Acute hypoxia enhances proteins' S-nitrosylation in endothelial cells

Shih-Chung Chen, Bin Huang, Yu Chi Liu, Kou-Gi Shyu, Pen Y. Lin, Danny Ling Wang

Research output: Contribution to journalArticlepeer-review

27 Citations (Scopus)


Hypoxia-induced responses are frequently encountered during cardiovascular injuries. Hypoxia triggers intracellular reactive oxygen species/nitric oxide (NO) imbalance. Recent studies indicate that NO-mediated S-nitrosylation (S-NO) of cysteine residue is a key posttranslational modification of proteins. We demonstrated that acute hypoxia to endothelial cells (ECs) transiently increased the NO levels via endothelial NO synthase (eNOS) activation. A modified biotin-switch method coupled with Western blot on 2-dimentional electrophoresis (2-DE) demonstrated that at least 11 major proteins have significant increase in S-NO after acute hypoxia. Mass analysis by CapLC/Q-TOF identified those as Ras-GTPase-activating protein, protein disulfide-isomerase, human elongation factor-1-delta, tyrosine 3/tryptophan 5-monooxygenase activating protein, and several cytoskeleton proteins. The S-nitrosylated cysteine residue on tropomyosin (Cys 170) and β-actin (Cys 285) was further verified with the trypsic peptides analyzed by MASCOT search program. Further understanding of the functional relevance of these S-nitrosylated proteins may provide a molecular basis for treating ischemia-induced vascular disorders.

Original languageEnglish
Pages (from-to)1274-1278
Number of pages5
JournalBiochemical and Biophysical Research Communications
Issue number4
Publication statusPublished - Dec 26 2008


  • Biotin-switch
  • Endothelial cell
  • Hypoxia
  • Nitric oxide
  • Proteomics
  • S-nitrosylation

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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