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Antioxid Redox Signal. 2010 Oct 1;13(7):1023-32. doi: 10.1089/ars.2010.3251.

Redox regulation of sirtuin-1 by S-glutathiolation.

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  • 1Vascular Biology, Whitaker Cardiovascular Institute, Boston University School of Medicine, Boston, Massachusetts, USA.

Abstract

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 SIRT1 deacetylase activity, but inhibited stimulation of activity by resveratrol (RSV) with an IC(50) of 69 microM. These observations indicate that S-glutathiolation of SIRT1 by low concentrations of reactive glutathione can modulate its enzymatic activity.

PMID:
20392170
[PubMed - indexed for MEDLINE]
PMCID:
PMC2959181
Free PMC Article
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