期刊
ANTIOXIDANTS & REDOX SIGNALING
卷 13, 期 7, 页码 1023-1032出版社
MARY ANN LIEBERT, INC
DOI: 10.1089/ars.2010.3251
关键词
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资金
- NIH [PO1 HL068758]
- National Heart, Lung, and Blood Institute [N01-HV-28178]
- NIH NCRR [P41-RR10888, S10-R15942, S10-RR20946]
Sirtuin-1 (SIRT1) is an NAD(+)-dependent protein deacetylase that is sensitive to oxidative signals. Our purpose was to determine whether SIRT1 activity is sensitive to the low molecular weight nitrosothiol, S-nitrosoglutathione (GSNO), which can transduce oxidative signals into physiological responses. SIRT1 formed mixed disulfides with GSNO-Sepharose, and mass spectrometry identified several cysteines that are modified by GSNO, including Cys-67 which was S-glutathiolated. GSNO had no effect on basal SIRT1deacetylase activity, but inhibited stimulation of activity by resveratrol (RSV) with an IC50 of 69 mu M. These observations indicate that S-glutathiolation of SIRT1 by low concentrations of reactive glutathione can modulate its enzymatic activity. Antioxid. Redox Signal. 13, 1023-1032.
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