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      MT1-MMP-mediated cleavage of decorin in corneal angiogenesis.

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      Publication date:
      Journal: Journal of Vascular Research
      Keywords: Animals, Aorta, enzymology, Cell Line, Cornea, Corneal Neovascularization, chemically induced, Culture Media, Conditioned, metabolism, Decorin, Dipeptides, pharmacology, Disease Models, Animal, Extracellular Matrix Proteins, Fibroblast Growth Factor 2, Kinetics, Matrix Metalloproteinase 14, deficiency, genetics, Matrix Metalloproteinase Inhibitors, Mice, Mice, Inbred C57BL, Mice, Knockout, Protease Inhibitors, Proteoglycans, Recombinant Proteins, Tissue Culture Techniques, Transfection

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          Abstract

          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. 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. 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. The proangiogenic role of MT1-MMP in the cornea may be mediated, in part, by facilitated cleavage of corneal decorin. Copyright 2009 S. Karger AG, Basel.

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          MMP-2, MT1-MMP, and TIMP-2 are essential for the invasive capacity of human mesenchymal stem cells: differential regulation by inflammatory cytokines.

          Christian Ries, Virginia Egea, Marisa Karow … (2007)
          Human mesenchymal stem cells (hMSCs) represent promising tools in various clinical applications, including the regeneration of injured tissues by endogenous or transplanted hMSCs. The molecular mechanisms, however, that control hMSC mobilization and homing which require invasion through extracellular matrix (ECM) barriers are almost unknown. We have analyzed bone marrow-derivedhMSCs and detected strong expression and synthesis of matrix metalloproteinase 2 (MMP-2), membrane type 1 MMP (MT1-MMP), tissue inhibitor of metalloproteinase 1 (TIMP-1), and TIMP-2. The ability of hMSCs to traverse reconstituted human basement membranes was effectively blocked in the presence of synthetic MMP inhibitors. Detailed studies by RNA interference revealed that gene knock-down of MMP-2, MT1-MMP, or TIMP-2 substantially impaired hMSC invasion, whereas silencing of TIMP-1 enhanced cell migration, indicating opposing roles of both TIMPs in this process. Moreover, the inflammatory cytokines TGF-beta1, IL-1beta, and TNF-alpha up-regulated MMP-2, MT1-MMP, and/or MMP-9 production in these cells, resulting in a strong stimulation of chemotactic migration through ECM, whereas the chemokine SDF-1alpha exhibited minor effects on MMP/TIMP expression and cell invasion. Thus, induction of specific MMP activity in hMSCs by inflammatory cytokines promotes directed cell migration across reconstituted basement membranes in vitro providing a potential mechanism in hMSC recruitment and extravasation into injured tissues in vivo.
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            Corneal neovascularization.

            Jin-Hong Chang, Eric Gabison, Takuji Kato … (2001)
            Corneal neovascularization (NV) is a sight-threatening condition usually associated with inflammatory or infectious disorders of the ocular surface. It has been shown in the field of cancer angiogenesis research that a balance exists between angiogenic factors (such as fibroblast growth factor and vascular endothelial growth factor) and anti-angiogenic molecules (such as angiostatin, endostatin, or pigment epithelium derived factor) in the cornea. Several inflammatory, infectious, degenerative, and traumatic disorders are associated with corneal NV, in which the balance is tilted towards angiogenesis. The pathogenesis of corneal NV may be influenced by matrix metalloproteinases and other proteolytic enzymes. New medical and surgical treatments, including angiostatic steroids, nonsteroidal inflammatory agents, argon laser photocoagulation, and photodynamic therapy have been effective in animal models to inhibit corneal NV and transiently restore corneal "angiogenic privilege."
            Article 0 comments Cited 134 times – based on 0 reviews     Review now
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              Membrane type 1 matrix metalloproteinase digests interstitial collagens and other extracellular matrix macromolecules.

              Y Fujii-Kuriyama, M Seiki, E Ohuchi … (1997)
              Membrane type 1 matrix metalloproteinase (MT1-MMP) is expressed on cancer cell membranes and activates the zymogen of MMP-2 (gelatinase A). We have recently isolated MT1-MMP complexed with tissue inhibitor of metalloproteinases 2 (TIMP-2) and demonstrated that MT1-MMP exhibits gelatinolytic activity by gelatin zymography (Imai, K., Ohuchi, E., Aoki, T., Nomura, H., Fujii, Y., Sato, H., Seiki, M., and Okada, Y. (1996) Cancer Res. 56, 2707-2710). In the present study, we have further purified to homogeneity a deletion mutant of MT1-MMP lacking the transmembrane domain (DeltaMT1) and native MT1-MMP secreted from a human breast carcinoma cell line (MDA-MB-231 cells) and examined their substrate specificities. Both proteinases are active, without any treatment for activation, and digest type I (guinea pig), II (bovine), and III (human) collagens into characteristic 3/4 and 1/4 fragments. The cleavage sites of type I collagen are the Gly775-Ile776 bond for alpha1(I) chains and the Gly775-Leu776 and Gly781-Ile782 bonds for alpha2(I) chains. DeltaMT1 hydrolyzes type I collagen 6.5- or 4-fold more preferentially than type II or III collagen, whereas MMP-1 (tissue collagenase) digests type III collagen more efficiently than the other two collagens. Quantitative analyses of the activity of DeltaMT1 and MMP-1 indicate that DeltaMT1 is 5-7.1-fold less efficient at cleaving type I collagen. On the other hand, gelatinolytic activity of DeltaMT1 is 8-fold higher than that of MMP-1. DeltaMT1 also digests cartilage proteoglycan, fibronectin, vitronectin and laminin-1 as well as alpha1-proteinase inhibitor and alpha2-macroglobulin. The activity of DeltaMT1 on type I collagen is synergistically increased with co-incubation with MMP-2. These results indicate that MT1-MMP is an extracellular matrix-degrading enzyme sharing the substrate specificity with interstitial collagenases, and suggest that MT1-MMP plays a dual role in pathophysiological digestion of extracellular matrix through direct cleavage of the substrates and activation of proMMP-2.
              Article 0 comments Cited 119 times – based on 0 reviews     Review now
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                Author and article information

                Journal
                PubMed ID:: 19571574
                PMC ID:: 3709025
                DOI:: 10.1159/000226222

                ScienceOpen disciplines: Chemistry
                Keywords: Animals,Aorta,enzymology,Cell Line,Cornea,Corneal Neovascularization,chemically induced,Culture Media, Conditioned,metabolism,Decorin,Dipeptides,pharmacology,Disease Models, Animal,Extracellular Matrix Proteins,Fibroblast Growth Factor 2,Kinetics,Matrix Metalloproteinase 14,deficiency,genetics,Matrix Metalloproteinase Inhibitors,Mice,Mice, Inbred C57BL,Mice, Knockout,Protease Inhibitors,Proteoglycans,Recombinant Proteins,Tissue Culture Techniques,Transfection
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                ScienceOpen disciplines: Chemistry
                Keywords: Animals, Aorta, enzymology, Cell Line, Cornea, Corneal Neovascularization, chemically induced, Culture Media, Conditioned, metabolism, Decorin, Dipeptides, pharmacology, Disease Models, Animal, Extracellular Matrix Proteins, Fibroblast Growth Factor 2, Kinetics, Matrix Metalloproteinase 14, deficiency, genetics, Matrix Metalloproteinase Inhibitors, Mice, Mice, Inbred C57BL, Mice, Knockout, Protease Inhibitors, Proteoglycans, Recombinant Proteins, Tissue Culture Techniques, Transfection

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