Emerging mechanisms of glutathione-dependent chemistry in biology and disease.
Identifieur interne : 000769 ( Main/Exploration ); précédent : 000768; suivant : 000770Emerging mechanisms of glutathione-dependent chemistry in biology and disease.
Auteurs : Yvonne M W. Janssen-Heininger [États-Unis] ; James D. Nolin ; Sidra M. Hoffman ; Jos L. Van Der Velden ; Jane E. Tully ; Karolyn G. Lahue ; Sarah T. Abdalla ; David G. Chapman ; Niki L. Reynaert ; Albert Van Der Vliet ; Vikas AnathySource :
- Journal of cellular biochemistry [ 1097-4644 ] ; 2013.
Descripteurs français
- KwdFr :
- MESH :
- métabolisme : Biotine, Glutarédoxines, Glutathion, Thiols.
- Animaux, Humains, Oxydoréduction.
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Biotin, Glutaredoxins, Glutathione, Sulfhydryl Compounds.
- Animals, Humans, Oxidation-Reduction.
Abstract
Glutathione has traditionally been considered as an antioxidant that protects cells against oxidative stress. Hence, the loss of reduced glutathione and formation of glutathione disulfide is considered a classical parameter of oxidative stress that is increased in diseases. Recent studies have emerged that demonstrate that glutathione plays a more direct role in biological and pathophysiological processes through covalent modification to reactive cysteines within proteins, a process known as S-glutathionylation. The formation of an S-glutathionylated moiety within the protein can lead to structural and functional modifications. Activation, inactivation, loss of function, and gain of function have all been attributed to S-glutathionylation. In pathophysiological settings, S-glutathionylation is tightly regulated. This perspective offers a concise overview of the emerging field of protein thiol redox modifications. We will also cover newly developed methodology to detect S-glutathionylation in situ, which will enable further discovery into the role of S-glutathionylation in biology and disease.
DOI: 10.1002/jcb.24551
PubMed: 23554102
PubMed Central: PMC3857728
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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<term>Biotin (metabolism)</term>
<term>Glutaredoxins (metabolism)</term>
<term>Glutathione (metabolism)</term>
<term>Humans (MeSH)</term>
<term>Oxidation-Reduction (MeSH)</term>
<term>Sulfhydryl Compounds (metabolism)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term>
<term>Biotine (métabolisme)</term>
<term>Glutarédoxines (métabolisme)</term>
<term>Glutathion (métabolisme)</term>
<term>Humains (MeSH)</term>
<term>Oxydoréduction (MeSH)</term>
<term>Thiols (métabolisme)</term>
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<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Biotin</term>
<term>Glutaredoxins</term>
<term>Glutathione</term>
<term>Sulfhydryl Compounds</term>
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<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Biotine</term>
<term>Glutarédoxines</term>
<term>Glutathion</term>
<term>Thiols</term>
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<term>Humans</term>
<term>Oxidation-Reduction</term>
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<front><div type="abstract" xml:lang="en">Glutathione has traditionally been considered as an antioxidant that protects cells against oxidative stress. Hence, the loss of reduced glutathione and formation of glutathione disulfide is considered a classical parameter of oxidative stress that is increased in diseases. Recent studies have emerged that demonstrate that glutathione plays a more direct role in biological and pathophysiological processes through covalent modification to reactive cysteines within proteins, a process known as S-glutathionylation. The formation of an S-glutathionylated moiety within the protein can lead to structural and functional modifications. Activation, inactivation, loss of function, and gain of function have all been attributed to S-glutathionylation. In pathophysiological settings, S-glutathionylation is tightly regulated. This perspective offers a concise overview of the emerging field of protein thiol redox modifications. We will also cover newly developed methodology to detect S-glutathionylation in situ, which will enable further discovery into the role of S-glutathionylation in biology and disease.</div>
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<Abstract><AbstractText>Glutathione has traditionally been considered as an antioxidant that protects cells against oxidative stress. Hence, the loss of reduced glutathione and formation of glutathione disulfide is considered a classical parameter of oxidative stress that is increased in diseases. Recent studies have emerged that demonstrate that glutathione plays a more direct role in biological and pathophysiological processes through covalent modification to reactive cysteines within proteins, a process known as S-glutathionylation. The formation of an S-glutathionylated moiety within the protein can lead to structural and functional modifications. Activation, inactivation, loss of function, and gain of function have all been attributed to S-glutathionylation. In pathophysiological settings, S-glutathionylation is tightly regulated. This perspective offers a concise overview of the emerging field of protein thiol redox modifications. We will also cover newly developed methodology to detect S-glutathionylation in situ, which will enable further discovery into the role of S-glutathionylation in biology and disease.</AbstractText>
<CopyrightInformation>Copyright © 2013 Wiley Periodicals, Inc.</CopyrightInformation>
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<Keyword MajorTopicYN="N">GLUTAREDOXIN-1</Keyword>
<Keyword MajorTopicYN="N">PROTEIN S-GLUTATHIONYLATION</Keyword>
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