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1دورية أكاديمية
مصطلحات موضوعية: Metalloproteinase, Membrane type 1-matrix metalloproteinase, Extracellular matrix, Decorin, Corneal neovascularization, Angiogenesis, MMP-14, Proteoglycans - metabolism, Cornea - enzymology, Corneal Neovascularization - chemically induced - enzymology, Extracellular Matrix Proteins - metabolism, Matrix Metalloproteinase 14 - antagonists and inhibitors - deficiency - genetics - metabolism
الوصف: Background/Aims: Decorin has been shown to have antiangiogenic properties. In this study, we evaluate the involvement of membrane type 1-matrix metalloproteinase (MT1-MMP), a proangiogenic enzyme, in decorin cleavage in the cornea. Methods: MT1-MMP expression was confirmed immunohistochemically in keratocytes and immortalized corneal fibroblast cell lines. Corneal micropockets of bFGF were used to assess the expression of decorin and MT1-MMP. Western blotting was used to evaluate decorin degradation by MT1-MMP. Aortic ring tube formation assays were used to assay the inhibitory effect of decorin and stimulatory effect of MT1-MMP on vascular endothelial cells in vitro. Results: We show that MT1-MMP expression is upregulated following bFGF pellet implantation in the cornea in vivo, and that MT1-MMP cleaves decorin in a time-and concentration-dependent manner in vitro. Furthermore, the addition of MT1-MMP reduces the inhibitory effects of decorin on aortic ring tube formation in vitro. Cleavage of decorin by MT1-MMP-deficient corneal cell lysates is diminished relative to that by wild-type corneal cell lysates, and an MT1-MMP knockin restores decorin processing in vitro. Conclusion: The proangiogenic role of MT1-MMP in the cornea may be mediated, in part, by facilitated cleavage of corneal decorin. © 2009 S. Karger AG, Basel. ; link_to_subscribed_fulltext
العلاقة: Journal of Vascular Research; http://www.scopus.com/mlt/select.url?eid=2-s2.0-67649424445&selection=ref&src=s&origin=recordpageTest; Journal Of Vascular Research, 2009, v. 46 n. 6, p. 541-550; 550; 167558; WOS:000270780200003; http://library.hku.hk:4550/resserv?sid=HKU:IR&issn=1018-1172&volume=46&issue=6&spage=541&epage=550&date=2009&atitle=MT1-MMP-mediated+cleavage+of+decorin+in+corneal+angiogenesisTest; eid_2-s2.0-67649424445; 541; http://hdl.handle.net/10722/58308Test; 46
الإتاحة: https://doi.org/10.1159/000226222Test
http://library.hku.hk:4550/resserv?sid=HKU:IR&issn=1018-1172&volume=46&issue=6&spage=541&epage=550&date=2009&atitle=MT1-MMP-mediated+cleavage+of+decorin+in+corneal+angiogenesisTest
http://hdl.handle.net/10722/58308Test -
2دورية أكاديمية
المؤلفون: SansilvestriMorel, P, Nonotte, I, FournetBourguignon, MP, Rupìn, A, Fabiani, JN, Verbeuren, TJ, Vanhoutte, PM
مصطلحات موضوعية: Aged, 80 And Over, Cell Division - Physiology, Cell Movement - Physiology, Cells, Cultured, Collagen - Metabolism, Extracellular Matrix Proteins - Metabolism, Female, Fibronectins - Metabolism, Humans, Male, Metalloendopeptidases - Metabolism, Middle Aged, Muscle, Smooth, Vascular - Metabolism - Pathology, Reference Values, Tissue Inhibitor Of Metalloproteinases - Metabolism, Varicose Veins - Metabolism - Pathology
الوصف: The aim of the present study was to verify whether the modifications of the extracellular matrix, described in varicose veins, are also present in cultures of smooth muscle cells from human varicose veins. The accumulation of collagen type Iii and fibronectin was determined by immunofluorescence in cultures of smooth muscle cells at passage 2-3 during the proliferation phase. After 5 days of culture, the immunostaining of both collagen type Iii and fibronectin was weaker in cells from varicose than in those of control veins while the expression of collagen type Iii and fibronectin messenger ribonucleic acids was not significantly different. Collagen type I and Iii synthesis were quantified by tritiated proline incorporation in control and varicose cell layers at postconfluence. Collagen type I deposition was similar in both types of cell layers while collagen type Iii was decreased in cell layers from varicose veins. Matrix metalloproteinases (mmps) and their inhibitors (timps) were also quantified by enzyme immunoassays in supernatants from smooth muscle cell cultures at postconfluence. No significant difference was observed in the synthesis of any of the Mmps (- 1, -2 and -9) or their inhibitors (- 1 and -2) tested. These data illustrate that smooth muscle cells cultured from varicose veins deposit less collagen type Iii and fibronectin than control cells despite comparable levels of mrnas for these proteins suggesting dysregulation of posttranslational steps in the synthesis of both proteins by smooth muscle cells from varicose veins. ; link_to_subscribed_fulltext
العلاقة: Journal of Vascular Research; http://www.scopus.com/mlt/select.url?eid=2-s2.0-0031896488&selection=ref&src=s&origin=recordpageTest; Journal Of Vascular Research, 1998, v. 35 n. 2, p. 115-123; 123; WOS:000073325900006; 9588875; eid_2-s2.0-0031896488; 115; http://hdl.handle.net/10722/171210Test; 35
