Kim, Young Mee Song, Eun Joo Seo, Jawon Kim, Hee-Jung Lee, Kong-Joo 2024-01-21T01:34:16Z 2024-01-21T01:34:16Z 2021-08-31 2007-02 1535-3893 https://pubs.kist.re.kr/handle/201004/134719 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 H2O2, 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 H2O2 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. English AMER CHEMICAL SOC HYDROGEN-PEROXIDE IDENTIFICATION ACTIVATION PROTEINS VEGF AUTOPHOSPHORYLATION DEPHOSPHORYLATION TRANSLOCATION RECEPTOR DOMAINS Proteomic analysis of tyrosine phosphorylations in vascular endothelial growth factor- and reactive oxygen species-mediated signaling pathway Article 10.1021/pr060326s 1 JOURNAL OF PROTEOME RESEARCH, v.6, no.2, pp.593 - 601 JOURNAL OF PROTEOME RESEARCH 6 2 593 601 scie scopus 000243927900015 Biochemical Research Methods Biochemistry & Molecular Biology Article HYDROGEN-PEROXIDE IDENTIFICATION ACTIVATION PROTEINS VEGF AUTOPHOSPHORYLATION DEPHOSPHORYLATION TRANSLOCATION RECEPTOR DOMAINS proteomic analysis VEGF ROS tyrosine phosphorylation 2D-gel electrophoresis mass spectrometry tubule formation HUVECs