Journal
ANTIOXIDANTS & REDOX SIGNALING
Volume 13, Issue 7, Pages 1023-1032Publisher
MARY ANN LIEBERT, INC
DOI: 10.1089/ars.2010.3251
Keywords
-
Funding
- NIH [PO1 HL068758]
- National Heart, Lung, and Blood Institute [N01-HV-28178]
- NIH NCRR [P41-RR10888, S10-R15942, S10-RR20946]
Ask authors/readers for more resources
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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available