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Laminin binding to the calreticulin fragment vasostatin regulates endothelial cell function
Author(s) -
Yao Lei,
Pike Sandra E.,
Tosato Giovanna
Publication year - 2002
Publication title -
journal of leukocyte biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.819
H-Index - 191
eISSN - 1938-3673
pISSN - 0741-5400
DOI - 10.1189/jlb.71.1.47
Subject(s) - biology , calreticulin , microbiology and biotechnology , function (biology) , fragment (logic) , laminin , computational biology , endoplasmic reticulum , computer science , extracellular matrix , programming language
Vasostatin, the 1–180 amino acids NH 2 domain ofcalreticulin, inhibits endothelial cell proliferation, angiogenesis, and tumor growth, but the mechanisms underlying these effects areunclear. We show that endothelial cells express the extracellularmatrix protein laminin, including chains α5 and γ1 and thatvasostatin specifically binds to laminin. When added to endothelialcell cultures, vasostatin specifically inhibits endothelial cellattachment to laminin and by this mechanism, can reduce subsequentendothelial cell growth induced by basic fibroblast growth factor. Asan angiogenesis inhibitor that specifically disrupts endothelial cellattachment to components of the extracellular matrix, vasostatin has aunique potential as a cancer therapeutic.