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VEGF Receptor Signaling and Endothelial Function
Author(s) -
Kliche Stefanie,
Waltenberger Johannes
Publication year - 2001
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216540252774784
Subject(s) - angiogenesis , microbiology and biotechnology , receptor tyrosine kinase , vascular endothelial growth factor a , protein kinase b , kinase insert domain receptor , cancer research , vascular endothelial growth factor , signal transduction , tyrosine kinase , endothelial stem cell , vascular endothelial growth factor b , ask1 , biology , chemistry , kinase , protein kinase a , mitogen activated protein kinase kinase , biochemistry , vegf receptors , in vitro
Angiogenesis, the formation of new blood vessels from preexisting ones, is a central process during normal development and during pathological repair. Vascular endothelial growth factor‐A (VEGF‐A) can stimulate both physiological and pathological angiogensis. VEGF‐A is a ligand for the two receptor tyrosine kinases VEGFR‐1 (Flt‐1) and VEGFR‐2 (KDR/Flk‐1). Most biological functions of VEGF‐A are mediated via VEGFR‐2, whereas the role of VEGFR‐1 is largely unknown. Activation of mitogenactivated kinase, stress‐activated kinase, protein kinase C, and the Akt pathway are implicated in VEGF‐A‐dependent endothelial function, including cell survival, proliferation, generation of nitric oxide, and the induction of angiogenesis. Induction of metalloproteinases, activation of focal adhesion kinase and of PI3‐kinase are implicated in VEGF‐A‐induced endothelial cell migration. The important role of nitric oxide as a mediator of endothelial function in vivo links the receptor signaling network to other biological effects.