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S-nitrosylation regulates apoptosis

Author

Listed:
  • Gerry Melino

    (Biochemistry Laboratory, Istituto Dermopatico Immacolata, University of Rome Tor Vergata
    Coppito, University of LAquila)

  • Francesca Bernassola

    (Biochemistry Laboratory, Istituto Dermopatico Immacolata, University of Rome Tor Vergata
    Coppito, University of LAquila)

  • Richard A. Knight

    (National Heart and Lung Institute, Imperial College)

  • Maria Tiziana Corasaniti

    (University of Rome Tor Vergata)

  • Giuseppe Nistic

    (University of Rome Tor Vergata)

  • Alessandro Finazzi-Agr

    (University of Rome Tor Vergata)

Abstract

Nitric oxide (NO) modulates the biological activity of proteins by direct interactions with their iron centres. It can also S-nitrosylate cysteines to form S-nitrosothiols. Such reactions affect the activity of membrane-bound, cytosolic and nuclear proteins including the NMDA receptor1, haemoglobin2 and transcription factors such as NF-κB3 and OxyR. NO is potentially toxic, inducing both apoptosis and necrosis. Here we show that NO-mediated S-nitrosylation of the cysteine-containing enzymes that mediate apoptosis (caspases and tissue-transglutaminase, tTG) regulates the balance between apoptosis and necrosis.

Suggested Citation

  • Gerry Melino & Francesca Bernassola & Richard A. Knight & Maria Tiziana Corasaniti & Giuseppe Nistic & Alessandro Finazzi-Agr, 1997. "S-nitrosylation regulates apoptosis," Nature, Nature, vol. 388(6641), pages 432-433, July.
    • Handle: RePEc:nat:nature:v:388:y:1997:i:6641:d:10.1038_41237
    DOI: 10.1038/41237
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