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Cited by 294

The DOI matches its Crossref record; 77 of the 77 references it cites were found in a registry or an index.

SIRT1 is a redox‐sensitive deacetylase that is post‐translationally modified by oxidants and carbonyl stress

Open access
Caito, Samuel, Rajendrasozhan, Saravanan, Cook, Suzanne, Chung, Sangwoon, Yao, Hongwei, Friedman, Alan E., Brookes, Paul S., Rahman, Irfan·2010·The FASEB Journal

Abstract

Sirtuinl (SIRT1) deacetylase levels are decreased in chronic inflammatory conditions and aging where oxidative stress occurs. We determined the mechanism of SIRT1 redox post‐translational modifications leading to its degradation. Human lung epithelial cells exposed to hydrogen peroxide (150–250 µM), aldehyde‐acrolein (10–30 µM), and cigarette smoke extract (CSE;0.1–1.5%) in the presence of intracellular glutathione‐modulating agents at 1–24 h, and oxidative post‐translational modifications were assayed in cells, as well as in lungs of mice lacking and overexpressing glutaredoxin‐1 (Glrx1), and wild‐type (WT) mice in response to cigarette smoke (CS). CSE and aldehydes dose and time dependently decreased SIRT1 protein levels, with EC 50 of 1% for CSE and 30 µM for acrolein at 6 h, and >80% inhibition at 24 h with CSE, which was regulated by modulation of intracellular thiol status of the cells. CS decreased the lung levels of SIRT1 in WT mice, which was enhanced by deficiency of Glrx1 and prevented by overexpression of Glrx1. Oxidants, aldehydes, and CS induced carbonyl modifications on SIRT1 on cysteine residues concomitant with decreased SIRT1 activity. Proteomics studies revealed alkylation of cysteine residue on SIRT1. Our data suggest that oxidants/aldehydes covalently modify SIRT1, decreasing enzymatic activity and marking the protein for proteasomal degradation, which has implications in inflammatory conditions.—Caito, S., Rajendrasozhan, S., Cook, S., Chung, S., Yao, H., Friedman, A. E., Brookes, P. S., Rahman, I. SIRT1 is a redox‐sensitive deacetylase that is post‐translationally modified by oxidants and carbonyl stress. FASEB J . 24, 3145–3159 (2010). www.fasebj.org

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Metadata

Authors
Caito, S., Rajendrasozhan, S., Cook, S., Chung, S., Yao, H., Friedman, A. E., Brookes, P. S., & Rahman, I.
Venue
The FASEB Journal
Publisher
Wiley
Published
2010-04-12
Volume
24
Issue
9
Pages
3145-3159
ISSN
  • 0892-6638 (ISSN-L)
  • 1530-6860
OpenAlex
W2113183122
Cited by
294
References
77
FWCI
7.40
Type
journal article
Language
en
Open access
green

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Caito, S., Rajendrasozhan, S., Cook, S., Chung, S., Yao, H., Friedman, A. E., Brookes, P. S., & Rahman, I. (2010). SIRT1 is a redox‐sensitive deacetylase that is post‐translationally modified by oxidants and carbonyl stress. The FASEB Journal. https://doi.org/10.1096/fj.09-151308

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