Premium
A metalloproteinase inhibitor as an inhibitor of neovascularization
Author(s) -
Moses Marsha A.,
Langer Robert
Publication year - 1991
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.240470308
Subject(s) - angiogenesis , matrix metalloproteinase , collagenase , neovascularization , metalloproteinase , matrix metalloproteinase inhibitor , in vivo , endogeny , proteolytic enzymes , angiogenesis inhibitor , chemistry , tissue inhibitor of metalloproteinase , in vitro , extracellular matrix , microbiology and biotechnology , enzyme , biochemistry , biology , cancer research
Metalloproteinases and their endogenous inhibitors are key components of an enzyme system which is important in a number of fundamental biochemical and cellular processes. Our recent work has focused on the role of a particular metalloproteinase, collagenase, and the role of an endogenous inhibitor of this enzyme in the control of neovascularization. The proteolytic degradation of extracellular matrix components by capillary endothelial cells (EC) has been shown to be one of the key prerequisites of the angiogenic process. As part of a study of the effect(s) of the inhibition of collagenase on neovascularization, we have recently reported the purification, characterization and partial NH 2 ‐terminal sequence of a cartilage‐derived inhibitor (CDI) of angiogenesis in vivo and in vitro. Evidence is presented which suggests that one means of controlling deregualted vascular growth characteristic of a number of “angiogenic diseases” may be at the level of the control of metalloproteinase activity.