Regulation of angiogenesis is often viewed as a balance between pro-angiogenic and anti-angiogenic factors, and when the balance shifts in favour of angiogenesis stimulators, an angiogenic switch turns on the normally inactive endothelial cells to grow new blood vessels. Recent studies have shown that PLCγ1 (phospholipase Cγ1), a major signalling substrate of VEGFR-2 (vascular endothelial growth factor receptor 2), undergoes c-Cbl-mediated ubiquitination. c-Cbl suppresses tyrosine phosphorylation of PLCγ1 and with it VEGF (vascular endothelial growth factor)-induced endothelial cell proliferation and angiogenesis. Loss of c-Cbl in mice results in enhanced retinal neovascularization, VEGF- and tumour-induced angiogenesis. Notably, this observation suggests that c-Cbl-mediated ubiquitination pathway plays a central role in the ‘angiogenic switch’ employed by the VEGF system. The present article highlights the recent findings demonstrating a novel role for protein ubiquitination in angiogenesis and its potential in angiogenesis-based therapy.
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December 2009
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November 19 2009
A role for protein ubiquitination in VEGFR-2 signalling and angiogenesis Available to Purchase
Nader Rahimi
Nader Rahimi
1
1Departments of Pathology and Ophthalmology, Boston University School of Medicine, 670 Albany Street, Boston, MA 02118, U.S.A.
1email [email protected]
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Publisher: Portland Press Ltd
Received:
June 26 2009
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© The Authors Journal compilation © 2009 Biochemical Society
2009
Biochem Soc Trans (2009) 37 (6): 1189–1192.
Article history
Received:
June 26 2009
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Nader Rahimi; A role for protein ubiquitination in VEGFR-2 signalling and angiogenesis. Biochem Soc Trans 1 December 2009; 37 (6): 1189–1192. doi: https://doi.org/10.1042/BST0371189
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