S -nitrosylation regulates apoptosis

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 receptor, haemoglobin a...

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Bibliographic Details
Published in:Nature (London) 1997-07, Vol.388 (6641), p.432-433
Main Authors: Melino, Gerry, Bernassola, Francesca, Knight, Richard A, Corasaniti, Maria Tiziana, Nistic, Giuseppe, Finazzi-Agr, Alessandro
Format: Article
Language:English
Subjects:
Antibodies
Apoptosis
Caspase 3
Caspases
Cell death
Cysteine - metabolism
Cysteine Endopeptidases - metabolism
Cytochrome
Enzymes
fas Receptor - metabolism
GTP Phosphohydrolases - metabolism
GTP-Binding Proteins
Humans
Jurkat Cells
Necrosis
Neuroblastoma
Nitric oxide
Nitric Oxide - metabolism
Penicillamine - analogs & derivatives
Penicillamine - metabolism
Poly(ADP-ribose) Polymerases - metabolism
S-Nitroso-N-Acetylpenicillamine
Transglutaminases - metabolism
Tumor Cells, Cultured
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Summary: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 receptor, haemoglobin and transcription factors such as NF-κB 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.
ISSN:0028-0836
1476-4687
DOI:10.1038/41237