The Collagen Binding Domain of Gelatinase A Modulates Degradation of Collagen IV by Gelatinase B
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چکیده
منابع مشابه
Gelatinase B participates in collagen II degradation and releases glycosylated remnant epitopes in rheumatoid arthritis.
Rheumatoid arthritis is an autoimmune disease characterized by chronic inflammation of the joints. It is associated with the activation of autoreactive T-cells and with production of autoantibodies. The main auto-antigen is collagen type II, which is a major constituent of the cartilage in the joint. The inflammation causes cartilage degradation, hyperplasia of synovial membranes, accumulation ...
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Anchoring functions of collagen VII depend on its ability to form homotypic fibrils and to bind to other macromolecules to form heterotypic complexes. Biosensor-based binding assays were employed to analyze the kinetics of the NC1 domain-mediated binding of collagen VII to laminin 5, collagen IV, and collagen I. We showed that collagen VII interacts with laminin 5 and collagen IV with a Kd valu...
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MMP-9 is a Zn+2 dependent endopeptidase, synthesized and secreted in monomeric form as zymogen. The structure is almost similar to MMP2, another member of matrixmetalloproteinase family. The nascent form of the protein shows an N-terminal signal sequence ('pre' domain) that directs the protein to the endoplasmic reticulum. The pre domain is followed by a propeptide-'pro' domain that maintains e...
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Objective Objective: Gelatinases degrade extracellular matrix (ECM) components to make physiological remodeling and contribute to pathological tissue destruction in endometriosis. It is known that gelatinases’ function is resistant to suppression by progesterone in endometriosis. The ability of progesterone to impact gene expression depends on the progesterone receptor-A/-B (PR-A/PR-B) ratio. A...
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ژورنال
عنوان ژورنال: Journal of Molecular Biology
سال: 2009
ISSN: 0022-2836
DOI: 10.1016/j.jmb.2008.12.021