Lipopolysaccharide activates matrix metalloproteinase-2 in endothelial cells through an NF-kappa B-dependent pathway

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Vascular endothelial cells release proteinases that degrade the extracellular matrix, thus enabling cell migration during angiogenesis and vasculogenesis. Endothelial cells secrete mainly the preform of matrix metalloproteinase-2 (proMMP-2). In this report, we examined several growth factors, cytokines, and other molecules for activation of MMP-2 by human umbilical vein endothelial cells. Of these factors, we found that lipopolysaccharide (LPS) is the strongest activator of MMP-2. LPS induced MMP-2 activation in a time- and dose-dependent manner. While pretreatment with zinc chelators or nuclear factor kappa B (NF-kappa B) inhibitors suppressed LPS-induced MMP-2 activation, pretreatment with phosphatidylinositol S'-kinase inhibitors had no effect. These results indicate that, in endothelial cells, LPS can directly enhance angiogenesis by inducing MMP-2 activation mediated through an NF-kappa B pathway, (C) 2000 Academic Press.
Publisher
ACADEMIC PRESS INC
Issue Date
2000-03
Language
English
Article Type
Article
Keywords

BACTERIAL LIPOPOLYSACCHARIDE; EXTRACELLULAR-MATRIX; ANGIOGENESIS; MECHANISMS; ENDOTOXIN

Citation

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.269, no.2, pp.401 - 405

ISSN
0006-291X
URI
http://hdl.handle.net/10203/73867
Appears in Collection
MSE-Journal Papers(저널논문)
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