Degradation of the COL1 Domain of Type XIV Collagen by 92-kDa Gelatinase

Sires, Ulrike I.; Dublet, Bernard; Aubert-Foucher, E.; Rest, Michel van der; Welgus, Howard G.

doi:10.1074/jbc.270.3.1062

Cited by 18 publications

(4 citation statements)

References 55 publications

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“…Other collagens may be present. MMP-9 also acts on types V and XIV collagens and on insoluble elastin, and MMP-2 acts on collagens type V, VII, and X, on elastin, and on fibronectin [7,[12][13][14]. Hence these gelatinases could participate in the degradation of other fetal membrane ECM components as well as type IV collagen.…”

Section: Discussionmentioning

confidence: 99%

92-kDa Gelatinase (Matrix Metalloproteinase-9) is Induced in Rat Amnion Immediately Prior to Parturition1

Lei

Vadillo-Ortega

Paavola

et al. 1995

Biology of Reproduction

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The fetal membranes undergo striking changes in structure before delivery that involve catabolism of the extracellular matrix. To investigate the role of specific enzymes in this process, we examined gelatinase activities in rat amnion, visceral yolk sac placenta, and placenta and amniotic fluid between Days 18-21 of pregnancy. Matrix metalloproteinase (MMP)-2 was present in amnion on all days, and its activity increased slightly on Day 21. The 92-kDa gelatinase, MMP-9, was not detected on Days 18-20 but appeared by the morning of Day 21. There was a marked increase in MMP-9 mRNA in the amnion on Day 20, preceding the appearance of MMP-9 activity. Western blotting confirmed an increase in MMP-9 protein in amnion on Day 21. MMP-2 and MMP-9 activities were detected in extracts of whole yolk sac placenta, placenta, and amniotic fluid, but there were no striking changes in these gelatinases between Days 18 and 21. However, the capsular regions of the visceral yolk sac placentae, which thin and rupture during labor, did show higher MMP-9 activity on Day 21 than on Days 18 and 20. We suggest that the striking increase in MMP-9 expression in amnion and possibly the capsular region of the visceral yolk sac placenta approximately 12 h prior to delivery is responsible, in part, for the alterations in the structure of these fetal membranes before parturition.

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Section: Discussionmentioning

confidence: 99%

92-kDa Gelatinase (Matrix Metalloproteinase-9) is Induced in Rat Amnion Immediately Prior to Parturition1

Lei

Vadillo-Ortega

Paavola

et al. 1995

Biology of Reproduction

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“…The mechanisms whereby MMP9 induces branching morphogenesis remain speculative. They may first involve degradation of type IV collagen, denatured collagen, or type XIV collagen, a newly described member of the fibrilassociated collagens with interrupted triple helices (FACITS) that has been localized to various embryonic tissues ( Sires et al, 1995 ). Alternatively, the proteolytic activity of MMP9 may not be limited to collagen molecules since it has been shown to cleave the extracellular collagenous domain of 180-kD bullous pemphigoid autoantigen, a transmembrane molecule of the epidermal hemidesmosome ( Stähle-Bäckdahl et al, 1994 ).…”

Section: Discussionmentioning

confidence: 99%

Matrix Metalloproteinases MMP2 and MMP9 Are Produced in Early Stages of Kidney Morphogenesis but Only MMP9 Is Required for Renal Organogenesis In Vitro

Lelongt

Trugnan

Murphy

et al. 1997

The Journal of Cell Biology

160

155

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We analyzed matrix metalloproteinase (MMP) production by 11-d embryonic mouse kidneys and the effects of these enzymes on subsequent renal organogenesis. In vivo, immunolocalization of metalloproteinases by laser scanning confocal microscopy and zymograms of kidney lysates showed that the mesenchyme of embryonic kidneys synthesized both MMP9 and MMP2 enzymes. In vitro, embryonic kidneys also secreted both enzymes when cultured in a medium devoid of hormone, growth factor, and serum for 24 h during which T-shaped branching of the ureter bud appeared. We then evaluated the role of MMP2 and MMP9 in kidney morphogenesis by adding anti-MMP2 or anti-MMP9 IgGs to the culture medium of 11-d kidneys for 24 or 72 h. Although it inhibited activity of the mouse enzyme, anti-MMP2 IgGs had no effect on kidney morphogenesis. In contrast, anti-MMP9 IgGs with enzyme-blocking activity impaired renal morphogenesis, in a concentration-dependent manner, by inhibiting T-shaped branching and further divisions of the ureter bud. This effect was irreversible, still observed after inductive events and reproduced by exogenous tissue inhibitor of metalloproteinase 1 (TIMP1), the natural inhibitor of MMP9. These data provide the first demonstration of MMP9 and MMP2 production in vivo by 11-d embryonic kidneys and further show that MMP9 is required in vitro for branching morphogenesis of the ureter bud.

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“…Enzymes and Substrates-Human pro-MMP-1 was purified by twostep chromatography from conditioned medium of phorbol-treated U937 cells as described (15). Matrilysin was purchased from Chemicon International, Inc. (Temecula, CA).…”

Section: Methodsmentioning

confidence: 99%

Pro-collagenase-1 (Matrix Metalloproteinase-1) Binds the α2β1 Integrin upon Release from Keratinocytes Migrating on Type I Collagen

Dumin

Dickeson

Stricker

et al. 2001

Journal of Biological Chemistry

193

138

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In injured skin, collagenase-1 (matrix metalloproteinase-1 (MMP-1)) is induced in migrating keratinocytes. This site-specific expression is regulated by binding of the ␣ 2 ␤ 1 integrin with dermal type I collagen, and the catalytic activity of MMP-1 is required for keratinocyte migration. Because of this functional association among substrate/ligand, receptor, and proteinase, we assessed whether the integrin also directs the compartmentalization of MMP-1 to its matrix target. Indeed, pro-MMP-1 co-localized to sites of ␣ 2 ␤ 1 contacts in migrating keratinocytes. Furthermore, pro-MMP-1 co-immunoprecipitated with ␣ 2 ␤ 1 from keratinocytes, and ␣ 2 ␤ 1 co-immunoprecipitated with pro-MMP-1. No other MMPs bound ␣ 2 ␤ 1 , and no other integrins interacted with MMP-1. Pro-MMP-1 also provided a substrate for ␣ 2 ␤ 1 -dependent adhesion of platelets. Complex formation on keratinocytes was most efficient on native type I collagen and reduced or ablated on denatured or cleaved collagen. Competition studies suggested that the ␣ 2 I domain interacts with the linker and hemopexin domains of pro-MMP-1, not with the pro-domain. These data indicate that the interaction of pro-MMP-1 with ␣ 2 ␤ 1 confines this proteinase to points of cell contact with collagen and that the ternary complex of integrin, enzyme, and substrate function together to drive and regulate keratinocyte migration.Cells, either resting or activated, use a variety of surface receptors to sense the presence and location of specific molecules in the extracellular space. For example, integrin-ligand interactions tell cells which structural proteins they have encountered in the extracellular space, and in turn, these contacts activate signaling pathways involved in differentiation, proliferation, and gene expression, among other processes. During migration, cells need to proteolyze, to some extent, nearby extracellular matrix proteins, and hence, cell-matrix contacts can also instruct cells which proteinases are needed and where the enzyme should be targeted and released.An example of cell-matrix-mediated spatial regulation of proteolysis is seen with collagenase-1 (MMP-1), 1 a matrix metalloproteinase, in human cutaneous wounds. In response to injury, collagenase-1 is induced in basal epidermal cells (keratinocytes) as the cells move off of the basement membrane and contact native type I collagen in the underlying dermis (1), and this inductive response is specifically controlled by the collagen-binding integrin ␣ 2 ␤ 1 (2). As we demonstrated in various experiments, the catalytic activity of collagenase-1 is required and sufficient for keratinocyte migration on complex matrices containing type I collagen. For example, keratinocytes plated on mutant, collagenase-resistant type I collagen do not migrate, even in the presence of fibronectin and vitronectin; yet they express MMP-1 at levels equivalent to those released by cells on wild-type collagen (2). Keratinocyte migration is also completely inhibited by anti-collagenase-1 antibodies, which block the catalytic a...

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Degradation of the COL1 Domain of Type XIV Collagen by 92-kDa Gelatinase

Cited by 18 publications

References 55 publications

92-kDa Gelatinase (Matrix Metalloproteinase-9) is Induced in Rat Amnion Immediately Prior to Parturition1

92-kDa Gelatinase (Matrix Metalloproteinase-9) is Induced in Rat Amnion Immediately Prior to Parturition1

Matrix Metalloproteinases MMP2 and MMP9 Are Produced in Early Stages of Kidney Morphogenesis but Only MMP9 Is Required for Renal Organogenesis In Vitro

Pro-collagenase-1 (Matrix Metalloproteinase-1) Binds the α2β1 Integrin upon Release from Keratinocytes Migrating on Type I Collagen

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