S-nitrosylation regulates apoptosis

被引：356

作者：

Melino, G

Bernassola, F

Knight, RA

Corasaniti, MT

Nistico, G

FinazziAgro, A

机构：

[1] UNIV AQUILA,COPPITO,DEPT BIOL,I-67100 LAQUILA,ITALY

[2] UNIV ROMA TOR VERGATA,IST DERMOPAT IMMACOLATA,BIOCHEM LAB,I-00133 ROME,ITALY

[3] UNIV LONDON IMPERIAL COLL SCI TECHNOL & MED,NATL HEART & LUNG INST,CYST FIBROSIS DEPT,LONDON SW3 6LR,ENGLAND

[4] UNIV ROMA TOR VERGATA,DEPT EXPT MED,I-00133 ROME,ITALY

来源：

NATURE | 1997年 / 388卷 / 6641期

关键词：

D O I：

10.1038/41237

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

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.

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页码：432 / 433

页数：2

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