Effects of peroxynitrite-induced protein modifications on tyrosine phosphorylation and degradation

Andrew J. Gow, Daniel Duran, Stuart Malcolm, Harry Ischiropoulos

    Research output: Contribution to journalArticlepeer-review

    390 Citations (Scopus)


    The ability of protein tyrosine kinases to phosphorylate a synthetic peptide was inhibited 51% by peroxynitrite-mediated nitration of tyrosine. Exposure of endothelial cells to peroxynitrite decreased the intensity of tyrosine phosphorylated proteins and increased the intensity of nitrotyrosine-containing proteins. Peroxynitrite-modified BSA was degraded by human red blood cell lysates. However, human plasma in a concentration-, time-, and temperature-dependent manner, removed the protein nitrotyrosine epitope. These results suggest that tyrosine nitration interferes with phosphorylation and targets proteins for degradation. Specific enzymatic process(es) for removing nitrotyrosine may be present in vivo.

    Original languageEnglish
    Pages (from-to)63-66
    Number of pages4
    JournalFEBS Letters
    Issue number1-2
    Publication statusPublished - 29 Apr 1996


    • Nitric oxide
    • Nitrotyrosine
    • Phosphotyrosine
    • Proteolytic degradation
    • Superoxide

    ASJC Scopus subject areas

    • Biochemistry
    • Biophysics
    • Molecular Biology

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