Protein S-nitrosylation in preconditioning and postconditioning

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Postconditioning leads to an increase in protein S-nitrosylation.

Previous studies have shown a role for nitric oxide and S-nitrosylation (SNO) in postconditioning (PostC), but specific SNO proteins and sites have not been identified in the myocardium after PostC. In this study, we examined SNO signaling in PostC using a Langendorff-perfused mouse heart model. After 20 min of equilibrium perfusion and 25 min of global ischemia, PostC was applied at the beginn...

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Ischaemic preconditioning preferentially increases protein S-nitrosylation in subsarcolemmal mitochondria.

Nitric oxide (NO) and protein S-nitrosylation (SNO) have been shown to play important roles in ischaemic preconditioning (IPC)-induced acute cardioprotection. The majority of proteins that show increased SNO following IPC are localized to the mitochondria, and our recent studies suggest that caveolae transduce acute NO/SNO cardioprotective signalling in IPC hearts. Due to the close association ...

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Protein S-nitrosylation and cardioprotection.

Nitric oxide (NO) plays an important role in the regulation of cardiovascular function. In addition to the classic NO activation of the cGMP-dependent pathway, NO can also regulate cell function through protein S-nitrosylation, a redox dependent, thiol-based, reversible posttranslational protein modification that involves attachment of an NO moiety to a nucleophilic protein sulfhydryl group. Th...

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Preconditioning and Postconditioning

Joseph T. McCabe1, Michael W. Bentley2 and Joseph C. O’Sullivan2 1Department of Anatomy, Physiology & Genetics, and The Center for Neuroscience & Regenerative Medicine, Uniformed Services University of the Health Sciences, Bethesda, Maryland 2U.S. Army Graduate School of Anesthesia Nursing, Graduate School, AMEDD Center and School, Academy of Health Sciences, Fort Sam Houston, San Antonio, Texa...

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Aberrant Protein S-Nitrosylation in Neurodegenerative Diseases

S-Nitrosylation is a redox-mediated posttranslational modification that regulates protein function via covalent reaction of nitric oxide (NO)-related species with a cysteine thiol group on the target protein. Under physiological conditions, S-nitrosylation can be an important modulator of signal transduction pathways, akin to phosphorylation. However, with aging or environmental toxins that gen...

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ژورنال

عنوان ژورنال: Experimental Biology and Medicine

سال: 2014

ISSN: 1535-3702,1535-3699

DOI: 10.1177/1535370214522935