Emerging mechanisms of glutathione-dependent chemistry in biology and disease

Janssen-Heininger, YMW; Nolin, JD; Hoffman, SM; Van Der Velden, JL; Tully, JE; Lahue, KG; Abdalla, ST; Chapman, DG; Reynaert, NL; Van Der Vliet, A; Anathy, V

Emerging mechanisms of glutathione-dependent chemistry in biology and disease

Janssen-Heininger, YMW Nolin, JD Hoffman, SM Van Der Velden, JL Tully, JE Lahue, KG Abdalla, ST Chapman, DG

Reynaert, NL Van Der Vliet, A Anathy, V

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Publication Type:: Journal Article
Citation:: Journal of Cellular Biochemistry, 2013, 114 (9), pp. 1962 - 1968
Issue Date:: 2013-08-16

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Field	Value	Language
dc.contributor.author	Janssen-Heininger, YMW	en_US
dc.contributor.author	Nolin, JD	en_US
dc.contributor.author	Hoffman, SM	en_US
dc.contributor.author	Van Der Velden, JL	en_US
dc.contributor.author	Tully, JE	en_US
dc.contributor.author	Lahue, KG	en_US
dc.contributor.author	Abdalla, ST	en_US
dc.contributor.author	Chapman, DG https://orcid.org/0000-0002-8211-1817	en_US
dc.contributor.author	Reynaert, NL	en_US
dc.contributor.author	Van Der Vliet, A	en_US
dc.contributor.author	Anathy, V	en_US
dc.date.available	2013-03-14	en_US
dc.date.issued	2013-08-16	en_US
dc.identifier.citation	Journal of Cellular Biochemistry, 2013, 114 (9), pp. 1962 - 1968	en_US
dc.identifier.issn	0730-2312	en_US
dc.identifier.uri	http://hdl.handle.net/10453/117192
dc.description.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. © 2013 Wiley Periodicals, Inc.	en_US
dc.relation.ispartof	Journal of Cellular Biochemistry	en_US
dc.relation.isbasedon	10.1002/jcb.24551	en_US
dc.subject.classification	Biochemistry & Molecular Biology	en_US
dc.subject.mesh	Animals	en_US
dc.subject.mesh	Humans	en_US
dc.subject.mesh	Sulfhydryl Compounds	en_US
dc.subject.mesh	Biotin	en_US
dc.subject.mesh	Glutathione	en_US
dc.subject.mesh	Oxidation-Reduction	en_US
dc.subject.mesh	Glutaredoxins	en_US
dc.title	Emerging mechanisms of glutathione-dependent chemistry in biology and disease	en_US
dc.type	Journal Article
utslib.citation.volume	9	en_US
utslib.citation.volume	114	en_US
utslib.for	0601 Biochemistry and Cell Biology	en_US
utslib.for	1116 Medical Physiology	en_US
pubs.embargo.period	Not known	en_US
pubs.organisational-group	/University of Technology Sydney
pubs.organisational-group	/University of Technology Sydney/Faculty of Science
pubs.organisational-group	/University of Technology Sydney/Faculty of Science/School of Life Sciences
utslib.copyright.status	closed_access
pubs.issue	9	en_US
pubs.publication-status	Published	en_US
pubs.volume	114	en_US

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. © 2013 Wiley Periodicals, Inc.

Please use this identifier to cite or link to this item:

http://hdl.handle.net/10453/117192