The chemical biology of protein hydropersulfides: Studies of a possible protective function of biological hydropersulfide generation.

Autor: Millikin R; Department of Chemistry, Sonoma State University, Rohnert Park, CA 94928, United States., Bianco CL; Department of Chemistry, Johns Hopkins University, Baltimore, MD 21218, United States., White C; Department of Chemistry, Sonoma State University, Rohnert Park, CA 94928, United States., Saund SS; Department of Chemistry, Sonoma State University, Rohnert Park, CA 94928, United States., Henriquez S; Department of Biology, Sonoma State University, Rohnert Park, CA 94928, United States., Sosa V; Department of Chemistry, Sonoma State University, Rohnert Park, CA 94928, United States., Akaike T; Department of Environmental Health Sciences and Molecular Toxicology, Tohoku University Graduate School of Medicine, Sendai 980-8575, Japan., Kumagai Y; Environmental Biology Section, Faculty of Medicine, University of Tsukuba, Tsukuba, Ibaraki 305-8575, Japan., Soeda S; Department of Chemistry, Sonoma State University, Rohnert Park, CA 94928, United States., Toscano JP; Department of Chemistry, Johns Hopkins University, Baltimore, MD 21218, United States., Lin J; Department of Biology, Sonoma State University, Rohnert Park, CA 94928, United States. Electronic address: linj@sonoma.edu., Fukuto JM; Department of Chemistry, Sonoma State University, Rohnert Park, CA 94928, United States. Electronic address: fukuto@sonoma.edu.
Jazyk: angličtina
Zdroj: Free radical biology & medicine [Free Radic Biol Med] 2016 Aug; Vol. 97, pp. 136-147. Date of Electronic Publication: 2016 May 27.
DOI: 10.1016/j.freeradbiomed.2016.05.013
Abstrakt: The recent discovery of significant hydropersulfide (RSSH) levels in mammalian tissues, fluids and cells has led to numerous questions regarding their possible physiological function. Cysteine hydropersulfides have been found in free cysteine, small molecule peptides as well as in proteins. Based on their chemical properties and likely cellular conditions associated with their biosynthesis, it has been proposed that they can serve a protective function. That is, hydropersulfide formation on critical thiols may protect them from irreversible oxidative or electrophilic inactivation. As a prelude to understanding the possible roles and functions of hydropersulfides in biological systems, this study utilizes primarily chemical experiments to delineate the possible mechanistic chemistry associated with cellular protection. Thus, the ability of hydropersulfides to protect against irreversible electrophilic and oxidative modification was examined. The results herein indicate that hydropersulfides are very reactive towards oxidants and electrophiles and are modified readily. However, reduction of these oxidized/modified species is facile generating the corresponding thiol, consistent with the idea that hydropersulfides can serve a protective function for thiol proteins.
(Copyright © 2016 Elsevier Inc. All rights reserved.)
Databáze: MEDLINE
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