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Sci. Signal., 1 January 2013
Vol. 6, Issue 256, p. rs1
[DOI: 10.1126/scisignal.2003252]

RESEARCH RESOURCES

Editor's Summary

Altering Metabolism Through S-Nitrosylation
Derivatives of the gasotransmitter nitric oxide can be covalently linked to cysteine residues through a process called S-nitrosylation. Using mass spectrometry, Doulias et al. identified S-nitrosylated proteins in multiple mouse tissues, including the liver. Many of the S-nitrosylated proteins had roles in metabolic processes that occur in mitochondria, such as β-oxidation of fatty acids. S-nitrosylation of VLCAD [very long chain acyl–coenzyme A (CoA) dehydrogenase], an enzyme in the liver that catalyzes the first committed step in fatty acid β-oxidation, improved its catalytic efficiency in vitro, which would be expected to increase fatty acid metabolism and decrease hepatic steatosis, or the accumulation of fat and triglycerides in the liver. Mice used as a model for obesity (ob/ob mice) spontaneously develop hepatic steatosis, and treatment of ob/ob mice with GSNO, a compound that releases nitric oxide, reduced liver triglyceride concentrations and fatty deposits in the liver. Thus, these results implicate S-nitrosylation in the regulation of the activity of several metabolic enzymes.

Citation: P.-T. Doulias, M. Tenopoulou, J. L. Greene, K. Raju, H. Ischiropoulos, Nitric Oxide Regulates Mitochondrial Fatty Acid Metabolism Through Reversible Protein S-Nitrosylation. Sci. Signal. 6, rs1 (2013).

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THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Protein Microarray Characterization of the S-Nitrosoproteome.
Y.-I. Lee, D. Giovinazzo, H. C. Kang, Y. Lee, J. S. Jeong, P.-T. Doulias, Z. Xie, J. Hu, M. Ghasemi, H. Ischiropoulos, et al. (2014)
Mol. Cell. Proteomics 13, 63-72
   Abstract »    Full Text »    PDF »
Regulation of Protein Function and Signaling by Reversible Cysteine S-Nitrosylation.
N. Gould, P.-T. Doulias, M. Tenopoulou, K. Raju, and H. Ischiropoulos (2013)
J. Biol. Chem. 288, 26473-26479
   Abstract »    Full Text »    PDF »

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