloproteinase-2 and its inhibitor in lens epithelial cells of diabetic cataract]. |
| 210 | 14597759 | Angiotensin II-accelerated atherosclerosis and aneurysm formation is attenuated in osteopontin-deficient mice. |
| 211 | 14597759 | To determine the role of OPN in atherogenesis, ApoE-/-OPN+/+, ApoE-/-OPN+/-, and ApoE-/-OPN-/- mice were infused with Ang II, inducing vascular OPN expression and accelerating atherosclerosis. |
| 212 | 14597759 | Compared with ApoE-/-OPN+/+ mice, ApoE-/-OPN+/- and ApoE-/-OPN-/- mice developed less Ang II-accelerated atherosclerosis. |
| 213 | 14597759 | ApoE-/- mice transplanted with bone marrow derived from ApoE-/-OPN-/- mice had less Ang II-induced atherosclerosis compared with animals receiving ApoE-/-OPN+/+ cells. |
| 214 | 14597759 | Aortae from Ang II-infused ApoE-/-OPN-/- mice expressed less CD68, C-C-chemokine receptor 2, and VCAM-1. |
| 215 | 14597759 | In response to intraperitoneal thioglycollate, recruitment of leukocytes in OPN-/- mice was impaired, and OPN-/- leukocytes exhibited decreased basal and MCP-1-directed migration. |
| 216 | 14597759 | Finally, Ang II-induced abdominal aortic aneurysm formation in ApoE-/-OPN-/- mice was reduced and associated with decreased MMP-2 and MMP-9 activity. |
| 217 | 14597759 | These data suggest an important role for leukocyte-derived OPN in mediating Ang II-accelerated atherosclerosis and aneurysm formation. |
| 218 | 15253387 | Topical administration of HGF, as well as basic fibroblast growth factor (bFGF), promoted the rate of wound closure and re-epithelialization. |
| 219 | 15253387 | Both HGF and bFGF enhanced expansion of the granulation tissue and stimulated neovascularization on day 7 postwounding, wherein the increase in microvessel density in HGF-treated wounds was higher than that in bFGF-treated wounds. |
| 220 | 15253387 | Matrix metalloproteinases (MMP-2 and MMP-9) activities involved in cell migration, angiogenesis, and extracellular matrix (ECM) remodeling, were enhanced by HGF-treatment on day 7. |
| 221 | 15345671 | Connective tissue growth factor (CTGF) expression is increased in diabetic nephropathy and is a downstream mediator of TGF-beta actions. |
| 222 | 15345671 | Matrix degradation was inhibited by rhCTGF in a dose-dependent manner, and the decrease in matrix degradation caused by high glucose and by TGF-beta was significantly attenuated by addition of CTGF-neutralizing antibody (by 40.2 and 69.1%, respectively). |
| 223 | 15345671 | Similar to 25 mM glucose, addition of rhCTGF increased MMP-2, TIMP-1, and TIMP-3 mRNA by 2.5-, 2.1-, and 1.6-fold, respectively (P < 0.05) but had no effect on membrane-type (MT)1-MMP or TIMP-2. |
| 224 | 15345671 | In vivo studies of glomeruli from diabetic and control rats showed that intensive insulin treatment prevented the increase in expression of CTGF and TIMP-1 and attenuated the decreased matrix degradation seen in diabetes. |
| 225 | 15345671 | In summary, CTGF inhibits matrix degradation by increasing TIMP-1 expression, and by this action it contributes to the inhibition of matrix breakdown by high glucose, implying that CTGF has a role in the reduced matrix degradation observed in diabetic nephropathy. |
| 226 | 15493832 | [Effects of puerarin on renal function, expressions of MMP-2 and TIMP-2 in diabetic rats]. |
| 227 | 15525599 | Transcripts involved in energy metabolism, such as glyceraldehyde-3-phosphate dehydrogenase, malic enzyme supernatant, fatty acid synthase, lipoprotein lipase, hormone-sensitive lipase and monoglyceride lipase, were upregulated by DHT. |
| 228 | 15525599 | Transcripts involved in adipogenesis, and cell cycle and cell shape organization, such as DDX5, C/EBPalpha, cyclin I, procollagen types I, III, IV, V and VI, SPARC and matrix metalloproteinase 2, were upregulated by DHT. |
| 229 | 15539012 | Altered local gene expression of humoral factors (eg, transforming growth factor-b, connective tissue growth factor, and platelet-derived growth factor) can lead to increased production of ECM components (eg, fibronectin and collagen IV) or decreased degradation through matrix metalloproteinases (eg, MMP-1, MMP-2). |
| 230 | 15711567 | The retinas of diabetic animals demonstrated elevated levels of MMP-2, MMP-9 and MMP-14 messenger RNA. |
| 231 | 15711567 | Both cell types treated with purified MMP-2 or MMP-9 were found to have alterations of tight junction function as shown by decreased TER. |
| 232 | 15711567 | Western blot analysis of cell extracts treated with MMP-2 or MMP-9, revealed specific degradation of the tight junction protein, occludin. |
| 233 | 15711567 | The retinas of diabetic animals demonstrated elevated levels of MMP-2, MMP-9 and MMP-14 messenger RNA. |
| 234 | 15711567 | Both cell types treated with purified MMP-2 or MMP-9 were found to have alterations of tight junction function as shown by decreased TER. |
| 235 | 15711567 | Western blot analysis of cell extracts treated with MMP-2 or MMP-9, revealed specific degradation of the tight junction protein, occludin. |
| 236 | 15711567 | The retinas of diabetic animals demonstrated elevated levels of MMP-2, MMP-9 and MMP-14 messenger RNA. |
| 237 | 15711567 | Both cell types treated with purified MMP-2 or MMP-9 were found to have alterations of tight junction function as shown by decreased TER. |
| 238 | 15711567 | Western blot analysis of cell extracts treated with MMP-2 or MMP-9, revealed specific degradation of the tight junction protein, occludin. |
| 239 | 15734845 | Cell culture studies suggest that matrix metalloproteinases (MMPs) 2 and 9 are required for islet formation. |
| 240 | 15734845 | To address whether MMP2 and MMP9 function are essential for endocrine cell migration and islet formation in vivo, we analyzed pancreas development in MMP2/MMP9 double-deficient mice. |
| 241 | 15734845 | Our results show that islet architecture and function are unperturbed in these knockout mice, demonstrating that both MMP2 and MMP9 functions are dispensable for islet formation and endocrine cell differentiation. |
| 242 | 15734845 | This observation suggests that other MMPs may substitute for MMP2 and MMP9 loss in pancreatic tissue. |
| 243 | 15734845 | Cell culture studies suggest that matrix metalloproteinases (MMPs) 2 and 9 are required for islet formation. |
| 244 | 15734845 | To address whether MMP2 and MMP9 function are essential for endocrine cell migration and islet formation in vivo, we analyzed pancreas development in MMP2/MMP9 double-deficient mice. |
| 245 | 15734845 | Our results show that islet architecture and function are unperturbed in these knockout mice, demonstrating that both MMP2 and MMP9 functions are dispensable for islet formation and endocrine cell differentiation. |
| 246 | 15734845 | This observation suggests that other MMPs may substitute for MMP2 and MMP9 loss in pancreatic tissue. |
| 247 | 15734845 | Cell culture studies suggest that matrix metalloproteinases (MMPs) 2 and 9 are required for islet formation. |
| 248 | 15734845 | To address whether MMP2 and MMP9 function are essential for endocrine cell migration and islet formation in vivo, we analyzed pancreas development in MMP2/MMP9 double-deficient mice. |
| 249 | 15734845 | Our results show that islet architecture and function are unperturbed in these knockout mice, demonstrating that both MMP2 and MMP9 functions are dispensable for islet formation and endocrine cell differentiation. |
| 250 | 15734845 | This observation suggests that other MMPs may substitute for MMP2 and MMP9 loss in pancreatic tissue. |
| 251 | 15734845 | Cell culture studies suggest that matrix metalloproteinases (MMPs) 2 and 9 are required for islet formation. |
| 252 | 15734845 | To address whether MMP2 and MMP9 function are essential for endocrine cell migration and islet formation in vivo, we analyzed pancreas development in MMP2/MMP9 double-deficient mice. |
| 253 | 15734845 | Our results show that islet architecture and function are unperturbed in these knockout mice, demonstrating that both MMP2 and MMP9 functions are dispensable for islet formation and endocrine cell differentiation. |
| 254 | 15734845 | This observation suggests that other MMPs may substitute for MMP2 and MMP9 loss in pancreatic tissue. |
| 255 | 15823620 | MMP-2 and MMP-9 immunolabelling was increased both in the labyrinth zone (p<0.001) and in the giant trophoblast cells of the junctional zone (p<0.001) from diabetic placenta, when compared with controls. |
| 256 | 15823620 | Also MMP-2 (p<0.01) and MMP-9 (p<0.005) activities were increased in both maternal and fetal sides of diabetic placenta when related to controls. |
| 257 | 15823620 | MMP-2 and MMP-9 immunolabelling was increased both in the labyrinth zone (p<0.001) and in the giant trophoblast cells of the junctional zone (p<0.001) from diabetic placenta, when compared with controls. |
| 258 | 15823620 | Also MMP-2 (p<0.01) and MMP-9 (p<0.005) activities were increased in both maternal and fetal sides of diabetic placenta when related to controls. |
| 259 | 15920993 | Plasma levels and zymographic activities of MMP-2 and MMP-9 were investigated in type II diabetics with (n = 51) or without (n = 42) peripheral artery disease (PAD) and in normal volunteers (n = 23). |
| 260 | 15920993 | Plasma zymographic activities of both MMP-2 and MMP-9 were positively correlated with their plasma levels. |
| 261 | 15920993 | Together, these results indicate that increased plasma levels and zymographic activities of MMP-2 and MMP-9 may contribute to PAD in type II diabetics. |
| 262 | 15920993 | Plasma levels and zymographic activities of MMP-2 and MMP-9 were investigated in type II diabetics with (n = 51) or without (n = 42) peripheral artery disease (PAD) and in normal volunteers (n = 23). |
| 263 | 15920993 | Plasma zymographic activities of both MMP-2 and MMP-9 were positively correlated with their plasma levels. |
| 264 | 15920993 | Together, these results indicate that increased plasma levels and zymographic activities of MMP-2 and MMP-9 may contribute to PAD in type II diabetics. |
| 265 | 15920993 | Plasma levels and zymographic activities of MMP-2 and MMP-9 were investigated in type II diabetics with (n = 51) or without (n = 42) peripheral artery disease (PAD) and in normal volunteers (n = 23). |
| 266 | 15920993 | Plasma zymographic activities of both MMP-2 and MMP-9 were positively correlated with their plasma levels. |
| 267 | 15920993 | Together, these results indicate that increased plasma levels and zymographic activities of MMP-2 and MMP-9 may contribute to PAD in type II diabetics. |
| 268 | 15978215 | Effects of irbesartan on the expression of matrix metalloproteinase-2/tissue inhibitor of metalloproteinase-2 in streptozotocin-induced diabetic rat kidney. |
| 269 | 15983226 | Signaling pathways involved in human vascular smooth muscle cell proliferation and matrix metalloproteinase-2 expression induced by leptin: inhibitory effect of metformin. |
| 270 | 15983226 | Incubation of HASMCs with leptin enhanced the proliferation and MMP-2 expression in these cells and increased the generation of intracellular reactive oxygen species (ROS). |
| 271 | 15983226 | Inhibition of NAD(P)H oxidase and protein kinase C (PKC) suppressed the effect of leptin on ROS production. |
| 272 | 15983226 | In HASMCs, leptin induced PKC, extracellular signal-regulated kinase (ERK)1/2, and nuclear factor-kappaB (NF-kappaB) activation and inhibition of these signaling pathways abrogated HASMC proliferation and MMP-2 expression induced by this hormone. |
| 273 | 15983226 | Treatment of HASMCs with metformin decreased leptin-induced ROS production and activation of PKC, ERK1/2, and NF-kappaB. |
| 274 | 15983226 | Metformin also inhibited the effect of leptin on HASMC proliferation and MMP-2 expression. |
| 275 | 15983226 | Overall, these results demonstrate that leptin induced HASMC proliferation and MMP-2 expression through a PKC-dependent activation of NAD(P)H oxidase with subsequent activation of the ERK1/2/NF-kappaB pathways and that therapeutic metformin concentrations effectively inhibit these biological effects. |
| 276 | 15983226 | Signaling pathways involved in human vascular smooth muscle cell proliferation and matrix metalloproteinase-2 expression induced by leptin: inhibitory effect of metformin. |
| 277 | 15983226 | Incubation of HASMCs with leptin enhanced the proliferation and MMP-2 expression in these cells and increased the generation of intracellular reactive oxygen species (ROS). |
| 278 | 15983226 | Inhibition of NAD(P)H oxidase and protein kinase C (PKC) suppressed the effect of leptin on ROS production. |
| 279 | 15983226 | In HASMCs, leptin induced PKC, extracellular signal-regulated kinase (ERK)1/2, and nuclear factor-kappaB (NF-kappaB) activation and inhibition of these signaling pathways abrogated HASMC proliferation and MMP-2 expression induced by this hormone. |
| 280 | 15983226 | Treatment of HASMCs with metformin decreased leptin-induced ROS production and activation of PKC, ERK1/2, and NF-kappaB. |
| 281 | 15983226 | Metformin also inhibited the effect of leptin on HASMC proliferation and MMP-2 expression. |
| 282 | 15983226 | Overall, these results demonstrate that leptin induced HASMC proliferation and MMP-2 expression through a PKC-dependent activation of NAD(P)H oxidase with subsequent activation of the ERK1/2/NF-kappaB pathways and that therapeutic metformin concentrations effectively inhibit these biological effects. |
| 283 | 15983226 | Signaling pathways involved in human vascular smooth muscle cell proliferation and matrix metalloproteinase-2 expression induced by leptin: inhibitory effect of metformin. |
| 284 | 15983226 | Incubation of HASMCs with leptin enhanced the proliferation and MMP-2 expression in these cells and increased the generation of intracellular reactive oxygen species (ROS). |
| 285 | 15983226 | Inhibition of NAD(P)H oxidase and protein kinase C (PKC) suppressed the effect of leptin on ROS production. |
| 286 | 15983226 | In HASMCs, leptin induced PKC, extracellular signal-regulated kinase (ERK)1/2, and nuclear factor-kappaB (NF-kappaB) activation and inhibition of these signaling pathways abrogated HASMC proliferation and MMP-2 expression induced by this hormone. |
| 287 | 15983226 | Treatment of HASMCs with metformin decreased leptin-induced ROS production and activation of PKC, ERK1/2, and NF-kappaB. |
| 288 | 15983226 | Metformin also inhibited the effect of leptin on HASMC proliferation and MMP-2 expression. |
| 289 | 15983226 | Overall, these results demonstrate that leptin induced HASMC proliferation and MMP-2 expression through a PKC-dependent activation of NAD(P)H oxidase with subsequent activation of the ERK1/2/NF-kappaB pathways and that therapeutic metformin concentrations effectively inhibit these biological effects. |
| 290 | 15983226 | Signaling pathways involved in human vascular smooth muscle cell proliferation and matrix metalloproteinase-2 expression induced by leptin: inhibitory effect of metformin. |
| 291 | 15983226 | Incubation of HASMCs with leptin enhanced the proliferation and MMP-2 expression in these cells and increased the generation of intracellular reactive oxygen species (ROS). |
| 292 | 15983226 | Inhibition of NAD(P)H oxidase and protein kinase C (PKC) suppressed the effect of leptin on ROS production. |
| 293 | 15983226 | In HASMCs, leptin induced PKC, extracellular signal-regulated kinase (ERK)1/2, and nuclear factor-kappaB (NF-kappaB) activation and inhibition of these signaling pathways abrogated HASMC proliferation and MMP-2 expression induced by this hormone. |
| 294 | 15983226 | Treatment of HASMCs with metformin decreased leptin-induced ROS production and activation of PKC, ERK1/2, and NF-kappaB. |
| 295 | 15983226 | Metformin also inhibited the effect of leptin on HASMC proliferation and MMP-2 expression. |
| 296 | 15983226 | Overall, these results demonstrate that leptin induced HASMC proliferation and MMP-2 expression through a PKC-dependent activation of NAD(P)H oxidase with subsequent activation of the ERK1/2/NF-kappaB pathways and that therapeutic metformin concentrations effectively inhibit these biological effects. |
| 297 | 15983226 | Signaling pathways involved in human vascular smooth muscle cell proliferation and matrix metalloproteinase-2 expression induced by leptin: inhibitory effect of metformin. |
| 298 | 15983226 | Incubation of HASMCs with leptin enhanced the proliferation and MMP-2 expression in these cells and increased the generation of intracellular reactive oxygen species (ROS). |
| 299 | 15983226 | Inhibition of NAD(P)H oxidase and protein kinase C (PKC) suppressed the effect of leptin on ROS production. |
| 300 | 15983226 | In HASMCs, leptin induced PKC, extracellular signal-regulated kinase (ERK)1/2, and nuclear factor-kappaB (NF-kappaB) activation and inhibition of these signaling pathways abrogated HASMC proliferation and MMP-2 expression induced by this hormone. |
| 301 | 15983226 | Treatment of HASMCs with metformin decreased leptin-induced ROS production and activation of PKC, ERK1/2, and NF-kappaB. |
| 302 | 15983226 | Metformin also inhibited the effect of leptin on HASMC proliferation and MMP-2 expression. |
| 303 | 15983226 | Overall, these results demonstrate that leptin induced HASMC proliferation and MMP-2 expression through a PKC-dependent activation of NAD(P)H oxidase with subsequent activation of the ERK1/2/NF-kappaB pathways and that therapeutic metformin concentrations effectively inhibit these biological effects. |
| 304 | 16005367 | Alterations in peripheral blood levels of TIMP-1, MMP-2, and MMP-9 in patients with type-2 diabetes. |
| 305 | 16174279 | Plasminogen activator (PA)/plasmin/PA inhibitor (PAI) system is involved in ECM degradation and PAI-1 plays a critical role in ECM remodeling in the kidney. |
| 306 | 16174279 | Recent studies utilizing PAI-1 deficient mice suggest that PAI-1 induce ECM deposition in diabetic kidney through increased ECM synthesis by TGF-beta1 up-regulation as well as through decreased ECM degradation by suppression of plasmin and MMP-2 activity. |
| 307 | 16188574 | Matrix metalloproteinases (MMPs) 2 and 9 are responsible for extracellular matrix breakdown and their abnormal circulating levels may pre-date clinical evidence of diabetic angiopathy. |
| 308 | 16188574 | We detected by ELISA, plasma MMP-2 and MMP-9 levels and associated activity in 25 children and adolescents with T1DM. |
| 309 | 16188574 | MMP-2 and MMP-9 levels and activity were detected in samples obtained at T1DM diagnosis and at the 5-year follow-up. |
| 310 | 16188574 | It is well known that MMP-9 is an index of the severity and stability of macroangiopathy while our results allow us to postulate that MMP-2 may be a marker of microangiopathy. |
| 311 | 16188574 | Matrix metalloproteinases (MMPs) 2 and 9 are responsible for extracellular matrix breakdown and their abnormal circulating levels may pre-date clinical evidence of diabetic angiopathy. |
| 312 | 16188574 | We detected by ELISA, plasma MMP-2 and MMP-9 levels and associated activity in 25 children and adolescents with T1DM. |
| 313 | 16188574 | MMP-2 and MMP-9 levels and activity were detected in samples obtained at T1DM diagnosis and at the 5-year follow-up. |
| 314 | 16188574 | It is well known that MMP-9 is an index of the severity and stability of macroangiopathy while our results allow us to postulate that MMP-2 may be a marker of microangiopathy. |
| 315 | 16188574 | Matrix metalloproteinases (MMPs) 2 and 9 are responsible for extracellular matrix breakdown and their abnormal circulating levels may pre-date clinical evidence of diabetic angiopathy. |
| 316 | 16188574 | We detected by ELISA, plasma MMP-2 and MMP-9 levels and associated activity in 25 children and adolescents with T1DM. |
| 317 | 16188574 | MMP-2 and MMP-9 levels and activity were detected in samples obtained at T1DM diagnosis and at the 5-year follow-up. |
| 318 | 16188574 | It is well known that MMP-9 is an index of the severity and stability of macroangiopathy while our results allow us to postulate that MMP-2 may be a marker of microangiopathy. |
| 319 | 16188574 | Matrix metalloproteinases (MMPs) 2 and 9 are responsible for extracellular matrix breakdown and their abnormal circulating levels may pre-date clinical evidence of diabetic angiopathy. |
| 320 | 16188574 | We detected by ELISA, plasma MMP-2 and MMP-9 levels and associated activity in 25 children and adolescents with T1DM. |
| 321 | 16188574 | MMP-2 and MMP-9 levels and activity were detected in samples obtained at T1DM diagnosis and at the 5-year follow-up. |
| 322 | 16188574 | It is well known that MMP-9 is an index of the severity and stability of macroangiopathy while our results allow us to postulate that MMP-2 may be a marker of microangiopathy. |
| 323 | 16242528 | C-reactive protein increases matrix metalloproteinase-2 expression and activity in cultured human vascular smooth muscle cells. |
| 324 | 16242528 | We aimed to evaluate whether in cultured human vascular smooth muscle cells (hVSMC) CRP modulates the synthesis and release of metalloproteinase-2 (MMP-2), which is deeply involved in plaque instabilization and vascular remodeling, and of the tissue inhibitor of metalloproteinase-2 (TIMP-2). |
| 325 | 16242528 | Both in supernatants and in cell lysates of cultured hVSMC exposed to CRP (0-10 mg/L), we evaluated MMP-2 activity (gelatin zymography), MMP-2 and TIMP-2 protein synthesis (immunoblotting), MMP-2 and TIMP-2 mRNA expression (reverse transcription-polymerase chain reaction). |
| 326 | 16242528 | CRP effects were also investigated after cell exposure to specific MEK inhibitor PD98059 (15-30 micromol/L) to evaluate the involvement of mitogen-activated protein kinase (MAPK). |
| 327 | 16242528 | CRP upregulated MMP-2 mRNA expression. |
| 328 | 16242528 | MMP-2 synthesis and activity were increased by 1-10 mg/L CRP starting from 8-hour incubation. |
| 329 | 16242528 | CRP did not modify TIMP-2 mRNA expression, protein synthesis, and secretion. |
| 330 | 16242528 | CRP, at concentrations that predict cardiovascular events, upregulates MMP-2 mRNA expression and increases MMP-2 protein synthesis and release in hVSMC through mechanisms involving activation of MAPK pathway. |
| 331 | 16242528 | C-reactive protein increases matrix metalloproteinase-2 expression and activity in cultured human vascular smooth muscle cells. |
| 332 | 16242528 | We aimed to evaluate whether in cultured human vascular smooth muscle cells (hVSMC) CRP modulates the synthesis and release of metalloproteinase-2 (MMP-2), which is deeply involved in plaque instabilization and vascular remodeling, and of the tissue inhibitor of metalloproteinase-2 (TIMP-2). |
| 333 | 16242528 | Both in supernatants and in cell lysates of cultured hVSMC exposed to CRP (0-10 mg/L), we evaluated MMP-2 activity (gelatin zymography), MMP-2 and TIMP-2 protein synthesis (immunoblotting), MMP-2 and TIMP-2 mRNA expression (reverse transcription-polymerase chain reaction). |
| 334 | 16242528 | CRP effects were also investigated after cell exposure to specific MEK inhibitor PD98059 (15-30 micromol/L) to evaluate the involvement of mitogen-activated protein kinase (MAPK). |
| 335 | 16242528 | CRP upregulated MMP-2 mRNA expression. |
| 336 | 16242528 | MMP-2 synthesis and activity were increased by 1-10 mg/L CRP starting from 8-hour incubation. |
| 337 | 16242528 | CRP did not modify TIMP-2 mRNA expression, protein synthesis, and secretion. |
| 338 | 16242528 | CRP, at concentrations that predict cardiovascular events, upregulates MMP-2 mRNA expression and increases MMP-2 protein synthesis and release in hVSMC through mechanisms involving activation of MAPK pathway. |
| 339 | 16242528 | C-reactive protein increases matrix metalloproteinase-2 expression and activity in cultured human vascular smooth muscle cells. |
| 340 | 16242528 | We aimed to evaluate whether in cultured human vascular smooth muscle cells (hVSMC) CRP modulates the synthesis and release of metalloproteinase-2 (MMP-2), which is deeply involved in plaque instabilization and vascular remodeling, and of the tissue inhibitor of metalloproteinase-2 (TIMP-2). |
| 341 | 16242528 | Both in supernatants and in cell lysates of cultured hVSMC exposed to CRP (0-10 mg/L), we evaluated MMP-2 activity (gelatin zymography), MMP-2 and TIMP-2 protein synthesis (immunoblotting), MMP-2 and TIMP-2 mRNA expression (reverse transcription-polymerase chain reaction). |
| 342 | 16242528 | CRP effects were also investigated after cell exposure to specific MEK inhibitor PD98059 (15-30 micromol/L) to evaluate the involvement of mitogen-activated protein kinase (MAPK). |
| 343 | 16242528 | CRP upregulated MMP-2 mRNA expression. |
| 344 | 16242528 | MMP-2 synthesis and activity were increased by 1-10 mg/L CRP starting from 8-hour incubation. |
| 345 | 16242528 | CRP did not modify TIMP-2 mRNA expression, protein synthesis, and secretion. |
| 346 | 16242528 | CRP, at concentrations that predict cardiovascular events, upregulates MMP-2 mRNA expression and increases MMP-2 protein synthesis and release in hVSMC through mechanisms involving activation of MAPK pathway. |
| 347 | 16242528 | C-reactive protein increases matrix metalloproteinase-2 expression and activity in cultured human vascular smooth muscle cells. |
| 348 | 16242528 | We aimed to evaluate whether in cultured human vascular smooth muscle cells (hVSMC) CRP modulates the synthesis and release of metalloproteinase-2 (MMP-2), which is deeply involved in plaque instabilization and vascular remodeling, and of the tissue inhibitor of metalloproteinase-2 (TIMP-2). |
| 349 | 16242528 | Both in supernatants and in cell lysates of cultured hVSMC exposed to CRP (0-10 mg/L), we evaluated MMP-2 activity (gelatin zymography), MMP-2 and TIMP-2 protein synthesis (immunoblotting), MMP-2 and TIMP-2 mRNA expression (reverse transcription-polymerase chain reaction). |
| 350 | 16242528 | CRP effects were also investigated after cell exposure to specific MEK inhibitor PD98059 (15-30 micromol/L) to evaluate the involvement of mitogen-activated protein kinase (MAPK). |
| 351 | 16242528 | CRP upregulated MMP-2 mRNA expression. |
| 352 | 16242528 | MMP-2 synthesis and activity were increased by 1-10 mg/L CRP starting from 8-hour incubation. |
| 353 | 16242528 | CRP did not modify TIMP-2 mRNA expression, protein synthesis, and secretion. |
| 354 | 16242528 | CRP, at concentrations that predict cardiovascular events, upregulates MMP-2 mRNA expression and increases MMP-2 protein synthesis and release in hVSMC through mechanisms involving activation of MAPK pathway. |
| 355 | 16242528 | C-reactive protein increases matrix metalloproteinase-2 expression and activity in cultured human vascular smooth muscle cells. |
| 356 | 16242528 | We aimed to evaluate whether in cultured human vascular smooth muscle cells (hVSMC) CRP modulates the synthesis and release of metalloproteinase-2 (MMP-2), which is deeply involved in plaque instabilization and vascular remodeling, and of the tissue inhibitor of metalloproteinase-2 (TIMP-2). |
| 357 | 16242528 | Both in supernatants and in cell lysates of cultured hVSMC exposed to CRP (0-10 mg/L), we evaluated MMP-2 activity (gelatin zymography), MMP-2 and TIMP-2 protein synthesis (immunoblotting), MMP-2 and TIMP-2 mRNA expression (reverse transcription-polymerase chain reaction). |
| 358 | 16242528 | CRP effects were also investigated after cell exposure to specific MEK inhibitor PD98059 (15-30 micromol/L) to evaluate the involvement of mitogen-activated protein kinase (MAPK). |
| 359 | 16242528 | CRP upregulated MMP-2 mRNA expression. |
| 360 | 16242528 | MMP-2 synthesis and activity were increased by 1-10 mg/L CRP starting from 8-hour incubation. |
| 361 | 16242528 | CRP did not modify TIMP-2 mRNA expression, protein synthesis, and secretion. |
| 362 | 16242528 | CRP, at concentrations that predict cardiovascular events, upregulates MMP-2 mRNA expression and increases MMP-2 protein synthesis and release in hVSMC through mechanisms involving activation of MAPK pathway. |
| 363 | 16242528 | C-reactive protein increases matrix metalloproteinase-2 expression and activity in cultured human vascular smooth muscle cells. |
| 364 | 16242528 | We aimed to evaluate whether in cultured human vascular smooth muscle cells (hVSMC) CRP modulates the synthesis and release of metalloproteinase-2 (MMP-2), which is deeply involved in plaque instabilization and vascular remodeling, and of the tissue inhibitor of metalloproteinase-2 (TIMP-2). |
| 365 | 16242528 | Both in supernatants and in cell lysates of cultured hVSMC exposed to CRP (0-10 mg/L), we evaluated MMP-2 activity (gelatin zymography), MMP-2 and TIMP-2 protein synthesis (immunoblotting), MMP-2 and TIMP-2 mRNA expression (reverse transcription-polymerase chain reaction). |
| 366 | 16242528 | CRP effects were also investigated after cell exposure to specific MEK inhibitor PD98059 (15-30 micromol/L) to evaluate the involvement of mitogen-activated protein kinase (MAPK). |
| 367 | 16242528 | CRP upregulated MMP-2 mRNA expression. |
| 368 | 16242528 | MMP-2 synthesis and activity were increased by 1-10 mg/L CRP starting from 8-hour incubation. |
| 369 | 16242528 | CRP did not modify TIMP-2 mRNA expression, protein synthesis, and secretion. |
| 370 | 16242528 | CRP, at concentrations that predict cardiovascular events, upregulates MMP-2 mRNA expression and increases MMP-2 protein synthesis and release in hVSMC through mechanisms involving activation of MAPK pathway. |
| 371 | 16303001 | However, transcription of genes previously linked to AR including CD8 (65.9 +/- 18.8) and related molecules IFN-gamma(55.1 +/- 17.0), CXCR3 (49.9 +/- 12.8) and perforin (153.8 +/- 50.4) were significantly higher in PVN compared to AR (30.9 +/- 2.0, 14.0 +/- 7.3, 12.1 +/- 7.3 and 15.6 +/- 3.8-fold, respectively; p < 0.01). |
| 372 | 16303001 | Importantly, transcription of molecules associated with graft fibrosis including matrix collagens, TGFbeta, MMP2 and 9, as well as markers of epithelial-mesenchymal transformation (EMT) were significantly higher in PVN than AR. |
| 373 | 16411407 | Homocysteine effects were investigated also after cell exposure to i) specific MEK inhibitor PD98059 (30 micromol/l) to evaluate the involvement of Mitogen-Activated Protein Kinase (MAPK) and ii) specific phosphatidylinositol 3-kinase (P13-K) inhibitor LY294002 (100 micromol/l) to evaluate the involvement of P13-K pathway. |
| 374 | 16411407 | Homocysteine, at concentrations associated with increased risk of cardiovascular events, increases MMP-2 activity, synthesis and secretion in VSMC through a mechanism involving the activation of MAPK and P13-K pathways. |
| 375 | 16424795 | Plasma thiobarbituric acid reactive species (TBA-RS) levels were measured to assess oxidative stress, and plasma MMP-2 and MMP-9 were assayed by gel zymography before and after treatment with placebo or lercanidipine. |
| 376 | 16436663 | Reverse transcription-polymerase chain reaction analysis showed that relative gene expression levels of matrix metalloproteinases (MMP-2 and MMP-9) and transforming growth factor-beta1 were increased in parallel with calcification. |
| 377 | 16436663 | Gene expression of core binding factor alpha-1, an osteoblast-specific transcription factor, increased in parallel with elastin calcification and attained approximately 9.5-fold higher expression at 21 days compared to 3 days after implantation. |
| 378 | 16436663 | Similarly, mRNA levels of the bone markers osteopontin and alkaline phosphatase also increased progressively, but osteocalcin levels remained unchanged. |
| 379 | 16446424 | Activation of the phosphatidylinositol 3-kinase (PI3K)-AKT/protein kinase B signaling pathway has been associated with multiple human cancers. |
| 380 | 16446424 | Recently we showed that AKT is activated in both the thyroid and metastatic lesions of a mouse model of follicular thyroid carcinoma [thyroid hormone beta receptor (TRbeta)(PV/PV) mice]. |
| 381 | 16446424 | Here we show that in thyroid tumors, PV mutant bound significantly more to the PI3K-regulatory subunit p85alpha, resulting in a greater increase in the kinase activity than did TRbeta1 in wild-type mice. |
| 382 | 16446424 | By confocal fluorescence microscopy, p85alpha was shown to colocalize with TRbeta1 or PV mainly in the nuclear compartment of cultured tumor cells from TRbeta(PV/PV) mice, but cytoplasmic p85alpha/PV or p85alpha/TRbeta1 complexes were also detectable. |
| 383 | 16446424 | Further biochemical analysis revealed that the activation of the PI3K-AKT-mammalian target of the rapamycin-p70(S6K) pathway was observed in both the cytoplasmic and nuclear compartments, whereas the activation of the PI3K-integrin-linked kinase-matrix metalloproteinase 2 pathway was detected mainly in the extranuclear compartments. |
| 384 | 16446424 | These results suggest that PV, via the activation of p85alpha, could act to affect PI3K downstream signaling in both the nuclear and extranuclear compartments, thereby contributing to thyroid carcinogenesis. |
| 385 | 16487958 | Matrix metalloproteinase 2 (MMP-2), 9 (MMP-9) and tissue inhibitor of metalloproteinase 1 (TIMP-1) were measured in induced sputum. |
| 386 | 16487958 | Log-normalized MMP-2, MMP-9, and TIMP-1 concentrations in sputum were not significantly different between towns. |
| 387 | 16487958 | However, after adjusting for town, asthma, diabetes, urinary monomethylarsonic acid/inorganic arsenic, and smoking history, total urinary arsenic was negatively associated with MMP-2 and TIMP-1 levels in sputum and positively associated with the ratio of MMP-2/TIMP-1 and MMP-9/TIMP-1 in sputum. |
| 388 | 16487958 | Matrix metalloproteinase 2 (MMP-2), 9 (MMP-9) and tissue inhibitor of metalloproteinase 1 (TIMP-1) were measured in induced sputum. |
| 389 | 16487958 | Log-normalized MMP-2, MMP-9, and TIMP-1 concentrations in sputum were not significantly different between towns. |
| 390 | 16487958 | However, after adjusting for town, asthma, diabetes, urinary monomethylarsonic acid/inorganic arsenic, and smoking history, total urinary arsenic was negatively associated with MMP-2 and TIMP-1 levels in sputum and positively associated with the ratio of MMP-2/TIMP-1 and MMP-9/TIMP-1 in sputum. |
| 391 | 16487958 | Matrix metalloproteinase 2 (MMP-2), 9 (MMP-9) and tissue inhibitor of metalloproteinase 1 (TIMP-1) were measured in induced sputum. |
| 392 | 16487958 | Log-normalized MMP-2, MMP-9, and TIMP-1 concentrations in sputum were not significantly different between towns. |
| 393 | 16487958 | However, after adjusting for town, asthma, diabetes, urinary monomethylarsonic acid/inorganic arsenic, and smoking history, total urinary arsenic was negatively associated with MMP-2 and TIMP-1 levels in sputum and positively associated with the ratio of MMP-2/TIMP-1 and MMP-9/TIMP-1 in sputum. |
| 394 | 16489101 | We tested the hypothesis that recovery from ailing to failing myocardium in diabetes by PPARgamma agonist is in part due to decreased matrix metalloproteinase-9 (MMP-9) activation and left ventricular (LV) tissue levels of homocysteine (Hcy). |
| 395 | 16489101 | Plasma and LV levels of MMP-2 and -9 activities were higher in the D group than in the N group but normalized after Pi treatment. |
| 396 | 16543722 | High ambient glucose levels modulates the production of MMP-9 and alpha5(IV) collagen by cultured podocytes. |
| 397 | 16543722 | The activity of 92-kDa (MMP-9) gelatinase, but not of 72 kDa (MMP-2), in an HG medium significantly increased during incubation of 2 to 3 days and decreased during incubation of more than 5 days revealed by Gelatin zymography. |
| 398 | 16543722 | Opposite to the increases in MMP-9 activity, HG medium produced significant decreases in the protein levels of alpha5(IV) collagen. |
| 399 | 16543722 | HG medium rapidly activated ERK1/2 MAPK in podocytes. |
| 400 | 16543722 | Moreover, ERK1/2 activation was required for HG-induced enhancement of MMP-9 activity and a decrease in the level of alpha5(IV) collagen. |
| 401 | 16543722 | Blocking the ERK pathway suppressed HG-induced expression and nuclear accumulation of transcriptional factor Ets-1, and MMP-9 mRNA expression. |
| 402 | 16543722 | We suggest that short- or long-term exposure to HG concentrations increases or decreases MMP-9 production and alpha5(IV) collagen expression in podocytes, this may contribute to the GBM abnormality caused by an imbalance in extracellular matrix (ECM) synthesis and degradation, and may play a critical role in the pathogenesis of proteinuria in diabetic nephropathy. |
| 403 | 16552358 | The following analyses were performed 6 h there after: (a) total and differential cell counts in bronchoalveolar lavage (BAL) fluid, (b) quantification of tumor necrosis factor alpha, interleukin (IL) 1beta, IL-10, and cytokine-induced neutrophil chemoattractant 1 in the BAL (enzyme-linked immunosorbent assay), (c)immunohistochemistry for intercellular adhesion molecule 1 and E-selectin on lung vessels, and (d) quantification of metalloproteinases (MMP) 2 and 9 in the BAL (zymography). |
| 404 | 16552358 | Relative to controls, diabetic rats exhibited a reduction in the number of neutrophils (80%) and reduced concentrations of tumor necrosis factor alpha (56%), IL-1beta (66%), and IL-10 (35%) after LPS instillation. |
| 405 | 16552358 | Despite no significant differences between diabetic and control groups, there was a remarkable increase in intercellular adhesion molecule 1 and E-selectin expression on lung vessels after insulin treatment. |
| 406 | 16552358 | Levels of MMP-2 and MMP-9 did not change after treatment with insulin. |
| 407 | 16552358 | Data presented suggest that insulin modulates the production/release of cytokines and the expression of adhesion molecules controlling, therefore, neutrophil migration during the course of LPS-induced acute lung inflammation. |
| 408 | 16609149 | Our hypothesis is that impairment of peroxisome proliferator-activated receptor-gamma (PPARgamma) initiates renal dysfunction by increasing renal glomerular matrix metalloproteinase-2 (MMP-2) activity because of increased renal homocysteine (Hcy) and decreased nitric oxide (NO) levels. |
| 409 | 16609149 | Glomerular levels of MMP-2 were increased in D mice compared with N mice, and there was no change in levels of MMP-9. |
| 410 | 16609149 | Results suggest that a PPARgamma agonist ameliorates preglomerular arteriole remodeling in diabetes by decreasing tissue levels of Hcy and MMP-2 activity and increasing NO. |
| 411 | 16609149 | Our hypothesis is that impairment of peroxisome proliferator-activated receptor-gamma (PPARgamma) initiates renal dysfunction by increasing renal glomerular matrix metalloproteinase-2 (MMP-2) activity because of increased renal homocysteine (Hcy) and decreased nitric oxide (NO) levels. |
| 412 | 16609149 | Glomerular levels of MMP-2 were increased in D mice compared with N mice, and there was no change in levels of MMP-9. |
| 413 | 16609149 | Results suggest that a PPARgamma agonist ameliorates preglomerular arteriole remodeling in diabetes by decreasing tissue levels of Hcy and MMP-2 activity and increasing NO. |
| 414 | 16609149 | Our hypothesis is that impairment of peroxisome proliferator-activated receptor-gamma (PPARgamma) initiates renal dysfunction by increasing renal glomerular matrix metalloproteinase-2 (MMP-2) activity because of increased renal homocysteine (Hcy) and decreased nitric oxide (NO) levels. |
| 415 | 16609149 | Glomerular levels of MMP-2 were increased in D mice compared with N mice, and there was no change in levels of MMP-9. |
| 416 | 16609149 | Results suggest that a PPARgamma agonist ameliorates preglomerular arteriole remodeling in diabetes by decreasing tissue levels of Hcy and MMP-2 activity and increasing NO. |
| 417 | 16643893 | Quantitative assays were performed for vitreous protein content, MMP-2, MMP-9, tissue inhibitor of metalloproteinases-1 (TIMP-1) and hemoglobin. |
| 418 | 16643893 | Qualitative evaluation of the MMP-2 and MMP-9 activation status was performed by zymography. |
| 419 | 16643893 | In addition, TIMP-1 levels were significantly increased in PDR patients (p=0.004) and functionally inhibited activation of MMP-9 in vitreous samples. |
| 420 | 16643893 | However, activated MMP-9 levels in vitreous samples of PDR patients with hemorrhage (75.7+/-106.3 scanning units per 2 microl) were significantly higher than those in PDR patients without hemorrhage (7.1+/-16.2 scanning units per 2 microl) (p<0.001) and strongly correlated with hemoglobin levels (r=0.7525; p<0.001). |
| 421 | 16643893 | Quantitative assays were performed for vitreous protein content, MMP-2, MMP-9, tissue inhibitor of metalloproteinases-1 (TIMP-1) and hemoglobin. |
| 422 | 16643893 | Qualitative evaluation of the MMP-2 and MMP-9 activation status was performed by zymography. |
| 423 | 16643893 | In addition, TIMP-1 levels were significantly increased in PDR patients (p=0.004) and functionally inhibited activation of MMP-9 in vitreous samples. |
| 424 | 16643893 | However, activated MMP-9 levels in vitreous samples of PDR patients with hemorrhage (75.7+/-106.3 scanning units per 2 microl) were significantly higher than those in PDR patients without hemorrhage (7.1+/-16.2 scanning units per 2 microl) (p<0.001) and strongly correlated with hemoglobin levels (r=0.7525; p<0.001). |
| 425 | 16732983 | Effects of benazepril on renal function and kidney expression of matrix metalloproteinase-2 and tissue inhibitor of metalloproteinase-2 in diabetic rats. |
| 426 | 16772710 | Neutrophil-gelatinase-associated lipocalin and renal function after percutaneous coronary interventions. |
| 427 | 16778129 | Reduced expression of vascular endothelial growth factor paralleled with the increased angiostatin expression resulting from the upregulated activities of matrix metalloproteinase-2 and -9 in human type 2 diabetic arterial vasculature. |
| 428 | 16778129 | We hypothesized that MMP-2 and -9 were upregulated in the diabetic vasculature, resulting in increased angiostatin production and reduced blood vessel formation. |
| 429 | 16778129 | Diabetes upregulated the expression and the gelatinolytic activity of MMP-2 and -9. |
| 430 | 16778129 | Active MMP-2 and -9 were released from diabetic arteries, but not from nondiabetic vessels, during phenylephrine-induced vasoconstriction. |
| 431 | 16778129 | Diabetes enhanced transcription and protein expression of tissue inhibitor of MMP (TIMP)-1 but had an opposite effect on TIMP-2. |
| 432 | 16778129 | In diabetic vessels angiostatin was increased by 62% and was positively correlated with the activities of MMP-2 and -9 (r2=0.806 and 0.742, respectively). |
| 433 | 16778129 | This report indicated a strong correlation between the upregulation of MMP-2 and MMP-9 and the increased angiostatin expression in the human diabetic arterial vasculature. |
| 434 | 16778129 | Reduced expression of vascular endothelial growth factor paralleled with the increased angiostatin expression resulting from the upregulated activities of matrix metalloproteinase-2 and -9 in human type 2 diabetic arterial vasculature. |
| 435 | 16778129 | We hypothesized that MMP-2 and -9 were upregulated in the diabetic vasculature, resulting in increased angiostatin production and reduced blood vessel formation. |
| 436 | 16778129 | Diabetes upregulated the expression and the gelatinolytic activity of MMP-2 and -9. |
| 437 | 16778129 | Active MMP-2 and -9 were released from diabetic arteries, but not from nondiabetic vessels, during phenylephrine-induced vasoconstriction. |
| 438 | 16778129 | Diabetes enhanced transcription and protein expression of tissue inhibitor of MMP (TIMP)-1 but had an opposite effect on TIMP-2. |
| 439 | 16778129 | In diabetic vessels angiostatin was increased by 62% and was positively correlated with the activities of MMP-2 and -9 (r2=0.806 and 0.742, respectively). |
| 440 | 16778129 | This report indicated a strong correlation between the upregulation of MMP-2 and MMP-9 and the increased angiostatin expression in the human diabetic arterial vasculature. |
| 441 | 16778129 | Reduced expression of vascular endothelial growth factor paralleled with the increased angiostatin expression resulting from the upregulated activities of matrix metalloproteinase-2 and -9 in human type 2 diabetic arterial vasculature. |
| 442 | 16778129 | We hypothesized that MMP-2 and -9 were upregulated in the diabetic vasculature, resulting in increased angiostatin production and reduced blood vessel formation. |
| 443 | 16778129 | Diabetes upregulated the expression and the gelatinolytic activity of MMP-2 and -9. |
| 444 | 16778129 | Active MMP-2 and -9 were released from diabetic arteries, but not from nondiabetic vessels, during phenylephrine-induced vasoconstriction. |
| 445 | 16778129 | Diabetes enhanced transcription and protein expression of tissue inhibitor of MMP (TIMP)-1 but had an opposite effect on TIMP-2. |
| 446 | 16778129 | In diabetic vessels angiostatin was increased by 62% and was positively correlated with the activities of MMP-2 and -9 (r2=0.806 and 0.742, respectively). |
| 447 | 16778129 | This report indicated a strong correlation between the upregulation of MMP-2 and MMP-9 and the increased angiostatin expression in the human diabetic arterial vasculature. |
| 448 | 16778129 | Reduced expression of vascular endothelial growth factor paralleled with the increased angiostatin expression resulting from the upregulated activities of matrix metalloproteinase-2 and -9 in human type 2 diabetic arterial vasculature. |
| 449 | 16778129 | We hypothesized that MMP-2 and -9 were upregulated in the diabetic vasculature, resulting in increased angiostatin production and reduced blood vessel formation. |
| 450 | 16778129 | Diabetes upregulated the expression and the gelatinolytic activity of MMP-2 and -9. |
| 451 | 16778129 | Active MMP-2 and -9 were released from diabetic arteries, but not from nondiabetic vessels, during phenylephrine-induced vasoconstriction. |
| 452 | 16778129 | Diabetes enhanced transcription and protein expression of tissue inhibitor of MMP (TIMP)-1 but had an opposite effect on TIMP-2. |
| 453 | 16778129 | In diabetic vessels angiostatin was increased by 62% and was positively correlated with the activities of MMP-2 and -9 (r2=0.806 and 0.742, respectively). |
| 454 | 16778129 | This report indicated a strong correlation between the upregulation of MMP-2 and MMP-9 and the increased angiostatin expression in the human diabetic arterial vasculature. |
| 455 | 16778129 | Reduced expression of vascular endothelial growth factor paralleled with the increased angiostatin expression resulting from the upregulated activities of matrix metalloproteinase-2 and -9 in human type 2 diabetic arterial vasculature. |
| 456 | 16778129 | We hypothesized that MMP-2 and -9 were upregulated in the diabetic vasculature, resulting in increased angiostatin production and reduced blood vessel formation. |
| 457 | 16778129 | Diabetes upregulated the expression and the gelatinolytic activity of MMP-2 and -9. |
| 458 | 16778129 | Active MMP-2 and -9 were released from diabetic arteries, but not from nondiabetic vessels, during phenylephrine-induced vasoconstriction. |
| 459 | 16778129 | Diabetes enhanced transcription and protein expression of tissue inhibitor of MMP (TIMP)-1 but had an opposite effect on TIMP-2. |
| 460 | 16778129 | In diabetic vessels angiostatin was increased by 62% and was positively correlated with the activities of MMP-2 and -9 (r2=0.806 and 0.742, respectively). |
| 461 | 16778129 | This report indicated a strong correlation between the upregulation of MMP-2 and MMP-9 and the increased angiostatin expression in the human diabetic arterial vasculature. |
| 462 | 16778129 | Reduced expression of vascular endothelial growth factor paralleled with the increased angiostatin expression resulting from the upregulated activities of matrix metalloproteinase-2 and -9 in human type 2 diabetic arterial vasculature. |
| 463 | 16778129 | We hypothesized that MMP-2 and -9 were upregulated in the diabetic vasculature, resulting in increased angiostatin production and reduced blood vessel formation. |
| 464 | 16778129 | Diabetes upregulated the expression and the gelatinolytic activity of MMP-2 and -9. |
| 465 | 16778129 | Active MMP-2 and -9 were released from diabetic arteries, but not from nondiabetic vessels, during phenylephrine-induced vasoconstriction. |
| 466 | 16778129 | Diabetes enhanced transcription and protein expression of tissue inhibitor of MMP (TIMP)-1 but had an opposite effect on TIMP-2. |
| 467 | 16778129 | In diabetic vessels angiostatin was increased by 62% and was positively correlated with the activities of MMP-2 and -9 (r2=0.806 and 0.742, respectively). |
| 468 | 16778129 | This report indicated a strong correlation between the upregulation of MMP-2 and MMP-9 and the increased angiostatin expression in the human diabetic arterial vasculature. |
| 469 | 16901490 | Pioglitazone inhibits connective tissue growth factor expression in advanced atherosclerotic plaques in low-density lipoprotein receptor-deficient mice. |
| 470 | 16901490 | Recent studies indicate that CTGF may also contribute to plaque destabilization as it induces apoptosis and stimulates MMP-2 expression in VSMCs. |
| 471 | 16901490 | Quantitative real-time PCR and Western blot showed that pioglitazone inhibited TGF-beta-stimulated CTGF expression. |
| 472 | 16931652 | Diabetes was also associated with a decrease in the expression of matrix metalloproteinase (MMP) isoform MMP-2 (ND, 0.79 +/- 0.01; D, 0.62 +/- 0.06 ROD; P < 0.05) and MMP-9 protein (ND, 0.49 +/- 0.02; D, 0.33 +/- 0.03 ROD; P < 0.05). |
| 473 | 16931652 | E2 supplementation restored MMP-2 and MMP-9 protein to levels similar or even greater than in the ND kidneys (MMP-2, 0.75 +/- 0.06; MMP-9, 0.73 +/- 0.01 ROD). |
| 474 | 16931652 | The activities of MMP-2 (ND, 7.88 +/- 0.44; D, 5.60 +/- 0.54 ROD; P < 0.05) and MMP-9 (ND, 29.9 +/- 1.8; D, 12.9 +/- 2.3 ROD; P < 0.05), as measured by zymography, were also decreased with D. |
| 475 | 16931652 | E2 supplementation restored MMP-2 and MMP-9 activity to levels similar to that in ND kidneys (MMP-2, 7.66 +/- 0.35; MMP-9, 21.4 +/- 2.9 ROD). |
| 476 | 16931652 | Diabetes was also associated with a decrease in the expression of matrix metalloproteinase (MMP) isoform MMP-2 (ND, 0.79 +/- 0.01; D, 0.62 +/- 0.06 ROD; P < 0.05) and MMP-9 protein (ND, 0.49 +/- 0.02; D, 0.33 +/- 0.03 ROD; P < 0.05). |
| 477 | 16931652 | E2 supplementation restored MMP-2 and MMP-9 protein to levels similar or even greater than in the ND kidneys (MMP-2, 0.75 +/- 0.06; MMP-9, 0.73 +/- 0.01 ROD). |
| 478 | 16931652 | The activities of MMP-2 (ND, 7.88 +/- 0.44; D, 5.60 +/- 0.54 ROD; P < 0.05) and MMP-9 (ND, 29.9 +/- 1.8; D, 12.9 +/- 2.3 ROD; P < 0.05), as measured by zymography, were also decreased with D. |
| 479 | 16931652 | E2 supplementation restored MMP-2 and MMP-9 activity to levels similar to that in ND kidneys (MMP-2, 7.66 +/- 0.35; MMP-9, 21.4 +/- 2.9 ROD). |
| 480 | 16931652 | Diabetes was also associated with a decrease in the expression of matrix metalloproteinase (MMP) isoform MMP-2 (ND, 0.79 +/- 0.01; D, 0.62 +/- 0.06 ROD; P < 0.05) and MMP-9 protein (ND, 0.49 +/- 0.02; D, 0.33 +/- 0.03 ROD; P < 0.05). |
| 481 | 16931652 | E2 supplementation restored MMP-2 and MMP-9 protein to levels similar or even greater than in the ND kidneys (MMP-2, 0.75 +/- 0.06; MMP-9, 0.73 +/- 0.01 ROD). |
| 482 | 16931652 | The activities of MMP-2 (ND, 7.88 +/- 0.44; D, 5.60 +/- 0.54 ROD; P < 0.05) and MMP-9 (ND, 29.9 +/- 1.8; D, 12.9 +/- 2.3 ROD; P < 0.05), as measured by zymography, were also decreased with D. |
| 483 | 16931652 | E2 supplementation restored MMP-2 and MMP-9 activity to levels similar to that in ND kidneys (MMP-2, 7.66 +/- 0.35; MMP-9, 21.4 +/- 2.9 ROD). |
| 484 | 16931652 | Diabetes was also associated with a decrease in the expression of matrix metalloproteinase (MMP) isoform MMP-2 (ND, 0.79 +/- 0.01; D, 0.62 +/- 0.06 ROD; P < 0.05) and MMP-9 protein (ND, 0.49 +/- 0.02; D, 0.33 +/- 0.03 ROD; P < 0.05). |
| 485 | 16931652 | E2 supplementation restored MMP-2 and MMP-9 protein to levels similar or even greater than in the ND kidneys (MMP-2, 0.75 +/- 0.06; MMP-9, 0.73 +/- 0.01 ROD). |
| 486 | 16931652 | The activities of MMP-2 (ND, 7.88 +/- 0.44; D, 5.60 +/- 0.54 ROD; P < 0.05) and MMP-9 (ND, 29.9 +/- 1.8; D, 12.9 +/- 2.3 ROD; P < 0.05), as measured by zymography, were also decreased with D. |
| 487 | 16931652 | E2 supplementation restored MMP-2 and MMP-9 activity to levels similar to that in ND kidneys (MMP-2, 7.66 +/- 0.35; MMP-9, 21.4 +/- 2.9 ROD). |
| 488 | 17020653 | [Metalloproteinases MMP-2 and MMP-9 and their inhibitors TIMP-1 and TIMP-2 levels in children and adolescents with type 1 diabetes]. |
| 489 | 17195891 | Increased circulatory MMP-2 and MMP-9 levels and activities in patients with type 1 diabetes mellitus. |
| 490 | 17203468 | Opposite effects of high glucose on MMP-2 and TIMP-2 in human endothelial cells. |
| 491 | 17203468 | HUVECs were treated with medium containing 5.5 mM or 33 mM of glucose in the presence or the absence of ascorbic acid and MMP inhibitors (GM6001 and endogenous tissue inhibitors of MMPs, TIMP-1, and TIMP-2). |
| 492 | 17203468 | The results revealed that high glucose-induced apoptosis could be suppressed by ascorbic acid, GM6001 and TIMP-2, but not by TIMP-1. |
| 493 | 17203468 | The activities of MMP-2, MMP-9 and its inhibitors, TIMP-1, TIMP-2 after high glucose treatment, were also detected by ELISA method. |
| 494 | 17203468 | We found that the activated form of MMP-2, but not MMP-9, was increased, while the level of TIMP-2, but not TIMP-1, was decreased. |
| 495 | 17203468 | In Western blot and RT-PCR analysis, the expression of TIMP-2, but not TIMP-1, after high glucose treatment was downregulated, whereas the levels of MMP-2 and -9 proteins and mRNA were not changed. |
| 496 | 17203468 | The present study indicated that oxidative stress induced by high glucose might be involved in the opposite effects on MMP-2 activation and TIMP-2 downregulation. |
| 497 | 17203468 | Opposite effects of high glucose on MMP-2 and TIMP-2 in human endothelial cells. |
| 498 | 17203468 | HUVECs were treated with medium containing 5.5 mM or 33 mM of glucose in the presence or the absence of ascorbic acid and MMP inhibitors (GM6001 and endogenous tissue inhibitors of MMPs, TIMP-1, and TIMP-2). |
| 499 | 17203468 | The results revealed that high glucose-induced apoptosis could be suppressed by ascorbic acid, GM6001 and TIMP-2, but not by TIMP-1. |
| 500 | 17203468 | The activities of MMP-2, MMP-9 and its inhibitors, TIMP-1, TIMP-2 after high glucose treatment, were also detected by ELISA method. |
| 501 | 17203468 | We found that the activated form of MMP-2, but not MMP-9, was increased, while the level of TIMP-2, but not TIMP-1, was decreased. |
| 502 | 17203468 | In Western blot and RT-PCR analysis, the expression of TIMP-2, but not TIMP-1, after high glucose treatment was downregulated, whereas the levels of MMP-2 and -9 proteins and mRNA were not changed. |
| 503 | 17203468 | The present study indicated that oxidative stress induced by high glucose might be involved in the opposite effects on MMP-2 activation and TIMP-2 downregulation. |
| 504 | 17203468 | Opposite effects of high glucose on MMP-2 and TIMP-2 in human endothelial cells. |
| 505 | 17203468 | HUVECs were treated with medium containing 5.5 mM or 33 mM of glucose in the presence or the absence of ascorbic acid and MMP inhibitors (GM6001 and endogenous tissue inhibitors of MMPs, TIMP-1, and TIMP-2). |
| 506 | 17203468 | The results revealed that high glucose-induced apoptosis could be suppressed by ascorbic acid, GM6001 and TIMP-2, but not by TIMP-1. |
| 507 | 17203468 | The activities of MMP-2, MMP-9 and its inhibitors, TIMP-1, TIMP-2 after high glucose treatment, were also detected by ELISA method. |
| 508 | 17203468 | We found that the activated form of MMP-2, but not MMP-9, was increased, while the level of TIMP-2, but not TIMP-1, was decreased. |
| 509 | 17203468 | In Western blot and RT-PCR analysis, the expression of TIMP-2, but not TIMP-1, after high glucose treatment was downregulated, whereas the levels of MMP-2 and -9 proteins and mRNA were not changed. |
| 510 | 17203468 | The present study indicated that oxidative stress induced by high glucose might be involved in the opposite effects on MMP-2 activation and TIMP-2 downregulation. |
| 511 | 17203468 | Opposite effects of high glucose on MMP-2 and TIMP-2 in human endothelial cells. |
| 512 | 17203468 | HUVECs were treated with medium containing 5.5 mM or 33 mM of glucose in the presence or the absence of ascorbic acid and MMP inhibitors (GM6001 and endogenous tissue inhibitors of MMPs, TIMP-1, and TIMP-2). |
| 513 | 17203468 | The results revealed that high glucose-induced apoptosis could be suppressed by ascorbic acid, GM6001 and TIMP-2, but not by TIMP-1. |
| 514 | 17203468 | The activities of MMP-2, MMP-9 and its inhibitors, TIMP-1, TIMP-2 after high glucose treatment, were also detected by ELISA method. |
| 515 | 17203468 | We found that the activated form of MMP-2, but not MMP-9, was increased, while the level of TIMP-2, but not TIMP-1, was decreased. |
| 516 | 17203468 | In Western blot and RT-PCR analysis, the expression of TIMP-2, but not TIMP-1, after high glucose treatment was downregulated, whereas the levels of MMP-2 and -9 proteins and mRNA were not changed. |
| 517 | 17203468 | The present study indicated that oxidative stress induced by high glucose might be involved in the opposite effects on MMP-2 activation and TIMP-2 downregulation. |
| 518 | 17203468 | Opposite effects of high glucose on MMP-2 and TIMP-2 in human endothelial cells. |
| 519 | 17203468 | HUVECs were treated with medium containing 5.5 mM or 33 mM of glucose in the presence or the absence of ascorbic acid and MMP inhibitors (GM6001 and endogenous tissue inhibitors of MMPs, TIMP-1, and TIMP-2). |
| 520 | 17203468 | The results revealed that high glucose-induced apoptosis could be suppressed by ascorbic acid, GM6001 and TIMP-2, but not by TIMP-1. |
| 521 | 17203468 | The activities of MMP-2, MMP-9 and its inhibitors, TIMP-1, TIMP-2 after high glucose treatment, were also detected by ELISA method. |
| 522 | 17203468 | We found that the activated form of MMP-2, but not MMP-9, was increased, while the level of TIMP-2, but not TIMP-1, was decreased. |
| 523 | 17203468 | In Western blot and RT-PCR analysis, the expression of TIMP-2, but not TIMP-1, after high glucose treatment was downregulated, whereas the levels of MMP-2 and -9 proteins and mRNA were not changed. |
| 524 | 17203468 | The present study indicated that oxidative stress induced by high glucose might be involved in the opposite effects on MMP-2 activation and TIMP-2 downregulation. |
| 525 | 17283886 | Extracellular matrix deposition in the kidney was examined by the protein expression of type IV collagen, connective tissue growth factor (CTGF) and matrix metalloproteinases 2 (MMP-2) using immunohistochemistry. |
| 526 | 17283886 | The expression of type IV collagen and CTGF was elevated whereas that of MMP-2 was reduced in the kidneys of HFSCD group compared with the CD group. |
| 527 | 17283886 | Extracellular matrix deposition in the kidney was examined by the protein expression of type IV collagen, connective tissue growth factor (CTGF) and matrix metalloproteinases 2 (MMP-2) using immunohistochemistry. |
| 528 | 17283886 | The expression of type IV collagen and CTGF was elevated whereas that of MMP-2 was reduced in the kidneys of HFSCD group compared with the CD group. |
| 529 | 17327431 | The total cardiac collagen content and collagen type 1 and 3 were measured by histochemistry, and MMP-2 activity was measured by gelatin zymography. |
| 530 | 17327431 | This was accompanied by increased TGFbeta, IL1beta, and fibrosis and decreased MMP-2 activity. |
| 531 | 17327431 | Treatment with irbesartan attenuated LV dysfunction, IL1beta, TGFbeta, and cardiac fibrosis compared with untreated diabetic animals and normalized MMP activity. |
| 532 | 17327431 | The total cardiac collagen content and collagen type 1 and 3 were measured by histochemistry, and MMP-2 activity was measured by gelatin zymography. |
| 533 | 17327431 | This was accompanied by increased TGFbeta, IL1beta, and fibrosis and decreased MMP-2 activity. |
| 534 | 17327431 | Treatment with irbesartan attenuated LV dysfunction, IL1beta, TGFbeta, and cardiac fibrosis compared with untreated diabetic animals and normalized MMP activity. |
| 535 | 17332085 | Our data showed that chemically induced diabetes of 6 months' duration significantly increased the expression and activity of both MMP-2 and its physiological activator MT1-MMP. |
| 536 | 17364896 | MMP-2, -9, and TIMP-1, -2 plasma levels were measured in diabetic patients with ACSs compared to nondiabetic patients with ACSs. |
| 537 | 17364896 | The following parameters were measured: body mass index (BMI), glycosylated hemoglobin (HbA1c), fasting plasma glucose (FPG), fasting plasma insulin (FPI), homeostasis model assessment index (HOMA index), systolic blood pressure (SBP), diastolic blood pressure (DBP), total cholesterol (TC), low-density lipoprotein cholesterol (LDL-C), high-density lipoprotein cholesterol (HDL-C), triglycerides (Tg), lipoprotein(a) [Lp(a)], plasminogen activator inhibitor-1 (PAI-1), homocysteine (Hct), fibrinogen (Fg), high-sensitivity C-reactive protein (hs-CRP), and plasma levels of MMP-2, MMP-9, TIMP-1, and TIMP-2. |
| 538 | 17364896 | MMP-9, TIMP-1, and TIMP-2 plasma levels were higher in diabetic patients with ACSs compared to nondiabetic patients with ACSs. |
| 539 | 17364896 | MMP-9, TIMP-1, and TIMP-2 plasma levels were increased in diabetic patients with ACSs, which may reflect abnormal extracellular matrix metabolism in diabetes during acute event. |
| 540 | 17364896 | MMP-2, -9, and TIMP-1, -2 plasma levels were measured in diabetic patients with ACSs compared to nondiabetic patients with ACSs. |
| 541 | 17364896 | The following parameters were measured: body mass index (BMI), glycosylated hemoglobin (HbA1c), fasting plasma glucose (FPG), fasting plasma insulin (FPI), homeostasis model assessment index (HOMA index), systolic blood pressure (SBP), diastolic blood pressure (DBP), total cholesterol (TC), low-density lipoprotein cholesterol (LDL-C), high-density lipoprotein cholesterol (HDL-C), triglycerides (Tg), lipoprotein(a) [Lp(a)], plasminogen activator inhibitor-1 (PAI-1), homocysteine (Hct), fibrinogen (Fg), high-sensitivity C-reactive protein (hs-CRP), and plasma levels of MMP-2, MMP-9, TIMP-1, and TIMP-2. |
| 542 | 17364896 | MMP-9, TIMP-1, and TIMP-2 plasma levels were higher in diabetic patients with ACSs compared to nondiabetic patients with ACSs. |
| 543 | 17364896 | MMP-9, TIMP-1, and TIMP-2 plasma levels were increased in diabetic patients with ACSs, which may reflect abnormal extracellular matrix metabolism in diabetes during acute event. |
| 544 | 17389601 | Filamin A-mediated down-regulation of the exchange factor Ras-GRF1 correlates with decreased matrix metalloproteinase-9 expression in human melanoma cells. |
| 545 | 17389601 | The lack of FLNa in human M2 melanoma cells was associated with constitutive and phorbol ester-induced expression and secretion of active MMP-9 in the absence of MMP-2 up-regulation. |
| 546 | 17389601 | M2 cells displayed stronger MMP-9 production and activity than their M2A7 counterparts where FLNa had been stably reintroduced. |
| 547 | 17389601 | Using an MMP-9 promoter construct (pMMP-9-Luc), in vitro kinase assays, and genetic and pharmacological approaches, we demonstrate that FLNa mediated transcriptional down-regulation of pMMP-9-Luc by suppressing the constitutive hyperactivity of the Ras/MAPK extracellular signal-regulated kinase (ERK) cascade. |
| 548 | 17389601 | Experimental evidence indicated that this phenomenon was associated with destabilization and ubiquitylation of Ras-GRF1, a guanine nucleotide exchange factor that activates H-Ras by facilitating the release of GDP. |
| 549 | 17389601 | Ectopic expression of Ras-GRF1 was accompanied by ERK activation and elevated levels of MMP-9 in M2A7 cells, whereas a catalytically inactive dominant negative Ras-GRF1, which prevented ERK activation, reduced MMP-9 expression in M2 cells. |
| 550 | 17389601 | Our results indicate that expression of FLNa regulates constitutive activation of the Ras/ERK pathway partly through a Ras-GRF1 mechanism to modulate the production of MMP-9. |
| 551 | 17487426 | Multivariable logistic regression analysis with adjustment for age, sex, body mass index, and the prevalence of smoking, hypertension, diabetes mellitus, and hyperchole-sterolemia as well as a stepwise forward selection procedure revealed that the -1306C-->T polymorphism of the matrix metalloproteinase 2 gene (MMP2) and the -592A-->C polymorphism of the interleukin 10 gene (IL10) were significantly (false discovery rate of <0.05) associated with the prevalence of AF. |
| 552 | 17487426 | The T allele of the MMP2 polymorphism and the C allele of the IL10 polymorphism were a risk factor for and protective factor against AF, respectively. |
| 553 | 17487426 | Multivariable logistic regression analysis with adjustment for age, sex, body mass index, and the prevalence of smoking, hypertension, diabetes mellitus, and hyperchole-sterolemia as well as a stepwise forward selection procedure revealed that the -1306C-->T polymorphism of the matrix metalloproteinase 2 gene (MMP2) and the -592A-->C polymorphism of the interleukin 10 gene (IL10) were significantly (false discovery rate of <0.05) associated with the prevalence of AF. |
| 554 | 17487426 | The T allele of the MMP2 polymorphism and the C allele of the IL10 polymorphism were a risk factor for and protective factor against AF, respectively. |
| 555 | 17496904 | Expression of matrix metalloproteinases MMP-2 and MMP-9 is altered during nephrogenesis in fetuses from diabetic rats. |
| 556 | 17496904 | Recent studies have emphasized the role of matrix metalloproteinases (MMP-2 and MMP-9) in normal mouse nephrogenesis. |
| 557 | 17496904 | Transforming growth factor-beta1 (TGF-beta1) and connective tissue growth factor (CTGF) are known to mediate high glucose effects on matrix degradation. |
| 558 | 17496904 | The aim of the present study was to address the expression of type IV collagenase and TGF-beta1/CTGF systems in rat kidney during normal development and after in utero exposure to maternal diabetes. |
| 559 | 17496904 | Both MMP-2 and MMP-9 mRNA metanephric expressions and activities were dramatically downregulated in kidneys issued from diabetic fetuses and in metanephros cultured in the presence of high glucose concentration. |
| 560 | 17496904 | TGF-beta1 and CTGF expressions were significantly enhanced in diabetic fetal kidneys and in high glucose cultured metanephroi. |
| 561 | 17496904 | In conclusion, in impaired nephrogenesis resulting from in utero exposure to maternal diabetes, alteration of both type IV collagenase and TGF-beta1/CTGF systems may lead to abnormal remodeling of ECM, which may, in turn, induce defects in ureteral bud branching leading to the observed reduction in the nephron number with consequences later in life: progression of chronic renal disease and hypertension. |
| 562 | 17496904 | Expression of matrix metalloproteinases MMP-2 and MMP-9 is altered during nephrogenesis in fetuses from diabetic rats. |
| 563 | 17496904 | Recent studies have emphasized the role of matrix metalloproteinases (MMP-2 and MMP-9) in normal mouse nephrogenesis. |
| 564 | 17496904 | Transforming growth factor-beta1 (TGF-beta1) and connective tissue growth factor (CTGF) are known to mediate high glucose effects on matrix degradation. |
| 565 | 17496904 | The aim of the present study was to address the expression of type IV collagenase and TGF-beta1/CTGF systems in rat kidney during normal development and after in utero exposure to maternal diabetes. |
| 566 | 17496904 | Both MMP-2 and MMP-9 mRNA metanephric expressions and activities were dramatically downregulated in kidneys issued from diabetic fetuses and in metanephros cultured in the presence of high glucose concentration. |
| 567 | 17496904 | TGF-beta1 and CTGF expressions were significantly enhanced in diabetic fetal kidneys and in high glucose cultured metanephroi. |
| 568 | 17496904 | In conclusion, in impaired nephrogenesis resulting from in utero exposure to maternal diabetes, alteration of both type IV collagenase and TGF-beta1/CTGF systems may lead to abnormal remodeling of ECM, which may, in turn, induce defects in ureteral bud branching leading to the observed reduction in the nephron number with consequences later in life: progression of chronic renal disease and hypertension. |
| 569 | 17496904 | Expression of matrix metalloproteinases MMP-2 and MMP-9 is altered during nephrogenesis in fetuses from diabetic rats. |
| 570 | 17496904 | Recent studies have emphasized the role of matrix metalloproteinases (MMP-2 and MMP-9) in normal mouse nephrogenesis. |
| 571 | 17496904 | Transforming growth factor-beta1 (TGF-beta1) and connective tissue growth factor (CTGF) are known to mediate high glucose effects on matrix degradation. |
| 572 | 17496904 | The aim of the present study was to address the expression of type IV collagenase and TGF-beta1/CTGF systems in rat kidney during normal development and after in utero exposure to maternal diabetes. |
| 573 | 17496904 | Both MMP-2 and MMP-9 mRNA metanephric expressions and activities were dramatically downregulated in kidneys issued from diabetic fetuses and in metanephros cultured in the presence of high glucose concentration. |
| 574 | 17496904 | TGF-beta1 and CTGF expressions were significantly enhanced in diabetic fetal kidneys and in high glucose cultured metanephroi. |
| 575 | 17496904 | In conclusion, in impaired nephrogenesis resulting from in utero exposure to maternal diabetes, alteration of both type IV collagenase and TGF-beta1/CTGF systems may lead to abnormal remodeling of ECM, which may, in turn, induce defects in ureteral bud branching leading to the observed reduction in the nephron number with consequences later in life: progression of chronic renal disease and hypertension. |
| 576 | 17587828 | Although a number of factors may initiate EMT in the kidney, the most potent is transforming growth factor-beta1 (TGF-beta1). |
| 577 | 17587828 | Moreover, many other prosclerotic factors have effects on EMT indirectly, via induction of TGF-beta1. |
| 578 | 17587828 | Signaling events in this pathway include activation of Smad/integrin-linked kinase (ILK) and connective tissue growth factor (CTGF). |
| 579 | 17587828 | In particular, overexpression of matrix metalloproteinase-2 has a key role in the initiation of EMT, membrane dissolution, and the interstitial transit of transformed mesenchymal cells. |
| 580 | 17826767 | The aim of the study was to determine the effect of PRP on the activity of matrix metalloproteinase-2 (MMP-2) and MMP-9, and also on the alpha(2)-Macroglobulin (alpha(2)M) proteolytic state in the vitreous of eyes with PDR. |
| 581 | 17826767 | Qualitative evaluation of the MMP-2 and MMP-9 activation status was performed by gelatin zymography and quantitative assay was carried out for vitreous total protein content and alpha(2)M. |
| 582 | 17826767 | The aim of the study was to determine the effect of PRP on the activity of matrix metalloproteinase-2 (MMP-2) and MMP-9, and also on the alpha(2)-Macroglobulin (alpha(2)M) proteolytic state in the vitreous of eyes with PDR. |
| 583 | 17826767 | Qualitative evaluation of the MMP-2 and MMP-9 activation status was performed by gelatin zymography and quantitative assay was carried out for vitreous total protein content and alpha(2)M. |
| 584 | 17879211 | Serum matrix metalloproteinases MMP-2 and MMP-9 and metalloproteinase tissue inhibitors TIMP-1 and TIMP-2 in diabetic nephropathy. |
| 585 | 17890296 | The role of nitric oxide on matrix metalloproteinase 2 (MMP2) and MMP9 in placenta and fetus from diabetic rats. |
| 586 | 17890296 | We found that NADPH-diaphorase activity, which reflects the distribution and activity of NO synthases (NOS), was increased in both placenta and fetuses from diabetic rats when compared with controls. |
| 587 | 17890296 | In addition, while a NO donor enhanced MMP2 and MMP9 activities, a NOS inhibitor reduced these activities in the maternal side of the placenta from control rats. |
| 588 | 17890296 | On the other hand, the NO donor did not modify MMP2 and MMP9 activities, while the NOS inhibitor reduced MMP9 activity in the fetal side of both control and diabetic placentas. |
| 589 | 17890296 | The role of nitric oxide on matrix metalloproteinase 2 (MMP2) and MMP9 in placenta and fetus from diabetic rats. |
| 590 | 17890296 | We found that NADPH-diaphorase activity, which reflects the distribution and activity of NO synthases (NOS), was increased in both placenta and fetuses from diabetic rats when compared with controls. |
| 591 | 17890296 | In addition, while a NO donor enhanced MMP2 and MMP9 activities, a NOS inhibitor reduced these activities in the maternal side of the placenta from control rats. |
| 592 | 17890296 | On the other hand, the NO donor did not modify MMP2 and MMP9 activities, while the NOS inhibitor reduced MMP9 activity in the fetal side of both control and diabetic placentas. |
| 593 | 17890296 | The role of nitric oxide on matrix metalloproteinase 2 (MMP2) and MMP9 in placenta and fetus from diabetic rats. |
| 594 | 17890296 | We found that NADPH-diaphorase activity, which reflects the distribution and activity of NO synthases (NOS), was increased in both placenta and fetuses from diabetic rats when compared with controls. |
| 595 | 17890296 | In addition, while a NO donor enhanced MMP2 and MMP9 activities, a NOS inhibitor reduced these activities in the maternal side of the placenta from control rats. |
| 596 | 17890296 | On the other hand, the NO donor did not modify MMP2 and MMP9 activities, while the NOS inhibitor reduced MMP9 activity in the fetal side of both control and diabetic placentas. |
| 597 | 17901710 | Could neutrophil-gelatinase-associated lipocalin and cystatin C predict the development of contrast-induced nephropathy after percutaneous coronary interventions in patients with stable angina and normal serum creatinine values? |
| 598 | 17901710 | The value of neutrophil-gelatinase-associated lipocalin (NGAL) was highlighted as a novel biomarker for the detection of acute renal failure. |
| 599 | 17901710 | In addition, we assessed serum and urinary NGAL in relation to cystatin C, estimated glomerular filtration rate, and serum and urinary creatinine in these patients. |
| 600 | 17901710 | The NGAL levels were significantly higher 2 h after the PCI (serum NGAL) or 4 h after the PCI (urinary NGAL), whereas the cystatin C values were higher only 8 and 24 h after a PCI procedure in patients with CIN. |
| 601 | 17901710 | Could neutrophil-gelatinase-associated lipocalin and cystatin C predict the development of contrast-induced nephropathy after percutaneous coronary interventions in patients with stable angina and normal serum creatinine values? |
| 602 | 17901710 | The value of neutrophil-gelatinase-associated lipocalin (NGAL) was highlighted as a novel biomarker for the detection of acute renal failure. |
| 603 | 17901710 | In addition, we assessed serum and urinary NGAL in relation to cystatin C, estimated glomerular filtration rate, and serum and urinary creatinine in these patients. |
| 604 | 17901710 | The NGAL levels were significantly higher 2 h after the PCI (serum NGAL) or 4 h after the PCI (urinary NGAL), whereas the cystatin C values were higher only 8 and 24 h after a PCI procedure in patients with CIN. |
| 605 | 17982970 | The roles of MMP-2/TIMP-2 in extracellular matrix remodelling in the hearts of STZ-induced diabetic rats. |
| 606 | 18043992 | We measured MMP-2, -9, and TIMP-1, -2 plasma levels in healthy subjects (controls), in type 2 diabetic patients, in nondiabetic patients with ACS (ACS) and in diabetic patients with ACS (DACS). |
| 607 | 18043992 | We measured also BMI (body mass index), HbA(1c) (glycated hemoglobin) FPG (fasting plasma glucosa), FPI (fasting plasma insulin), HOMA index (homeostasis model assessment index), SBP (systolic blood pressure), DBP (diastolic blood pressure), TC (total cholesterol), LDL-C (low density lipoprotein cholesterol), HDL-C (high-density lipoprotein cholesterol), Tg (triglycerides), Lp(a) (lipoprotein(a)) PAI-1 (plasminogen activator inhibitor-1), Hct (homocysteine), Fg (fibrinogen), and hs-CRP (high-sensitivity C-reactive protein). |
| 608 | 18043992 | Higher MMP-2, MMP-9, TIMP-1, and TIMP-2 levels were present in diabetic, ACS, and DACS patients compared to controls. |
| 609 | 18043992 | Significant MMP-2, TIMP-1, and TIMP-2 increases were observed in ACS and DACS groups, while MMP-9 decreased in these patients compared to diabetics. |
| 610 | 18043992 | In conclusion, MMP-2, MMP-9, TIMP-1, and TIMP-2 plasma levels were higher in diabetic, ACS, and DACS patients, which may reflect abnormal extracellular matrix metabolism in diabetes and in acute coronary syndrome. |
| 611 | 18043992 | We measured MMP-2, -9, and TIMP-1, -2 plasma levels in healthy subjects (controls), in type 2 diabetic patients, in nondiabetic patients with ACS (ACS) and in diabetic patients with ACS (DACS). |
| 612 | 18043992 | We measured also BMI (body mass index), HbA(1c) (glycated hemoglobin) FPG (fasting plasma glucosa), FPI (fasting plasma insulin), HOMA index (homeostasis model assessment index), SBP (systolic blood pressure), DBP (diastolic blood pressure), TC (total cholesterol), LDL-C (low density lipoprotein cholesterol), HDL-C (high-density lipoprotein cholesterol), Tg (triglycerides), Lp(a) (lipoprotein(a)) PAI-1 (plasminogen activator inhibitor-1), Hct (homocysteine), Fg (fibrinogen), and hs-CRP (high-sensitivity C-reactive protein). |
| 613 | 18043992 | Higher MMP-2, MMP-9, TIMP-1, and TIMP-2 levels were present in diabetic, ACS, and DACS patients compared to controls. |
| 614 | 18043992 | Significant MMP-2, TIMP-1, and TIMP-2 increases were observed in ACS and DACS groups, while MMP-9 decreased in these patients compared to diabetics. |
| 615 | 18043992 | In conclusion, MMP-2, MMP-9, TIMP-1, and TIMP-2 plasma levels were higher in diabetic, ACS, and DACS patients, which may reflect abnormal extracellular matrix metabolism in diabetes and in acute coronary syndrome. |
| 616 | 18043992 | We measured MMP-2, -9, and TIMP-1, -2 plasma levels in healthy subjects (controls), in type 2 diabetic patients, in nondiabetic patients with ACS (ACS) and in diabetic patients with ACS (DACS). |
| 617 | 18043992 | We measured also BMI (body mass index), HbA(1c) (glycated hemoglobin) FPG (fasting plasma glucosa), FPI (fasting plasma insulin), HOMA index (homeostasis model assessment index), SBP (systolic blood pressure), DBP (diastolic blood pressure), TC (total cholesterol), LDL-C (low density lipoprotein cholesterol), HDL-C (high-density lipoprotein cholesterol), Tg (triglycerides), Lp(a) (lipoprotein(a)) PAI-1 (plasminogen activator inhibitor-1), Hct (homocysteine), Fg (fibrinogen), and hs-CRP (high-sensitivity C-reactive protein). |
| 618 | 18043992 | Higher MMP-2, MMP-9, TIMP-1, and TIMP-2 levels were present in diabetic, ACS, and DACS patients compared to controls. |
| 619 | 18043992 | Significant MMP-2, TIMP-1, and TIMP-2 increases were observed in ACS and DACS groups, while MMP-9 decreased in these patients compared to diabetics. |
| 620 | 18043992 | In conclusion, MMP-2, MMP-9, TIMP-1, and TIMP-2 plasma levels were higher in diabetic, ACS, and DACS patients, which may reflect abnormal extracellular matrix metabolism in diabetes and in acute coronary syndrome. |
| 621 | 18043992 | We measured MMP-2, -9, and TIMP-1, -2 plasma levels in healthy subjects (controls), in type 2 diabetic patients, in nondiabetic patients with ACS (ACS) and in diabetic patients with ACS (DACS). |
| 622 | 18043992 | We measured also BMI (body mass index), HbA(1c) (glycated hemoglobin) FPG (fasting plasma glucosa), FPI (fasting plasma insulin), HOMA index (homeostasis model assessment index), SBP (systolic blood pressure), DBP (diastolic blood pressure), TC (total cholesterol), LDL-C (low density lipoprotein cholesterol), HDL-C (high-density lipoprotein cholesterol), Tg (triglycerides), Lp(a) (lipoprotein(a)) PAI-1 (plasminogen activator inhibitor-1), Hct (homocysteine), Fg (fibrinogen), and hs-CRP (high-sensitivity C-reactive protein). |
| 623 | 18043992 | Higher MMP-2, MMP-9, TIMP-1, and TIMP-2 levels were present in diabetic, ACS, and DACS patients compared to controls. |
| 624 | 18043992 | Significant MMP-2, TIMP-1, and TIMP-2 increases were observed in ACS and DACS groups, while MMP-9 decreased in these patients compared to diabetics. |
| 625 | 18043992 | In conclusion, MMP-2, MMP-9, TIMP-1, and TIMP-2 plasma levels were higher in diabetic, ACS, and DACS patients, which may reflect abnormal extracellular matrix metabolism in diabetes and in acute coronary syndrome. |
| 626 | 18187544 | The matricellular proteins, cysteine-rich protein 61 (Cyr61) and connective tissue growth factor (CTGF), are aberrantly expressed in the retinal vasculature from the early stages of DR, but their effects on retinal pericytes are unknown. |
| 627 | 18187544 | We show herein that rat retinal pericytes (RRPs) exposed to advanced glycosylation-end products, an important injurious stimulus of diabetes, express increased levels of both Cyr61 and CTGF, and concomitantly undergo anoikis, a form of apoptosis by loss of cell-matrix interactions. |
| 628 | 18187544 | Adenovirus-mediated expression of Cyr61 and/or CTGF conferred an anoikis-prone phenotype to rat retinal pericytes, including decreased phosphotyrosine protein levels at focal adhesion points and formation of cortical actin rings. |
| 629 | 18187544 | When used as substrates for pericyte attachment and compared with other matrix proteins (e.g. type IV collagen), recombinant Cyr61 and CTGF proteins exhibited antiadhesive and apoptogenic activities. |
| 630 | 18187544 | Phosphatase inhibitors reversed these effects, suggesting that Cyr61 and CTGF promote dephosphorylation events. |
| 631 | 18187544 | Furthermore, Cyr61- and CTGF-induced apoptosis was mediated through the intrinsic pathway and involved the expression of genes that have been functionally grouped as p53 target genes. |
| 632 | 18187544 | Expression of the matrix metalloproteinase-2 gene, a known target of p53, was increased in pericytes overexpressing either Cyr61 or CTGF. |
| 633 | 18187544 | Inhibition of matrix metalloproteinase-2 had, at least in part, a protective effect against Cyr61- and CTGF-induced apoptosis. |
| 634 | 18187544 | Taken together, these findings support the involvement of Cyr61 and CTGF in pericyte detachment and anoikis, implicating these proteins in the pathogenesis of DR. |
| 635 | 18187544 | The matricellular proteins, cysteine-rich protein 61 (Cyr61) and connective tissue growth factor (CTGF), are aberrantly expressed in the retinal vasculature from the early stages of DR, but their effects on retinal pericytes are unknown. |
| 636 | 18187544 | We show herein that rat retinal pericytes (RRPs) exposed to advanced glycosylation-end products, an important injurious stimulus of diabetes, express increased levels of both Cyr61 and CTGF, and concomitantly undergo anoikis, a form of apoptosis by loss of cell-matrix interactions. |
| 637 | 18187544 | Adenovirus-mediated expression of Cyr61 and/or CTGF conferred an anoikis-prone phenotype to rat retinal pericytes, including decreased phosphotyrosine protein levels at focal adhesion points and formation of cortical actin rings. |
| 638 | 18187544 | When used as substrates for pericyte attachment and compared with other matrix proteins (e.g. type IV collagen), recombinant Cyr61 and CTGF proteins exhibited antiadhesive and apoptogenic activities. |
| 639 | 18187544 | Phosphatase inhibitors reversed these effects, suggesting that Cyr61 and CTGF promote dephosphorylation events. |
| 640 | 18187544 | Furthermore, Cyr61- and CTGF-induced apoptosis was mediated through the intrinsic pathway and involved the expression of genes that have been functionally grouped as p53 target genes. |
| 641 | 18187544 | Expression of the matrix metalloproteinase-2 gene, a known target of p53, was increased in pericytes overexpressing either Cyr61 or CTGF. |
| 642 | 18187544 | Inhibition of matrix metalloproteinase-2 had, at least in part, a protective effect against Cyr61- and CTGF-induced apoptosis. |
| 643 | 18187544 | Taken together, these findings support the involvement of Cyr61 and CTGF in pericyte detachment and anoikis, implicating these proteins in the pathogenesis of DR. |
| 644 | 18237111 | Recent data demonstrates that increased intracellular glycosylation of proteins via O-GlcNAc can induce insulin resistance and that a rodent model with genetically elevated O-GlcNAc levels in muscle and fat displays hyperleptinemia. |
| 645 | 18237111 | The link between O-GlcNAc levels, insulin resistance, and adipocytokine secretion is further explored here. |
| 646 | 18237111 | By the use of two protocols for inducing insulin resistance, classical hyperglycemia with chronic insulin exposure and pharmacological elevation of O-GlcNAc levels, several proteins are identified that are regulated in a similar fashion under both conditions including HCNP, Quiescin Q6, Angiotensin, lipoprotein lipase, matrix metalloproteinase 2, and slit homologue 3. |
| 647 | 18286426 | Studies have demonstrated MSCs transplantation can prevent apoptosis of ischemic heart via upregulation of Akt and eNOS and inhibit myocardial fibrosis of dilated cardiomyopathy by decreasing the expression of matrix metalloproteinase (MMP) in rat models. |
| 648 | 18286426 | Using independent experimental approaches, we showed that MSCs presented in the myocardium 4 weeks after transplantation and some of them were positive for the cardiac markers Troponin T and myosin heavy chain. |
| 649 | 18286426 | Furthermore, MSCs transplantation increased MMP-2 activity and decreased transcriptional level of MMP-9. |
| 650 | 18355769 | Circulating matrix metalloproteinase-2 is associated with cystatin C level, posttransplant duration, and diabetes mellitus in kidney transplant recipients. |
| 651 | 18355769 | Univariate and stepwise regression analysis demonstrated the MMP-2 level was associated with cystatin C level (P < 0.001), creatinine level (P = 0.036), proteinuria (P = 0.043), posttransplant days (P = 0.025), and posttransplant diabetes mellitus (P = 0.03). |
| 652 | 18355769 | We conclude that circulating MMP-2 is associated with cystatin C, posttransplant duration, and diabetes mellitus in kidney transplant recipients and suggest that MMP-2 may be critical for graft survival. |
| 653 | 18355769 | Circulating matrix metalloproteinase-2 is associated with cystatin C level, posttransplant duration, and diabetes mellitus in kidney transplant recipients. |
| 654 | 18355769 | Univariate and stepwise regression analysis demonstrated the MMP-2 level was associated with cystatin C level (P < 0.001), creatinine level (P = 0.036), proteinuria (P = 0.043), posttransplant days (P = 0.025), and posttransplant diabetes mellitus (P = 0.03). |
| 655 | 18355769 | We conclude that circulating MMP-2 is associated with cystatin C, posttransplant duration, and diabetes mellitus in kidney transplant recipients and suggest that MMP-2 may be critical for graft survival. |
| 656 | 18355769 | Circulating matrix metalloproteinase-2 is associated with cystatin C level, posttransplant duration, and diabetes mellitus in kidney transplant recipients. |
| 657 | 18355769 | Univariate and stepwise regression analysis demonstrated the MMP-2 level was associated with cystatin C level (P < 0.001), creatinine level (P = 0.036), proteinuria (P = 0.043), posttransplant days (P = 0.025), and posttransplant diabetes mellitus (P = 0.03). |
| 658 | 18355769 | We conclude that circulating MMP-2 is associated with cystatin C, posttransplant duration, and diabetes mellitus in kidney transplant recipients and suggest that MMP-2 may be critical for graft survival. |
| 659 | 18363935 | Neprilysin and insulin-degrading enzyme (IDE), which have been most extensively studied, are expressed both neuronally and within the vasculature. |
| 660 | 18363935 | Other enzymes shown capable of degrading Abetain vitro or in animal studies include plasmin; endothelin-converting enzymes ECE-1 and -2; matrix metalloproteinases MMP-2, -3 and -9; and angiotensin-converting enzyme (ACE). |
| 661 | 18363935 | The levels of plasmin and plasminogen activators (uPA and tPA) and ECE-2 are reported to be reduced in AD. |
| 662 | 18363935 | Reductions in neprilysin, IDE and plasmin in AD have been associated with possession of APOEepsilon4. |
| 663 | 18363935 | The level and activity of ACE are increased, the level being directly related to Abeta plaque load. |
| 664 | 18413675 | The mRNA expressions for peroxisome proliferator-activated receptor-alpha, genes for triacylglycerol synthesis, and lipoprotein lipase were increased with diabetes in Wt hearts, whereas this induction was absent in Tg hearts. |
| 665 | 18413675 | However, Tg hearts displayed no overt fibrosis, concomitant with decreased expression of collagens, transforming growth factor-beta, and matrix metalloproteinase 2. |
| 666 | 18552985 | Genetic variations and plasma levels of gelatinase A (matrix metalloproteinase-2) and gelatinase B (matrix metalloproteinase-9) in proliferative diabetic retinopathy. |
| 667 | 18580857 | Megsin potentially inhibits total enzymatic activities of MMP-2 and -9 and plasmin, indicating decreased degradation of mesangial matrix. |
| 668 | 18619973 | As we have recently shown, expression and activity of the matrix degrading cysteine protease cathepsin L in EPC is required for tissue invasion and EPC-mediated improvement of neovascularization. |
| 669 | 18619973 | In contrast, other proteases of the cathepsin family such as cathepsins D and O, and the matrix metalloproteinases MMP-2 and MMP-9 were not altered with high glucose. |
| 670 | 18661413 | Serum neutrophil gelatinase-associated lipocalin as a marker of renal function in non-diabetic patients with stage 2-4 chronic kidney disease. |
| 671 | 18661413 | Serum and urinary NGAL as well as serum cystatin C were measured using commercially available kits. |
| 672 | 18661413 | Serum NGAL was related, in univariate analysis, to serum creatinine, urinary NGAL, hemoglobin, hematocrit, leukocyte count, eGFR, and cystatin C. |
| 673 | 18661413 | Urinary NGAL correlated with age, hemoglobin, hematocrit, serum creatinine, and eGFR. |
| 674 | 18661413 | In multiple regression analysis, predictors of serum NGAL were creatinine (beta value = 0.97, p = 0.005), cystatin C (beta = 0.34, p = 0.01), and eGFR (beta value = 1.77, p = 0.001). |
| 675 | 18661413 | In the healthy volunteers, serum NGAL correlated with age, serum creatinine, eGFR, leukocyte count, and cystatin C. |
| 676 | 18663625 | The authors hypothesized that MMP-2 and MMP-9 levels might be abnormal in obesity, reflecting alterations in extracellular matrix (ECM) turnover. |
| 677 | 18663625 | The following were measured: body mass index (BMI), waist circumference (WC), fasting plasma glucose (FPG), fasting plasma insulin (FPI), homeostasis model assessment (HOMA) index, systolic blood pressure (SBP), diastolic blood pressure (DBP), total cholesterol (TC), low-density lipoprotein cholesterol (LDL-C), high-density lipoprotein cholesterol (HDL-C), triglycerides (Tg), lipoprotein(a) (Lp(a)), and plasma levels of MMP-2 and MMP-9. |
| 678 | 18663625 | MMP-2 and MMP-9 levels were significantly higher in obese group (p< .0001). |
| 679 | 18663625 | Plasma levels of MMP-2 and MMP-9 are increased in obese patients which may reflect abnormal ECM metabolism. |
| 680 | 18663625 | The authors hypothesized that MMP-2 and MMP-9 levels might be abnormal in obesity, reflecting alterations in extracellular matrix (ECM) turnover. |
| 681 | 18663625 | The following were measured: body mass index (BMI), waist circumference (WC), fasting plasma glucose (FPG), fasting plasma insulin (FPI), homeostasis model assessment (HOMA) index, systolic blood pressure (SBP), diastolic blood pressure (DBP), total cholesterol (TC), low-density lipoprotein cholesterol (LDL-C), high-density lipoprotein cholesterol (HDL-C), triglycerides (Tg), lipoprotein(a) (Lp(a)), and plasma levels of MMP-2 and MMP-9. |
| 682 | 18663625 | MMP-2 and MMP-9 levels were significantly higher in obese group (p< .0001). |
| 683 | 18663625 | Plasma levels of MMP-2 and MMP-9 are increased in obese patients which may reflect abnormal ECM metabolism. |
| 684 | 18663625 | The authors hypothesized that MMP-2 and MMP-9 levels might be abnormal in obesity, reflecting alterations in extracellular matrix (ECM) turnover. |
| 685 | 18663625 | The following were measured: body mass index (BMI), waist circumference (WC), fasting plasma glucose (FPG), fasting plasma insulin (FPI), homeostasis model assessment (HOMA) index, systolic blood pressure (SBP), diastolic blood pressure (DBP), total cholesterol (TC), low-density lipoprotein cholesterol (LDL-C), high-density lipoprotein cholesterol (HDL-C), triglycerides (Tg), lipoprotein(a) (Lp(a)), and plasma levels of MMP-2 and MMP-9. |
| 686 | 18663625 | MMP-2 and MMP-9 levels were significantly higher in obese group (p< .0001). |
| 687 | 18663625 | Plasma levels of MMP-2 and MMP-9 are increased in obese patients which may reflect abnormal ECM metabolism. |
| 688 | 18663625 | The authors hypothesized that MMP-2 and MMP-9 levels might be abnormal in obesity, reflecting alterations in extracellular matrix (ECM) turnover. |
| 689 | 18663625 | The following were measured: body mass index (BMI), waist circumference (WC), fasting plasma glucose (FPG), fasting plasma insulin (FPI), homeostasis model assessment (HOMA) index, systolic blood pressure (SBP), diastolic blood pressure (DBP), total cholesterol (TC), low-density lipoprotein cholesterol (LDL-C), high-density lipoprotein cholesterol (HDL-C), triglycerides (Tg), lipoprotein(a) (Lp(a)), and plasma levels of MMP-2 and MMP-9. |
| 690 | 18663625 | MMP-2 and MMP-9 levels were significantly higher in obese group (p< .0001). |
| 691 | 18663625 | Plasma levels of MMP-2 and MMP-9 are increased in obese patients which may reflect abnormal ECM metabolism. |
| 692 | 18688800 | Pretreatment with ABO decreased high glucose-induced increase of MMP-2/-9 activities in a dose-dependent manner. |
| 693 | 18688800 | Real time qRT-PCR revealed that high glucose-induced MMP-2/-9 mRNA expression levels were attenuated by pretreatment with ABO. |
| 694 | 18688800 | High glucose-induced MCP-1 and IL-8 mRNA expression levels also decreased by ABO. |
| 695 | 18688800 | Pretreatment with ABO decreased high glucose-induced increase of MMP-2/-9 activities in a dose-dependent manner. |
| 696 | 18688800 | Real time qRT-PCR revealed that high glucose-induced MMP-2/-9 mRNA expression levels were attenuated by pretreatment with ABO. |
| 697 | 18688800 | High glucose-induced MCP-1 and IL-8 mRNA expression levels also decreased by ABO. |
| 698 | 18772236 | Aldose reductase regulates high glucose-induced ectodomain shedding of tumor necrosis factor (TNF)-alpha via protein kinase C-delta and TNF-alpha converting enzyme in vascular smooth muscle cells. |
| 699 | 18772236 | This decrease in unprocessed TNF-alpha was prevented by the aldose reductase (AR) inhibitor sorbinil and AR small interference RNA. |
| 700 | 18772236 | Treatment with HG, but not equimolar mannitol or 3-O-methyl glucose, resulted in phosphorylation and activation of TNF-alpha converting enzyme (TACE) (ADAM17), which were attenuated by sorbinil or AR-specific small interference RNA. |
| 701 | 18772236 | HG-induced TACE phosphorylation and TNF-alpha processing were also prevented by TNF-alpha protease inhibitor-1, an inhibitor of TACE. |
| 702 | 18772236 | Inhibition of protein kinase C (PKC)-delta by rottlerin prevented HG-induced TACE activation and the accumulation of unprocessed TNF-alpha. |
| 703 | 18772236 | Sorbinil treatment also decreased the expression of TNF-alpha, matrix metalloproteinase-2, matrix metalloproteinase-9, and increased tissue inhibitor of metalloproteinase-3 in vascular smooth muscle cells treated with HG and in balloon-injured carotid arteries of diabetic rats. |
| 704 | 18772236 | These results indicate that HG-induced TNF-alpha shedding could be attributed to TACE activation, which is regulated, in part, by PKC-delta and AR. |
| 705 | 18772236 | Therefore, inhibition of TACE by TNF-alpha protease inhibitor-1, or pharmacological inhibition of PKC-delta or AR may represent useful strategies for treating vascular inflammation associated with diabetes. |
| 706 | 18772849 | Of the MMPs, MMP-2 and MMP-9 are especially active in the degradation of type IV collagen, the main constituent of the basement membrane. |
| 707 | 18772849 | MMP-9 has the ability to degrade insulin and is able to activate IL-8, the main chemoattractant factor for neutrophils and monocytes. |
| 708 | 18780770 | Glomerular MMP-2 and MMP-9 activities as well as TIMP-1 expression were increased robustly in diabetic mice and normalized with CZ treatment. |
| 709 | 18780770 | Interestingly, TIMP-4 expression was opposite to that of TIMP-1 in diabetic and CZ-treated groups. |
| 710 | 18930722 | MMP-2 levels were determined by gelatin zymography, and MMP-2/tissue inhibitor of metalloproteinases (TIMP)-2 mRNA levels were determined by quantitative real time RT-PCR. |
| 711 | 18930722 | While diabetes induced no major structural changes, it caused a 16-fold increase in the ratio of MMP-2/TIMP-2 mRNA expression, which was completely reversed by lercanidipine (both P<0.001). |
| 712 | 18930722 | These results show that antioxidant and beneficial vascular effects produced by lercanidipine in diabetic rats are associated with reversion of the imbalance in vascular MMP-2/TIMP-2 expression. |
| 713 | 18930722 | MMP-2 levels were determined by gelatin zymography, and MMP-2/tissue inhibitor of metalloproteinases (TIMP)-2 mRNA levels were determined by quantitative real time RT-PCR. |
| 714 | 18930722 | While diabetes induced no major structural changes, it caused a 16-fold increase in the ratio of MMP-2/TIMP-2 mRNA expression, which was completely reversed by lercanidipine (both P<0.001). |
| 715 | 18930722 | These results show that antioxidant and beneficial vascular effects produced by lercanidipine in diabetic rats are associated with reversion of the imbalance in vascular MMP-2/TIMP-2 expression. |
| 716 | 18930722 | MMP-2 levels were determined by gelatin zymography, and MMP-2/tissue inhibitor of metalloproteinases (TIMP)-2 mRNA levels were determined by quantitative real time RT-PCR. |
| 717 | 18930722 | While diabetes induced no major structural changes, it caused a 16-fold increase in the ratio of MMP-2/TIMP-2 mRNA expression, which was completely reversed by lercanidipine (both P<0.001). |
| 718 | 18930722 | These results show that antioxidant and beneficial vascular effects produced by lercanidipine in diabetic rats are associated with reversion of the imbalance in vascular MMP-2/TIMP-2 expression. |
| 719 | 18940384 | Plasma activity of MMP-2 and MMP-9, high-sensitivity C-reactive protein concentration, dense low-density lipoprotein, and insulin-resistance markers were measured in 38 nondiabetic women with (n = 19) and without (n = 19) MetS. |
| 720 | 18940384 | MMP-2 activity positively correlated with waist, homeostasis model assessment, and high-sensitivity C-reactive protein (P < .02) as well as with apolipoprotein B, dense low-density lipoprotein, triglycerides/high-density lipoprotein cholesterol index (P < .001) and negatively with high-density lipoprotein cholesterol (P < .002). |
| 721 | 19003945 | In the presence of high glucose, the levels of matrix metalloproteinase-2 (MMP-2), matrix metalloproteinase-9 (MMP-9) and extracellular matrix metalloproteinase inducer (EMMPRIN) were decreased significantly, and the levels of tissue inhibitor of metalloproteinase-2 (TIMP-2), tissue inhibitor of metalloproteinase-1 (TIMP-1) and plasminogen activator inhibitor-1 (PAI-1) were increased significantly. |
| 722 | 19003945 | GbE lowered the levels of transforming growth factor-beta(1) (TGF-beta(1)), insulin-like growth factor-1 (IGF-1) and connective tissue growth factor (CTGF) of the high glucose group. |
| 723 | 19003945 | Furthermore, GbE also decreased the expressions of collagen IV and laminin of the high glucose group. |
| 724 | 19062310 | Plasma levels of MMP-2, MMP-9 and TIMP-1 are not associated with arterial stiffness in subjects with type 2 diabetes mellitus. |
| 725 | 19074676 | Expression of angiostatin, endostatin, their precursors (plasminogen and collagen XVIII, respectively), enzymes leading to their production [matrix metalloprotease (MMP)-2 and -9, cathepsin L], and an inhibitor of MMPs (tissue inhibitor of metalloproteinase) was assessed with Western blotting. |
| 726 | 19074676 | Plasminogen and collagen XVIII expression were similar between groups. |
| 727 | 19074676 | MMP-9 expression was no different between groups, whereas MMP-2 expression decreased 1.8-fold in diabetics (P = 0.003). |
| 728 | 19074676 | MMP-2 and -9 activity decreased 1.33-fold (P = 0.03) and 1.57-fold (P = 0.04), respectively, in diabetic patients. |
| 729 | 19074676 | Myocardial endostatin expression correlated strongly with the percentage of hemoglobin A(1c) (r = 0.742, P = 0.0001). |
| 730 | 19074676 | Expression of angiostatin, endostatin, their precursors (plasminogen and collagen XVIII, respectively), enzymes leading to their production [matrix metalloprotease (MMP)-2 and -9, cathepsin L], and an inhibitor of MMPs (tissue inhibitor of metalloproteinase) was assessed with Western blotting. |
| 731 | 19074676 | Plasminogen and collagen XVIII expression were similar between groups. |
| 732 | 19074676 | MMP-9 expression was no different between groups, whereas MMP-2 expression decreased 1.8-fold in diabetics (P = 0.003). |
| 733 | 19074676 | MMP-2 and -9 activity decreased 1.33-fold (P = 0.03) and 1.57-fold (P = 0.04), respectively, in diabetic patients. |
| 734 | 19074676 | Myocardial endostatin expression correlated strongly with the percentage of hemoglobin A(1c) (r = 0.742, P = 0.0001). |
| 735 | 19148153 | Urinary neutrophil gelatinase-associated lipocalin levels reflect damage to glomeruli, proximal tubules, and distal nephrons. |
| 736 | 19148153 | Urinary neutrophil gelatinase-associated lipocalin (Ngal or lipocalin 2) is a very early and sensitive biomarker of kidney injury. |
| 737 | 19148153 | Urinary neutrophil gelatinase-associated lipocalin levels reflect damage to glomeruli, proximal tubules, and distal nephrons. |
| 738 | 19148153 | Urinary neutrophil gelatinase-associated lipocalin (Ngal or lipocalin 2) is a very early and sensitive biomarker of kidney injury. |
| 739 | 19230716 | After APS/NS administration at a dose of 1 g/kg per day for 10 weeks, hemodynamic parameters, levels of insulin (INS), C-peptide (C-P), glycosylated serum protein (GSP), lipoproteins, myocardial enzymes, and Ang II (plasma and myocardial) were tested; myocardial collagen (type I and III), myocardial ultrastructure, and activities of matrix metalloproteinase (MMPs) were measured; activities and expression of cardiac chymase and ACE were detected by using quantitative real-time RT-PCR and RIA; protein expression of cardiac phosphoric extracellular signal-regulated kinase 1/2 (p-ERK1/2) was measured by Western blot. |
| 740 | 19230716 | AP-administrated diabetic hamsters had lower levels of GSP, lipoproteins, myocardial enzymes, myocardial Ang II, expression of collagen I and I/ III, activities of pro-MMP-2 and MMP-2, activities and expression of chymase, and expression of p-ERK1/2 than NS-administrated diabetic hamsters and could better protect the myocardial ultrastructure. |
| 741 | 19321980 | Neutrophil gelatinase-associated lipocalin as an early biomarker of nephropathy in diabetic patients. |
| 742 | 19345729 | The effects of mitochondrial superoxide scavenger on glucose-induced alterations in MMP-2, and its proenzyme activator MT1-MMP and physiological inhibitor TIMP-2, were determined in retinal endothelial cells, and the regulation of their glucose-induced accelerated apoptosis by the inhibitors of MMP-2 was accessed. |
| 743 | 19345729 | To confirm in vitro results, the effects of antioxidant supplementation on MMP-2, MT1-MMP, and TIMP-2 were investigated in the retina of streptozotocin-induced diabetic rats. |
| 744 | 19345729 | Glucose-induced activation of retinal capillary cell MMP-2 and MT1-MMP and decrease in TIMP-2 were inhibited by superoxide scavengers, and their accelerated apoptosis was prevented by the inhibitors of MMP-2. |
| 745 | 19345729 | The effects of mitochondrial superoxide scavenger on glucose-induced alterations in MMP-2, and its proenzyme activator MT1-MMP and physiological inhibitor TIMP-2, were determined in retinal endothelial cells, and the regulation of their glucose-induced accelerated apoptosis by the inhibitors of MMP-2 was accessed. |
| 746 | 19345729 | To confirm in vitro results, the effects of antioxidant supplementation on MMP-2, MT1-MMP, and TIMP-2 were investigated in the retina of streptozotocin-induced diabetic rats. |
| 747 | 19345729 | Glucose-induced activation of retinal capillary cell MMP-2 and MT1-MMP and decrease in TIMP-2 were inhibited by superoxide scavengers, and their accelerated apoptosis was prevented by the inhibitors of MMP-2. |
| 748 | 19345729 | The effects of mitochondrial superoxide scavenger on glucose-induced alterations in MMP-2, and its proenzyme activator MT1-MMP and physiological inhibitor TIMP-2, were determined in retinal endothelial cells, and the regulation of their glucose-induced accelerated apoptosis by the inhibitors of MMP-2 was accessed. |
| 749 | 19345729 | To confirm in vitro results, the effects of antioxidant supplementation on MMP-2, MT1-MMP, and TIMP-2 were investigated in the retina of streptozotocin-induced diabetic rats. |
| 750 | 19345729 | Glucose-induced activation of retinal capillary cell MMP-2 and MT1-MMP and decrease in TIMP-2 were inhibited by superoxide scavengers, and their accelerated apoptosis was prevented by the inhibitors of MMP-2. |
| 751 | 19350199 | In this study, we investigated the effects of APS treatment on cardiac function, myocardial collagen expression, cardiac ultrastructure, cardiac matrix metalloproteinase (MMP) activity, levels of plasma glycosylated serum protein (GSP), and myocardial enzymes, and the expression of Ang II, chymase, and angiotensin-converting enzyme (ACE) in the diabetic hamster myocardium. |
| 752 | 19350199 | Compared with insulin treatment, APS treatment significantly reduced myocardial collagen (type I and III) expression and lowered cardiac MMP-2 activity, myocardial Ang II levels, myocardial chymase expression, and p-ERK1/2 kinase expression. |
| 753 | 19350199 | In diabetic hamsters, myocardial ACE expression and plasma Ang II levels was not altered by insulin or APS treatment. |
| 754 | 19360430 | Based on our results, we suggest that the MMP-2 located in the psoriasis susceptibility region on 16q (psoriasis susceptibility 8, PSORS8) should be considered as a gene modulator of psoriasis in specific subgroups of patients. |
| 755 | 19390997 | Changes of serum and urine neutrophil gelatinase-associated lipocalin in type-2 diabetic patients with nephropathy: one year observational follow-up study. |
| 756 | 19390997 | We initiated the present work to explore whether neutrophil gelatinase-associated lipocalin (NGAL) could be used to predict the progression of diabetic nephropathy in type-2 diabetic patients. |
| 757 | 19390997 | Moreover, urine NGAL was found to be correlated positively with cystatin C, urea nitrogen, and serum creatinine (SCr), and inversely with glomerular filtration rate (GFR), while serum NGAL correlated negatively with cystatin C and urea nitrogen, at both baseline and follow-up levels. |
| 758 | 19390997 | Changes of serum and urine neutrophil gelatinase-associated lipocalin in type-2 diabetic patients with nephropathy: one year observational follow-up study. |
| 759 | 19390997 | We initiated the present work to explore whether neutrophil gelatinase-associated lipocalin (NGAL) could be used to predict the progression of diabetic nephropathy in type-2 diabetic patients. |
| 760 | 19390997 | Moreover, urine NGAL was found to be correlated positively with cystatin C, urea nitrogen, and serum creatinine (SCr), and inversely with glomerular filtration rate (GFR), while serum NGAL correlated negatively with cystatin C and urea nitrogen, at both baseline and follow-up levels. |
| 761 | 19406980 | TIMP3 is the most highly expressed tissue inhibitor of metalloproteinase (TIMP) in the kidney, but its function in renal disease is incompletely understood. |
| 762 | 19406980 | In addition, TIMP3-/- mice had greater interstitial fibrosis; increased synthesis and deposition of type I collagen; increased activation of fibroblasts; enhanced apoptosis; and greater activation of MMP2, but not MMP9, after UUO. |
| 763 | 19406980 | TIMP3 deficiency also led to accelerated processing of TNFalpha, demonstrated by significantly higher TACE activity and greater soluble TNFalpha levels by 3 d after UUO. |
| 764 | 19406980 | Moreover, inhibition of MMPs in TIMP3-/-/TNFalpha-/- mice further abrogated postobstructive injury and prevented tubulointerestitial fibrosis. |
| 765 | 19474274 | Reduction in urinary excretion of neutrophil gelatinase-associated lipocalin by angiotensin receptor blockers in hypertensive patients. |
| 766 | 19505525 | Our results also showed that exposure of macrophages to U-PM caused an increase in cytokine mRNA expression level and activity of matrix metalloproteinase 9 (MMP-9), but not MMP-2, and that these effects were greater in macrophages from DM rabbits. |
| 767 | 19506087 | Glomerular protein levels of matrix metalloproteinase-1 and tissue inhibitor of metalloproteinase-1 are lower in diabetic subjects. |
| 768 | 19506087 | We investigated protein levels of multiple MMPs (MMP-1, MMP-2, MMP-3, and MMP-9) and TIMP-1 in glomeruli and investigated whether disease phenotypes were associated with levels of these proteins. |
| 769 | 19506087 | We observed significantly decreased glomerular MMP-1 and TIMP-1 staining in subjects with diabetes, hypertension, and an estimated glomerular filtration rate <30 ml/min/1.73 m(2) in univariate analyses. |
| 770 | 19506087 | MMP-1 staining, but not TIMP-1 staining, was inversely correlated with increased glomerular fibrosis (r = -0.40). |
| 771 | 19506087 | This study indicates that in human subjects, the long-term sequelae of diseases such as diabetes that cause chronic renal failure result in decreased TIMP-1 and MMP-1 proteins in renal glomeruli. |
| 772 | 19526397 | Serum levels of matrix metalloproteinases MMP-2 and MMP-9 and their inhibitors in women with glucose intolerance in pregnancy and normal controls. |
| 773 | 19542742 | The mRNA of procollagen types I and III, and RLX-1 were assessed by real time PCR and procollagen type I C-terminal peptide (PICP) and procollagen type III amino terminal peptide (PIIINP), matrix metalloproteinases 2 (MMP2), MMP9 were assessed by enzyme linked immunosorbent assay. |
| 774 | 19542742 | The results are as follows: a) CF proliferation was significantly increased by HG; rhRLX significantly inhibited HG fibroblast proliferation, while it had no marked effect on CF proliferation in NG. b) CF treated with HG significantly increased the production of PICP and PIIINP. rhRLX had no marked effect on production of PICP and PIIINP in NG. rhRLX blocked the HG-induced increases in collagen synthesis. c) The production of MMP2 and MMP9 is significantly increased by HG. rhRLX decreased overproduction of MMP2 and MMP9 in the presence of HG. d) The RLX- 1 mRNA expression of HG group was higher than in the NG group. |
| 775 | 19542742 | The mRNA of procollagen types I and III, and RLX-1 were assessed by real time PCR and procollagen type I C-terminal peptide (PICP) and procollagen type III amino terminal peptide (PIIINP), matrix metalloproteinases 2 (MMP2), MMP9 were assessed by enzyme linked immunosorbent assay. |
| 776 | 19542742 | The results are as follows: a) CF proliferation was significantly increased by HG; rhRLX significantly inhibited HG fibroblast proliferation, while it had no marked effect on CF proliferation in NG. b) CF treated with HG significantly increased the production of PICP and PIIINP. rhRLX had no marked effect on production of PICP and PIIINP in NG. rhRLX blocked the HG-induced increases in collagen synthesis. c) The production of MMP2 and MMP9 is significantly increased by HG. rhRLX decreased overproduction of MMP2 and MMP9 in the presence of HG. d) The RLX- 1 mRNA expression of HG group was higher than in the NG group. |
| 777 | 19906504 | Height and body weight, BMI, glycemic and lipid profile, blood pressure, Nitrites/nitrates, ADP, resistin, MMP-2, and MMP-9 were evaluated at titration beginning, after 3, 6 months, and at the study end in 473 type 2 diabetic patients. |
| 778 | 20029543 | Biochemical data showed that this treatment significantly prevented important changes, such as inhibition of MMP-2 and MMP-9 activity, loss of tissue inhibitor of matrix metalloproteinase-4 (TIMP-4) protein, increase in tissue levels of thiol oxidation, endothelin-1, protein kinase C (PKC), and cAMP production, and decrease in tissue level of nitrite. |
| 779 | 20038211 | Analysis of culture supernatant and gene arrays indicated that ASCs formulated as three-dimensional aggregates produce significantly more extracellular matrix proteins (e.g., tenascin C, collagen VI alpha3, and fibronectin) and secreted soluble factors (e.g., hepatocyte growth factor, matrix metalloproteinase-2, and matrix metalloproteinase-14) compared to monolayer culture. |
| 780 | 20051380 | We show by semiquantitative RT-PCR and immunostaining over the time course from embryonic day 18/20 to birth, 1 day, 2 days, 3 days, 7 days, and adult that MMP-2, CK-19, and SPD are truly markers of new and immature beta-cells and that their expression transiently peaks in the perinatal period and is not entirely synchronous. |
| 781 | 20079360 | All patients underwent basal measurements of blood glucose (BG), nitrites/nitrates, adiponectin (ADP), matrix metalloproteinase-2 (MMP-2), and matrix metalloproteinase-9 (MMP-9) before and after OGTT. |
| 782 | 20096949 | TIMP-1 and collagen degradation products were also measured. |
| 783 | 20096949 | MMPs (-1, -3 and -7) and TIMP-1 were measured by ELISA, MMP-2 and -9 by zymography and collagen degradation products by radioimmunoassay. |
| 784 | 20096949 | Differences in the pattern of MMPs/TIMPs and collagen degradation products were observed. |
| 785 | 20146476 | Enhanced expression and secretion of connective tissue growth factor (CTGF) play an important role in the expansion of glomerular mesangial matrix mostly composed of type IV collagen. |
| 786 | 20146476 | The present study was to investigate whether nontoxic isoliquiritigenin inhibited high glucose (HG)-induced mesangial fibrosis by retarding formation of type IV collagen as well as CTGF in human mesangial cells (HRMC). |
| 787 | 20146476 | Exposure of cells to HG caused marked increases in collagen secretion and CTGF expression, which was dose-dependently reversed by isoliquiritigenin at the transcriptional levels. |
| 788 | 20146476 | Additionally, isoliquiritigenin boosted HG-plummeted type matrix metalloproteinase-1 (MT-1 MMP) expression and dampened HG-elevated tissue inhibitor of MMP-2 (TIMP-2) expression, facilitating the degradation of mesangial matrix. |
| 789 | 20146476 | Isoliquiritigenin inhibited HG-upregulated CTGF and TIMP-2 expression via disturbing TGF-beta1 signaling in HRMC, as evidenced by TGF-beta receptor I kinase (TGF-beta RI) inhibitor. |
| 790 | 20146476 | HG-activated SMAD2 through autocrine TGF-beta signaling was repealed by > or =10 microM isoliquiritigenin. |
| 791 | 20146476 | HG induced SMAD4 expression of HRMC and obliterated antagonistic SMAD7, whereas isoliquiritigenin suppressed induction of TGF-beta RII and TGF-beta RI with blunting their downstream SMAD signaling. |
| 792 | 20157738 | The aim of this study was to evaluate the level of neutrophil-gelatinase-associated lipocalin (NGAL) and interleukin (IL)-18 and their relations to albumin excretion rate (AER) in children with normal-range albuminuria, e.g. in those considered as not presenting diabetic nephropathy. |
| 793 | 20213226 | Enhanced production of matrix metalloproteinase-2 (MMP-2) and matrix metalloproteinase-9 (MMP-9) in diabetes leads to degradation of extracellular matrix in blood vessels and leads to complications of diabetes. |
| 794 | 20213226 | In the present study, we have targeted MMP-2 and MMP-9 overactivation in diabetic neuropathy using a known MMP-2 and MMP-9 inhibitor, minocycline, with a non-selective COX inhibitor, aspirin. |
| 795 | 20213226 | The results of the present study suggest that MMP-2 and MMP-9 inhibition in the presence of COX inhibitor prevents the development of experimental diabetic neuropathy in rats and can be a potential approach for the treatment. |
| 796 | 20213226 | Enhanced production of matrix metalloproteinase-2 (MMP-2) and matrix metalloproteinase-9 (MMP-9) in diabetes leads to degradation of extracellular matrix in blood vessels and leads to complications of diabetes. |
| 797 | 20213226 | In the present study, we have targeted MMP-2 and MMP-9 overactivation in diabetic neuropathy using a known MMP-2 and MMP-9 inhibitor, minocycline, with a non-selective COX inhibitor, aspirin. |
| 798 | 20213226 | The results of the present study suggest that MMP-2 and MMP-9 inhibition in the presence of COX inhibitor prevents the development of experimental diabetic neuropathy in rats and can be a potential approach for the treatment. |
| 799 | 20213226 | Enhanced production of matrix metalloproteinase-2 (MMP-2) and matrix metalloproteinase-9 (MMP-9) in diabetes leads to degradation of extracellular matrix in blood vessels and leads to complications of diabetes. |
| 800 | 20213226 | In the present study, we have targeted MMP-2 and MMP-9 overactivation in diabetic neuropathy using a known MMP-2 and MMP-9 inhibitor, minocycline, with a non-selective COX inhibitor, aspirin. |
| 801 | 20213226 | The results of the present study suggest that MMP-2 and MMP-9 inhibition in the presence of COX inhibitor prevents the development of experimental diabetic neuropathy in rats and can be a potential approach for the treatment. |
| 802 | 20348234 | PGIS nitration, nitric oxide synthases, adhesion molecules, myeloperoxidase, osteopontin, and matrix metalloproteinase (MMP) were measured by using immunohistochemistry and Western blotting. |
| 803 | 20348234 | In both diabetic and nondiabetic patients, MMP-2 and MMP-9 protein levels were significantly increased in the arteries with high stenosis as compared with those with low stenosis. |
| 804 | 20348234 | Moreover, diabetes enhanced inducible nitric oxide synthase expression in the plaques from low stenosis areas and up-regulated myeloperoxidase expression in the plaques from both high and low stenosis areas. |
| 805 | 20382513 | Roasted licorice extracts dampen high glucose-induced mesangial hyperplasia and matrix deposition through blocking Akt activation and TGF-beta signaling. |
| 806 | 20382513 | Exposure of cells to HG caused significant increases in collagen IV secretion and connective tissue growth factor (CTGF) expression, which was appeased by RLW and RLE at transcriptional levels. |
| 807 | 20382513 | In addition, RLW and RLE but not LW modulated membrane type matrix metalloproteinase-1 (MT-1 MMP) expression, MMP-2 activity and tissue inhibitor of MMP-2 (TIMP-2), which facilitated the degradation of mesangial matrix. |
| 808 | 20382513 | Furthermore, the augmented expression of CTGF and TIMP-2 in HG-exposed cells was mediated by Akt activation and TGF-beta/Smad signaling through PKCbeta2-responsive signaling pathways. |
| 809 | 20382513 | However, HG-down-regulated MT-1 MMP expression was independent of activation of ERK1/2 and Akt when using their inhibitors of DB98059 (ERK1/2) and LY294002 (Akt) alone or in combination. |
| 810 | 20407607 | Attenuation of diabetic retinopathy by enhanced inhibition of MMP-2 and MMP-9 using aspirin and minocycline in streptozotocin-diabetic rats. |
| 811 | 20407607 | Interruptions of Matrix Metalloproteinase-2 (MMP-2) and Matrix Metalloproteinase-9 (MMP-9) have been shown to reduce the ensuing threatening risk factors of vascular complications of diabetes by alteration in Extracellular Matrix (ECM). |
| 812 | 20407607 | We hypothesized that minocycline induced MMP-2 and MMP-9 inhibition can be enhanced by aspirin, a non-selective COX and tPA inhibitor and this combination can reduce progression of diabetic retinopathy. |
| 813 | 20407607 | Zymography was carried out for MMP-2 and MMP-9 level determinations. |
| 814 | 20407607 | Results of the present study suggest that MMP-2 and MMP-9 inhibition in presence of COX inhibitor prevents the development of experimental diabetic retinopathy in rats and can be a potential approach for the treatment. |
| 815 | 20407607 | Attenuation of diabetic retinopathy by enhanced inhibition of MMP-2 and MMP-9 using aspirin and minocycline in streptozotocin-diabetic rats. |
| 816 | 20407607 | Interruptions of Matrix Metalloproteinase-2 (MMP-2) and Matrix Metalloproteinase-9 (MMP-9) have been shown to reduce the ensuing threatening risk factors of vascular complications of diabetes by alteration in Extracellular Matrix (ECM). |
| 817 | 20407607 | We hypothesized that minocycline induced MMP-2 and MMP-9 inhibition can be enhanced by aspirin, a non-selective COX and tPA inhibitor and this combination can reduce progression of diabetic retinopathy. |
| 818 | 20407607 | Zymography was carried out for MMP-2 and MMP-9 level determinations. |
| 819 | 20407607 | Results of the present study suggest that MMP-2 and MMP-9 inhibition in presence of COX inhibitor prevents the development of experimental diabetic retinopathy in rats and can be a potential approach for the treatment. |
| 820 | 20407607 | Attenuation of diabetic retinopathy by enhanced inhibition of MMP-2 and MMP-9 using aspirin and minocycline in streptozotocin-diabetic rats. |
| 821 | 20407607 | Interruptions of Matrix Metalloproteinase-2 (MMP-2) and Matrix Metalloproteinase-9 (MMP-9) have been shown to reduce the ensuing threatening risk factors of vascular complications of diabetes by alteration in Extracellular Matrix (ECM). |
| 822 | 20407607 | We hypothesized that minocycline induced MMP-2 and MMP-9 inhibition can be enhanced by aspirin, a non-selective COX and tPA inhibitor and this combination can reduce progression of diabetic retinopathy. |
| 823 | 20407607 | Zymography was carried out for MMP-2 and MMP-9 level determinations. |
| 824 | 20407607 | Results of the present study suggest that MMP-2 and MMP-9 inhibition in presence of COX inhibitor prevents the development of experimental diabetic retinopathy in rats and can be a potential approach for the treatment. |
| 825 | 20407607 | Attenuation of diabetic retinopathy by enhanced inhibition of MMP-2 and MMP-9 using aspirin and minocycline in streptozotocin-diabetic rats. |
| 826 | 20407607 | Interruptions of Matrix Metalloproteinase-2 (MMP-2) and Matrix Metalloproteinase-9 (MMP-9) have been shown to reduce the ensuing threatening risk factors of vascular complications of diabetes by alteration in Extracellular Matrix (ECM). |
| 827 | 20407607 | We hypothesized that minocycline induced MMP-2 and MMP-9 inhibition can be enhanced by aspirin, a non-selective COX and tPA inhibitor and this combination can reduce progression of diabetic retinopathy. |
| 828 | 20407607 | Zymography was carried out for MMP-2 and MMP-9 level determinations. |
| 829 | 20407607 | Results of the present study suggest that MMP-2 and MMP-9 inhibition in presence of COX inhibitor prevents the development of experimental diabetic retinopathy in rats and can be a potential approach for the treatment. |
| 830 | 20407607 | Attenuation of diabetic retinopathy by enhanced inhibition of MMP-2 and MMP-9 using aspirin and minocycline in streptozotocin-diabetic rats. |
| 831 | 20407607 | Interruptions of Matrix Metalloproteinase-2 (MMP-2) and Matrix Metalloproteinase-9 (MMP-9) have been shown to reduce the ensuing threatening risk factors of vascular complications of diabetes by alteration in Extracellular Matrix (ECM). |
| 832 | 20407607 | We hypothesized that minocycline induced MMP-2 and MMP-9 inhibition can be enhanced by aspirin, a non-selective COX and tPA inhibitor and this combination can reduce progression of diabetic retinopathy. |
| 833 | 20407607 | Zymography was carried out for MMP-2 and MMP-9 level determinations. |
| 834 | 20407607 | Results of the present study suggest that MMP-2 and MMP-9 inhibition in presence of COX inhibitor prevents the development of experimental diabetic retinopathy in rats and can be a potential approach for the treatment. |
| 835 | 20425065 | Recent markers such as neutrophil gelatinase-associated lipocalin (NGAL), kidney injury molecule-1 (KIM-1), and podocin have garnered a lot of attention. |
| 836 | 20479714 | The effect of inhibiting diabetes-induced retinal superoxide accumulation on MMP2 and its regulators was investigated in diabetic mice overexpressing mitochondrial superoxide dismutase (MnSOD). |
| 837 | 20479714 | Inhibition of MMP2 ameliorated glucose-induced increase in mitochondrial superoxide and membrane permeability, prevented cytochrome c leakage from the mitochondria, and inhibited capillary cell apoptosis. |
| 838 | 20479714 | Overexpression of MnSOD protected the retina from diabetes-induced increase in MMP2 and its membrane activator (MT1-MMP), and decrease in its tissue inhibitor (TIMP-2). |
| 839 | 20479714 | The effect of inhibiting diabetes-induced retinal superoxide accumulation on MMP2 and its regulators was investigated in diabetic mice overexpressing mitochondrial superoxide dismutase (MnSOD). |
| 840 | 20479714 | Inhibition of MMP2 ameliorated glucose-induced increase in mitochondrial superoxide and membrane permeability, prevented cytochrome c leakage from the mitochondria, and inhibited capillary cell apoptosis. |
| 841 | 20479714 | Overexpression of MnSOD protected the retina from diabetes-induced increase in MMP2 and its membrane activator (MT1-MMP), and decrease in its tissue inhibitor (TIMP-2). |
| 842 | 20479714 | The effect of inhibiting diabetes-induced retinal superoxide accumulation on MMP2 and its regulators was investigated in diabetic mice overexpressing mitochondrial superoxide dismutase (MnSOD). |
| 843 | 20479714 | Inhibition of MMP2 ameliorated glucose-induced increase in mitochondrial superoxide and membrane permeability, prevented cytochrome c leakage from the mitochondria, and inhibited capillary cell apoptosis. |
| 844 | 20479714 | Overexpression of MnSOD protected the retina from diabetes-induced increase in MMP2 and its membrane activator (MT1-MMP), and decrease in its tissue inhibitor (TIMP-2). |
| 845 | 20620526 | Serum neutrophil gelatinase-associated lipocalin correlates with kidney function in heart allograft recipients. |
| 846 | 20620526 | The value of neutrophil gelatinase-associated lipocalin (NGAL) as a novel marker for early detection of acute renal failure has been highlighted recently. |
| 847 | 20620526 | On univariate analysis serum NGAL strongly correlated with serum creatinine (r = .70, P < .001), estimated GFR (CKD-EPI, r = -.57, P < .001, MDRD r = .56, P < .001, Cockcroft-Gault, r = -.56, P < .001), 24-hour creatinine clearance (r = .43, P < .001), and cystatin C (r = .74, P < .001). |
| 848 | 20620526 | In contrast, it was moderately correlated with red blood cell count (r = -.39, P < .01), hemoglobin level (r = -.42, P < .01), NT-proBNP (r = .25, P < .01), and only weakly with New York Heart Association class (r = .21, P < .05), time after transplantation (r = .21, P < .05), or age (r = .19, P < .05) upon multiple regression analysis, the best predictor of serum NGAL was estimated GFR (beta -0.87, P < .0001), explaining 89% of the NGAL concentrations. |
| 849 | 20620526 | Serum neutrophil gelatinase-associated lipocalin correlates with kidney function in heart allograft recipients. |
| 850 | 20620526 | The value of neutrophil gelatinase-associated lipocalin (NGAL) as a novel marker for early detection of acute renal failure has been highlighted recently. |
| 851 | 20620526 | On univariate analysis serum NGAL strongly correlated with serum creatinine (r = .70, P < .001), estimated GFR (CKD-EPI, r = -.57, P < .001, MDRD r = .56, P < .001, Cockcroft-Gault, r = -.56, P < .001), 24-hour creatinine clearance (r = .43, P < .001), and cystatin C (r = .74, P < .001). |
| 852 | 20620526 | In contrast, it was moderately correlated with red blood cell count (r = -.39, P < .01), hemoglobin level (r = -.42, P < .01), NT-proBNP (r = .25, P < .01), and only weakly with New York Heart Association class (r = .21, P < .05), time after transplantation (r = .21, P < .05), or age (r = .19, P < .05) upon multiple regression analysis, the best predictor of serum NGAL was estimated GFR (beta -0.87, P < .0001), explaining 89% of the NGAL concentrations. |
| 853 | 20726708 | Furthermore, low-dose radiation-induced improvement in healing was associated with increases in bone marrow and circulating CD31(+)/CD34(+) stem cells, vessel regeneration and cell proliferation in the wound tissue, and matrix metalloproteinase 2 and 9 expression. |
| 854 | 20810913 | Culture of THP-1 monocytes in the presence of AGEs or HG significantly increased CD147 at the gene and protein level. |
| 855 | 20810913 | Addition of AGEs or HG also increased expression of monocyte MMP-1 and MMP-9 but not MMP-2. |
| 856 | 20810913 | Inhibition of NF-κB or addition of antibodies to either TNF-α or the receptor for AGE (RAGE) each significantly prevented in a dose-dependent manner the induction of CD147 gene and protein by AGE and also decreased MMP-1 and MMP-9. |
| 857 | 20854382 | Neutrophil Gelatinase-Associated Lipocalin (NGAL) and Kidney Injury Molecule 1 (KIM1) in patients with diabetic nephropathy: a cross-sectional study and the effects of lisinopril. |
| 858 | 21102505 | Novel genes that were altered at both 1 and 2 weeks of high-glucose exposure included neutrophil gelatinase-associated lipocalin (LCN2 or NGAL, decreased by 3.2-fold at 1 week and by 7.2-fold at 2 weeks), endothelial lipase (EL, increased by 3.6-fold at 1 week and 3.9-fold at 2 week) and UDP-glucuronosyltransferase 8 (UGT8, increased by 3.9-fold at 1 week and 5.0-fold at 2 weeks). |
| 859 | 21102505 | A more detailed time course revealed changes in LCN2 and EL mRNA levels as early as 6 hours and in UGT8 mRNA level at 12 hours post high-glucose exposure. |
| 860 | 21160226 | Urinary neutrophil gelatinase-associated lipocalin and progression of diabetic nephropathy in type 1 diabetic patients in a four-year follow-up study. |
| 861 | 21219209 | Degradation of extracellular matrix (ECM) by enhanced production of matrix metalloproteinase-2 (MMP-2) and matrix metalloproteinase-9 (MMP-9) in diabetes leads to nephropathy. |
| 862 | 21219209 | The objective of present study was to inhibit MMP-2 and MMP-9 by combination of minocycline and aspirin to treat diabetic nephropathy. |
| 863 | 21219209 | Results of present study suggest that MMP-2 and MMP-9 inhibition in presence of COX inhibitor prevents the development of experimental diabetic nephropathy in rats and can be a potential approach for the treatment. |
| 864 | 21219209 | Degradation of extracellular matrix (ECM) by enhanced production of matrix metalloproteinase-2 (MMP-2) and matrix metalloproteinase-9 (MMP-9) in diabetes leads to nephropathy. |
| 865 | 21219209 | The objective of present study was to inhibit MMP-2 and MMP-9 by combination of minocycline and aspirin to treat diabetic nephropathy. |
| 866 | 21219209 | Results of present study suggest that MMP-2 and MMP-9 inhibition in presence of COX inhibitor prevents the development of experimental diabetic nephropathy in rats and can be a potential approach for the treatment. |
| 867 | 21219209 | Degradation of extracellular matrix (ECM) by enhanced production of matrix metalloproteinase-2 (MMP-2) and matrix metalloproteinase-9 (MMP-9) in diabetes leads to nephropathy. |
| 868 | 21219209 | The objective of present study was to inhibit MMP-2 and MMP-9 by combination of minocycline and aspirin to treat diabetic nephropathy. |
| 869 | 21219209 | Results of present study suggest that MMP-2 and MMP-9 inhibition in presence of COX inhibitor prevents the development of experimental diabetic nephropathy in rats and can be a potential approach for the treatment. |
| 870 | 21264951 | The number of microglia time dependently increased at demyelinative lesion sites, proliferated, and expressed tumor necrosis factor (TNF)-α, interleukin (IL)-1β, IL-6, inducible nitric oxide synthase, and MMP2, 9, and 12 at the early phase. |
| 871 | 21264951 | The number of astrocytes time dependently increased around demyelinative lesions, extended processes to lesions, proliferated, and expressed nerve growth factor and glial cell line-derived neurotrophic factor at the late phase. |
| 872 | 21270761 | To examine whether markers of tubular damage are useful in monitoring the progression of disease, we measured urinary levels of neutrophil gelatinase-associated lipocalin (NGAL), liver-fatty acid-binding protein (LFABP), and kidney injury molecule-1 (KIM-1) in a 3-year intervention study of 63 type 1 diabetic patients with kidney disease. |
| 873 | 21270761 | Patients with the highest compared with the lowest quartile of urinary NGAL at baseline had higher urinary KIM-1 levels and a significant decrease in their GFR each year. |
| 874 | 21270761 | Using linear regression analysis, we found that elevated urinary NGAL and KIM-1 concentrations were associated with a faster decline in GFR, but not after adjustment for known promoters of progression. |
| 875 | 21311195 | Neutrophil gelatinase-associated lipocalin as a predictor of complications and mortality in patients undergoing non-cardiac major surgery. |
| 876 | 21360312 | Increased membrane protein level of caveolin-1, elevated ratio of PKC in particulate and cytosolic fraction, and increased protein level of cytosolic endothelin-1 in diabetic rats were also significantly prevented with doxycycline treatment. |
| 877 | 21360312 | Moreover, diabetes-induced another type of oxidative stress markers in rats, matrix metalloproteinases, MMP-2, and MMP-9 were also normalized with doxycycline treatment in blood. |
| 878 | 21389974 | Hematopoietic growth factor inducible neurokinin-1 (Gpnmb/Osteoactivin) is a biomarker of progressive renal injury across species. |
| 879 | 21389974 | We sought to find a urinary biomarker for chronic kidney disease and tested hematopoietic growth factor inducible neurokinin-1 (HGFIN, also known as Gpnmb/Osteoactivin) as it was found to be a kidney injury biomarker in microarray studies. |
| 880 | 21389974 | The urine HGFIN-to-creatinine ratio compared favorably with the urine neutrophil gelatinase-associated lipocalin (NGAL)-to-creatinine ratio (both measured by commercial enzyme-linked immunosorbent assays (ELISAs)), and correlated strongly with proteinuria, but weakly with estimated glomerular filtration rate and serum creatinine. |
| 881 | 21478477 | Cation-independent mannose 6-phosphate receptor inhibitor (PXS25) inhibits fibrosis in human proximal tubular cells by inhibiting conversion of latent to active TGF-beta1. |
| 882 | 21478477 | Cellular fibronectin, collagen IV, and matrix metalloproteinase-2 (MMP-2) and MMP-9 were assessed. |
| 883 | 21478477 | Hyperglycemia induced fibronectin and collagen IV production (P < 0.05), as did hypoxia, but only hyperglycemia-induced increases in matrix proteins were suppressed by concurrent PXS25 exposure. |
| 884 | 21478477 | High glucose induced MMP-2 and -9 in normoxic and hypoxic conditions, which was not modified in the presence of PXS25. |
| 885 | 21478477 | Cation-independent mannose 6-phosphate receptor inhibitor (PXS25) inhibits fibrosis in human proximal tubular cells by inhibiting conversion of latent to active TGF-beta1. |
| 886 | 21478477 | Cellular fibronectin, collagen IV, and matrix metalloproteinase-2 (MMP-2) and MMP-9 were assessed. |
| 887 | 21478477 | Hyperglycemia induced fibronectin and collagen IV production (P < 0.05), as did hypoxia, but only hyperglycemia-induced increases in matrix proteins were suppressed by concurrent PXS25 exposure. |
| 888 | 21478477 | High glucose induced MMP-2 and -9 in normoxic and hypoxic conditions, which was not modified in the presence of PXS25. |
| 889 | 21547674 | LEJ showed potent inhibitory effects on MMP-2 and MMP-9 activities and expressions via down-regulation of NF-κB translocation to the nucleus in B16F10 cells. |
| 890 | 21547674 | Moreover, we isolated the compounds ursolic acid and 2α-hydroxyursolic acid from LEJ and both compounds also significantly suppressed MMP-2 and MMP-9 activities, indicating that they are the active components of LEJ. |
| 891 | 21547674 | LEJ showed potent inhibitory effects on MMP-2 and MMP-9 activities and expressions via down-regulation of NF-κB translocation to the nucleus in B16F10 cells. |
| 892 | 21547674 | Moreover, we isolated the compounds ursolic acid and 2α-hydroxyursolic acid from LEJ and both compounds also significantly suppressed MMP-2 and MMP-9 activities, indicating that they are the active components of LEJ. |
| 893 | 21670771 | Elevated levels of neutrophil gelatinase-associated lipocalin in bile from patients with malignant pancreatobiliary disease. |
| 894 | 21779943 | Tubular markers, such as neutrophil gelatinase-associated lipocalin (NGAL), N-acetyl-β-D: -glucosaminidase (NAG), and kidney injury molecule 1 (KIM-1), as well as urinary albumin excretion were measured in voided urine. |
| 895 | 21779943 | Compared with the control group, Urinary NGAL [median (IQR)][83.6(41.4-138.7) μg/gcr vs. 32.9(26.1-64.5) μg/gcr], NAG [13.5(8.7-17.9) U/gcr vs. 7.6(6.5-13.0) U/gcr] and KIM-1 [120.0(98.4-139.9) ng/gcr vs. 103.1(86.8-106.2) ng/gcr] in the T2DM were all markedly increased. |
| 896 | 21805479 | Diabetic HDL, glycated HDL and oxidized HDL also induced higher synthesis and secretion of VEGF-C, MMP-2 and MMP-9 from malondialdehyde (MDA)-MB-231 cells. |
| 897 | 21805479 | It was indicated that diabetic, glycated and oxidized HDL promote MDA-MB-231 cell migration and invasion through ERK and p38 MAPK pathways, and Akt pathway plays an important role as well in MDA-MB-231 cell invasion. |
| 898 | 21805479 | The Akt, ERK and p38 MAPK pathways are also involved in VEGF-C and MMP-9 secretion induced by diabetic, glycated and oxidized HDL. |
| 899 | 21872946 | Prognostic value of neutrophil gelatinase-associated lipocalin in acute heart failure. |
| 900 | 21904663 | The percentage change in neutrophil gelatinase-associated lipocalin (NGAL), a protein whose expression is increased with renal ischemia, was then used to determine the extent of injury. |
| 901 | 21918531 | We measured the circulating MMP-2, MMP-9, TIMP-1 and TIMP-2 levels in ED patients, with or without diabetes mellitus (DM), and in healthy controls. |
| 902 | 21918531 | MMP-2, MMP-9, TIMP-1 and TIMP-2 plasma levels were measured by enzyme-linked immunosorbent assay and zymography. |
| 903 | 21918531 | However, while patients in the ED group had similar TIMP-1 levels compared with those found in the control group, we found higher TIMP-1 levels and lower MMP-9/TIMP-1 ratios in the ED/DM group compared with controls (P<0.05). |
| 904 | 21918531 | While both groups of patients (ED and ED/DM) had slightly lower MMP-2 levels compared with controls (P<0.05), we found no differences in TIMP-2 levels among the study groups (P>0.05), and no differences in MMP-2/TIMP-2 ratios (P>0.05). |
| 905 | 21918531 | We found evidence indicating lack of significant alterations in circulating net MMP-9 and MMP-2 activities in patients with ED, and lower net MMP-9 activity in diabetic patients with ED. |
| 906 | 21918531 | We measured the circulating MMP-2, MMP-9, TIMP-1 and TIMP-2 levels in ED patients, with or without diabetes mellitus (DM), and in healthy controls. |
| 907 | 21918531 | MMP-2, MMP-9, TIMP-1 and TIMP-2 plasma levels were measured by enzyme-linked immunosorbent assay and zymography. |
| 908 | 21918531 | However, while patients in the ED group had similar TIMP-1 levels compared with those found in the control group, we found higher TIMP-1 levels and lower MMP-9/TIMP-1 ratios in the ED/DM group compared with controls (P<0.05). |
| 909 | 21918531 | While both groups of patients (ED and ED/DM) had slightly lower MMP-2 levels compared with controls (P<0.05), we found no differences in TIMP-2 levels among the study groups (P>0.05), and no differences in MMP-2/TIMP-2 ratios (P>0.05). |
| 910 | 21918531 | We found evidence indicating lack of significant alterations in circulating net MMP-9 and MMP-2 activities in patients with ED, and lower net MMP-9 activity in diabetic patients with ED. |
| 911 | 21918531 | We measured the circulating MMP-2, MMP-9, TIMP-1 and TIMP-2 levels in ED patients, with or without diabetes mellitus (DM), and in healthy controls. |
| 912 | 21918531 | MMP-2, MMP-9, TIMP-1 and TIMP-2 plasma levels were measured by enzyme-linked immunosorbent assay and zymography. |
| 913 | 21918531 | However, while patients in the ED group had similar TIMP-1 levels compared with those found in the control group, we found higher TIMP-1 levels and lower MMP-9/TIMP-1 ratios in the ED/DM group compared with controls (P<0.05). |
| 914 | 21918531 | While both groups of patients (ED and ED/DM) had slightly lower MMP-2 levels compared with controls (P<0.05), we found no differences in TIMP-2 levels among the study groups (P>0.05), and no differences in MMP-2/TIMP-2 ratios (P>0.05). |
| 915 | 21918531 | We found evidence indicating lack of significant alterations in circulating net MMP-9 and MMP-2 activities in patients with ED, and lower net MMP-9 activity in diabetic patients with ED. |
| 916 | 21918531 | We measured the circulating MMP-2, MMP-9, TIMP-1 and TIMP-2 levels in ED patients, with or without diabetes mellitus (DM), and in healthy controls. |
| 917 | 21918531 | MMP-2, MMP-9, TIMP-1 and TIMP-2 plasma levels were measured by enzyme-linked immunosorbent assay and zymography. |
| 918 | 21918531 | However, while patients in the ED group had similar TIMP-1 levels compared with those found in the control group, we found higher TIMP-1 levels and lower MMP-9/TIMP-1 ratios in the ED/DM group compared with controls (P<0.05). |
| 919 | 21918531 | While both groups of patients (ED and ED/DM) had slightly lower MMP-2 levels compared with controls (P<0.05), we found no differences in TIMP-2 levels among the study groups (P>0.05), and no differences in MMP-2/TIMP-2 ratios (P>0.05). |
| 920 | 21918531 | We found evidence indicating lack of significant alterations in circulating net MMP-9 and MMP-2 activities in patients with ED, and lower net MMP-9 activity in diabetic patients with ED. |
| 921 | 21921021 | Activities of MMP-2, MMP-9, and its complex with neutrophil gelatinase-associated lipocalin (NGAL/MMP-9) were measured by substrate gel zymography in urine from nondiabetic (ND) and type 1 diabetic (T1D) rodents that were susceptible to both T1D-induced plaque angiogenesis and nephropathy, or nephropathy alone. |
| 922 | 21921021 | Urinary MMP-9, MMP-2, and NGAL/MMP-9 activities were increased and more prevalent in T1D compared with ND controls. |
| 923 | 21921021 | In nephropathy models, urinary NGAL/MMP-9 and MMP-9 activities appeared before onset of albuminuria, whereas MMP-2 was absent or delayed. |
| 924 | 21921021 | Activities of MMP-2, MMP-9, and its complex with neutrophil gelatinase-associated lipocalin (NGAL/MMP-9) were measured by substrate gel zymography in urine from nondiabetic (ND) and type 1 diabetic (T1D) rodents that were susceptible to both T1D-induced plaque angiogenesis and nephropathy, or nephropathy alone. |
| 925 | 21921021 | Urinary MMP-9, MMP-2, and NGAL/MMP-9 activities were increased and more prevalent in T1D compared with ND controls. |
| 926 | 21921021 | In nephropathy models, urinary NGAL/MMP-9 and MMP-9 activities appeared before onset of albuminuria, whereas MMP-2 was absent or delayed. |
| 927 | 21921021 | Activities of MMP-2, MMP-9, and its complex with neutrophil gelatinase-associated lipocalin (NGAL/MMP-9) were measured by substrate gel zymography in urine from nondiabetic (ND) and type 1 diabetic (T1D) rodents that were susceptible to both T1D-induced plaque angiogenesis and nephropathy, or nephropathy alone. |
| 928 | 21921021 | Urinary MMP-9, MMP-2, and NGAL/MMP-9 activities were increased and more prevalent in T1D compared with ND controls. |
| 929 | 21921021 | In nephropathy models, urinary NGAL/MMP-9 and MMP-9 activities appeared before onset of albuminuria, whereas MMP-2 was absent or delayed. |
| 930 | 21963884 | Matrix metalloproteinase-2 (MMP-2) and MMP-9 are two relevant MMPs for embryo development. |
| 931 | 21963884 | Here, we addressed whether changes in these MMPs and in tissue inhibitor of matrix metalloproteinase-1 (TIMP-1) and TIMP-2 are altered in embryos and decidua from type 1 diabetic rats during early organogenesis. |
| 932 | 21963884 | Our results demonstrate MMP-2 and MMP-9 overactivities and overexpression, together with increases in lipid peroxidation and nitric oxide production in embryos and decidua from diabetic animals. |
| 933 | 21963884 | There is a concomitant increase in the inhibitory activity of TIMP-1 and TIMP-2 in embryos and decidua, and an increase in protein expression of embryonic TIMP-1 and TIMP-2. |
| 934 | 21963884 | Matrix metalloproteinase-2 (MMP-2) and MMP-9 are two relevant MMPs for embryo development. |
| 935 | 21963884 | Here, we addressed whether changes in these MMPs and in tissue inhibitor of matrix metalloproteinase-1 (TIMP-1) and TIMP-2 are altered in embryos and decidua from type 1 diabetic rats during early organogenesis. |
| 936 | 21963884 | Our results demonstrate MMP-2 and MMP-9 overactivities and overexpression, together with increases in lipid peroxidation and nitric oxide production in embryos and decidua from diabetic animals. |
| 937 | 21963884 | There is a concomitant increase in the inhibitory activity of TIMP-1 and TIMP-2 in embryos and decidua, and an increase in protein expression of embryonic TIMP-1 and TIMP-2. |
| 938 | 22045867 | Upregulation of matrix metalloproteinase-2 (MMP-2) and matrix metalloproteinase-9 (MMP-9) in diabetes appears to play a role in vascular complications of diabetes. |
| 939 | 22045867 | We hypothesised that inhibition of MMP-2 and MMP-9 by minocycline can be potentiated by aspirin through inhibition of cyclooxygenase-2 and tissue plasminogen activator, resulting in amelioration of clinical cerebral ischaemia in diabetes. |
| 940 | 22045867 | Moreover, this therapy was associated with significantly lower mortality and reduction in MMP-2 and MMP-9 levels. |
| 941 | 22045867 | Our data indicate that combination of aspirin and minocycline therapy protects from the consequences of cerebral ischaemia in animal models of diabetes and is associated with inhibition of MMP-2 and MMP-9. |
| 942 | 22045867 | Upregulation of matrix metalloproteinase-2 (MMP-2) and matrix metalloproteinase-9 (MMP-9) in diabetes appears to play a role in vascular complications of diabetes. |
| 943 | 22045867 | We hypothesised that inhibition of MMP-2 and MMP-9 by minocycline can be potentiated by aspirin through inhibition of cyclooxygenase-2 and tissue plasminogen activator, resulting in amelioration of clinical cerebral ischaemia in diabetes. |
| 944 | 22045867 | Moreover, this therapy was associated with significantly lower mortality and reduction in MMP-2 and MMP-9 levels. |
| 945 | 22045867 | Our data indicate that combination of aspirin and minocycline therapy protects from the consequences of cerebral ischaemia in animal models of diabetes and is associated with inhibition of MMP-2 and MMP-9. |
| 946 | 22045867 | Upregulation of matrix metalloproteinase-2 (MMP-2) and matrix metalloproteinase-9 (MMP-9) in diabetes appears to play a role in vascular complications of diabetes. |
| 947 | 22045867 | We hypothesised that inhibition of MMP-2 and MMP-9 by minocycline can be potentiated by aspirin through inhibition of cyclooxygenase-2 and tissue plasminogen activator, resulting in amelioration of clinical cerebral ischaemia in diabetes. |
| 948 | 22045867 | Moreover, this therapy was associated with significantly lower mortality and reduction in MMP-2 and MMP-9 levels. |
| 949 | 22045867 | Our data indicate that combination of aspirin and minocycline therapy protects from the consequences of cerebral ischaemia in animal models of diabetes and is associated with inhibition of MMP-2 and MMP-9. |
| 950 | 22045867 | Upregulation of matrix metalloproteinase-2 (MMP-2) and matrix metalloproteinase-9 (MMP-9) in diabetes appears to play a role in vascular complications of diabetes. |
| 951 | 22045867 | We hypothesised that inhibition of MMP-2 and MMP-9 by minocycline can be potentiated by aspirin through inhibition of cyclooxygenase-2 and tissue plasminogen activator, resulting in amelioration of clinical cerebral ischaemia in diabetes. |
| 952 | 22045867 | Moreover, this therapy was associated with significantly lower mortality and reduction in MMP-2 and MMP-9 levels. |
| 953 | 22045867 | Our data indicate that combination of aspirin and minocycline therapy protects from the consequences of cerebral ischaemia in animal models of diabetes and is associated with inhibition of MMP-2 and MMP-9. |
| 954 | 22094062 | Apocynin significantly attenuates the impaired glomerular function, concentration of Na(+), K(+), alpha glutathione S-transferase levels in urine and neutrophil gelatinase-associated lipocalin levels in plasma caused by iomeprol. |
| 955 | 22094062 | In kidney, immunohistochemical analysis of some inflammatory mediators, such as nitrotyrosine, poly-ADP-ribosyl polymerase, tumor necrosis factor-α, interleukin-1β as well as apoptosis (evaluated as terminal deoxynucleotidyltransferase-mediated UTP end labeling assay) revealed positive staining in tissue obtained from iomeprol group. |
| 956 | 22171077 | SV exposed to DM conditions demonstrated a notable increase in MMP-2 and MMP-9 but a significant decrease in TIMP-2 and TIMP-3 in protein concentration compared with control group. |
| 957 | 22180326 | Embryos and decidua were explanted on Day 10.5 of gestation for further analysis of embryo resorptions and malformations, MMP-2 and MMP-9 activities, TIMP-1 and TIMP-2 levels, NO production and lipid peroxidation. |
| 958 | 22180326 | MMP-2 and MMP-9 activities were increased in embryos and decidua from diabetic rats and decreased with safflower oil and folic acid supplementations. |
| 959 | 22180326 | Embryos and decidua were explanted on Day 10.5 of gestation for further analysis of embryo resorptions and malformations, MMP-2 and MMP-9 activities, TIMP-1 and TIMP-2 levels, NO production and lipid peroxidation. |
| 960 | 22180326 | MMP-2 and MMP-9 activities were increased in embryos and decidua from diabetic rats and decreased with safflower oil and folic acid supplementations. |
| 961 | 22211962 | The butanol fraction of guava (Psidium cattleianum Sabine) leaf extract suppresses MMP-2 and MMP-9 expression and activity through the suppression of the ERK1/2 MAPK signaling pathway. |
| 962 | 22211962 | Interestingly, we observed for the first time that GBF suppressed both matrix metalloproteinases (MMP)-9 and MMP-2 expression and activity in part through the downregulation of the ERK1/2 activation in lung cancer cells. |
| 963 | 22211962 | The butanol fraction of guava (Psidium cattleianum Sabine) leaf extract suppresses MMP-2 and MMP-9 expression and activity through the suppression of the ERK1/2 MAPK signaling pathway. |
| 964 | 22211962 | Interestingly, we observed for the first time that GBF suppressed both matrix metalloproteinases (MMP)-9 and MMP-2 expression and activity in part through the downregulation of the ERK1/2 activation in lung cancer cells. |
| 965 | 22261714 | Furthermore, the gene expression of matrix metalloproteinase 2 (MMP-2) decreased, while the gene expression of tissue inhibitor of metalloproteinase 2 (TIMP-2) increased in the hearts of DN rats. |
| 966 | 22261714 | Our findings suggest that upregulation of cardiac TGF-β1 gene along with the imbalance between MMP-2 and TIMP-2 expressions is critically involved in cardiac fibrosis associated with diabetic nephropathy. |
| 967 | 22261714 | Pioglitazone can ameliorate cardiac remodeling by suppressing the gene expression of TGF-β1 and regulating the MMP-2/TIMP-2 system. |
| 968 | 22261714 | Furthermore, the gene expression of matrix metalloproteinase 2 (MMP-2) decreased, while the gene expression of tissue inhibitor of metalloproteinase 2 (TIMP-2) increased in the hearts of DN rats. |
| 969 | 22261714 | Our findings suggest that upregulation of cardiac TGF-β1 gene along with the imbalance between MMP-2 and TIMP-2 expressions is critically involved in cardiac fibrosis associated with diabetic nephropathy. |
| 970 | 22261714 | Pioglitazone can ameliorate cardiac remodeling by suppressing the gene expression of TGF-β1 and regulating the MMP-2/TIMP-2 system. |
| 971 | 22261714 | Furthermore, the gene expression of matrix metalloproteinase 2 (MMP-2) decreased, while the gene expression of tissue inhibitor of metalloproteinase 2 (TIMP-2) increased in the hearts of DN rats. |
| 972 | 22261714 | Our findings suggest that upregulation of cardiac TGF-β1 gene along with the imbalance between MMP-2 and TIMP-2 expressions is critically involved in cardiac fibrosis associated with diabetic nephropathy. |
| 973 | 22261714 | Pioglitazone can ameliorate cardiac remodeling by suppressing the gene expression of TGF-β1 and regulating the MMP-2/TIMP-2 system. |
| 974 | 22344735 | This work aimed to determine MMP-2 and MMP-9 activities and nitration in term placentas from type 2 diabetic patients and verify the hypothesis that peroxynitrites are positive regulators of placental MMP-2 and MMP-9 activities. |
| 975 | 22344735 | For this purpose, term placentas from healthy and type 2 diabetic patients were analyzed for MMP-2 and MMP-9 levels and activities, protein nitration, and nitration of MMP-2 and MMP-9. |
| 976 | 22344735 | Villous explants were cultured in the presence of peroxynitrites for further evaluation of MMP-2 and MMP-9 activities. |
| 977 | 22344735 | We found that MMP-2 and MMP-9 activities were increased in term placentas from diabetic patients. |
| 978 | 22344735 | These changes were found even when MMP-2 protein concentrations were diminished and MMP-9 protein concentrations were not changed in the diabetic group. |
| 979 | 22344735 | Increased protein nitration and specific nitration of MMP-2 and MMP-9 were found in term placentas from diabetic patients. |
| 980 | 22344735 | Peroxynitrites were able to increase the activity of placental MMP-2 and MMP-9. |
| 981 | 22344735 | Taken together, this study has shown for first time that peroxynitrites can nitrate and activate MMP-2 and MMP-9 in the placenta, a nitrative pathway possibly related to MMPs overactivity in the placentas from type 2 diabetic patients. |
| 982 | 22344735 | This work aimed to determine MMP-2 and MMP-9 activities and nitration in term placentas from type 2 diabetic patients and verify the hypothesis that peroxynitrites are positive regulators of placental MMP-2 and MMP-9 activities. |
| 983 | 22344735 | For this purpose, term placentas from healthy and type 2 diabetic patients were analyzed for MMP-2 and MMP-9 levels and activities, protein nitration, and nitration of MMP-2 and MMP-9. |
| 984 | 22344735 | Villous explants were cultured in the presence of peroxynitrites for further evaluation of MMP-2 and MMP-9 activities. |
| 985 | 22344735 | We found that MMP-2 and MMP-9 activities were increased in term placentas from diabetic patients. |
| 986 | 22344735 | These changes were found even when MMP-2 protein concentrations were diminished and MMP-9 protein concentrations were not changed in the diabetic group. |
| 987 | 22344735 | Increased protein nitration and specific nitration of MMP-2 and MMP-9 were found in term placentas from diabetic patients. |
| 988 | 22344735 | Peroxynitrites were able to increase the activity of placental MMP-2 and MMP-9. |
| 989 | 22344735 | Taken together, this study has shown for first time that peroxynitrites can nitrate and activate MMP-2 and MMP-9 in the placenta, a nitrative pathway possibly related to MMPs overactivity in the placentas from type 2 diabetic patients. |
| 990 | 22344735 | This work aimed to determine MMP-2 and MMP-9 activities and nitration in term placentas from type 2 diabetic patients and verify the hypothesis that peroxynitrites are positive regulators of placental MMP-2 and MMP-9 activities. |
| 991 | 22344735 | For this purpose, term placentas from healthy and type 2 diabetic patients were analyzed for MMP-2 and MMP-9 levels and activities, protein nitration, and nitration of MMP-2 and MMP-9. |
| 992 | 22344735 | Villous explants were cultured in the presence of peroxynitrites for further evaluation of MMP-2 and MMP-9 activities. |
| 993 | 22344735 | We found that MMP-2 and MMP-9 activities were increased in term placentas from diabetic patients. |
| 994 | 22344735 | These changes were found even when MMP-2 protein concentrations were diminished and MMP-9 protein concentrations were not changed in the diabetic group. |
| 995 | 22344735 | Increased protein nitration and specific nitration of MMP-2 and MMP-9 were found in term placentas from diabetic patients. |
| 996 | 22344735 | Peroxynitrites were able to increase the activity of placental MMP-2 and MMP-9. |
| 997 | 22344735 | Taken together, this study has shown for first time that peroxynitrites can nitrate and activate MMP-2 and MMP-9 in the placenta, a nitrative pathway possibly related to MMPs overactivity in the placentas from type 2 diabetic patients. |
| 998 | 22344735 | This work aimed to determine MMP-2 and MMP-9 activities and nitration in term placentas from type 2 diabetic patients and verify the hypothesis that peroxynitrites are positive regulators of placental MMP-2 and MMP-9 activities. |
| 999 | 22344735 | For this purpose, term placentas from healthy and type 2 diabetic patients were analyzed for MMP-2 and MMP-9 levels and activities, protein nitration, and nitration of MMP-2 and MMP-9. |
| 1000 | 22344735 | Villous explants were cultured in the presence of peroxynitrites for further evaluation of MMP-2 and MMP-9 activities. |
| 1001 | 22344735 | We found that MMP-2 and MMP-9 activities were increased in term placentas from diabetic patients. |
| 1002 | 22344735 | These changes were found even when MMP-2 protein concentrations were diminished and MMP-9 protein concentrations were not changed in the diabetic group. |
| 1003 | 22344735 | Increased protein nitration and specific nitration of MMP-2 and MMP-9 were found in term placentas from diabetic patients. |
| 1004 | 22344735 | Peroxynitrites were able to increase the activity of placental MMP-2 and MMP-9. |
| 1005 | 22344735 | Taken together, this study has shown for first time that peroxynitrites can nitrate and activate MMP-2 and MMP-9 in the placenta, a nitrative pathway possibly related to MMPs overactivity in the placentas from type 2 diabetic patients. |
| 1006 | 22344735 | This work aimed to determine MMP-2 and MMP-9 activities and nitration in term placentas from type 2 diabetic patients and verify the hypothesis that peroxynitrites are positive regulators of placental MMP-2 and MMP-9 activities. |
| 1007 | 22344735 | For this purpose, term placentas from healthy and type 2 diabetic patients were analyzed for MMP-2 and MMP-9 levels and activities, protein nitration, and nitration of MMP-2 and MMP-9. |
| 1008 | 22344735 | Villous explants were cultured in the presence of peroxynitrites for further evaluation of MMP-2 and MMP-9 activities. |
| 1009 | 22344735 | We found that MMP-2 and MMP-9 activities were increased in term placentas from diabetic patients. |
| 1010 | 22344735 | These changes were found even when MMP-2 protein concentrations were diminished and MMP-9 protein concentrations were not changed in the diabetic group. |
| 1011 | 22344735 | Increased protein nitration and specific nitration of MMP-2 and MMP-9 were found in term placentas from diabetic patients. |
| 1012 | 22344735 | Peroxynitrites were able to increase the activity of placental MMP-2 and MMP-9. |
| 1013 | 22344735 | Taken together, this study has shown for first time that peroxynitrites can nitrate and activate MMP-2 and MMP-9 in the placenta, a nitrative pathway possibly related to MMPs overactivity in the placentas from type 2 diabetic patients. |
| 1014 | 22344735 | This work aimed to determine MMP-2 and MMP-9 activities and nitration in term placentas from type 2 diabetic patients and verify the hypothesis that peroxynitrites are positive regulators of placental MMP-2 and MMP-9 activities. |
| 1015 | 22344735 | For this purpose, term placentas from healthy and type 2 diabetic patients were analyzed for MMP-2 and MMP-9 levels and activities, protein nitration, and nitration of MMP-2 and MMP-9. |
| 1016 | 22344735 | Villous explants were cultured in the presence of peroxynitrites for further evaluation of MMP-2 and MMP-9 activities. |
| 1017 | 22344735 | We found that MMP-2 and MMP-9 activities were increased in term placentas from diabetic patients. |
| 1018 | 22344735 | These changes were found even when MMP-2 protein concentrations were diminished and MMP-9 protein concentrations were not changed in the diabetic group. |
| 1019 | 22344735 | Increased protein nitration and specific nitration of MMP-2 and MMP-9 were found in term placentas from diabetic patients. |
| 1020 | 22344735 | Peroxynitrites were able to increase the activity of placental MMP-2 and MMP-9. |
| 1021 | 22344735 | Taken together, this study has shown for first time that peroxynitrites can nitrate and activate MMP-2 and MMP-9 in the placenta, a nitrative pathway possibly related to MMPs overactivity in the placentas from type 2 diabetic patients. |
| 1022 | 22344735 | This work aimed to determine MMP-2 and MMP-9 activities and nitration in term placentas from type 2 diabetic patients and verify the hypothesis that peroxynitrites are positive regulators of placental MMP-2 and MMP-9 activities. |
| 1023 | 22344735 | For this purpose, term placentas from healthy and type 2 diabetic patients were analyzed for MMP-2 and MMP-9 levels and activities, protein nitration, and nitration of MMP-2 and MMP-9. |
| 1024 | 22344735 | Villous explants were cultured in the presence of peroxynitrites for further evaluation of MMP-2 and MMP-9 activities. |
| 1025 | 22344735 | We found that MMP-2 and MMP-9 activities were increased in term placentas from diabetic patients. |
| 1026 | 22344735 | These changes were found even when MMP-2 protein concentrations were diminished and MMP-9 protein concentrations were not changed in the diabetic group. |
| 1027 | 22344735 | Increased protein nitration and specific nitration of MMP-2 and MMP-9 were found in term placentas from diabetic patients. |
| 1028 | 22344735 | Peroxynitrites were able to increase the activity of placental MMP-2 and MMP-9. |
| 1029 | 22344735 | Taken together, this study has shown for first time that peroxynitrites can nitrate and activate MMP-2 and MMP-9 in the placenta, a nitrative pathway possibly related to MMPs overactivity in the placentas from type 2 diabetic patients. |
| 1030 | 22344735 | This work aimed to determine MMP-2 and MMP-9 activities and nitration in term placentas from type 2 diabetic patients and verify the hypothesis that peroxynitrites are positive regulators of placental MMP-2 and MMP-9 activities. |
| 1031 | 22344735 | For this purpose, term placentas from healthy and type 2 diabetic patients were analyzed for MMP-2 and MMP-9 levels and activities, protein nitration, and nitration of MMP-2 and MMP-9. |
| 1032 | 22344735 | Villous explants were cultured in the presence of peroxynitrites for further evaluation of MMP-2 and MMP-9 activities. |
| 1033 | 22344735 | We found that MMP-2 and MMP-9 activities were increased in term placentas from diabetic patients. |
| 1034 | 22344735 | These changes were found even when MMP-2 protein concentrations were diminished and MMP-9 protein concentrations were not changed in the diabetic group. |
| 1035 | 22344735 | Increased protein nitration and specific nitration of MMP-2 and MMP-9 were found in term placentas from diabetic patients. |
| 1036 | 22344735 | Peroxynitrites were able to increase the activity of placental MMP-2 and MMP-9. |
| 1037 | 22344735 | Taken together, this study has shown for first time that peroxynitrites can nitrate and activate MMP-2 and MMP-9 in the placenta, a nitrative pathway possibly related to MMPs overactivity in the placentas from type 2 diabetic patients. |
| 1038 | 22492942 | Also, renal levels of interleukin-6 (IL-6), tumor necrosis factor-α (TNF-α), ED-1, hypoxia-inducible factor-1α (HIF-1α), and neutrophil gelatinase-associated lipocalin (NGAL) were determined by immunohistochemistry and immunoblotting. |
| 1039 | 22492942 | Additionally, ANG-(1-7) reduced renal fibrosis, decreased thiobarbituric acid-reactive substances, and restored the activity of both renal superoxide dismutase and catalase in ZDF. |
| 1040 | 22492942 | This attenuation of renal oxidative stress proceeded with decreased renal immunostaining of IL-6, TNF-α, ED-1, HIF-1α, and NGAL to values similar to those displayed by LZR. |
| 1041 | 22492942 | Angiotensin-converting enzyme type 2 (ACE2) and ANG II levels remained unchanged after treatment with ANG-(1-7). |
| 1042 | 22586582 | We observed comparable MMP-2 mRNA expressions in control and transplanted groups of mice, whereas MMP-9 mRNA and protein expression levels increased after islet transplantation. |
| 1043 | 22586582 | Immunostaining for CD11b (Mac-1)-expressing leukocytes (macrophage, neutrophils) and Ly6G (neutrophils) revealed substantially reduced inflammatory cell migration into islet-transplanted liver in MMP-9 knockout recipients. |
| 1044 | 22611374 | Immunohistochemical procedures for MMP-2, MMP-9, TNF-α, IL-1β, IL-6, RANKL, and RAGE were performed in rats after 1, 3, 6, 9, and 12 months of diabetes induction. |
| 1045 | 22749388 | Associations of urinary levels of kidney injury molecule 1 (KIM-1) and neutrophil gelatinase-associated lipocalin (NGAL) with kidney function decline in the Multi-Ethnic Study of Atherosclerosis (MESA). |
| 1046 | 22858798 | NZ10 mice on CD showed increased body weight, hyperglycemia, and hyperinsulinemia at 25 weeks whereas those on HPO diet retained normal insulin levels and were normoglycemic. |
| 1047 | 22858798 | Real time-PCR (RT-PCR) confirmed markedly increased expression of matrix metalloproteinases (MMPs) 2, 3, 11, and 12, vascular endothelial growth factor-A and C (VEGF-A and C), Von Willebrand Factor, and peroxisome proliferator-activated receptor-γ (PPAR-γ) selectively in the NZ10/CD group. |
| 1048 | 22858798 | Protein levels of MMP2, 3, and 9 were significantly increased in the VA of NZ10 mice fed CD while those of MMP7 were downregulated. |
| 1049 | 22858798 | NZ10 mice on CD showed increased body weight, hyperglycemia, and hyperinsulinemia at 25 weeks whereas those on HPO diet retained normal insulin levels and were normoglycemic. |
| 1050 | 22858798 | Real time-PCR (RT-PCR) confirmed markedly increased expression of matrix metalloproteinases (MMPs) 2, 3, 11, and 12, vascular endothelial growth factor-A and C (VEGF-A and C), Von Willebrand Factor, and peroxisome proliferator-activated receptor-γ (PPAR-γ) selectively in the NZ10/CD group. |
| 1051 | 22858798 | Protein levels of MMP2, 3, and 9 were significantly increased in the VA of NZ10 mice fed CD while those of MMP7 were downregulated. |
| 1052 | 23041150 | We used reverse transcription polymerase chain reaction and western blotting to determine the expression of Toll-like receptor 4 (TLR4), matrix metalloproteinase-2 (MMP-2) and NF-κB p65 in MSCs under high glucose (HG) with or without pretreatment with AS-IV. |
| 1053 | 23041150 | The surface expression of TLR4 was checked by flow cytometry and the expression of TNF-α and MCP-1 were detected by ELISA in diabetes patients treated with AS-IV. |
| 1054 | 23041150 | AS-IV decreased the TLR4, TNF-α and MCP-1 expression in patients. |
| 1055 | 23052196 | Results show a consistent down-regulation of HNF1α and HNF4α under a scenario of exposure where HepG2 cells (1) gained resistance to arsenic-induced toxicity/apoptosis, (2) attained loss of tissue-specific features (as shown by the observed down-regulation of ALDOB, PEPCK and CYP1A2, triggering of the epithelial-to-mesenchymal transition program and the hypersecretion of matrix metalloproteinase-2 and 9), (3) failed to maintain balanced expression of the "stemness" genes C-MYC, OCT3/4, LIN28 and NOTCH2 and (4) showed glucose metabolism impairment. |
| 1056 | 23054594 | In proliferative diabetic retinopathy (PDR), vascular endothelial growth factor (VEGF) and CCN2 (connective tissue growth factor; CTGF) cause blindness by neovascularization and subsequent fibrosis. |
| 1057 | 23054594 | This angio-fibrotic switch is associated with a shift in the balance between vitreous levels of CCN2 and VEGF in the eye. |
| 1058 | 23054594 | Here, we investigated the possible involvement of other important mediators of fibrosis, tissue inhibitor of metalloproteinases (TIMP)-1 and transforming growth factor (TGF)-β2, and of the matrix metalloproteinases (MMP)-2 and MMP-9, in the natural course of PDR. |
| 1059 | 23054594 | TIMP-1, activated TGF-β2, CCN2 and VEGF levels were measured by ELISA in 78 vitreous samples of patients with PDR (n = 28), diabetic patients without PDR (n = 24), and patients with the diabetes-unrelated retinal conditions macular hole (n = 10) or macular pucker (n = 16), and were related to MMP-2 and MMP-9 activity on zymograms and to clinical data, including degree of intra-ocular neovascularization and fibrosis. |
| 1060 | 23054594 | TIMP-1, CCN2 and VEGF levels, but not activated TGF-β2 levels, were significantly increased in the vitreous of diabetic patients, with the highest levels in PDR patients. |
| 1061 | 23054594 | CCN2 and the CCN2/VEGF ratio were the strongest predictors of degree of fibrosis. |
| 1062 | 23054594 | In diabetic patients with or without PDR, activated TGF-β2 levels correlated with TIMP-1 levels, whereas in PDR patients, TIMP-1 levels, MMP-2 and proMMP-9 were associated with degree of neovascularization, like VEGF levels, but not with fibrosis. |
| 1063 | 23054594 | We confirm here our previous findings that retinal fibrosis in PDR patients is significantly correlated with vitreous CCN2 levels and the CCN2/VEGF ratio. |
| 1064 | 23054594 | In contrast, TIMP-1, MMP-2 and MMP-9 appear to have a role in the angiogenic phase rather than in the fibrotic phase of PDR. |
| 1065 | 23054594 | In proliferative diabetic retinopathy (PDR), vascular endothelial growth factor (VEGF) and CCN2 (connective tissue growth factor; CTGF) cause blindness by neovascularization and subsequent fibrosis. |
| 1066 | 23054594 | This angio-fibrotic switch is associated with a shift in the balance between vitreous levels of CCN2 and VEGF in the eye. |
| 1067 | 23054594 | Here, we investigated the possible involvement of other important mediators of fibrosis, tissue inhibitor of metalloproteinases (TIMP)-1 and transforming growth factor (TGF)-β2, and of the matrix metalloproteinases (MMP)-2 and MMP-9, in the natural course of PDR. |
| 1068 | 23054594 | TIMP-1, activated TGF-β2, CCN2 and VEGF levels were measured by ELISA in 78 vitreous samples of patients with PDR (n = 28), diabetic patients without PDR (n = 24), and patients with the diabetes-unrelated retinal conditions macular hole (n = 10) or macular pucker (n = 16), and were related to MMP-2 and MMP-9 activity on zymograms and to clinical data, including degree of intra-ocular neovascularization and fibrosis. |
| 1069 | 23054594 | TIMP-1, CCN2 and VEGF levels, but not activated TGF-β2 levels, were significantly increased in the vitreous of diabetic patients, with the highest levels in PDR patients. |
| 1070 | 23054594 | CCN2 and the CCN2/VEGF ratio were the strongest predictors of degree of fibrosis. |
| 1071 | 23054594 | In diabetic patients with or without PDR, activated TGF-β2 levels correlated with TIMP-1 levels, whereas in PDR patients, TIMP-1 levels, MMP-2 and proMMP-9 were associated with degree of neovascularization, like VEGF levels, but not with fibrosis. |
| 1072 | 23054594 | We confirm here our previous findings that retinal fibrosis in PDR patients is significantly correlated with vitreous CCN2 levels and the CCN2/VEGF ratio. |
| 1073 | 23054594 | In contrast, TIMP-1, MMP-2 and MMP-9 appear to have a role in the angiogenic phase rather than in the fibrotic phase of PDR. |
| 1074 | 23054594 | In proliferative diabetic retinopathy (PDR), vascular endothelial growth factor (VEGF) and CCN2 (connective tissue growth factor; CTGF) cause blindness by neovascularization and subsequent fibrosis. |
| 1075 | 23054594 | This angio-fibrotic switch is associated with a shift in the balance between vitreous levels of CCN2 and VEGF in the eye. |
| 1076 | 23054594 | Here, we investigated the possible involvement of other important mediators of fibrosis, tissue inhibitor of metalloproteinases (TIMP)-1 and transforming growth factor (TGF)-β2, and of the matrix metalloproteinases (MMP)-2 and MMP-9, in the natural course of PDR. |
| 1077 | 23054594 | TIMP-1, activated TGF-β2, CCN2 and VEGF levels were measured by ELISA in 78 vitreous samples of patients with PDR (n = 28), diabetic patients without PDR (n = 24), and patients with the diabetes-unrelated retinal conditions macular hole (n = 10) or macular pucker (n = 16), and were related to MMP-2 and MMP-9 activity on zymograms and to clinical data, including degree of intra-ocular neovascularization and fibrosis. |
| 1078 | 23054594 | TIMP-1, CCN2 and VEGF levels, but not activated TGF-β2 levels, were significantly increased in the vitreous of diabetic patients, with the highest levels in PDR patients. |
| 1079 | 23054594 | CCN2 and the CCN2/VEGF ratio were the strongest predictors of degree of fibrosis. |
| 1080 | 23054594 | In diabetic patients with or without PDR, activated TGF-β2 levels correlated with TIMP-1 levels, whereas in PDR patients, TIMP-1 levels, MMP-2 and proMMP-9 were associated with degree of neovascularization, like VEGF levels, but not with fibrosis. |
| 1081 | 23054594 | We confirm here our previous findings that retinal fibrosis in PDR patients is significantly correlated with vitreous CCN2 levels and the CCN2/VEGF ratio. |
| 1082 | 23054594 | In contrast, TIMP-1, MMP-2 and MMP-9 appear to have a role in the angiogenic phase rather than in the fibrotic phase of PDR. |
| 1083 | 23073918 | Matrix metalloproteinases (MMPs), their inhibitors (TIMPs) and inflammatory cytokines, such as interleukin-1 (IL-1), are considered markers of evolution and/or instability of atherosclerotic plaques. |
| 1084 | 23073918 | Aim of the present study was to analyse the levels of pentosidine, a fluorescent AGE, and to evaluate the expression of MMP-2, TIMP-3, and IL-1 in an ex vivo model of human advanced atherosclerotic plaques. |
| 1085 | 23073918 | We found that diabetic plaques showed higher level of pentosidine, as expected, but much lower, or even undetectable, expression levels of MMP-2 and TIMP-3; IL-1 expression was not different between diabetic and non diabetic plaques. |
| 1086 | 23073918 | Although the statistical correlations between the expression of the considered genes and pentosidine did not reach significance, slight negative trends were noted between TIMP-3 and IL-1 expression vs. pentosidine content. |
| 1087 | 23073918 | Matrix metalloproteinases (MMPs), their inhibitors (TIMPs) and inflammatory cytokines, such as interleukin-1 (IL-1), are considered markers of evolution and/or instability of atherosclerotic plaques. |
| 1088 | 23073918 | Aim of the present study was to analyse the levels of pentosidine, a fluorescent AGE, and to evaluate the expression of MMP-2, TIMP-3, and IL-1 in an ex vivo model of human advanced atherosclerotic plaques. |
| 1089 | 23073918 | We found that diabetic plaques showed higher level of pentosidine, as expected, but much lower, or even undetectable, expression levels of MMP-2 and TIMP-3; IL-1 expression was not different between diabetic and non diabetic plaques. |
| 1090 | 23073918 | Although the statistical correlations between the expression of the considered genes and pentosidine did not reach significance, slight negative trends were noted between TIMP-3 and IL-1 expression vs. pentosidine content. |
| 1091 | 23144821 | The characterization of DA water-extracts used various methods; after inducing cellular fibrosis in NRK-49F cells by treatment with β-hydroxybutyrate (β-HB) (10 mM), we used Western blotting to examine the protein expression in the TGF-β-related signal protein type I and type II TGF-β receptors, Smads2 and Smad3 (Smad2/3), pSmad2 and Smad3 (pSmad2/3), Smads4, Smads7, and EMT markers. |
| 1092 | 23144821 | These markers included E-cadherin, alpha-smooth muscle actin (α-SMA), and matrix metalloproteinase-2 (MMP-2). |
| 1093 | 23144821 | DA extract dose-dependently (50-200 µg/mL) suppressed β-HB-induced expression of fibronectin in NRK-49F cells concomitantly with the inhibition of Smad2/3, pSmad2/3, and Smad4. |
| 1094 | 23144821 | DA extract caused a decrease in α-SMA (α-smooth muscle actin) and MMP-2 levels, and an increase in E-cadherin expression. |
| 1095 | 23144821 | The characterization of DA water-extracts used various methods; after inducing cellular fibrosis in NRK-49F cells by treatment with β-hydroxybutyrate (β-HB) (10 mM), we used Western blotting to examine the protein expression in the TGF-β-related signal protein type I and type II TGF-β receptors, Smads2 and Smad3 (Smad2/3), pSmad2 and Smad3 (pSmad2/3), Smads4, Smads7, and EMT markers. |
| 1096 | 23144821 | These markers included E-cadherin, alpha-smooth muscle actin (α-SMA), and matrix metalloproteinase-2 (MMP-2). |
| 1097 | 23144821 | DA extract dose-dependently (50-200 µg/mL) suppressed β-HB-induced expression of fibronectin in NRK-49F cells concomitantly with the inhibition of Smad2/3, pSmad2/3, and Smad4. |
| 1098 | 23144821 | DA extract caused a decrease in α-SMA (α-smooth muscle actin) and MMP-2 levels, and an increase in E-cadherin expression. |
| 1099 | 23229548 | Matrix metalloproteinase-9 reduces islet amyloid formation by degrading islet amyloid polypeptide. |
| 1100 | 23229548 | Deposition of islet amyloid polypeptide (IAPP) as amyloid is a pathological hallmark of the islet in type 2 diabetes, which is toxic to β-cells. |
| 1101 | 23229548 | We previously showed that the enzyme neprilysin reduces islet amyloid deposition and thereby reduces β-cell apoptosis, by inhibiting fibril formation. |
| 1102 | 23229548 | Two other enzymes, matrix metalloproteinase (MMP)-2 and MMP-9, are extracellular gelatinases capable of degrading another amyloidogenic peptide, Aβ, the constituent of amyloid deposits in Alzheimer disease. |
| 1103 | 23229548 | We therefore investigated whether MMP-2 and MMP-9 play a role in reducing islet amyloid deposition. |
| 1104 | 23229548 | MMP-2 and MMP-9 mRNA were present in mouse islets but only MMP-9 activity was detectable. |
| 1105 | 23229548 | In an islet culture model where human IAPP (hIAPP) transgenic mouse islets develop amyloid but nontransgenic islets do not, a broad spectrum MMP inhibitor (GM6001) and an MMP-2/9 inhibitor increased amyloid formation and the resultant β-cell apoptosis. |
| 1106 | 23229548 | In contrast, a specific MMP-2 inhibitor had no effect on either amyloid deposition or β-cell apoptosis. |
| 1107 | 23229548 | Thus, MMP-9 constitutes an endogenous islet protease that limits islet amyloid deposition and its toxic effects via degradation of hIAPP. |
| 1108 | 23229548 | Because islet MMP-9 mRNA levels are decreased in type 2 diabetic subjects, islet MMP-9 activity may also be decreased in human type 2 diabetes, thereby contributing to increased islet amyloid deposition and β-cell loss. |
| 1109 | 23229548 | Approaches to increase islet MMP-9 activity could reduce or prevent amyloid deposition and its toxic effects in type 2 diabetes. |
| 1110 | 23229548 | Matrix metalloproteinase-9 reduces islet amyloid formation by degrading islet amyloid polypeptide. |
| 1111 | 23229548 | Deposition of islet amyloid polypeptide (IAPP) as amyloid is a pathological hallmark of the islet in type 2 diabetes, which is toxic to β-cells. |
| 1112 | 23229548 | We previously showed that the enzyme neprilysin reduces islet amyloid deposition and thereby reduces β-cell apoptosis, by inhibiting fibril formation. |
| 1113 | 23229548 | Two other enzymes, matrix metalloproteinase (MMP)-2 and MMP-9, are extracellular gelatinases capable of degrading another amyloidogenic peptide, Aβ, the constituent of amyloid deposits in Alzheimer disease. |
| 1114 | 23229548 | We therefore investigated whether MMP-2 and MMP-9 play a role in reducing islet amyloid deposition. |
| 1115 | 23229548 | MMP-2 and MMP-9 mRNA were present in mouse islets but only MMP-9 activity was detectable. |
| 1116 | 23229548 | In an islet culture model where human IAPP (hIAPP) transgenic mouse islets develop amyloid but nontransgenic islets do not, a broad spectrum MMP inhibitor (GM6001) and an MMP-2/9 inhibitor increased amyloid formation and the resultant β-cell apoptosis. |
| 1117 | 23229548 | In contrast, a specific MMP-2 inhibitor had no effect on either amyloid deposition or β-cell apoptosis. |
| 1118 | 23229548 | Thus, MMP-9 constitutes an endogenous islet protease that limits islet amyloid deposition and its toxic effects via degradation of hIAPP. |
| 1119 | 23229548 | Because islet MMP-9 mRNA levels are decreased in type 2 diabetic subjects, islet MMP-9 activity may also be decreased in human type 2 diabetes, thereby contributing to increased islet amyloid deposition and β-cell loss. |
| 1120 | 23229548 | Approaches to increase islet MMP-9 activity could reduce or prevent amyloid deposition and its toxic effects in type 2 diabetes. |
| 1121 | 23229548 | Matrix metalloproteinase-9 reduces islet amyloid formation by degrading islet amyloid polypeptide. |
| 1122 | 23229548 | Deposition of islet amyloid polypeptide (IAPP) as amyloid is a pathological hallmark of the islet in type 2 diabetes, which is toxic to β-cells. |
| 1123 | 23229548 | We previously showed that the enzyme neprilysin reduces islet amyloid deposition and thereby reduces β-cell apoptosis, by inhibiting fibril formation. |
| 1124 | 23229548 | Two other enzymes, matrix metalloproteinase (MMP)-2 and MMP-9, are extracellular gelatinases capable of degrading another amyloidogenic peptide, Aβ, the constituent of amyloid deposits in Alzheimer disease. |
| 1125 | 23229548 | We therefore investigated whether MMP-2 and MMP-9 play a role in reducing islet amyloid deposition. |
| 1126 | 23229548 | MMP-2 and MMP-9 mRNA were present in mouse islets but only MMP-9 activity was detectable. |
| 1127 | 23229548 | In an islet culture model where human IAPP (hIAPP) transgenic mouse islets develop amyloid but nontransgenic islets do not, a broad spectrum MMP inhibitor (GM6001) and an MMP-2/9 inhibitor increased amyloid formation and the resultant β-cell apoptosis. |
| 1128 | 23229548 | In contrast, a specific MMP-2 inhibitor had no effect on either amyloid deposition or β-cell apoptosis. |
| 1129 | 23229548 | Thus, MMP-9 constitutes an endogenous islet protease that limits islet amyloid deposition and its toxic effects via degradation of hIAPP. |
| 1130 | 23229548 | Because islet MMP-9 mRNA levels are decreased in type 2 diabetic subjects, islet MMP-9 activity may also be decreased in human type 2 diabetes, thereby contributing to increased islet amyloid deposition and β-cell loss. |
| 1131 | 23229548 | Approaches to increase islet MMP-9 activity could reduce or prevent amyloid deposition and its toxic effects in type 2 diabetes. |
| 1132 | 23229548 | Matrix metalloproteinase-9 reduces islet amyloid formation by degrading islet amyloid polypeptide. |
| 1133 | 23229548 | Deposition of islet amyloid polypeptide (IAPP) as amyloid is a pathological hallmark of the islet in type 2 diabetes, which is toxic to β-cells. |
| 1134 | 23229548 | We previously showed that the enzyme neprilysin reduces islet amyloid deposition and thereby reduces β-cell apoptosis, by inhibiting fibril formation. |
| 1135 | 23229548 | Two other enzymes, matrix metalloproteinase (MMP)-2 and MMP-9, are extracellular gelatinases capable of degrading another amyloidogenic peptide, Aβ, the constituent of amyloid deposits in Alzheimer disease. |
| 1136 | 23229548 | We therefore investigated whether MMP-2 and MMP-9 play a role in reducing islet amyloid deposition. |
| 1137 | 23229548 | MMP-2 and MMP-9 mRNA were present in mouse islets but only MMP-9 activity was detectable. |
| 1138 | 23229548 | In an islet culture model where human IAPP (hIAPP) transgenic mouse islets develop amyloid but nontransgenic islets do not, a broad spectrum MMP inhibitor (GM6001) and an MMP-2/9 inhibitor increased amyloid formation and the resultant β-cell apoptosis. |
| 1139 | 23229548 | In contrast, a specific MMP-2 inhibitor had no effect on either amyloid deposition or β-cell apoptosis. |
| 1140 | 23229548 | Thus, MMP-9 constitutes an endogenous islet protease that limits islet amyloid deposition and its toxic effects via degradation of hIAPP. |
| 1141 | 23229548 | Because islet MMP-9 mRNA levels are decreased in type 2 diabetic subjects, islet MMP-9 activity may also be decreased in human type 2 diabetes, thereby contributing to increased islet amyloid deposition and β-cell loss. |
| 1142 | 23229548 | Approaches to increase islet MMP-9 activity could reduce or prevent amyloid deposition and its toxic effects in type 2 diabetes. |
| 1143 | 23428182 | Advanced glycation end-products disrupt the blood-brain barrier by stimulating the release of transforming growth factor-β by pericytes and vascular endothelial growth factor and matrix metalloproteinase-2 by endothelial cells in vitro. |
| 1144 | 23428182 | AGEs reduced the expression of claudin-5 in BMECs by increasing the autocrine signaling through vascular endothelial growth factor (VEGF) and matrix metalloproteinase-2 (MMP-2) secreted by the BMECs themselves. |
| 1145 | 23428182 | These results indicated that AGEs induce basement membrane hypertrophy of the BBB by increasing the degree of autocrine TGF-β signaling by pericytes, and thereby disrupt the BBB through the up-regulation of VEGF and MMP-2 in BMECs under diabetic conditions. |
| 1146 | 23428182 | Advanced glycation end-products disrupt the blood-brain barrier by stimulating the release of transforming growth factor-β by pericytes and vascular endothelial growth factor and matrix metalloproteinase-2 by endothelial cells in vitro. |
| 1147 | 23428182 | AGEs reduced the expression of claudin-5 in BMECs by increasing the autocrine signaling through vascular endothelial growth factor (VEGF) and matrix metalloproteinase-2 (MMP-2) secreted by the BMECs themselves. |
| 1148 | 23428182 | These results indicated that AGEs induce basement membrane hypertrophy of the BBB by increasing the degree of autocrine TGF-β signaling by pericytes, and thereby disrupt the BBB through the up-regulation of VEGF and MMP-2 in BMECs under diabetic conditions. |
| 1149 | 23428182 | Advanced glycation end-products disrupt the blood-brain barrier by stimulating the release of transforming growth factor-β by pericytes and vascular endothelial growth factor and matrix metalloproteinase-2 by endothelial cells in vitro. |
| 1150 | 23428182 | AGEs reduced the expression of claudin-5 in BMECs by increasing the autocrine signaling through vascular endothelial growth factor (VEGF) and matrix metalloproteinase-2 (MMP-2) secreted by the BMECs themselves. |
| 1151 | 23428182 | These results indicated that AGEs induce basement membrane hypertrophy of the BBB by increasing the degree of autocrine TGF-β signaling by pericytes, and thereby disrupt the BBB through the up-regulation of VEGF and MMP-2 in BMECs under diabetic conditions. |
| 1152 | 23463906 | Wound-healing effects of low-level laser therapy in diabetic rats involve the modulation of MMP-2 and MMP-9 and the redistribution of collagen types I and III. |
| 1153 | 23463906 | The present study aimed to determine if LLLT restores the balance between mRNA expression of matrix metalloproteinases (MMP-2 and MMP-9) and also the balance between collagen types I and III during the healing process of diabetic wounds. |
| 1154 | 23463906 | Twenty-four hours after LLLT application, rats were euthanized, the scarred areas were collected for MMP-2 and MMP-9 mRNA analysis and also for histological analysis (inflammation and types I and III collagen). |
| 1155 | 23463906 | The results demonstrated that scare in untreated diabetic rats significantly increased the MMP-2 and MMP-9 expression compared with that in non-diabetic rats (p < 0.05), while LLLT significantly reduced MMP-2 and MMP-9 expression compared with that in untreated diabetic rats (p < 0.05). |
| 1156 | 23463906 | To conclude, the results also showed that LLLT was able to alter the expression of MMP-9 as well as accelerate the production of collagen and increase the total percentage of collagen type III in diabetic animals. |
| 1157 | 23463906 | Wound-healing effects of low-level laser therapy in diabetic rats involve the modulation of MMP-2 and MMP-9 and the redistribution of collagen types I and III. |
| 1158 | 23463906 | The present study aimed to determine if LLLT restores the balance between mRNA expression of matrix metalloproteinases (MMP-2 and MMP-9) and also the balance between collagen types I and III during the healing process of diabetic wounds. |
| 1159 | 23463906 | Twenty-four hours after LLLT application, rats were euthanized, the scarred areas were collected for MMP-2 and MMP-9 mRNA analysis and also for histological analysis (inflammation and types I and III collagen). |
| 1160 | 23463906 | The results demonstrated that scare in untreated diabetic rats significantly increased the MMP-2 and MMP-9 expression compared with that in non-diabetic rats (p < 0.05), while LLLT significantly reduced MMP-2 and MMP-9 expression compared with that in untreated diabetic rats (p < 0.05). |
| 1161 | 23463906 | To conclude, the results also showed that LLLT was able to alter the expression of MMP-9 as well as accelerate the production of collagen and increase the total percentage of collagen type III in diabetic animals. |
| 1162 | 23463906 | Wound-healing effects of low-level laser therapy in diabetic rats involve the modulation of MMP-2 and MMP-9 and the redistribution of collagen types I and III. |
| 1163 | 23463906 | The present study aimed to determine if LLLT restores the balance between mRNA expression of matrix metalloproteinases (MMP-2 and MMP-9) and also the balance between collagen types I and III during the healing process of diabetic wounds. |
| 1164 | 23463906 | Twenty-four hours after LLLT application, rats were euthanized, the scarred areas were collected for MMP-2 and MMP-9 mRNA analysis and also for histological analysis (inflammation and types I and III collagen). |
| 1165 | 23463906 | The results demonstrated that scare in untreated diabetic rats significantly increased the MMP-2 and MMP-9 expression compared with that in non-diabetic rats (p < 0.05), while LLLT significantly reduced MMP-2 and MMP-9 expression compared with that in untreated diabetic rats (p < 0.05). |
| 1166 | 23463906 | To conclude, the results also showed that LLLT was able to alter the expression of MMP-9 as well as accelerate the production of collagen and increase the total percentage of collagen type III in diabetic animals. |
| 1167 | 23463906 | Wound-healing effects of low-level laser therapy in diabetic rats involve the modulation of MMP-2 and MMP-9 and the redistribution of collagen types I and III. |
| 1168 | 23463906 | The present study aimed to determine if LLLT restores the balance between mRNA expression of matrix metalloproteinases (MMP-2 and MMP-9) and also the balance between collagen types I and III during the healing process of diabetic wounds. |
| 1169 | 23463906 | Twenty-four hours after LLLT application, rats were euthanized, the scarred areas were collected for MMP-2 and MMP-9 mRNA analysis and also for histological analysis (inflammation and types I and III collagen). |
| 1170 | 23463906 | The results demonstrated that scare in untreated diabetic rats significantly increased the MMP-2 and MMP-9 expression compared with that in non-diabetic rats (p < 0.05), while LLLT significantly reduced MMP-2 and MMP-9 expression compared with that in untreated diabetic rats (p < 0.05). |
| 1171 | 23463906 | To conclude, the results also showed that LLLT was able to alter the expression of MMP-9 as well as accelerate the production of collagen and increase the total percentage of collagen type III in diabetic animals. |
| 1172 | 23549462 | We found decreased macrophages, matrix metalloproteinase-2 (MMP-2), MMP-3, MMP-8 and interleukin-6 (IL-6) concentrations (P<0.05) in the atherosclerotic plaques of the exercise group. |
| 1173 | 23549462 | Compared to both control and sedentary groups, exercise training significantly increased collagen (P<0.05), elastin (P<0.001), and tissue inhibitor of matrix metalloproteinase-2 (TIMP-2) (P<0.001) content in the atherosclerotic plaques. |
| 1174 | 23549462 | Plasma MMP-2 and MMP-3 concentrations in atherosclerotic tissues followed a similar trend. |
| 1175 | 23549462 | We found decreased macrophages, matrix metalloproteinase-2 (MMP-2), MMP-3, MMP-8 and interleukin-6 (IL-6) concentrations (P<0.05) in the atherosclerotic plaques of the exercise group. |
| 1176 | 23549462 | Compared to both control and sedentary groups, exercise training significantly increased collagen (P<0.05), elastin (P<0.001), and tissue inhibitor of matrix metalloproteinase-2 (TIMP-2) (P<0.001) content in the atherosclerotic plaques. |
| 1177 | 23549462 | Plasma MMP-2 and MMP-3 concentrations in atherosclerotic tissues followed a similar trend. |
| 1178 | 23549462 | We found decreased macrophages, matrix metalloproteinase-2 (MMP-2), MMP-3, MMP-8 and interleukin-6 (IL-6) concentrations (P<0.05) in the atherosclerotic plaques of the exercise group. |
| 1179 | 23549462 | Compared to both control and sedentary groups, exercise training significantly increased collagen (P<0.05), elastin (P<0.001), and tissue inhibitor of matrix metalloproteinase-2 (TIMP-2) (P<0.001) content in the atherosclerotic plaques. |
| 1180 | 23549462 | Plasma MMP-2 and MMP-3 concentrations in atherosclerotic tissues followed a similar trend. |
| 1181 | 23636268 | Zymography assay was utilized for the analysis of MMP-2 and MMP-9 activity. |
| 1182 | 23636268 | TACE activity was evaluated by a specific fluorimetric assay. mRNA levels of MMPs as well as TIMPs were detected using quantitative real-time polymerase chain reaction. |
| 1183 | 23636268 | The activity of MMP9 and A Disintegrin and A MetalloProtease Domain 17/TNF-Alpha Converting Enzyme (ADAM17/TACE) was significantly increased in ischemic compared to neuropathic biopsies. |
| 1184 | 23636268 | The combination of increased activity of MMP9 and ADAM17/TACE with decreased concentrations of TIMP-3 mRNA expression in ischemic diabetic foot ulcers compared to neuropathic samples suggests that the increased proteolytic environment may represent a causative factor in the ulcer progression. |
| 1185 | 23734516 | It is established that the studied tetrapeptide increases the expression of matrix metalloproteinase MMP2, MMP9, serotonin, glycoprotein CD79alpha, antiapoptotic protein Mcl1, proliferation markers PCNA and Ki67 and decreases the expression of proapoptotic protein p53 in aged pancreatic cell cultures. |
| 1186 | 23754672 | The aim of this study was to demonstrate that neutrophil gelatinase-associated lipocalin (NGAL) increased before the onset of microalbuminuria in patients with type 1 diabetes mellitus (T1DM), representing an important biochemical parameter with high sensitivity and specificity to make a precocious diagnosis of "normoalbuminuric" diabetic nephropathy (DN). |
| 1187 | 23798543 | Increased expression of the inflammatory response stimulating S100 proteins, predominantly S100A8 and S100A9 (almost tenfold), was identified. |
| 1188 | 23798543 | Matrix metalloproteinases (MMPs) MMP1, MMP2, and MMP8 were identified to be elevated in chronic wounds with significant impact on collagen degradation and tissue destruction. |
| 1189 | 23818285 | Neutrophil gelatinase-associated lipocalin, a marker of tubular dysfunction, is not increased in long-term virologically controlled patients receiving a tenofovir/emtricitabine + nevirapine regimen. |
| 1190 | 23833698 | MMPs are a large family of proteinases that remodel extracellular matrix components, and under pathological condition, its induction is considered as a negative regulator of cell survival; and in diabetes, latent MMPs are activated in the retina and its capillary cells, and activation of MMP-2 and -9 induces apoptosis of retinal capillary cells. |
| 1191 | 23833698 | This review will focus on the MMP-2 and MMP-9 in the diabetic retina with special reference to oxidative stress, mitochondria dysfunction, inflammation and angiogenesis, as well as summarizing the current information linking these proteins to pathogenesis of diabetic retinopathy. |
| 1192 | 23833698 | MMPs are a large family of proteinases that remodel extracellular matrix components, and under pathological condition, its induction is considered as a negative regulator of cell survival; and in diabetes, latent MMPs are activated in the retina and its capillary cells, and activation of MMP-2 and -9 induces apoptosis of retinal capillary cells. |
| 1193 | 23833698 | This review will focus on the MMP-2 and MMP-9 in the diabetic retina with special reference to oxidative stress, mitochondria dysfunction, inflammation and angiogenesis, as well as summarizing the current information linking these proteins to pathogenesis of diabetic retinopathy. |
| 1194 | 23884892 | VEGF secreted by hypoxic Müller cells induces MMP-2 expression and activity in endothelial cells to promote retinal neovascularization in proliferative diabetic retinopathy. |
| 1195 | 23884892 | We demonstrate that accumulation of hypoxia-inducible factor-1α in Müller cells induces the expression of VEGF, which, in turn, promotes increased MMP-2 expression and activity in neighboring endothelial cells (ECs). |
| 1196 | 23884892 | VEGF secreted by hypoxic Müller cells induces MMP-2 expression and activity in endothelial cells to promote retinal neovascularization in proliferative diabetic retinopathy. |
| 1197 | 23884892 | We demonstrate that accumulation of hypoxia-inducible factor-1α in Müller cells induces the expression of VEGF, which, in turn, promotes increased MMP-2 expression and activity in neighboring endothelial cells (ECs). |
| 1198 | 23891690 | Diabetes activates retinal matrix metalloproteinases (MMP-9 and MMP-2), damages retinal mitochondria and activates the apoptotic machinery. |
| 1199 | 23891690 | Time course of activation of cytosolic MMP-9 and MMP-2 was investigated in the retinal endothelial cells incubated in high glucose for 6-96 h, and correlated with their mitochondrial accumulation and mitochondrial damage. |
| 1200 | 23891690 | The results show that the activation of cytosolic MMP-9 and MMP-2 is an early event, which is followed by their accumulation in the mitochondria. |
| 1201 | 23891690 | Diabetes activates retinal matrix metalloproteinases (MMP-9 and MMP-2), damages retinal mitochondria and activates the apoptotic machinery. |
| 1202 | 23891690 | Time course of activation of cytosolic MMP-9 and MMP-2 was investigated in the retinal endothelial cells incubated in high glucose for 6-96 h, and correlated with their mitochondrial accumulation and mitochondrial damage. |
| 1203 | 23891690 | The results show that the activation of cytosolic MMP-9 and MMP-2 is an early event, which is followed by their accumulation in the mitochondria. |
| 1204 | 23891690 | Diabetes activates retinal matrix metalloproteinases (MMP-9 and MMP-2), damages retinal mitochondria and activates the apoptotic machinery. |
| 1205 | 23891690 | Time course of activation of cytosolic MMP-9 and MMP-2 was investigated in the retinal endothelial cells incubated in high glucose for 6-96 h, and correlated with their mitochondrial accumulation and mitochondrial damage. |
| 1206 | 23891690 | The results show that the activation of cytosolic MMP-9 and MMP-2 is an early event, which is followed by their accumulation in the mitochondria. |
| 1207 | 23949118 | Our results showed significant increases in collagen IV and fibronectin protein levels and a marked decrease in matrix metalloproteinase-2 (MMP-2) activity measured by gelatin-gel zymography alongside elevated cardiac transforming growth factor (TGF)-β level determined using ELISA or immunohistochemistry in cardiac tissues of diabetic rats compared with control. |
| 1208 | 23966807 | The aim of this study was to assess serum cystatin C and 2 renal tubular enzymes, neutrophil gelatinase associated lipocalin (NGAL) and N-acetyl-beta-D-glucosaminidase (NAG), as screening markers for early renal dysfunction in patients with type 2 diabetes mellitus (T2DM). |
| 1209 | 23983782 | Results showed that the hyperglycemia-induced GAG alterations in the cell surface perlecan as well as in the ECM indeed upregulated the expressions of IL-6, IL-8, and MCP-1 and the activities of MMP-2 and MMP-9 and downregulated the expressions of TIMP-2. |
| 1210 | 23992308 | Moreover, the protein levels of MMP-2, MMP-9, and VEGF were increased in PC cells transfected with Si-E-cad. |
| 1211 | 23992308 | Finally, the activation of the PI3K/AKT/GSK-3β signaling pathway was demonstrated to be involved in indometacin reversing HG-induced cell proliferation and invasion in PC cells. |