Sirtuin Oxidative Post-translational Modifications

Increased sirtuin deacylase activity is correlated with increased lifespan and healthspan in eukaryotes. Conversely, decreased sirtuin deacylase activity is correlated with increased susceptibility to aging-related diseases. However, the mechanisms leading to decreased sirtuin activity during aging...

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Autores principales:	Kelsey S. Kalous, Sarah L. Wynia-Smith, Brian C. Smith
Formato:	article
Lenguaje:	EN
Publicado:	Frontiers Media S.A. 2021
Materias:	sirtuin (SIRT) nitrosation glutathionylation sulfhydration sulfenylation nitration Physiology QP1-981
Acceso en línea:	https://doaj.org/article/6c73bd3b04864ad2be85781ed3403023
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spelling	oai:doaj.org-article:6c73bd3b04864ad2be85781ed34030232021-11-30T17:54:56ZSirtuin Oxidative Post-translational Modifications1664-042X10.3389/fphys.2021.763417https://doaj.org/article/6c73bd3b04864ad2be85781ed34030232021-11-01T00:00:00Zhttps://www.frontiersin.org/articles/10.3389/fphys.2021.763417/fullhttps://doaj.org/toc/1664-042XIncreased sirtuin deacylase activity is correlated with increased lifespan and healthspan in eukaryotes. Conversely, decreased sirtuin deacylase activity is correlated with increased susceptibility to aging-related diseases. However, the mechanisms leading to decreased sirtuin activity during aging are poorly understood. Recent work has shown that oxidative post-translational modification by reactive oxygen (ROS) or nitrogen (RNS) species results in inhibition of sirtuin deacylase activity through cysteine nitrosation, glutathionylation, sulfenylation, and sulfhydration as well as tyrosine nitration. The prevalence of ROS/RNS (e.g., nitric oxide, S-nitrosoglutathione, hydrogen peroxide, oxidized glutathione, and peroxynitrite) is increased during inflammation and as a result of electron transport chain dysfunction. With age, cellular production of ROS/RNS increases; thus, cellular oxidants may serve as a causal link between loss of sirtuin activity and aging-related disease development. Therefore, the prevention of inhibitory oxidative modification may represent a novel means to increase sirtuin activity during aging. In this review, we explore the role of cellular oxidants in inhibiting individual sirtuin human isoform deacylase activity and clarify the relevance of ROS/RNS as regulatory molecules of sirtuin deacylase activity in the context of health and disease.Kelsey S. KalousSarah L. Wynia-SmithBrian C. SmithFrontiers Media S.A.articlesirtuin (SIRT)nitrosationglutathionylationsulfhydrationsulfenylationnitrationPhysiologyQP1-981ENFrontiers in Physiology, Vol 12 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	sirtuin (SIRT) nitrosation glutathionylation sulfhydration sulfenylation nitration Physiology QP1-981
spellingShingle	sirtuin (SIRT) nitrosation glutathionylation sulfhydration sulfenylation nitration Physiology QP1-981 Kelsey S. Kalous Sarah L. Wynia-Smith Brian C. Smith Sirtuin Oxidative Post-translational Modifications
description	Increased sirtuin deacylase activity is correlated with increased lifespan and healthspan in eukaryotes. Conversely, decreased sirtuin deacylase activity is correlated with increased susceptibility to aging-related diseases. However, the mechanisms leading to decreased sirtuin activity during aging are poorly understood. Recent work has shown that oxidative post-translational modification by reactive oxygen (ROS) or nitrogen (RNS) species results in inhibition of sirtuin deacylase activity through cysteine nitrosation, glutathionylation, sulfenylation, and sulfhydration as well as tyrosine nitration. The prevalence of ROS/RNS (e.g., nitric oxide, S-nitrosoglutathione, hydrogen peroxide, oxidized glutathione, and peroxynitrite) is increased during inflammation and as a result of electron transport chain dysfunction. With age, cellular production of ROS/RNS increases; thus, cellular oxidants may serve as a causal link between loss of sirtuin activity and aging-related disease development. Therefore, the prevention of inhibitory oxidative modification may represent a novel means to increase sirtuin activity during aging. In this review, we explore the role of cellular oxidants in inhibiting individual sirtuin human isoform deacylase activity and clarify the relevance of ROS/RNS as regulatory molecules of sirtuin deacylase activity in the context of health and disease.
format	article
author	Kelsey S. Kalous Sarah L. Wynia-Smith Brian C. Smith
author_facet	Kelsey S. Kalous Sarah L. Wynia-Smith Brian C. Smith
author_sort	Kelsey S. Kalous
title	Sirtuin Oxidative Post-translational Modifications
title_short	Sirtuin Oxidative Post-translational Modifications
title_full	Sirtuin Oxidative Post-translational Modifications
title_fullStr	Sirtuin Oxidative Post-translational Modifications
title_full_unstemmed	Sirtuin Oxidative Post-translational Modifications
title_sort	sirtuin oxidative post-translational modifications
publisher	Frontiers Media S.A.
publishDate	2021
url	https://doaj.org/article/6c73bd3b04864ad2be85781ed3403023
work_keys_str_mv	AT kelseyskalous sirtuinoxidativeposttranslationalmodifications AT sarahlwyniasmith sirtuinoxidativeposttranslationalmodifications AT briancsmith sirtuinoxidativeposttranslationalmodifications
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Sirtuin Oxidative Post-translational Modifications

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