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Gene Information
Gene symbol: MMP9
Gene name: matrix metallopeptidase 9 (gelatinase B, 92kDa gelatinase, 92kDa type IV collagenase)
HGNC ID: 7176
Related Genes
Related Sentences
| # | PMID | Sentence |
| 1 | 34694755 | Diabetes was associated with increases in blood glucose level, 24-h urinary albumin excretion rate, glomerular basement membrane thickness, renal oxidative stress markers, and renal mRNA or protein expression of transforming growth factor-β1, fibronectin, collagen-IV, tumour necrosis factor-α and vascular endothelial growth factor-A. |
| 2 | 34694755 | Moreover, the expression of nephrin and podocin, and the mRNA expression of matrix metalloproteinase-9 were decreased in the diabetic group. |
| 3 | 31502757 | By 72 hr after IR procedure, the circulatory levels of creatinine, blood urine nitrogen and inflammatory biomarkers (interleukin [IL]-6/tumor necrosis factor [TNF]-α), and ratio of urine protein to urine creatinine were significantly higher in Group 3 than in other groups and significantly higher in Group 4 than in Groups 1 and 2, but they showed no different between Groups 1 and 2 (all p < .001). |
| 4 | 31502757 | The microscopic findings showed that the expressions of kidney injury score, cellular inflammation (MMP-9/CD14//F4/80), and fibrotic area were identical to the circulatory inflammation, whereas the integrity of podocyte components (ZO-1/synaptopodin/podocin) exhibited an opposite to circulatory inflammation among the four groups (all p < .0001). |
| 5 | 31502757 | The protein expressions of inflammatory (TNF-α/IL-1ß/NF-κB/iNOS/TRAF6/MyD88/TLR-4), apoptotic/cell death (mitochondrial Bax/cleaved caspase-3/p-53), oxidized protein, mitogen-activated protein kinase family (p-38/p-JNK/p-c-JUN), and mitochondrial-damaged biomarkers displayed a similar pattern, whereas the antiapoptotic (Bcl-2/Bcl-XL) and integrity of mitochondrial biomarkers followed an opposite trend to circulatory inflammation among the four groups (all p < .001). |
| 6 | 30770219 | Both serum from patients with chronic kidney disease and exogenous advanced oxidation protein products induced Wnt1 and Wnt7a expression, activated β-catenin, and reduced expression of podocyte-specific markers in vitro and in vivo. |
| 7 | 30770219 | Blockade of Wnt signaling by Klotho or knockdown of β-catenin by shRNA in podocytes abolished β-catenin activation and the upregulation of fibronectin, desmin, matrix metalloproteinase-9, and Snail1 triggered by advanced oxidation protein products. |
| 8 | 30770219 | The action of Wnt/β-catenin was dependent on the receptor of advanced glycation end products (RAGE)-mediated NADPH oxidase induction, reactive oxygen species generation, and nuclear factor-κB activation. |
| 9 | 30125361 | Van Gogh-like 2 (Vangl2) is a key PCP protein that is required for the normal differentiation of kidney glomeruli and tubules. |
| 10 | 30125361 | Van Gogh-like 2 (Vangl2) is a key PCP protein that is required for the normal differentiation of kidney glomeruli and tubules. |
| 11 | 30125361 | In each proteinuric model, genetic deletion of Vangl2 in podocytes was associated with an increased ratio of active-MMP9 to inactive MMP9, an enzyme involved in tissue remodelling. |
| 12 | 30125361 | In each proteinuric model, genetic deletion of Vangl2 in podocytes was associated with an increased ratio of active-MMP9 to inactive MMP9, an enzyme involved in tissue remodelling. |
| 13 | 30125361 | These observations support the conclusion that Vangl2 modulates glomerular injury, at least in part by acting as a brake on MMP9, a potentially harmful endogenous enzyme. © 2018 The Authors. |
| 14 | 30125361 | These observations support the conclusion that Vangl2 modulates glomerular injury, at least in part by acting as a brake on MMP9, a potentially harmful endogenous enzyme. © 2018 The Authors. |
| 15 | 29367812 | We noted a reduction of insulin-like growth factor 1 receptor (IGFR1) expression, decrease in extracellular signal-regulated kinase (ERK) activation, decrease in reactive oxygen species (ROS), and decrease in cleaved-caspase 3 expression. |
| 16 | 29367812 | We found an increase in [3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide] (MTT) and an increase in matrix metalloproteinases (MMP-2 and MMP-9) activity. |
| 17 | 29367812 | In isolated podocytes, we confirmed reduction of ERα expression in conjunction with a decrease in IGFR1 expression, ERK and increase of MMP-2 similar to that of our in vitro treatment with RSV. |
| 18 | 29245956 | Protein expressions of inflammatory (MMP-9/TNF-α/NF-κB/IL-1ß/ICAM-1), oxidative-stress (NOX-1/NOX-2/oxidized protein), apoptotic (mitochondrial-Bax/cleaved-caspase-3/cleaved-PARP) and fibrotic/DNA-damaged (Smad3/TGF-ß/γ-H2AX) biomarkers showed an identical pattern, whereas anti-fibrotic (BMP-2/Smad1/5), anti-apoptotic/endothelial-integrity (Bcl-2/eNOS) and podocyte-integrity (ZO-1/p-cadherin) biomarkers exhibited an opposite pattern of kidney-injury score among the six groups (all P>0.0001). |
| 19 | 29245956 | Cellular expressions of inflammatory (CD14/CD68) and glomerulus/tubular-injury (WT-1/KIM-1) biomarkers displayed an identical pattern, whereas glomerulus/podocyte-component (dystroglycan/nephrin/ZO-1/fibronectin/p-cadherin) biomarkers showed an opposite kidney-injury score among the six groups (all P<0.0001). |
| 20 | 28645189 | The potential role of retinoic acid receptor α on glomerulosclerosis in rats and podocytes injury is associated with the induction of MMP2 and MMP9. |
| 21 | 28645189 | The potential role of retinoic acid receptor α on glomerulosclerosis in rats and podocytes injury is associated with the induction of MMP2 and MMP9. |
| 22 | 28645189 | The potential role of retinoic acid receptor α on glomerulosclerosis in rats and podocytes injury is associated with the induction of MMP2 and MMP9. |
| 23 | 28645189 | Further experiments indicated that RARα inhibited the accumulation of TGF-β1, α-smooth muscle actin, collagen IV, and fibronectin, while it induced MMP2 and MMP9 excessive expression in podocytes in vitro. |
| 24 | 28645189 | Further experiments indicated that RARα inhibited the accumulation of TGF-β1, α-smooth muscle actin, collagen IV, and fibronectin, while it induced MMP2 and MMP9 excessive expression in podocytes in vitro. |
| 25 | 28645189 | Further experiments indicated that RARα inhibited the accumulation of TGF-β1, α-smooth muscle actin, collagen IV, and fibronectin, while it induced MMP2 and MMP9 excessive expression in podocytes in vitro. |
| 26 | 28645189 | RARα improved the renal function and attenuated the progression of GS that was associated with the over-expression of MMP2 and MMP9. |
| 27 | 28645189 | RARα improved the renal function and attenuated the progression of GS that was associated with the over-expression of MMP2 and MMP9. |
| 28 | 28645189 | RARα improved the renal function and attenuated the progression of GS that was associated with the over-expression of MMP2 and MMP9. |
| 29 | 28560004 | Protein expressions of inflammation (IL-1β/MMP-9), oxidative stress (NOX-1/NOX-2/oxidized protein, angiotensin-II receptor), apoptosis (Bax, cleaved caspase-3/PARP), fibrosis (Smad3/TGF-β), and kidney injured (KIM-1/FSP-1) markers showed an identical pattern, whereas anti-fibrosis (Smad5/BMP-2) indices exhibited an opposite pattern compared to that of creatinine level among all groups (all p < 0.01). |
| 30 | 28560004 | Cellular expressions of inflammation (CD14/CD68), DNA-damage (γ-H2AX, CD90/XRCC1) and proximal-renal tubule (KIM-1) biomarkers displayed an identical pattern, whereas podocyte-integrity markers (podocin/ZO-1/p-cadherin/synaptopodin) showed a pattern opposite to that of creatinine level among all groups (all p < 0.001). |
| 31 | 28419530 | In addition, Na+/K+ ATPase subunit α-2 and matrix metalloproteinase 9 levels were significantly downregulated after PSTK overexpression, but significantly upregulated upon PSTK knockdown. |
| 32 | 28360429 | Interleukin (IL)-20, a proinflammatory cytokine of the IL-10 family, is involved in acute and chronic renal failure. |
| 33 | 28360429 | We found that IL-20 and its receptor IL-20R1 were upregulated in the kidneys of mice and rats with STZ-induced diabetes. |
| 34 | 28360429 | In vitro, IL-20 induced MMP-9, MCP-1, TGF-β1 and VEGF expression in podocytes. |
| 35 | 28360429 | In addition, IL-20 induced apoptosis in podocytes by activating caspase-8. |
| 36 | 28337255 | The kidney protein expressions of inflammation (TNF-α/NF-κB/MMP-9/iNOS/RANTES), oxidative stress (NOX-1/NOX-2/NOX-4/oxidized protein), apoptosis (cleaved caspase-3/cleaved PARP/Bax), DNA-damaged marker (γ-H2AX) and fibrosis (p-mad3/TFG-β) showed identical patterns of creatinine level, whereas kidney protein expressions of GLP-1R showed a progressive increase from SC to CRS-Mel-Ex4 (all P<0.0001). |
| 37 | 28337255 | Cellular expressions of inflammatory (CD14/CD68), DNA/kidney-damaged (γ-H2AX/KIM-1) and podocyte/renal tubule dysfunction signaling (β-catenin/Wnt1/Wnt4) biomarkers in kidney tissue exhibited an identical pattern of creatinine level (all P<0.0001). |
| 38 | 27704688 | FAK contributes to proteinuria in hypercholesterolaemic rats and modulates podocyte F-actin re-organization via activating p38 in response to ox-LDL. |
| 39 | 27704688 | FAK is also an adaptor protein initiating cascades of intracellular signals including c-Src, Rho GTPase and mitogen-activated protein kinase (MAPK). |
| 40 | 27704688 | Our cell culture data revealed oxidized low-density lipoprotein (ox-LDL) triggered hyper-phosphorylation of FAK and p38, ectopic expression of cellular markers (manifested as decreased WT1, podocin and NEPH1, and increased vimentin and mmp9), and re-arrangement of F-actin filaments with enhanced cell motility; these mutations were significantly rectified by FAK shRNA. |
| 41 | 27704688 | Notably, pre-treatment of p38 inhibitor did not alter FAK activation, albeit its deletion of p38 hyper-activity and attenuation of cellular abnormalities, demonstrating that p38 acted as a downstream effector of FAK signalling and ox-LDL damaged podocytes in a FAK/p38-dependent manner. |
| 42 | 27704688 | This was further identified by animal data that p38 activation was also abrogated by TAE226 treatment in hypercholesterolaemic rats, suggesting that FAK/p38 axis might also be involved in in vivo events. |
| 43 | 27070919 | CD154 Induces Matrix Metalloproteinase-9 Secretion in Human Podocytes. |
| 44 | 27070919 | CD154 Induces Matrix Metalloproteinase-9 Secretion in Human Podocytes. |
| 45 | 27070919 | CD154 Induces Matrix Metalloproteinase-9 Secretion in Human Podocytes. |
| 46 | 27070919 | The CD40/CD154 signaling pathway modulates matrix remodeling through the synthesis of MMPs and tissue inhibitors of MMPs. |
| 47 | 27070919 | The CD40/CD154 signaling pathway modulates matrix remodeling through the synthesis of MMPs and tissue inhibitors of MMPs. |
| 48 | 27070919 | The CD40/CD154 signaling pathway modulates matrix remodeling through the synthesis of MMPs and tissue inhibitors of MMPs. |
| 49 | 27070919 | Here we studied, the impact of the CD154/CD40 pathway on MMP-9 expression by cultured human podocytes. |
| 50 | 27070919 | Here we studied, the impact of the CD154/CD40 pathway on MMP-9 expression by cultured human podocytes. |
| 51 | 27070919 | Here we studied, the impact of the CD154/CD40 pathway on MMP-9 expression by cultured human podocytes. |
| 52 | 27070919 | The role of CD40/CD154 was evaluated upon exposure of podocytes to recombinant human CD154 (rhCD154) or activated platelet supernatants from healthy human subjects. |
| 53 | 27070919 | The role of CD40/CD154 was evaluated upon exposure of podocytes to recombinant human CD154 (rhCD154) or activated platelet supernatants from healthy human subjects. |
| 54 | 27070919 | The role of CD40/CD154 was evaluated upon exposure of podocytes to recombinant human CD154 (rhCD154) or activated platelet supernatants from healthy human subjects. |
| 55 | 27070919 | Our results underscore a potential role for platelets through the CD40/CD154 signaling pathway in the control of GBM synthesis and degradation, via its regulatory role on MMP-9 production. |
| 56 | 27070919 | Our results underscore a potential role for platelets through the CD40/CD154 signaling pathway in the control of GBM synthesis and degradation, via its regulatory role on MMP-9 production. |
| 57 | 27070919 | Our results underscore a potential role for platelets through the CD40/CD154 signaling pathway in the control of GBM synthesis and degradation, via its regulatory role on MMP-9 production. |
| 58 | 26671966 | These biomarkers included 1) podocyte glycoproteins nephrin and podocalyxin, 2) matrix metallopeptidase (MMP)-2 and MMP-9 and their inhibitor tissue inhibitor of metalloproteinase-2, 3) inflammatory molecules and cytokines soluble VCAM-1, TNF-α, soluble TNF receptor receptor-1, IL-6, IL-8, IL-10, and IL-18, and 4) kidney injury biomarkers neutrophil gelatinase-associated lipocalin and kidney injury molecule-1. |
| 59 | 26671966 | These biomarkers included 1) podocyte glycoproteins nephrin and podocalyxin, 2) matrix metallopeptidase (MMP)-2 and MMP-9 and their inhibitor tissue inhibitor of metalloproteinase-2, 3) inflammatory molecules and cytokines soluble VCAM-1, TNF-α, soluble TNF receptor receptor-1, IL-6, IL-8, IL-10, and IL-18, and 4) kidney injury biomarkers neutrophil gelatinase-associated lipocalin and kidney injury molecule-1. |
| 60 | 26671966 | We found that, first, urine levels of nephrin, MMP-2, MMP-9, and kidney injury molecule-1 were significantly higher before delivery in severe preeclampsia than normotensive groups. |
| 61 | 26671966 | We found that, first, urine levels of nephrin, MMP-2, MMP-9, and kidney injury molecule-1 were significantly higher before delivery in severe preeclampsia than normotensive groups. |
| 62 | 26671966 | Second, soluble VCAM-1, soluble TNF receptor-1, and neutrophil gelatinase-associated lipocalin levels were significantly increased in the severe preeclampsia group compared with the normotensive control group before delivery, but levels of these molecules were significantly reduced in postpartum specimens in both groups. |
| 63 | 26671966 | Second, soluble VCAM-1, soluble TNF receptor-1, and neutrophil gelatinase-associated lipocalin levels were significantly increased in the severe preeclampsia group compared with the normotensive control group before delivery, but levels of these molecules were significantly reduced in postpartum specimens in both groups. |
| 64 | 26671966 | Third, IL-6 and IL-8 levels were not different between preeclampsia and normotensive groups but significantly increased in pregnancy complicated with chronic hypertension. |
| 65 | 26671966 | Third, IL-6 and IL-8 levels were not different between preeclampsia and normotensive groups but significantly increased in pregnancy complicated with chronic hypertension. |
| 66 | 26671966 | Finally, tissue inhibitor of metalloproteinase-2 and IL-18 levels were not different among the study groups before delivery but were significantly reduced in postpartum specimens from normotensive controls. |
| 67 | 26671966 | Finally, tissue inhibitor of metalloproteinase-2 and IL-18 levels were not different among the study groups before delivery but were significantly reduced in postpartum specimens from normotensive controls. |
| 68 | 26309060 | Immunohistochemical microscopic findings of the expressions of FSP-1 and WT-1 (two glomerular damage indicators) and KIM-1 and snail (two renal tubular-damaged indicators) showed an identical pattern, whereas the expressions of ZO-1, p-cadherin, podocin, dystroglycan, fibronectin, and synaptopodin (six indices of glomerular integrity) demonstrated an opposite pattern compared to that of PIS among five groups (all P < 0.001). |
| 69 | 26309060 | Protein expressions of inflammatory (TNF-α/NF-κB/MMP-9) and oxidative stress (NOX-1, NOX-2, oxidized protein) biomarkers exhibited an identical pattern to that of PIS among five groups (all P < 0.001). |
| 70 | 25902289 | Angiotensin II (Ang II), an important member of the renin-angiotensin system, stimulates the accumulation of extracellular matrix components in glomerular disease; however, the exact mechanisms involved remain to be elucidated. |
| 71 | 25902289 | Angiotensin II (Ang II), an important member of the renin-angiotensin system, stimulates the accumulation of extracellular matrix components in glomerular disease; however, the exact mechanisms involved remain to be elucidated. |
| 72 | 25902289 | Angiotensin II (Ang II), an important member of the renin-angiotensin system, stimulates the accumulation of extracellular matrix components in glomerular disease; however, the exact mechanisms involved remain to be elucidated. |
| 73 | 25902289 | Angiotensin II (Ang II), an important member of the renin-angiotensin system, stimulates the accumulation of extracellular matrix components in glomerular disease; however, the exact mechanisms involved remain to be elucidated. |
| 74 | 25902289 | Angiotensin II (Ang II), an important member of the renin-angiotensin system, stimulates the accumulation of extracellular matrix components in glomerular disease; however, the exact mechanisms involved remain to be elucidated. |
| 75 | 25902289 | Angiotensin II (Ang II), an important member of the renin-angiotensin system, stimulates the accumulation of extracellular matrix components in glomerular disease; however, the exact mechanisms involved remain to be elucidated. |
| 76 | 25902289 | The protein levels of Notch1, Notch intracellular domain 1 (NICD1), hairy and enhancer of split-1 (Hes1), matrix metalloproteinase (MMP)-2, MMP-9, transforming growth factor-β1 (TGF-β1), type IV collagen and laminin were determined by western blot analysis. |
| 77 | 25902289 | The protein levels of Notch1, Notch intracellular domain 1 (NICD1), hairy and enhancer of split-1 (Hes1), matrix metalloproteinase (MMP)-2, MMP-9, transforming growth factor-β1 (TGF-β1), type IV collagen and laminin were determined by western blot analysis. |
| 78 | 25902289 | The protein levels of Notch1, Notch intracellular domain 1 (NICD1), hairy and enhancer of split-1 (Hes1), matrix metalloproteinase (MMP)-2, MMP-9, transforming growth factor-β1 (TGF-β1), type IV collagen and laminin were determined by western blot analysis. |
| 79 | 25902289 | The protein levels of Notch1, Notch intracellular domain 1 (NICD1), hairy and enhancer of split-1 (Hes1), matrix metalloproteinase (MMP)-2, MMP-9, transforming growth factor-β1 (TGF-β1), type IV collagen and laminin were determined by western blot analysis. |
| 80 | 25902289 | The protein levels of Notch1, Notch intracellular domain 1 (NICD1), hairy and enhancer of split-1 (Hes1), matrix metalloproteinase (MMP)-2, MMP-9, transforming growth factor-β1 (TGF-β1), type IV collagen and laminin were determined by western blot analysis. |
| 81 | 25902289 | The protein levels of Notch1, Notch intracellular domain 1 (NICD1), hairy and enhancer of split-1 (Hes1), matrix metalloproteinase (MMP)-2, MMP-9, transforming growth factor-β1 (TGF-β1), type IV collagen and laminin were determined by western blot analysis. |
| 82 | 25902289 | The Notch1, Hes1, MMP-2, MMP-9, TGF-β1, type IV collagen and laminin mRNA levels were detected by RT-PCR. |
| 83 | 25902289 | The Notch1, Hes1, MMP-2, MMP-9, TGF-β1, type IV collagen and laminin mRNA levels were detected by RT-PCR. |
| 84 | 25902289 | The Notch1, Hes1, MMP-2, MMP-9, TGF-β1, type IV collagen and laminin mRNA levels were detected by RT-PCR. |
| 85 | 25902289 | The Notch1, Hes1, MMP-2, MMP-9, TGF-β1, type IV collagen and laminin mRNA levels were detected by RT-PCR. |
| 86 | 25902289 | The Notch1, Hes1, MMP-2, MMP-9, TGF-β1, type IV collagen and laminin mRNA levels were detected by RT-PCR. |
| 87 | 25902289 | The Notch1, Hes1, MMP-2, MMP-9, TGF-β1, type IV collagen and laminin mRNA levels were detected by RT-PCR. |
| 88 | 25902289 | The MMP-2 and MMP-9 activity was measured using a cell active fluorescence assay kit. |
| 89 | 25902289 | The MMP-2 and MMP-9 activity was measured using a cell active fluorescence assay kit. |
| 90 | 25902289 | The MMP-2 and MMP-9 activity was measured using a cell active fluorescence assay kit. |
| 91 | 25902289 | The MMP-2 and MMP-9 activity was measured using a cell active fluorescence assay kit. |
| 92 | 25902289 | The MMP-2 and MMP-9 activity was measured using a cell active fluorescence assay kit. |
| 93 | 25902289 | The MMP-2 and MMP-9 activity was measured using a cell active fluorescence assay kit. |
| 94 | 25902289 | Our results revealed that Ang II upregulated Notch1, NICD1, Hes1, TGF-β1, type IV collagen and laminin expression and downregulated MMP-2 and MMP-9 expression in the cultured podocytes. |
| 95 | 25902289 | Our results revealed that Ang II upregulated Notch1, NICD1, Hes1, TGF-β1, type IV collagen and laminin expression and downregulated MMP-2 and MMP-9 expression in the cultured podocytes. |
| 96 | 25902289 | Our results revealed that Ang II upregulated Notch1, NICD1, Hes1, TGF-β1, type IV collagen and laminin expression and downregulated MMP-2 and MMP-9 expression in the cultured podocytes. |
| 97 | 25902289 | Our results revealed that Ang II upregulated Notch1, NICD1, Hes1, TGF-β1, type IV collagen and laminin expression and downregulated MMP-2 and MMP-9 expression in the cultured podocytes. |
| 98 | 25902289 | Our results revealed that Ang II upregulated Notch1, NICD1, Hes1, TGF-β1, type IV collagen and laminin expression and downregulated MMP-2 and MMP-9 expression in the cultured podocytes. |
| 99 | 25902289 | Our results revealed that Ang II upregulated Notch1, NICD1, Hes1, TGF-β1, type IV collagen and laminin expression and downregulated MMP-2 and MMP-9 expression in the cultured podocytes. |
| 100 | 25902289 | The inhibition of the Notch pathway by sh-Notch1 or GSI increased MMP-2 and MMP-9 expression, decreased the TGF-β1 level and suppressed type IV collagen and laminin expression. |
| 101 | 25902289 | The inhibition of the Notch pathway by sh-Notch1 or GSI increased MMP-2 and MMP-9 expression, decreased the TGF-β1 level and suppressed type IV collagen and laminin expression. |
| 102 | 25902289 | The inhibition of the Notch pathway by sh-Notch1 or GSI increased MMP-2 and MMP-9 expression, decreased the TGF-β1 level and suppressed type IV collagen and laminin expression. |
| 103 | 25902289 | The inhibition of the Notch pathway by sh-Notch1 or GSI increased MMP-2 and MMP-9 expression, decreased the TGF-β1 level and suppressed type IV collagen and laminin expression. |
| 104 | 25902289 | The inhibition of the Notch pathway by sh-Notch1 or GSI increased MMP-2 and MMP-9 expression, decreased the TGF-β1 level and suppressed type IV collagen and laminin expression. |
| 105 | 25902289 | The inhibition of the Notch pathway by sh-Notch1 or GSI increased MMP-2 and MMP-9 expression, decreased the TGF-β1 level and suppressed type IV collagen and laminin expression. |
| 106 | 25902289 | The inhibition of the Notch pathway by sh-Notch1 or GSI also increased MMP-2 and MMP-9 activity, and decreased TGF-β1 levels, type IV collagen levels and laminin secretion. |
| 107 | 25902289 | The inhibition of the Notch pathway by sh-Notch1 or GSI also increased MMP-2 and MMP-9 activity, and decreased TGF-β1 levels, type IV collagen levels and laminin secretion. |
| 108 | 25902289 | The inhibition of the Notch pathway by sh-Notch1 or GSI also increased MMP-2 and MMP-9 activity, and decreased TGF-β1 levels, type IV collagen levels and laminin secretion. |
| 109 | 25902289 | The inhibition of the Notch pathway by sh-Notch1 or GSI also increased MMP-2 and MMP-9 activity, and decreased TGF-β1 levels, type IV collagen levels and laminin secretion. |
| 110 | 25902289 | The inhibition of the Notch pathway by sh-Notch1 or GSI also increased MMP-2 and MMP-9 activity, and decreased TGF-β1 levels, type IV collagen levels and laminin secretion. |
| 111 | 25902289 | The inhibition of the Notch pathway by sh-Notch1 or GSI also increased MMP-2 and MMP-9 activity, and decreased TGF-β1 levels, type IV collagen levels and laminin secretion. |
| 112 | 25849723 | Matrix metalloproteinase-9 expression is enhanced in renal parietal epithelial cells of zucker diabetic Fatty rats and is induced by albumin in in vitro primary parietal cell culture. |
| 113 | 25849723 | Matrix metalloproteinase-9 expression is enhanced in renal parietal epithelial cells of zucker diabetic Fatty rats and is induced by albumin in in vitro primary parietal cell culture. |
| 114 | 25849723 | Matrix metalloproteinase-9 expression is enhanced in renal parietal epithelial cells of zucker diabetic Fatty rats and is induced by albumin in in vitro primary parietal cell culture. |
| 115 | 25849723 | Matrix metalloproteinase-9 expression is enhanced in renal parietal epithelial cells of zucker diabetic Fatty rats and is induced by albumin in in vitro primary parietal cell culture. |
| 116 | 25849723 | Matrix metalloproteinase-9 expression is enhanced in renal parietal epithelial cells of zucker diabetic Fatty rats and is induced by albumin in in vitro primary parietal cell culture. |
| 117 | 25849723 | Matrix metalloproteinase-9 expression is enhanced in renal parietal epithelial cells of zucker diabetic Fatty rats and is induced by albumin in in vitro primary parietal cell culture. |
| 118 | 25849723 | Matrix metalloproteinase-9 expression is enhanced in renal parietal epithelial cells of zucker diabetic Fatty rats and is induced by albumin in in vitro primary parietal cell culture. |
| 119 | 25849723 | Matrix metalloproteinase-9 expression is enhanced in renal parietal epithelial cells of zucker diabetic Fatty rats and is induced by albumin in in vitro primary parietal cell culture. |
| 120 | 25849723 | Matrix metalloproteinase-9 expression is enhanced in renal parietal epithelial cells of zucker diabetic Fatty rats and is induced by albumin in in vitro primary parietal cell culture. |
| 121 | 25849723 | Matrix metalloproteinase-9 expression is enhanced in renal parietal epithelial cells of zucker diabetic Fatty rats and is induced by albumin in in vitro primary parietal cell culture. |
| 122 | 25849723 | Matrix metalloproteinase-9 expression is enhanced in renal parietal epithelial cells of zucker diabetic Fatty rats and is induced by albumin in in vitro primary parietal cell culture. |
| 123 | 25849723 | As a subfamily of matrix metalloproteinases (MMPs), gelatinases including MMP-2 and MMP-9 play an important role in remodeling and homeostasis of the extracellular matrix. |
| 124 | 25849723 | As a subfamily of matrix metalloproteinases (MMPs), gelatinases including MMP-2 and MMP-9 play an important role in remodeling and homeostasis of the extracellular matrix. |
| 125 | 25849723 | As a subfamily of matrix metalloproteinases (MMPs), gelatinases including MMP-2 and MMP-9 play an important role in remodeling and homeostasis of the extracellular matrix. |
| 126 | 25849723 | As a subfamily of matrix metalloproteinases (MMPs), gelatinases including MMP-2 and MMP-9 play an important role in remodeling and homeostasis of the extracellular matrix. |
| 127 | 25849723 | As a subfamily of matrix metalloproteinases (MMPs), gelatinases including MMP-2 and MMP-9 play an important role in remodeling and homeostasis of the extracellular matrix. |
| 128 | 25849723 | As a subfamily of matrix metalloproteinases (MMPs), gelatinases including MMP-2 and MMP-9 play an important role in remodeling and homeostasis of the extracellular matrix. |
| 129 | 25849723 | As a subfamily of matrix metalloproteinases (MMPs), gelatinases including MMP-2 and MMP-9 play an important role in remodeling and homeostasis of the extracellular matrix. |
| 130 | 25849723 | As a subfamily of matrix metalloproteinases (MMPs), gelatinases including MMP-2 and MMP-9 play an important role in remodeling and homeostasis of the extracellular matrix. |
| 131 | 25849723 | As a subfamily of matrix metalloproteinases (MMPs), gelatinases including MMP-2 and MMP-9 play an important role in remodeling and homeostasis of the extracellular matrix. |
| 132 | 25849723 | As a subfamily of matrix metalloproteinases (MMPs), gelatinases including MMP-2 and MMP-9 play an important role in remodeling and homeostasis of the extracellular matrix. |
| 133 | 25849723 | As a subfamily of matrix metalloproteinases (MMPs), gelatinases including MMP-2 and MMP-9 play an important role in remodeling and homeostasis of the extracellular matrix. |
| 134 | 25849723 | This study investigated whether and how MMP-9 expression and activity were changed in glomerular epithelial cells upon albumin overload. |
| 135 | 25849723 | This study investigated whether and how MMP-9 expression and activity were changed in glomerular epithelial cells upon albumin overload. |
| 136 | 25849723 | This study investigated whether and how MMP-9 expression and activity were changed in glomerular epithelial cells upon albumin overload. |
| 137 | 25849723 | This study investigated whether and how MMP-9 expression and activity were changed in glomerular epithelial cells upon albumin overload. |
| 138 | 25849723 | This study investigated whether and how MMP-9 expression and activity were changed in glomerular epithelial cells upon albumin overload. |
| 139 | 25849723 | This study investigated whether and how MMP-9 expression and activity were changed in glomerular epithelial cells upon albumin overload. |
| 140 | 25849723 | This study investigated whether and how MMP-9 expression and activity were changed in glomerular epithelial cells upon albumin overload. |
| 141 | 25849723 | This study investigated whether and how MMP-9 expression and activity were changed in glomerular epithelial cells upon albumin overload. |
| 142 | 25849723 | This study investigated whether and how MMP-9 expression and activity were changed in glomerular epithelial cells upon albumin overload. |
| 143 | 25849723 | This study investigated whether and how MMP-9 expression and activity were changed in glomerular epithelial cells upon albumin overload. |
| 144 | 25849723 | This study investigated whether and how MMP-9 expression and activity were changed in glomerular epithelial cells upon albumin overload. |
| 145 | 25849723 | Increased glomerular MMP-9 staining was mainly observed in hyperplastic parietal epithelial cells (PECs) expressing claudin-1 in the diabetic kidneys. |
| 146 | 25849723 | Increased glomerular MMP-9 staining was mainly observed in hyperplastic parietal epithelial cells (PECs) expressing claudin-1 in the diabetic kidneys. |
| 147 | 25849723 | Increased glomerular MMP-9 staining was mainly observed in hyperplastic parietal epithelial cells (PECs) expressing claudin-1 in the diabetic kidneys. |
| 148 | 25849723 | Increased glomerular MMP-9 staining was mainly observed in hyperplastic parietal epithelial cells (PECs) expressing claudin-1 in the diabetic kidneys. |
| 149 | 25849723 | Increased glomerular MMP-9 staining was mainly observed in hyperplastic parietal epithelial cells (PECs) expressing claudin-1 in the diabetic kidneys. |
| 150 | 25849723 | Increased glomerular MMP-9 staining was mainly observed in hyperplastic parietal epithelial cells (PECs) expressing claudin-1 in the diabetic kidneys. |
| 151 | 25849723 | Increased glomerular MMP-9 staining was mainly observed in hyperplastic parietal epithelial cells (PECs) expressing claudin-1 in the diabetic kidneys. |
| 152 | 25849723 | Increased glomerular MMP-9 staining was mainly observed in hyperplastic parietal epithelial cells (PECs) expressing claudin-1 in the diabetic kidneys. |
| 153 | 25849723 | Increased glomerular MMP-9 staining was mainly observed in hyperplastic parietal epithelial cells (PECs) expressing claudin-1 in the diabetic kidneys. |
| 154 | 25849723 | Increased glomerular MMP-9 staining was mainly observed in hyperplastic parietal epithelial cells (PECs) expressing claudin-1 in the diabetic kidneys. |
| 155 | 25849723 | Increased glomerular MMP-9 staining was mainly observed in hyperplastic parietal epithelial cells (PECs) expressing claudin-1 in the diabetic kidneys. |
| 156 | 25849723 | Interestingly, increased parietal MMP-9 was often accompanied by decreased staining for podocyte markers (nephrin and podocalyxin) in the sclerotic area of affected glomeruli in diabetic rats. |
| 157 | 25849723 | Interestingly, increased parietal MMP-9 was often accompanied by decreased staining for podocyte markers (nephrin and podocalyxin) in the sclerotic area of affected glomeruli in diabetic rats. |
| 158 | 25849723 | Interestingly, increased parietal MMP-9 was often accompanied by decreased staining for podocyte markers (nephrin and podocalyxin) in the sclerotic area of affected glomeruli in diabetic rats. |
| 159 | 25849723 | Interestingly, increased parietal MMP-9 was often accompanied by decreased staining for podocyte markers (nephrin and podocalyxin) in the sclerotic area of affected glomeruli in diabetic rats. |
| 160 | 25849723 | Interestingly, increased parietal MMP-9 was often accompanied by decreased staining for podocyte markers (nephrin and podocalyxin) in the sclerotic area of affected glomeruli in diabetic rats. |
| 161 | 25849723 | Interestingly, increased parietal MMP-9 was often accompanied by decreased staining for podocyte markers (nephrin and podocalyxin) in the sclerotic area of affected glomeruli in diabetic rats. |
| 162 | 25849723 | Interestingly, increased parietal MMP-9 was often accompanied by decreased staining for podocyte markers (nephrin and podocalyxin) in the sclerotic area of affected glomeruli in diabetic rats. |
| 163 | 25849723 | Interestingly, increased parietal MMP-9 was often accompanied by decreased staining for podocyte markers (nephrin and podocalyxin) in the sclerotic area of affected glomeruli in diabetic rats. |
| 164 | 25849723 | Interestingly, increased parietal MMP-9 was often accompanied by decreased staining for podocyte markers (nephrin and podocalyxin) in the sclerotic area of affected glomeruli in diabetic rats. |
| 165 | 25849723 | Interestingly, increased parietal MMP-9 was often accompanied by decreased staining for podocyte markers (nephrin and podocalyxin) in the sclerotic area of affected glomeruli in diabetic rats. |
| 166 | 25849723 | Interestingly, increased parietal MMP-9 was often accompanied by decreased staining for podocyte markers (nephrin and podocalyxin) in the sclerotic area of affected glomeruli in diabetic rats. |
| 167 | 25849723 | Additionally, urinary excretion of podocyte marker proteins was significantly increased in association with the levels of MMP-9 and albumin in the urine of diabetic animals. |
| 168 | 25849723 | Additionally, urinary excretion of podocyte marker proteins was significantly increased in association with the levels of MMP-9 and albumin in the urine of diabetic animals. |
| 169 | 25849723 | Additionally, urinary excretion of podocyte marker proteins was significantly increased in association with the levels of MMP-9 and albumin in the urine of diabetic animals. |
| 170 | 25849723 | Additionally, urinary excretion of podocyte marker proteins was significantly increased in association with the levels of MMP-9 and albumin in the urine of diabetic animals. |
| 171 | 25849723 | Additionally, urinary excretion of podocyte marker proteins was significantly increased in association with the levels of MMP-9 and albumin in the urine of diabetic animals. |
| 172 | 25849723 | Additionally, urinary excretion of podocyte marker proteins was significantly increased in association with the levels of MMP-9 and albumin in the urine of diabetic animals. |
| 173 | 25849723 | Additionally, urinary excretion of podocyte marker proteins was significantly increased in association with the levels of MMP-9 and albumin in the urine of diabetic animals. |
| 174 | 25849723 | Additionally, urinary excretion of podocyte marker proteins was significantly increased in association with the levels of MMP-9 and albumin in the urine of diabetic animals. |
| 175 | 25849723 | Additionally, urinary excretion of podocyte marker proteins was significantly increased in association with the levels of MMP-9 and albumin in the urine of diabetic animals. |
| 176 | 25849723 | Additionally, urinary excretion of podocyte marker proteins was significantly increased in association with the levels of MMP-9 and albumin in the urine of diabetic animals. |
| 177 | 25849723 | Additionally, urinary excretion of podocyte marker proteins was significantly increased in association with the levels of MMP-9 and albumin in the urine of diabetic animals. |
| 178 | 25849723 | To evaluate the direct effect of albumin on expression and activity of MMP-9, primary cultured rat glomerular PECs were incubated with rat serum albumin (0.25 - 1 mg/ml) for 24 - 48 hrs. |
| 179 | 25849723 | To evaluate the direct effect of albumin on expression and activity of MMP-9, primary cultured rat glomerular PECs were incubated with rat serum albumin (0.25 - 1 mg/ml) for 24 - 48 hrs. |
| 180 | 25849723 | To evaluate the direct effect of albumin on expression and activity of MMP-9, primary cultured rat glomerular PECs were incubated with rat serum albumin (0.25 - 1 mg/ml) for 24 - 48 hrs. |
| 181 | 25849723 | To evaluate the direct effect of albumin on expression and activity of MMP-9, primary cultured rat glomerular PECs were incubated with rat serum albumin (0.25 - 1 mg/ml) for 24 - 48 hrs. |
| 182 | 25849723 | To evaluate the direct effect of albumin on expression and activity of MMP-9, primary cultured rat glomerular PECs were incubated with rat serum albumin (0.25 - 1 mg/ml) for 24 - 48 hrs. |
| 183 | 25849723 | To evaluate the direct effect of albumin on expression and activity of MMP-9, primary cultured rat glomerular PECs were incubated with rat serum albumin (0.25 - 1 mg/ml) for 24 - 48 hrs. |
| 184 | 25849723 | To evaluate the direct effect of albumin on expression and activity of MMP-9, primary cultured rat glomerular PECs were incubated with rat serum albumin (0.25 - 1 mg/ml) for 24 - 48 hrs. |
| 185 | 25849723 | To evaluate the direct effect of albumin on expression and activity of MMP-9, primary cultured rat glomerular PECs were incubated with rat serum albumin (0.25 - 1 mg/ml) for 24 - 48 hrs. |
| 186 | 25849723 | To evaluate the direct effect of albumin on expression and activity of MMP-9, primary cultured rat glomerular PECs were incubated with rat serum albumin (0.25 - 1 mg/ml) for 24 - 48 hrs. |
| 187 | 25849723 | To evaluate the direct effect of albumin on expression and activity of MMP-9, primary cultured rat glomerular PECs were incubated with rat serum albumin (0.25 - 1 mg/ml) for 24 - 48 hrs. |
| 188 | 25849723 | To evaluate the direct effect of albumin on expression and activity of MMP-9, primary cultured rat glomerular PECs were incubated with rat serum albumin (0.25 - 1 mg/ml) for 24 - 48 hrs. |
| 189 | 25849723 | MMP-9 mRNA levels were significantly increased following albumin treatment. |
| 190 | 25849723 | MMP-9 mRNA levels were significantly increased following albumin treatment. |
| 191 | 25849723 | MMP-9 mRNA levels were significantly increased following albumin treatment. |
| 192 | 25849723 | MMP-9 mRNA levels were significantly increased following albumin treatment. |
| 193 | 25849723 | MMP-9 mRNA levels were significantly increased following albumin treatment. |
| 194 | 25849723 | MMP-9 mRNA levels were significantly increased following albumin treatment. |
| 195 | 25849723 | MMP-9 mRNA levels were significantly increased following albumin treatment. |
| 196 | 25849723 | MMP-9 mRNA levels were significantly increased following albumin treatment. |
| 197 | 25849723 | MMP-9 mRNA levels were significantly increased following albumin treatment. |
| 198 | 25849723 | MMP-9 mRNA levels were significantly increased following albumin treatment. |
| 199 | 25849723 | MMP-9 mRNA levels were significantly increased following albumin treatment. |
| 200 | 25849723 | Meanwhile, albumin administration resulted in a dose-dependent increase in MMP-9 protein and activity in culture supernatants of PECs. |
| 201 | 25849723 | Meanwhile, albumin administration resulted in a dose-dependent increase in MMP-9 protein and activity in culture supernatants of PECs. |
| 202 | 25849723 | Meanwhile, albumin administration resulted in a dose-dependent increase in MMP-9 protein and activity in culture supernatants of PECs. |
| 203 | 25849723 | Meanwhile, albumin administration resulted in a dose-dependent increase in MMP-9 protein and activity in culture supernatants of PECs. |
| 204 | 25849723 | Meanwhile, albumin administration resulted in a dose-dependent increase in MMP-9 protein and activity in culture supernatants of PECs. |
| 205 | 25849723 | Meanwhile, albumin administration resulted in a dose-dependent increase in MMP-9 protein and activity in culture supernatants of PECs. |
| 206 | 25849723 | Meanwhile, albumin administration resulted in a dose-dependent increase in MMP-9 protein and activity in culture supernatants of PECs. |
| 207 | 25849723 | Meanwhile, albumin administration resulted in a dose-dependent increase in MMP-9 protein and activity in culture supernatants of PECs. |
| 208 | 25849723 | Meanwhile, albumin administration resulted in a dose-dependent increase in MMP-9 protein and activity in culture supernatants of PECs. |
| 209 | 25849723 | Meanwhile, albumin administration resulted in a dose-dependent increase in MMP-9 protein and activity in culture supernatants of PECs. |
| 210 | 25849723 | Meanwhile, albumin administration resulted in a dose-dependent increase in MMP-9 protein and activity in culture supernatants of PECs. |
| 211 | 25849723 | Moreover, albumin activated p44/42 mitogen-activated protein kinase (MAPK) in PECs. |
| 212 | 25849723 | Moreover, albumin activated p44/42 mitogen-activated protein kinase (MAPK) in PECs. |
| 213 | 25849723 | Moreover, albumin activated p44/42 mitogen-activated protein kinase (MAPK) in PECs. |
| 214 | 25849723 | Moreover, albumin activated p44/42 mitogen-activated protein kinase (MAPK) in PECs. |
| 215 | 25849723 | Moreover, albumin activated p44/42 mitogen-activated protein kinase (MAPK) in PECs. |
| 216 | 25849723 | Moreover, albumin activated p44/42 mitogen-activated protein kinase (MAPK) in PECs. |
| 217 | 25849723 | Moreover, albumin activated p44/42 mitogen-activated protein kinase (MAPK) in PECs. |
| 218 | 25849723 | Moreover, albumin activated p44/42 mitogen-activated protein kinase (MAPK) in PECs. |
| 219 | 25849723 | Moreover, albumin activated p44/42 mitogen-activated protein kinase (MAPK) in PECs. |
| 220 | 25849723 | Moreover, albumin activated p44/42 mitogen-activated protein kinase (MAPK) in PECs. |
| 221 | 25849723 | Moreover, albumin activated p44/42 mitogen-activated protein kinase (MAPK) in PECs. |
| 222 | 25849723 | Inhibition of p44/42 MAPK suppressed albumin-induced MMP-9 secretion from glomerular PECs. |
| 223 | 25849723 | Inhibition of p44/42 MAPK suppressed albumin-induced MMP-9 secretion from glomerular PECs. |
| 224 | 25849723 | Inhibition of p44/42 MAPK suppressed albumin-induced MMP-9 secretion from glomerular PECs. |
| 225 | 25849723 | Inhibition of p44/42 MAPK suppressed albumin-induced MMP-9 secretion from glomerular PECs. |
| 226 | 25849723 | Inhibition of p44/42 MAPK suppressed albumin-induced MMP-9 secretion from glomerular PECs. |
| 227 | 25849723 | Inhibition of p44/42 MAPK suppressed albumin-induced MMP-9 secretion from glomerular PECs. |
| 228 | 25849723 | Inhibition of p44/42 MAPK suppressed albumin-induced MMP-9 secretion from glomerular PECs. |
| 229 | 25849723 | Inhibition of p44/42 MAPK suppressed albumin-induced MMP-9 secretion from glomerular PECs. |
| 230 | 25849723 | Inhibition of p44/42 MAPK suppressed albumin-induced MMP-9 secretion from glomerular PECs. |
| 231 | 25849723 | Inhibition of p44/42 MAPK suppressed albumin-induced MMP-9 secretion from glomerular PECs. |
| 232 | 25849723 | Inhibition of p44/42 MAPK suppressed albumin-induced MMP-9 secretion from glomerular PECs. |
| 233 | 25849723 | Albumin overload may induce MMP-9 expression and secretion by PECs via the activation of p44/42 MAPK pathway. |
| 234 | 25849723 | Albumin overload may induce MMP-9 expression and secretion by PECs via the activation of p44/42 MAPK pathway. |
| 235 | 25849723 | Albumin overload may induce MMP-9 expression and secretion by PECs via the activation of p44/42 MAPK pathway. |
| 236 | 25849723 | Albumin overload may induce MMP-9 expression and secretion by PECs via the activation of p44/42 MAPK pathway. |
| 237 | 25849723 | Albumin overload may induce MMP-9 expression and secretion by PECs via the activation of p44/42 MAPK pathway. |
| 238 | 25849723 | Albumin overload may induce MMP-9 expression and secretion by PECs via the activation of p44/42 MAPK pathway. |
| 239 | 25849723 | Albumin overload may induce MMP-9 expression and secretion by PECs via the activation of p44/42 MAPK pathway. |
| 240 | 25849723 | Albumin overload may induce MMP-9 expression and secretion by PECs via the activation of p44/42 MAPK pathway. |
| 241 | 25849723 | Albumin overload may induce MMP-9 expression and secretion by PECs via the activation of p44/42 MAPK pathway. |
| 242 | 25849723 | Albumin overload may induce MMP-9 expression and secretion by PECs via the activation of p44/42 MAPK pathway. |
| 243 | 25849723 | Albumin overload may induce MMP-9 expression and secretion by PECs via the activation of p44/42 MAPK pathway. |
| 244 | 24915008 | Analysis of glomerular mRNA from both models demonstrates significant induction of MMP-9, MMP-10, MMP-12, MMPs linked to GBM destruction in Alport disease models, as well as the pro-inflammatory cytokine IL-6. |
| 245 | 24915008 | Analysis of glomerular mRNA from both models demonstrates significant induction of MMP-9, MMP-10, MMP-12, MMPs linked to GBM destruction in Alport disease models, as well as the pro-inflammatory cytokine IL-6. |
| 246 | 24915008 | Analysis of glomerular mRNA from both models demonstrates significant induction of MMP-9, MMP-10, MMP-12, MMPs linked to GBM destruction in Alport disease models, as well as the pro-inflammatory cytokine IL-6. |
| 247 | 24915008 | SiRNA knockdown of FAK in cultured podocytes significantly reduced expression of MMP-9, MMP-10 and IL-6, but not MMP-12. |
| 248 | 24915008 | SiRNA knockdown of FAK in cultured podocytes significantly reduced expression of MMP-9, MMP-10 and IL-6, but not MMP-12. |
| 249 | 24915008 | SiRNA knockdown of FAK in cultured podocytes significantly reduced expression of MMP-9, MMP-10 and IL-6, but not MMP-12. |
| 250 | 24915008 | Glomerular expression of MMP-9, MMP-10 and MMP-12 mRNAs was significantly reduced in TAE226 treated animals. |
| 251 | 24915008 | Glomerular expression of MMP-9, MMP-10 and MMP-12 mRNAs was significantly reduced in TAE226 treated animals. |
| 252 | 24915008 | Glomerular expression of MMP-9, MMP-10 and MMP-12 mRNAs was significantly reduced in TAE226 treated animals. |
| 253 | 24694005 | Potential signal pathway of all-trans retinoic acid for MMP-2 and MMP-9 expression in injury podocyte induced by adriamycin. |
| 254 | 24694005 | Potential signal pathway of all-trans retinoic acid for MMP-2 and MMP-9 expression in injury podocyte induced by adriamycin. |
| 255 | 24694005 | Potential signal pathway of all-trans retinoic acid for MMP-2 and MMP-9 expression in injury podocyte induced by adriamycin. |
| 256 | 24694005 | Potential signal pathway of all-trans retinoic acid for MMP-2 and MMP-9 expression in injury podocyte induced by adriamycin. |
| 257 | 24694005 | Potential signal pathway of all-trans retinoic acid for MMP-2 and MMP-9 expression in injury podocyte induced by adriamycin. |
| 258 | 24694005 | Potential signal pathway of all-trans retinoic acid for MMP-2 and MMP-9 expression in injury podocyte induced by adriamycin. |
| 259 | 24694005 | Potential signal pathway of all-trans retinoic acid for MMP-2 and MMP-9 expression in injury podocyte induced by adriamycin. |
| 260 | 24694005 | Potential signal pathway of all-trans retinoic acid for MMP-2 and MMP-9 expression in injury podocyte induced by adriamycin. |
| 261 | 24694005 | All-trans-retinoic acid (ATRA) can regulate some specific genes expression in various tissue and cells via nuclear retinoic acid receptors (RARs), including three subtypes: retinoic acid receptor-alpha (RAR-α), retinoic acid receptor-beta (RAR-β) and retinoic acid receptor-gamma (RAR-γ). |
| 262 | 24694005 | All-trans-retinoic acid (ATRA) can regulate some specific genes expression in various tissue and cells via nuclear retinoic acid receptors (RARs), including three subtypes: retinoic acid receptor-alpha (RAR-α), retinoic acid receptor-beta (RAR-β) and retinoic acid receptor-gamma (RAR-γ). |
| 263 | 24694005 | All-trans-retinoic acid (ATRA) can regulate some specific genes expression in various tissue and cells via nuclear retinoic acid receptors (RARs), including three subtypes: retinoic acid receptor-alpha (RAR-α), retinoic acid receptor-beta (RAR-β) and retinoic acid receptor-gamma (RAR-γ). |
| 264 | 24694005 | All-trans-retinoic acid (ATRA) can regulate some specific genes expression in various tissue and cells via nuclear retinoic acid receptors (RARs), including three subtypes: retinoic acid receptor-alpha (RAR-α), retinoic acid receptor-beta (RAR-β) and retinoic acid receptor-gamma (RAR-γ). |
| 265 | 24694005 | All-trans-retinoic acid (ATRA) can regulate some specific genes expression in various tissue and cells via nuclear retinoic acid receptors (RARs), including three subtypes: retinoic acid receptor-alpha (RAR-α), retinoic acid receptor-beta (RAR-β) and retinoic acid receptor-gamma (RAR-γ). |
| 266 | 24694005 | All-trans-retinoic acid (ATRA) can regulate some specific genes expression in various tissue and cells via nuclear retinoic acid receptors (RARs), including three subtypes: retinoic acid receptor-alpha (RAR-α), retinoic acid receptor-beta (RAR-β) and retinoic acid receptor-gamma (RAR-γ). |
| 267 | 24694005 | All-trans-retinoic acid (ATRA) can regulate some specific genes expression in various tissue and cells via nuclear retinoic acid receptors (RARs), including three subtypes: retinoic acid receptor-alpha (RAR-α), retinoic acid receptor-beta (RAR-β) and retinoic acid receptor-gamma (RAR-γ). |
| 268 | 24694005 | All-trans-retinoic acid (ATRA) can regulate some specific genes expression in various tissue and cells via nuclear retinoic acid receptors (RARs), including three subtypes: retinoic acid receptor-alpha (RAR-α), retinoic acid receptor-beta (RAR-β) and retinoic acid receptor-gamma (RAR-γ). |
| 269 | 24694005 | This study was performed to study the potential signal pathway of ATRA in the expression of matrix metalloproteinases-2 (MMP-2) and matrix metalloproteinases-9 (MMP-9) in injury podocyte. |
| 270 | 24694005 | This study was performed to study the potential signal pathway of ATRA in the expression of matrix metalloproteinases-2 (MMP-2) and matrix metalloproteinases-9 (MMP-9) in injury podocyte. |
| 271 | 24694005 | This study was performed to study the potential signal pathway of ATRA in the expression of matrix metalloproteinases-2 (MMP-2) and matrix metalloproteinases-9 (MMP-9) in injury podocyte. |
| 272 | 24694005 | This study was performed to study the potential signal pathway of ATRA in the expression of matrix metalloproteinases-2 (MMP-2) and matrix metalloproteinases-9 (MMP-9) in injury podocyte. |
| 273 | 24694005 | This study was performed to study the potential signal pathway of ATRA in the expression of matrix metalloproteinases-2 (MMP-2) and matrix metalloproteinases-9 (MMP-9) in injury podocyte. |
| 274 | 24694005 | This study was performed to study the potential signal pathway of ATRA in the expression of matrix metalloproteinases-2 (MMP-2) and matrix metalloproteinases-9 (MMP-9) in injury podocyte. |
| 275 | 24694005 | This study was performed to study the potential signal pathway of ATRA in the expression of matrix metalloproteinases-2 (MMP-2) and matrix metalloproteinases-9 (MMP-9) in injury podocyte. |
| 276 | 24694005 | This study was performed to study the potential signal pathway of ATRA in the expression of matrix metalloproteinases-2 (MMP-2) and matrix metalloproteinases-9 (MMP-9) in injury podocyte. |
| 277 | 24694005 | MMP-2 and MMP-9 enzymic activity was detected using the gelatin zymography method. |
| 278 | 24694005 | MMP-2 and MMP-9 enzymic activity was detected using the gelatin zymography method. |
| 279 | 24694005 | MMP-2 and MMP-9 enzymic activity was detected using the gelatin zymography method. |
| 280 | 24694005 | MMP-2 and MMP-9 enzymic activity was detected using the gelatin zymography method. |
| 281 | 24694005 | MMP-2 and MMP-9 enzymic activity was detected using the gelatin zymography method. |
| 282 | 24694005 | MMP-2 and MMP-9 enzymic activity was detected using the gelatin zymography method. |
| 283 | 24694005 | MMP-2 and MMP-9 enzymic activity was detected using the gelatin zymography method. |
| 284 | 24694005 | MMP-2 and MMP-9 enzymic activity was detected using the gelatin zymography method. |
| 285 | 24694005 | Protein and mRNA expressions of MMP-2, MMP-9, RAR-α, RAR-β and RAR-γ were measured by western-blot and real-time RT-PCR. |
| 286 | 24694005 | Protein and mRNA expressions of MMP-2, MMP-9, RAR-α, RAR-β and RAR-γ were measured by western-blot and real-time RT-PCR. |
| 287 | 24694005 | Protein and mRNA expressions of MMP-2, MMP-9, RAR-α, RAR-β and RAR-γ were measured by western-blot and real-time RT-PCR. |
| 288 | 24694005 | Protein and mRNA expressions of MMP-2, MMP-9, RAR-α, RAR-β and RAR-γ were measured by western-blot and real-time RT-PCR. |
| 289 | 24694005 | Protein and mRNA expressions of MMP-2, MMP-9, RAR-α, RAR-β and RAR-γ were measured by western-blot and real-time RT-PCR. |
| 290 | 24694005 | Protein and mRNA expressions of MMP-2, MMP-9, RAR-α, RAR-β and RAR-γ were measured by western-blot and real-time RT-PCR. |
| 291 | 24694005 | Protein and mRNA expressions of MMP-2, MMP-9, RAR-α, RAR-β and RAR-γ were measured by western-blot and real-time RT-PCR. |
| 292 | 24694005 | Protein and mRNA expressions of MMP-2, MMP-9, RAR-α, RAR-β and RAR-γ were measured by western-blot and real-time RT-PCR. |
| 293 | 24694005 | Enzymatic activity of MMP-2 and MMP-9 in group AA was significantly enhanced compared to AI group after ATRA-treated 24 h (p < 0.05). |
| 294 | 24694005 | Enzymatic activity of MMP-2 and MMP-9 in group AA was significantly enhanced compared to AI group after ATRA-treated 24 h (p < 0.05). |
| 295 | 24694005 | Enzymatic activity of MMP-2 and MMP-9 in group AA was significantly enhanced compared to AI group after ATRA-treated 24 h (p < 0.05). |
| 296 | 24694005 | Enzymatic activity of MMP-2 and MMP-9 in group AA was significantly enhanced compared to AI group after ATRA-treated 24 h (p < 0.05). |
| 297 | 24694005 | Enzymatic activity of MMP-2 and MMP-9 in group AA was significantly enhanced compared to AI group after ATRA-treated 24 h (p < 0.05). |
| 298 | 24694005 | Enzymatic activity of MMP-2 and MMP-9 in group AA was significantly enhanced compared to AI group after ATRA-treated 24 h (p < 0.05). |
| 299 | 24694005 | Enzymatic activity of MMP-2 and MMP-9 in group AA was significantly enhanced compared to AI group after ATRA-treated 24 h (p < 0.05). |
| 300 | 24694005 | Enzymatic activity of MMP-2 and MMP-9 in group AA was significantly enhanced compared to AI group after ATRA-treated 24 h (p < 0.05). |
| 301 | 24694005 | The protein and mRNA expressions of MMP-2/MMP-9 in group AA were significantly increased than those in group AI at both 12 and 24 h time points (p < 0.05). |
| 302 | 24694005 | The protein and mRNA expressions of MMP-2/MMP-9 in group AA were significantly increased than those in group AI at both 12 and 24 h time points (p < 0.05). |
| 303 | 24694005 | The protein and mRNA expressions of MMP-2/MMP-9 in group AA were significantly increased than those in group AI at both 12 and 24 h time points (p < 0.05). |
| 304 | 24694005 | The protein and mRNA expressions of MMP-2/MMP-9 in group AA were significantly increased than those in group AI at both 12 and 24 h time points (p < 0.05). |
| 305 | 24694005 | The protein and mRNA expressions of MMP-2/MMP-9 in group AA were significantly increased than those in group AI at both 12 and 24 h time points (p < 0.05). |
| 306 | 24694005 | The protein and mRNA expressions of MMP-2/MMP-9 in group AA were significantly increased than those in group AI at both 12 and 24 h time points (p < 0.05). |
| 307 | 24694005 | The protein and mRNA expressions of MMP-2/MMP-9 in group AA were significantly increased than those in group AI at both 12 and 24 h time points (p < 0.05). |
| 308 | 24694005 | The protein and mRNA expressions of MMP-2/MMP-9 in group AA were significantly increased than those in group AI at both 12 and 24 h time points (p < 0.05). |
| 309 | 24694005 | RAR-α protein level was positively correlated with MMP-2 or MMP-9 protein expression (p < 0.05), and RAR-γ protein level was also positively correlated with MMP-2 or MMP-9 protein expression (p < 0.05). |
| 310 | 24694005 | RAR-α protein level was positively correlated with MMP-2 or MMP-9 protein expression (p < 0.05), and RAR-γ protein level was also positively correlated with MMP-2 or MMP-9 protein expression (p < 0.05). |
| 311 | 24694005 | RAR-α protein level was positively correlated with MMP-2 or MMP-9 protein expression (p < 0.05), and RAR-γ protein level was also positively correlated with MMP-2 or MMP-9 protein expression (p < 0.05). |
| 312 | 24694005 | RAR-α protein level was positively correlated with MMP-2 or MMP-9 protein expression (p < 0.05), and RAR-γ protein level was also positively correlated with MMP-2 or MMP-9 protein expression (p < 0.05). |
| 313 | 24694005 | RAR-α protein level was positively correlated with MMP-2 or MMP-9 protein expression (p < 0.05), and RAR-γ protein level was also positively correlated with MMP-2 or MMP-9 protein expression (p < 0.05). |
| 314 | 24694005 | RAR-α protein level was positively correlated with MMP-2 or MMP-9 protein expression (p < 0.05), and RAR-γ protein level was also positively correlated with MMP-2 or MMP-9 protein expression (p < 0.05). |
| 315 | 24694005 | RAR-α protein level was positively correlated with MMP-2 or MMP-9 protein expression (p < 0.05), and RAR-γ protein level was also positively correlated with MMP-2 or MMP-9 protein expression (p < 0.05). |
| 316 | 24694005 | RAR-α protein level was positively correlated with MMP-2 or MMP-9 protein expression (p < 0.05), and RAR-γ protein level was also positively correlated with MMP-2 or MMP-9 protein expression (p < 0.05). |
| 317 | 24694005 | In conclusion, ATRA may increase expression of MMP-2 and MMP-9 by the potential signal pathway of RAR-α and RAR-γ in injury podocyte induced by adriamycin, but not RAR-β. |
| 318 | 24694005 | In conclusion, ATRA may increase expression of MMP-2 and MMP-9 by the potential signal pathway of RAR-α and RAR-γ in injury podocyte induced by adriamycin, but not RAR-β. |
| 319 | 24694005 | In conclusion, ATRA may increase expression of MMP-2 and MMP-9 by the potential signal pathway of RAR-α and RAR-γ in injury podocyte induced by adriamycin, but not RAR-β. |
| 320 | 24694005 | In conclusion, ATRA may increase expression of MMP-2 and MMP-9 by the potential signal pathway of RAR-α and RAR-γ in injury podocyte induced by adriamycin, but not RAR-β. |
| 321 | 24694005 | In conclusion, ATRA may increase expression of MMP-2 and MMP-9 by the potential signal pathway of RAR-α and RAR-γ in injury podocyte induced by adriamycin, but not RAR-β. |
| 322 | 24694005 | In conclusion, ATRA may increase expression of MMP-2 and MMP-9 by the potential signal pathway of RAR-α and RAR-γ in injury podocyte induced by adriamycin, but not RAR-β. |
| 323 | 24694005 | In conclusion, ATRA may increase expression of MMP-2 and MMP-9 by the potential signal pathway of RAR-α and RAR-γ in injury podocyte induced by adriamycin, but not RAR-β. |
| 324 | 24694005 | In conclusion, ATRA may increase expression of MMP-2 and MMP-9 by the potential signal pathway of RAR-α and RAR-γ in injury podocyte induced by adriamycin, but not RAR-β. |
| 325 | 24670409 | In cultured podocytes, various cytokines related to diabetic nephropathy including TGF-β1, TNF-α, and VEGF stimulated MMP-9 secretion. |
| 326 | 24670409 | In cultured podocytes, various cytokines related to diabetic nephropathy including TGF-β1, TNF-α, and VEGF stimulated MMP-9 secretion. |
| 327 | 24670409 | MMP-9 also interrupted podocyte cell integrity, promoted podocyte monolayer permeability to albumin, and extracellular matrix protein synthesis. |
| 328 | 24670409 | MMP-9 also interrupted podocyte cell integrity, promoted podocyte monolayer permeability to albumin, and extracellular matrix protein synthesis. |
| 329 | 24578133 | The HIV-1 transactivator of transcription (Tat), combined with fibroblast growth factor-2 (FGF-2), can induce the dedifferentiation and proliferation of cultured human podocytes. |
| 330 | 24578133 | Furthermore, we identified arginines in the basic domain (RKKRRQRRR) of Tat as essential for (1) targeting Tat to LRs, (2) Tat-mediated increases in the expression of Rho-A and matrix metalloproteinase-9 in LRs, and (3) Tat-mediated enhancement of FGF-2 signaling in human podocytes and HIV-transgenic mouse kidneys and the exacerbation of renal lesions in these mice. |
| 331 | 23954273 | Excess podocyte semaphorin-3A leads to glomerular disease involving plexinA1-nephrin interaction. |
| 332 | 23954273 | Mechanistically, excess Sema3a induces dysregulation of nephrin, matrix metalloproteinase 9, and αvβ3 integrin in vivo. |
| 333 | 23954273 | We identified a novel direct interaction between the Sema3a signaling receptor plexinA1 and nephrin, linking extracellular Sema3a signals to the slit-diaphragm signaling complex. |
| 334 | 23954273 | Our findings demonstrate a crosstalk between Sema3a and nephrin signaling pathways that is functionally relevant both in vivo and in vitro. |
| 335 | 23710468 | Compared to KK-a/a controls, 26-week-old KK-A (y) mice had elevated HbA1c, insulin, leptin, triglycerides, and cholesterol, and Unx further elevated these markers of metabolic dysregulation. |
| 336 | 23710468 | Consistent with functional and histological evidence of increased injury, fibrotic (fibronectin 1, MMP9, and TGF β 1) and inflammatory (IL-6, CD68) genes were markedly upregulated in Unx KK-A (y) mice, while podocyte markers (nephrin and podocin) were significantly decreased. |
| 337 | 21832980 | Canonical Wnt/β-catenin signaling mediates transforming growth factor-β1-driven podocyte injury and proteinuria. |
| 338 | 21832980 | Ectopic expression of Wnt1 or β-catenin mimicked TGF-β1, induced Snail1, and suppressed nephrin expression. |
| 339 | 21832980 | The Wnt antagonist, Dickkopf-1, blocked TGF-β1-induced β-catenin activation, Snail1 induction, and nephrin suppression. |
| 340 | 21832980 | In vivo, ectopic expression of TGF-β1 induced Wnt1 expression, activated β-catenin, and upregulated Wnt target genes such as Snail1, MMP-7, MMP-9, desmin, Fsp1, and PAI-1 in mouse glomeruli, leading to podocyte injury and albuminuria. |
| 341 | 21832980 | Consistently, concomitant expression of Dickkopf-1 gene abolished β-catenin activation, inhibited TGF-β1-triggered Wnt target gene expression, and mitigated albuminuria. |
| 342 | 20960272 | Disease and gender-specific dysregulation of NGAL and MMP-9 in type 1 diabetes mellitus. |
| 343 | 20960272 | Disease and gender-specific dysregulation of NGAL and MMP-9 in type 1 diabetes mellitus. |
| 344 | 20960272 | Disease and gender-specific dysregulation of NGAL and MMP-9 in type 1 diabetes mellitus. |
| 345 | 20960272 | Disease and gender-specific dysregulation of NGAL and MMP-9 in type 1 diabetes mellitus. |
| 346 | 20960272 | Disease and gender-specific dysregulation of NGAL and MMP-9 in type 1 diabetes mellitus. |
| 347 | 20960272 | Disease and gender-specific dysregulation of NGAL and MMP-9 in type 1 diabetes mellitus. |
| 348 | 20960272 | Disease and gender-specific dysregulation of NGAL and MMP-9 in type 1 diabetes mellitus. |
| 349 | 20960272 | Neutrophil gelatinase-associated lipocalin (NGAL), a biomarker of renal injury, can bind matrix metalloproteinase-9 (MMP-9) and inhibit its degradation, thereby sustaining MMP-9 proteolytic activity. |
| 350 | 20960272 | Neutrophil gelatinase-associated lipocalin (NGAL), a biomarker of renal injury, can bind matrix metalloproteinase-9 (MMP-9) and inhibit its degradation, thereby sustaining MMP-9 proteolytic activity. |
| 351 | 20960272 | Neutrophil gelatinase-associated lipocalin (NGAL), a biomarker of renal injury, can bind matrix metalloproteinase-9 (MMP-9) and inhibit its degradation, thereby sustaining MMP-9 proteolytic activity. |
| 352 | 20960272 | Neutrophil gelatinase-associated lipocalin (NGAL), a biomarker of renal injury, can bind matrix metalloproteinase-9 (MMP-9) and inhibit its degradation, thereby sustaining MMP-9 proteolytic activity. |
| 353 | 20960272 | Neutrophil gelatinase-associated lipocalin (NGAL), a biomarker of renal injury, can bind matrix metalloproteinase-9 (MMP-9) and inhibit its degradation, thereby sustaining MMP-9 proteolytic activity. |
| 354 | 20960272 | Neutrophil gelatinase-associated lipocalin (NGAL), a biomarker of renal injury, can bind matrix metalloproteinase-9 (MMP-9) and inhibit its degradation, thereby sustaining MMP-9 proteolytic activity. |
| 355 | 20960272 | Neutrophil gelatinase-associated lipocalin (NGAL), a biomarker of renal injury, can bind matrix metalloproteinase-9 (MMP-9) and inhibit its degradation, thereby sustaining MMP-9 proteolytic activity. |
| 356 | 20960272 | Our objective was to determine whether NGAL/MMP-9 dysregulation might contribute to or serve as a biomarker of diabetic nephropathy in type 1 DM (T1DM). |
| 357 | 20960272 | Our objective was to determine whether NGAL/MMP-9 dysregulation might contribute to or serve as a biomarker of diabetic nephropathy in type 1 DM (T1DM). |
| 358 | 20960272 | Our objective was to determine whether NGAL/MMP-9 dysregulation might contribute to or serve as a biomarker of diabetic nephropathy in type 1 DM (T1DM). |
| 359 | 20960272 | Our objective was to determine whether NGAL/MMP-9 dysregulation might contribute to or serve as a biomarker of diabetic nephropathy in type 1 DM (T1DM). |
| 360 | 20960272 | Our objective was to determine whether NGAL/MMP-9 dysregulation might contribute to or serve as a biomarker of diabetic nephropathy in type 1 DM (T1DM). |
| 361 | 20960272 | Our objective was to determine whether NGAL/MMP-9 dysregulation might contribute to or serve as a biomarker of diabetic nephropathy in type 1 DM (T1DM). |
| 362 | 20960272 | Our objective was to determine whether NGAL/MMP-9 dysregulation might contribute to or serve as a biomarker of diabetic nephropathy in type 1 DM (T1DM). |
| 363 | 20960272 | Plasma MMP-9, and urine NGAL and MMP-9 concentrations were measured in 121 T1DM and 55 control subjects and examined relative to indicators of glycemia, renal function, and degree of albuminuria. |
| 364 | 20960272 | Plasma MMP-9, and urine NGAL and MMP-9 concentrations were measured in 121 T1DM and 55 control subjects and examined relative to indicators of glycemia, renal function, and degree of albuminuria. |
| 365 | 20960272 | Plasma MMP-9, and urine NGAL and MMP-9 concentrations were measured in 121 T1DM and 55 control subjects and examined relative to indicators of glycemia, renal function, and degree of albuminuria. |
| 366 | 20960272 | Plasma MMP-9, and urine NGAL and MMP-9 concentrations were measured in 121 T1DM and 55 control subjects and examined relative to indicators of glycemia, renal function, and degree of albuminuria. |
| 367 | 20960272 | Plasma MMP-9, and urine NGAL and MMP-9 concentrations were measured in 121 T1DM and 55 control subjects and examined relative to indicators of glycemia, renal function, and degree of albuminuria. |
| 368 | 20960272 | Plasma MMP-9, and urine NGAL and MMP-9 concentrations were measured in 121 T1DM and 55 control subjects and examined relative to indicators of glycemia, renal function, and degree of albuminuria. |
| 369 | 20960272 | Plasma MMP-9, and urine NGAL and MMP-9 concentrations were measured in 121 T1DM and 55 control subjects and examined relative to indicators of glycemia, renal function, and degree of albuminuria. |
| 370 | 20960272 | T1DM was associated with a significant increase in urinary excretion of both NGAL and MMP-9, and urine NGAL:Cr (NGAL corrected to urine creatinine) and urine MMP-9:Cr concentrations were highly correlated with each other. |
| 371 | 20960272 | T1DM was associated with a significant increase in urinary excretion of both NGAL and MMP-9, and urine NGAL:Cr (NGAL corrected to urine creatinine) and urine MMP-9:Cr concentrations were highly correlated with each other. |
| 372 | 20960272 | T1DM was associated with a significant increase in urinary excretion of both NGAL and MMP-9, and urine NGAL:Cr (NGAL corrected to urine creatinine) and urine MMP-9:Cr concentrations were highly correlated with each other. |
| 373 | 20960272 | T1DM was associated with a significant increase in urinary excretion of both NGAL and MMP-9, and urine NGAL:Cr (NGAL corrected to urine creatinine) and urine MMP-9:Cr concentrations were highly correlated with each other. |
| 374 | 20960272 | T1DM was associated with a significant increase in urinary excretion of both NGAL and MMP-9, and urine NGAL:Cr (NGAL corrected to urine creatinine) and urine MMP-9:Cr concentrations were highly correlated with each other. |
| 375 | 20960272 | T1DM was associated with a significant increase in urinary excretion of both NGAL and MMP-9, and urine NGAL:Cr (NGAL corrected to urine creatinine) and urine MMP-9:Cr concentrations were highly correlated with each other. |
| 376 | 20960272 | T1DM was associated with a significant increase in urinary excretion of both NGAL and MMP-9, and urine NGAL:Cr (NGAL corrected to urine creatinine) and urine MMP-9:Cr concentrations were highly correlated with each other. |
| 377 | 20960272 | Plasma MMP-9, urine MMP-9, and urine NGAL concentrations were significantly higher in females compared to males, and urine MMP-9:Cr concentrations displayed a menstrual cycle specific pattern. |
| 378 | 20960272 | Plasma MMP-9, urine MMP-9, and urine NGAL concentrations were significantly higher in females compared to males, and urine MMP-9:Cr concentrations displayed a menstrual cycle specific pattern. |
| 379 | 20960272 | Plasma MMP-9, urine MMP-9, and urine NGAL concentrations were significantly higher in females compared to males, and urine MMP-9:Cr concentrations displayed a menstrual cycle specific pattern. |
| 380 | 20960272 | Plasma MMP-9, urine MMP-9, and urine NGAL concentrations were significantly higher in females compared to males, and urine MMP-9:Cr concentrations displayed a menstrual cycle specific pattern. |
| 381 | 20960272 | Plasma MMP-9, urine MMP-9, and urine NGAL concentrations were significantly higher in females compared to males, and urine MMP-9:Cr concentrations displayed a menstrual cycle specific pattern. |
| 382 | 20960272 | Plasma MMP-9, urine MMP-9, and urine NGAL concentrations were significantly higher in females compared to males, and urine MMP-9:Cr concentrations displayed a menstrual cycle specific pattern. |
| 383 | 20960272 | Plasma MMP-9, urine MMP-9, and urine NGAL concentrations were significantly higher in females compared to males, and urine MMP-9:Cr concentrations displayed a menstrual cycle specific pattern. |
| 384 | 20960272 | Increased urinary excretion of NGAL and MMP-9 supports a role for NGAL/MMP-9 dysregulation in renal dysfunction; moreover, gender-specific differences could support a gender contribution to pathological mechanisms or susceptibility for the development of renal complications in diabetes mellitus. |
| 385 | 20960272 | Increased urinary excretion of NGAL and MMP-9 supports a role for NGAL/MMP-9 dysregulation in renal dysfunction; moreover, gender-specific differences could support a gender contribution to pathological mechanisms or susceptibility for the development of renal complications in diabetes mellitus. |
| 386 | 20960272 | Increased urinary excretion of NGAL and MMP-9 supports a role for NGAL/MMP-9 dysregulation in renal dysfunction; moreover, gender-specific differences could support a gender contribution to pathological mechanisms or susceptibility for the development of renal complications in diabetes mellitus. |
| 387 | 20960272 | Increased urinary excretion of NGAL and MMP-9 supports a role for NGAL/MMP-9 dysregulation in renal dysfunction; moreover, gender-specific differences could support a gender contribution to pathological mechanisms or susceptibility for the development of renal complications in diabetes mellitus. |
| 388 | 20960272 | Increased urinary excretion of NGAL and MMP-9 supports a role for NGAL/MMP-9 dysregulation in renal dysfunction; moreover, gender-specific differences could support a gender contribution to pathological mechanisms or susceptibility for the development of renal complications in diabetes mellitus. |
| 389 | 20960272 | Increased urinary excretion of NGAL and MMP-9 supports a role for NGAL/MMP-9 dysregulation in renal dysfunction; moreover, gender-specific differences could support a gender contribution to pathological mechanisms or susceptibility for the development of renal complications in diabetes mellitus. |
| 390 | 20960272 | Increased urinary excretion of NGAL and MMP-9 supports a role for NGAL/MMP-9 dysregulation in renal dysfunction; moreover, gender-specific differences could support a gender contribution to pathological mechanisms or susceptibility for the development of renal complications in diabetes mellitus. |
| 391 | 20505657 | ILK expression was induced in mouse podocytes by various injurious stimuli known to cause proteinuria including TGF-beta1, adriamycin, puromycin, and high ambient glucose. |
| 392 | 20505657 | ILK expression was induced in mouse podocytes by various injurious stimuli known to cause proteinuria including TGF-beta1, adriamycin, puromycin, and high ambient glucose. |
| 393 | 20505657 | Ectopic expression of ILK in podocytes decreased levels of the epithelial markers nephrin and ZO-1, induced mesenchymal markers such as desmin, fibronectin, matrix metalloproteinase-9 (MMP-9), and alpha-smooth muscle actin (alpha-SMA), promoted cell migration, and increased the paracellular albumin flux across podocyte monolayers. |
| 394 | 20505657 | Ectopic expression of ILK in podocytes decreased levels of the epithelial markers nephrin and ZO-1, induced mesenchymal markers such as desmin, fibronectin, matrix metalloproteinase-9 (MMP-9), and alpha-smooth muscle actin (alpha-SMA), promoted cell migration, and increased the paracellular albumin flux across podocyte monolayers. |
| 395 | 20505657 | ILK also induced Snail, a key transcription factor mediating epithelial-mesenchymal transition (EMT). |
| 396 | 20505657 | ILK also induced Snail, a key transcription factor mediating epithelial-mesenchymal transition (EMT). |
| 397 | 20505657 | Blockade of ILK activity with a highly selective small molecule inhibitor reduced Snail induction and preserved podocyte phenotypes following TGF-beta1 or adriamycin stimulation. |
| 398 | 20505657 | Blockade of ILK activity with a highly selective small molecule inhibitor reduced Snail induction and preserved podocyte phenotypes following TGF-beta1 or adriamycin stimulation. |
| 399 | 20505657 | In vivo, this ILK inhibitor ameliorated albuminuria, repressed glomerular induction of MMP-9 and alpha-SMA, and preserved nephrin expression in murine adriamycin nephropathy. |
| 400 | 20505657 | In vivo, this ILK inhibitor ameliorated albuminuria, repressed glomerular induction of MMP-9 and alpha-SMA, and preserved nephrin expression in murine adriamycin nephropathy. |
| 401 | 20505657 | Our results show that upregulation of ILK is a convergent pathway leading to podocyte EMT, migration, and dysfunction. |
| 402 | 20505657 | Our results show that upregulation of ILK is a convergent pathway leading to podocyte EMT, migration, and dysfunction. |
| 403 | 20150534 | All glomerular cells contained genes whose expression changed "linearly" during adult life from 2 to 24 months: mesangial cells (e.g., MMP9), endothelial cells (e.g., ICAM and VCAM), parietal epithelial cells (e.g., ceruloplasmin), and podocytes (e.g., nephrin and prepronociceptin). |
| 404 | 20037812 | To investigate the effects of albumin on the production of matrix metalloproteinases-2 (MMP-2) and matrix metalloproteinases-9 (MMP-9) in podocytes. |
| 405 | 20037812 | To investigate the effects of albumin on the production of matrix metalloproteinases-2 (MMP-2) and matrix metalloproteinases-9 (MMP-9) in podocytes. |
| 406 | 20037812 | To investigate the effects of albumin on the production of matrix metalloproteinases-2 (MMP-2) and matrix metalloproteinases-9 (MMP-9) in podocytes. |
| 407 | 20037812 | To investigate the effects of albumin on the production of matrix metalloproteinases-2 (MMP-2) and matrix metalloproteinases-9 (MMP-9) in podocytes. |
| 408 | 20037812 | To investigate the effects of albumin on the production of matrix metalloproteinases-2 (MMP-2) and matrix metalloproteinases-9 (MMP-9) in podocytes. |
| 409 | 20037812 | The expression of MMP-2 and MMP-9 was assayed by gelatin zymography, RT-PCR and Western blotting analysis. |
| 410 | 20037812 | The expression of MMP-2 and MMP-9 was assayed by gelatin zymography, RT-PCR and Western blotting analysis. |
| 411 | 20037812 | The expression of MMP-2 and MMP-9 was assayed by gelatin zymography, RT-PCR and Western blotting analysis. |
| 412 | 20037812 | The expression of MMP-2 and MMP-9 was assayed by gelatin zymography, RT-PCR and Western blotting analysis. |
| 413 | 20037812 | The expression of MMP-2 and MMP-9 was assayed by gelatin zymography, RT-PCR and Western blotting analysis. |
| 414 | 20037812 | Our results showed that in comparison with the control group, BSA increased the expression of MMP-2 and MMP-9 mRNA and protein in a dose- and time-dependent manner (P<0.05). |
| 415 | 20037812 | Our results showed that in comparison with the control group, BSA increased the expression of MMP-2 and MMP-9 mRNA and protein in a dose- and time-dependent manner (P<0.05). |
| 416 | 20037812 | Our results showed that in comparison with the control group, BSA increased the expression of MMP-2 and MMP-9 mRNA and protein in a dose- and time-dependent manner (P<0.05). |
| 417 | 20037812 | Our results showed that in comparison with the control group, BSA increased the expression of MMP-2 and MMP-9 mRNA and protein in a dose- and time-dependent manner (P<0.05). |
| 418 | 20037812 | Our results showed that in comparison with the control group, BSA increased the expression of MMP-2 and MMP-9 mRNA and protein in a dose- and time-dependent manner (P<0.05). |
| 419 | 20037812 | Meanwhile, the enzymatic activities of MMP-2 and MMP-9 in the culture supernatants of podocytes were also increased (P<0.05). |
| 420 | 20037812 | Meanwhile, the enzymatic activities of MMP-2 and MMP-9 in the culture supernatants of podocytes were also increased (P<0.05). |
| 421 | 20037812 | Meanwhile, the enzymatic activities of MMP-2 and MMP-9 in the culture supernatants of podocytes were also increased (P<0.05). |
| 422 | 20037812 | Meanwhile, the enzymatic activities of MMP-2 and MMP-9 in the culture supernatants of podocytes were also increased (P<0.05). |
| 423 | 20037812 | Meanwhile, the enzymatic activities of MMP-2 and MMP-9 in the culture supernatants of podocytes were also increased (P<0.05). |
| 424 | 20037812 | It is concluded that albumin up-regulated the expression of MMP-2 and MMP-9 at gene and protein levels in a time- and dose-dependent manner. |
| 425 | 20037812 | It is concluded that albumin up-regulated the expression of MMP-2 and MMP-9 at gene and protein levels in a time- and dose-dependent manner. |
| 426 | 20037812 | It is concluded that albumin up-regulated the expression of MMP-2 and MMP-9 at gene and protein levels in a time- and dose-dependent manner. |
| 427 | 20037812 | It is concluded that albumin up-regulated the expression of MMP-2 and MMP-9 at gene and protein levels in a time- and dose-dependent manner. |
| 428 | 20037812 | It is concluded that albumin up-regulated the expression of MMP-2 and MMP-9 at gene and protein levels in a time- and dose-dependent manner. |
| 429 | 18202193 | TGF-beta1 suppressed the slit diaphragm-associated protein P-cadherin, zonula occludens-1, and nephrin, a change consistent with loss of the epithelial feature. |
| 430 | 18202193 | TGF-beta1 suppressed the slit diaphragm-associated protein P-cadherin, zonula occludens-1, and nephrin, a change consistent with loss of the epithelial feature. |
| 431 | 18202193 | Meanwhile, TGF-beta1 induced the expression of the intermediate filament protein desmin and interstitial matrix components fibronectin and collagen I. |
| 432 | 18202193 | Meanwhile, TGF-beta1 induced the expression of the intermediate filament protein desmin and interstitial matrix components fibronectin and collagen I. |
| 433 | 18202193 | Furthermore, TGF-beta1 promoted the expression and secretion of matrix metalloproteinase-9 by podocytes. |
| 434 | 18202193 | Furthermore, TGF-beta1 promoted the expression and secretion of matrix metalloproteinase-9 by podocytes. |
| 435 | 18202193 | Functionally, TGF-beta1 increased albumin permeability across podocyte monolayers, as demonstrated by a paracellular albumin influx assay. |
| 436 | 18202193 | Functionally, TGF-beta1 increased albumin permeability across podocyte monolayers, as demonstrated by a paracellular albumin influx assay. |
| 437 | 18202193 | The expression of Snail, a key transcriptional factor that has been implicated in initiating epithelial-to-mesenchymal transition, was induced by TGF-beta1, and ectopic expression of Snail suppressed P-cadherin and nephrin in podocytes. |
| 438 | 18202193 | The expression of Snail, a key transcriptional factor that has been implicated in initiating epithelial-to-mesenchymal transition, was induced by TGF-beta1, and ectopic expression of Snail suppressed P-cadherin and nephrin in podocytes. |
| 439 | 18202193 | In vivo, in addition to loss of nephrin and zonula occludens-1, mesenchymal markers such as desmin, fibroblast-specific protein-1, and matrix metalloproteinase-9 could be observed in glomerular podocytes of diabetic nephropathy. |
| 440 | 18202193 | In vivo, in addition to loss of nephrin and zonula occludens-1, mesenchymal markers such as desmin, fibroblast-specific protein-1, and matrix metalloproteinase-9 could be observed in glomerular podocytes of diabetic nephropathy. |
| 441 | 17392157 | These were accompanied by an imbalance in the plasminogen/plasmin and metalloprotease systems characterized by the increased renal expression of plasminogen activator inhibitor-1, tissue plasminogen activator, and urokinase plasminogen activator; the net result was an increase in plasmin and matrix metalloproteinase (MMP)-2 and a reduction in MMP-9 activity. |
| 442 | 17392157 | These were accompanied by an imbalance in the plasminogen/plasmin and metalloprotease systems characterized by the increased renal expression of plasminogen activator inhibitor-1, tissue plasminogen activator, and urokinase plasminogen activator; the net result was an increase in plasmin and matrix metalloproteinase (MMP)-2 and a reduction in MMP-9 activity. |
| 443 | 17392157 | Chronic treatment with the hydrophilic rosuvastatin had renoprotective effects in terms of morphology and inflammation and prevented the changes in plasmin, MMP-2, and MMP-9 activity. |
| 444 | 17392157 | Chronic treatment with the hydrophilic rosuvastatin had renoprotective effects in terms of morphology and inflammation and prevented the changes in plasmin, MMP-2, and MMP-9 activity. |
| 445 | 16543722 | High ambient glucose levels modulates the production of MMP-9 and alpha5(IV) collagen by cultured podocytes. |
| 446 | 16543722 | High ambient glucose levels modulates the production of MMP-9 and alpha5(IV) collagen by cultured podocytes. |
| 447 | 16543722 | High ambient glucose levels modulates the production of MMP-9 and alpha5(IV) collagen by cultured podocytes. |
| 448 | 16543722 | High ambient glucose levels modulates the production of MMP-9 and alpha5(IV) collagen by cultured podocytes. |
| 449 | 16543722 | High ambient glucose levels modulates the production of MMP-9 and alpha5(IV) collagen by cultured podocytes. |
| 450 | 16543722 | High ambient glucose levels modulates the production of MMP-9 and alpha5(IV) collagen by cultured podocytes. |
| 451 | 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. |
| 452 | 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. |
| 453 | 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. |
| 454 | 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. |
| 455 | 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. |
| 456 | 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. |
| 457 | 16543722 | Opposite to the increases in MMP-9 activity, HG medium produced significant decreases in the protein levels of alpha5(IV) collagen. |
| 458 | 16543722 | Opposite to the increases in MMP-9 activity, HG medium produced significant decreases in the protein levels of alpha5(IV) collagen. |
| 459 | 16543722 | Opposite to the increases in MMP-9 activity, HG medium produced significant decreases in the protein levels of alpha5(IV) collagen. |
| 460 | 16543722 | Opposite to the increases in MMP-9 activity, HG medium produced significant decreases in the protein levels of alpha5(IV) collagen. |
| 461 | 16543722 | Opposite to the increases in MMP-9 activity, HG medium produced significant decreases in the protein levels of alpha5(IV) collagen. |
| 462 | 16543722 | Opposite to the increases in MMP-9 activity, HG medium produced significant decreases in the protein levels of alpha5(IV) collagen. |
| 463 | 16543722 | HG medium rapidly activated ERK1/2 MAPK in podocytes. |
| 464 | 16543722 | HG medium rapidly activated ERK1/2 MAPK in podocytes. |
| 465 | 16543722 | HG medium rapidly activated ERK1/2 MAPK in podocytes. |
| 466 | 16543722 | HG medium rapidly activated ERK1/2 MAPK in podocytes. |
| 467 | 16543722 | HG medium rapidly activated ERK1/2 MAPK in podocytes. |
| 468 | 16543722 | HG medium rapidly activated ERK1/2 MAPK in podocytes. |
| 469 | 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. |
| 470 | 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. |
| 471 | 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. |
| 472 | 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. |
| 473 | 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. |
| 474 | 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. |
| 475 | 16543722 | Blocking the ERK pathway suppressed HG-induced expression and nuclear accumulation of transcriptional factor Ets-1, and MMP-9 mRNA expression. |
| 476 | 16543722 | Blocking the ERK pathway suppressed HG-induced expression and nuclear accumulation of transcriptional factor Ets-1, and MMP-9 mRNA expression. |
| 477 | 16543722 | Blocking the ERK pathway suppressed HG-induced expression and nuclear accumulation of transcriptional factor Ets-1, and MMP-9 mRNA expression. |
| 478 | 16543722 | Blocking the ERK pathway suppressed HG-induced expression and nuclear accumulation of transcriptional factor Ets-1, and MMP-9 mRNA expression. |
| 479 | 16543722 | Blocking the ERK pathway suppressed HG-induced expression and nuclear accumulation of transcriptional factor Ets-1, and MMP-9 mRNA expression. |
| 480 | 16543722 | Blocking the ERK pathway suppressed HG-induced expression and nuclear accumulation of transcriptional factor Ets-1, and MMP-9 mRNA expression. |
| 481 | 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. |
| 482 | 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. |
| 483 | 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. |
| 484 | 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. |
| 485 | 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. |
| 486 | 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. |
| 487 | 16301820 | ERK-dependent signaling pathway and transcriptional factor Ets-1 regulate matrix metalloproteinase-9 production in transforming growth factor-beta1 stimulated glomerular podocytes. |
| 488 | 16301820 | ERK-dependent signaling pathway and transcriptional factor Ets-1 regulate matrix metalloproteinase-9 production in transforming growth factor-beta1 stimulated glomerular podocytes. |
| 489 | 16301820 | ERK-dependent signaling pathway and transcriptional factor Ets-1 regulate matrix metalloproteinase-9 production in transforming growth factor-beta1 stimulated glomerular podocytes. |
| 490 | 16301820 | ERK-dependent signaling pathway and transcriptional factor Ets-1 regulate matrix metalloproteinase-9 production in transforming growth factor-beta1 stimulated glomerular podocytes. |
| 491 | 16301820 | ERK-dependent signaling pathway and transcriptional factor Ets-1 regulate matrix metalloproteinase-9 production in transforming growth factor-beta1 stimulated glomerular podocytes. |
| 492 | 16301820 | ERK-dependent signaling pathway and transcriptional factor Ets-1 regulate matrix metalloproteinase-9 production in transforming growth factor-beta1 stimulated glomerular podocytes. |
| 493 | 16301820 | The present study examined the effects and the underlying molecular mechanism of transforming growth factor beta1 (TGFbeta1) on the production of gelatinase in cultured murine podocytes. |
| 494 | 16301820 | The present study examined the effects and the underlying molecular mechanism of transforming growth factor beta1 (TGFbeta1) on the production of gelatinase in cultured murine podocytes. |
| 495 | 16301820 | The present study examined the effects and the underlying molecular mechanism of transforming growth factor beta1 (TGFbeta1) on the production of gelatinase in cultured murine podocytes. |
| 496 | 16301820 | The present study examined the effects and the underlying molecular mechanism of transforming growth factor beta1 (TGFbeta1) on the production of gelatinase in cultured murine podocytes. |
| 497 | 16301820 | The present study examined the effects and the underlying molecular mechanism of transforming growth factor beta1 (TGFbeta1) on the production of gelatinase in cultured murine podocytes. |
| 498 | 16301820 | The present study examined the effects and the underlying molecular mechanism of transforming growth factor beta1 (TGFbeta1) on the production of gelatinase in cultured murine podocytes. |
| 499 | 16301820 | Our results showed that TGFbeta1 is the most potent inducer of MMP-9 secretion in both a dose- and time-dependent manner, but has very little effect on MMP-2 secretion. |
| 500 | 16301820 | Our results showed that TGFbeta1 is the most potent inducer of MMP-9 secretion in both a dose- and time-dependent manner, but has very little effect on MMP-2 secretion. |
| 501 | 16301820 | Our results showed that TGFbeta1 is the most potent inducer of MMP-9 secretion in both a dose- and time-dependent manner, but has very little effect on MMP-2 secretion. |
| 502 | 16301820 | Our results showed that TGFbeta1 is the most potent inducer of MMP-9 secretion in both a dose- and time-dependent manner, but has very little effect on MMP-2 secretion. |
| 503 | 16301820 | Our results showed that TGFbeta1 is the most potent inducer of MMP-9 secretion in both a dose- and time-dependent manner, but has very little effect on MMP-2 secretion. |
| 504 | 16301820 | Our results showed that TGFbeta1 is the most potent inducer of MMP-9 secretion in both a dose- and time-dependent manner, but has very little effect on MMP-2 secretion. |
| 505 | 16301820 | TGFbeta1 upregulated MMP-9 mRNA levels, but did not affect the expression of matrix mettaloproteinases TIMP-1 mRNA. |
| 506 | 16301820 | TGFbeta1 upregulated MMP-9 mRNA levels, but did not affect the expression of matrix mettaloproteinases TIMP-1 mRNA. |
| 507 | 16301820 | TGFbeta1 upregulated MMP-9 mRNA levels, but did not affect the expression of matrix mettaloproteinases TIMP-1 mRNA. |
| 508 | 16301820 | TGFbeta1 upregulated MMP-9 mRNA levels, but did not affect the expression of matrix mettaloproteinases TIMP-1 mRNA. |
| 509 | 16301820 | TGFbeta1 upregulated MMP-9 mRNA levels, but did not affect the expression of matrix mettaloproteinases TIMP-1 mRNA. |
| 510 | 16301820 | TGFbeta1 upregulated MMP-9 mRNA levels, but did not affect the expression of matrix mettaloproteinases TIMP-1 mRNA. |
| 511 | 16301820 | TGFbeta1 induced activation of both Smad2 and extracellular signal-regulated kinases (ERK1/2). |
| 512 | 16301820 | TGFbeta1 induced activation of both Smad2 and extracellular signal-regulated kinases (ERK1/2). |
| 513 | 16301820 | TGFbeta1 induced activation of both Smad2 and extracellular signal-regulated kinases (ERK1/2). |
| 514 | 16301820 | TGFbeta1 induced activation of both Smad2 and extracellular signal-regulated kinases (ERK1/2). |
| 515 | 16301820 | TGFbeta1 induced activation of both Smad2 and extracellular signal-regulated kinases (ERK1/2). |
| 516 | 16301820 | TGFbeta1 induced activation of both Smad2 and extracellular signal-regulated kinases (ERK1/2). |
| 517 | 16301820 | However, blockade of Smad2 signaling pathway by Staurosporine did not affect the TGFbeta1-stimulated secretion of MMP-9, whereas inhibition of activation of ERK1/2 by PD98059 abolished TGFbeta1-stimulated secretion of MMP-9 and expression of MMP-9 mRNA. |
| 518 | 16301820 | However, blockade of Smad2 signaling pathway by Staurosporine did not affect the TGFbeta1-stimulated secretion of MMP-9, whereas inhibition of activation of ERK1/2 by PD98059 abolished TGFbeta1-stimulated secretion of MMP-9 and expression of MMP-9 mRNA. |
| 519 | 16301820 | However, blockade of Smad2 signaling pathway by Staurosporine did not affect the TGFbeta1-stimulated secretion of MMP-9, whereas inhibition of activation of ERK1/2 by PD98059 abolished TGFbeta1-stimulated secretion of MMP-9 and expression of MMP-9 mRNA. |
| 520 | 16301820 | However, blockade of Smad2 signaling pathway by Staurosporine did not affect the TGFbeta1-stimulated secretion of MMP-9, whereas inhibition of activation of ERK1/2 by PD98059 abolished TGFbeta1-stimulated secretion of MMP-9 and expression of MMP-9 mRNA. |
| 521 | 16301820 | However, blockade of Smad2 signaling pathway by Staurosporine did not affect the TGFbeta1-stimulated secretion of MMP-9, whereas inhibition of activation of ERK1/2 by PD98059 abolished TGFbeta1-stimulated secretion of MMP-9 and expression of MMP-9 mRNA. |
| 522 | 16301820 | However, blockade of Smad2 signaling pathway by Staurosporine did not affect the TGFbeta1-stimulated secretion of MMP-9, whereas inhibition of activation of ERK1/2 by PD98059 abolished TGFbeta1-stimulated secretion of MMP-9 and expression of MMP-9 mRNA. |
| 523 | 16301820 | Our data also showed that blockage of ERK1/2 activation by PD98059 led to a reduction in the level of Ets-1 protein and to a consequent decrease in MMP-9 mRNA levels. |
| 524 | 16301820 | Our data also showed that blockage of ERK1/2 activation by PD98059 led to a reduction in the level of Ets-1 protein and to a consequent decrease in MMP-9 mRNA levels. |
| 525 | 16301820 | Our data also showed that blockage of ERK1/2 activation by PD98059 led to a reduction in the level of Ets-1 protein and to a consequent decrease in MMP-9 mRNA levels. |
| 526 | 16301820 | Our data also showed that blockage of ERK1/2 activation by PD98059 led to a reduction in the level of Ets-1 protein and to a consequent decrease in MMP-9 mRNA levels. |
| 527 | 16301820 | Our data also showed that blockage of ERK1/2 activation by PD98059 led to a reduction in the level of Ets-1 protein and to a consequent decrease in MMP-9 mRNA levels. |
| 528 | 16301820 | Our data also showed that blockage of ERK1/2 activation by PD98059 led to a reduction in the level of Ets-1 protein and to a consequent decrease in MMP-9 mRNA levels. |
| 529 | 16301820 | These results demonstrate that TGFbeta1 can induce the production of MMP-9 in podocytes through the ERK1/2 MAPK pathway, and suggested that an increase in MMP-9 enzymatic activities may be involved in the damage of the GBM in response to inflammatory factors, ultimately leading to glomerulosclerosis. |
| 530 | 16301820 | These results demonstrate that TGFbeta1 can induce the production of MMP-9 in podocytes through the ERK1/2 MAPK pathway, and suggested that an increase in MMP-9 enzymatic activities may be involved in the damage of the GBM in response to inflammatory factors, ultimately leading to glomerulosclerosis. |
| 531 | 16301820 | These results demonstrate that TGFbeta1 can induce the production of MMP-9 in podocytes through the ERK1/2 MAPK pathway, and suggested that an increase in MMP-9 enzymatic activities may be involved in the damage of the GBM in response to inflammatory factors, ultimately leading to glomerulosclerosis. |
| 532 | 16301820 | These results demonstrate that TGFbeta1 can induce the production of MMP-9 in podocytes through the ERK1/2 MAPK pathway, and suggested that an increase in MMP-9 enzymatic activities may be involved in the damage of the GBM in response to inflammatory factors, ultimately leading to glomerulosclerosis. |
| 533 | 16301820 | These results demonstrate that TGFbeta1 can induce the production of MMP-9 in podocytes through the ERK1/2 MAPK pathway, and suggested that an increase in MMP-9 enzymatic activities may be involved in the damage of the GBM in response to inflammatory factors, ultimately leading to glomerulosclerosis. |
| 534 | 16301820 | These results demonstrate that TGFbeta1 can induce the production of MMP-9 in podocytes through the ERK1/2 MAPK pathway, and suggested that an increase in MMP-9 enzymatic activities may be involved in the damage of the GBM in response to inflammatory factors, ultimately leading to glomerulosclerosis. |
| 535 | 16061020 | [High glucose regulates the production of MMP-9 in podocyte through ERK1/2 signal pathway]. |
| 536 | 15854510 | [Transforming growth factor-beta1 stimulates matrix metalloproteinase-9 production through ERK activation pathway and upregulation of Ets-1 protein]. |
| 537 | 15545511 | Improvement of structural injury in glomeruli and podocytes was accompanied by a reduction of the expression of matrix metalloproteinase-9 and p21Cip1/WAF1. |
| 538 | 12437116 | We demonstrate that ILK activity is also associated with upregulation of matrix metalloproteinase-9 (MMP-9) mRNA levels during podocyte stress. |
| 539 | 12437116 | We demonstrate that ILK activity is also associated with upregulation of matrix metalloproteinase-9 (MMP-9) mRNA levels during podocyte stress. |
| 540 | 12437116 | We demonstrate that ILK activity is also associated with upregulation of matrix metalloproteinase-9 (MMP-9) mRNA levels during podocyte stress. |
| 541 | 12437116 | A synthetic ILK inhibitor blocked MMP-9 mRNA upregulation but showed no effect on TIMP-1 or MMP-2 mRNA expression. |
| 542 | 12437116 | A synthetic ILK inhibitor blocked MMP-9 mRNA upregulation but showed no effect on TIMP-1 or MMP-2 mRNA expression. |
| 543 | 12437116 | A synthetic ILK inhibitor blocked MMP-9 mRNA upregulation but showed no effect on TIMP-1 or MMP-2 mRNA expression. |
| 544 | 12437116 | Interestingly, a corresponding increase in MMP-9 secretion was not observed, suggesting that MMP-9 mRNA production in podocytes is regulated via ILK, whereas additional signaling pathways may mediate the post-transcriptional regulation of MMP-9. |
| 545 | 12437116 | Interestingly, a corresponding increase in MMP-9 secretion was not observed, suggesting that MMP-9 mRNA production in podocytes is regulated via ILK, whereas additional signaling pathways may mediate the post-transcriptional regulation of MMP-9. |
| 546 | 12437116 | Interestingly, a corresponding increase in MMP-9 secretion was not observed, suggesting that MMP-9 mRNA production in podocytes is regulated via ILK, whereas additional signaling pathways may mediate the post-transcriptional regulation of MMP-9. |