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

Young-Mee Kim, Jawon Seo, Hee Kim Yung, Jaeho Jeong, Joon Joo Hye, Dong Hee Lee, Young Koh Gou, Kong Joo Lee

Research output: Contribution to journalArticle

17 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)3278-3290
Number of pages13
JournalJournal of Proteome Research
Volume6
Issue number8
DOIs
StatePublished - Aug 1 2007

Keywords

  • 2D gel electrophoresis
  • Angiogenesis
  • COMP-Ang1
  • Cell migration
  • HUVECs
  • Proteomics
  • Tyrosine phosphorylation
  • p54nrb

ASJC Scopus subject areas

  • Biochemistry
  • Chemistry(all)

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