S-nitrosylation regulates apoptosis

Gerry Melino (), Francesca Bernassola, Richard A. Knight, Maria Tiziana Corasaniti, Giuseppe Nistic and Alessandro Finazzi-Agr
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Gerry Melino: Biochemistry Laboratory, Istituto Dermopatico Immacolata, University of Rome Tor Vergata
Francesca Bernassola: Biochemistry Laboratory, Istituto Dermopatico Immacolata, University of Rome Tor Vergata
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

Nature, 1997, vol. 388, issue 6641, 432-433

Abstract: 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.

Date: 1997
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DOI: 10.1038/41237

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