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Systemic analysis of tyrosine phosphorylated proteins in angiopoietin-1 induced signaling pathway of endothelial cells

Title
Systemic analysis of tyrosine phosphorylated proteins in angiopoietin-1 induced signaling pathway of endothelial cells
Authors
Young M.K.Seo J.Yung H.K.Jeong J.Hye J.J.Lee D.-H.Gou Y.K.Lee K.-J.
Ewha Authors
이동희이공주
SCOPUS Author ID
이동희scopus; 이공주scopus
Issue Date
2007
Journal Title
Journal of Proteome Research
ISSN
1535-3893JCR Link
Citation
vol. 6, no. 8, pp. 3278 - 3290
Indexed
SCI; SCIE; SCOPUS WOS scopus
Abstract
Angiogenesis is an essential process in physiological and pathological processes and is well-regulated to maintain the cellular homeostasis by balancing the endothelial cells in proliferation and apoptosis. Angiopoietin-1 (Ang1) regulates angiogenesis as a ligand of Tie 2 receptor tyrosine kinase. However, the regulation pathways are not well-understood. To date, only a few of the signaling molecules involved in the Tie 2 receptor tyrosine kinase-mediated angiogenesis have been identified. In this study, we systematically identified tyrosine-phosphorylated proteins in Ang1-induced signaling cascade in human umbilical vein endothelial cells (HUVECs), employing proteomic analyses combining two-dimensional gel electrophoresis. Western analysis using phosphotyrosine antibody and mass spectrometry (MALDITOF MS and nanoLC-ESI-q-TOF tandem MS). We report here the identification, semiquantitative analysis, and kinetic changes of tyrosine-phosphorylated proteins in response to Ang1 in HUVECs and identified 66 proteins among 69 protein spots showing significant changes. Of these, p54nrb was validated as a molecule involved in cell migration. These results suggest that Ang1 induces stabilization of neo-vessel network by regulating the phosphorylations of metabolic and structural proteins. © 2007 American Chemical Society.
DOI
10.1021/pr070168k
Appears in Collections:
일반대학원 > 바이오융합과학과 > Journal papers
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