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Proteomic analysis of tyrosine phosphorylations in vascular endothelial growth factor- and reactive oxygen species-mediated signaling pathway

Title
Proteomic analysis of tyrosine phosphorylations in vascular endothelial growth factor- and reactive oxygen species-mediated signaling pathway
Authors
Young M.K.Eun J.S.Seo J.Kim H.-J.Lee K.-J.
Ewha Authors
이공주김영미김희정
SCOPUS Author ID
이공주scopus; 김영미scopus; 김희정scopusscopusscopus
Issue Date
2007
Journal Title
Journal of Proteome Research
ISSN
1535-3893JCR Link
Citation
vol. 6, no. 2, pp. 593 - 601
Indexed
SCI; SCIE; SCOPUS WOS scopus
Abstract
Vascular endothelial growth factor (VEGF) mediates angiogenic signaling by activating tyrosine kinase receptors. Endothelial cells treated with VEGF are known to increase reactive oxygen species (ROS) production and activate the MAPK pathway. To identify the target proteins of the VEGF receptor, we treated human umbilical vein endothelial cells (HUVECs) with VEGF or H2O 2, and identified and semiquantified tyrosine-phosphorylated proteins, combining 2D-gel electrophoresis, Western analysis using antibody against phospho-tyrosine, and mass spectrometry. We detected 95 proteins that were differentially phosphorylated; some were specifically phosphorylated by VEGF but not by H2O2. 2D-gel electrophoresis revealed that heterogeneous populations of the same protein responded differently to H 2O2 and VEGF. Bioinformatic studies examining the nature of the differential phosphorylation in various subpopulations of proteins should provide new insights into VEGF- and H2O2-induced signaling pathways. © 2007 American Chemical Society.
DOI
10.1021/pr060326s
Appears in Collections:
약학대학 > 약학과 > Journal papers
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