Suppression of Oxidative Stress by β-Hydroxybutyrate, an Endogenous Histone Deacetylase Inhibitor-Reference-Cited by-同舟云学术

Suppression of Oxidative Stress by β-Hydroxybutyrate, an Endogenous Histone Deacetylase Inhibitor

Published:2013-01-11 Issue:6116 Volume:339 Page:211-214
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Shimazu Tadahiro¹²,Hirschey Matthew D.¹²,Newman John¹²,He Wenjuan¹²,Shirakawa Kotaro¹²,Le Moan Natacha³,Grueter Carrie A.⁴⁵,Lim Hyungwook¹²,Saunders Laura R.¹²,Stevens Robert D.⁶,Newgard Christopher B.⁶,Farese Robert V.²⁴⁵,de Cabo Rafael⁷,Ulrich Scott⁸,Akassoglou Katerina³,Verdin Eric¹²

Affiliation:

1. Gladstone Institute of Virology and Immunology, San Francisco, CA 94158, USA.

2. Department of Medicine, University of California, San Francisco, CA 94143, USA.

3. Gladstone Institute of Neurological Disease, San Francisco, CA 94158, USA.

4. Gladstone Institute of Cardiovascular Disease, San Francisco, CA 94158, USA.

5. Department of Biochemistry and Biophysics, University of California, San Francisco, CA 94143, USA.

6. Sarah W. Stedman Nutrition and Metabolism Center, and Departments of Pharmacology and Cancer Biology and Medicine, Duke University Medical Center, Durham, NC 27704, USA.

7. Laboratory of Experimental Gerontology, National Institute on Aging, National Institutes of Health, Baltimore, MD 21224, USA.

8. Department of Chemistry, Ithaca College, Ithaca, NY 14850, USA.

Abstract

Stress Protector During prolonged fasting, the oxidation of fatty acids leads to increased accumulation of d -β-hydroxybutyrate (βOHB) in the bloodstream. Such increased concentrations of βOHB inhibit class I histone deacetylases. Histone acetylation in turn influences transcriptional activity at various genes. Shimazu et al. (p. 211 , published online 6 December; see the Perspective by Sassone-Corsi ) found that among the genes showing increased transcription in animals treated with high concentrations of βOHB were two genes implicated in cellular responses to oxidative stress. When treated ahead of time with βOHB, mice were protected from the toxic effects of the oxidative stress causing poison paraquat.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference26 articles.

1. Rheostat Control of Gene Expression by Metabolites

2. ATP-Citrate Lyase Links Cellular Metabolism to Histone Acetylation

3. Nucleocytosolic Acetyl-Coenzyme A Synthetase Is Required for Histone Acetylation and Global Transcription

4. Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase

5. Sodium butyrate inhibits histone deacetylation in cultured cells

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