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Role of the Matrix Metalloproteinase and Plasminogen Activator–Plasmin Systems in Angiogenesis
Author(s) -
Michael S. Pepper
Publication year - 2001
Publication title -
arteriosclerosis thrombosis and vascular biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.007
H-Index - 270
eISSN - 1524-4636
pISSN - 1079-5642
DOI - 10.1161/hq0701.093685
Subject(s) - angiogenesis , plasmin , matrix metalloproteinase , plasminogen activator , neovascularization , extracellular matrix , urokinase receptor , urokinase , vitronectin , cancer research , metalloproteinase , chemistry , microbiology and biotechnology , proteolysis , immunology , biology , medicine , endocrinology , biochemistry , enzyme , fibronectin
—Extracellular proteolysis is an absolute requirement for new blood vessel formation (angiogenesis). This review examines the role of the matrix metalloproteinase (MMP) and plasminogen activator (PA)–plasmin systems during angiogenesis. Specifically, a role for gelatinases (MMP-2, MMP-9), membrane-type 1 MMP (MMP-14), the urokinase-type PA receptor, and PA inhibitor 1 has been clearly defined in a number of model systems. The MMP and PA-plasmin systems have also been implicated in experimental vascular tumor formation, and their role during this process will be examined. Antiproteolysis, particularly in the context of angiogenesis, has become a key target in therapeutic strategies aimed at inhibiting tumor growth and other diseases associated with neovascularization.

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