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Caveolin‐1 scaffolding domain peptides inhibits endothelial cell proliferation
Author(s) -
Fang Kai,
Terracciano Justin,
Kevil Christopher G
Publication year - 2009
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.23.1_supplement.116.8
Subject(s) - caveolin 1 , angiogenesis , caveolae , microbiology and biotechnology , cell growth , endothelial stem cell , caveolin , chemistry , mapk/erk pathway , phosphorylation , scaffold protein , signal transduction , biology , cancer research , biochemistry , in vitro
Angiogenesis is the process of new blood vessel sprouts from existing capillary networks with endothelial cell proliferation serving an essential role in this process. Caveolin‐1 protein is a plasma membrane protein governing caveolae formation that interacts with several signaling receptors and when over‐expressed can inhibit endothelial cell proliferation. However, the molecular mechanism of caveolin‐1 inhibition of endothelial proliferation is not known. Here we demonstrate that the Cav‐1 scaffolding domain (AP‐Cav amino acids 82‐101) significantly inhibits VEGF stimulation of Erk 1/2 phosphorylation and BrdU incorporation of endothelial cells compared to control AP peptide. Our studies demonstrate that the caveolin‐1 scaffolding domain peptide functionally inhibits endothelial cell proliferation which may be useful in designing novel types of angiogenesis inhibitors.