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Citation
Tags
HERO ID
4302231
Reference Type
Journal Article
Subtype
Review
Title
Glutathione peroxidases
Author(s)
Brigelius-Flohé, R; Maiorino, M
Year
2013
Is Peer Reviewed?
1
Journal
Biochimica et Biophysica Acta
ISSN:
0006-3002
EISSN:
1878-2434
Publisher
ELSEVIER SCIENCE BV
Location
AMSTERDAM
Volume
1830
Issue
5
Page Numbers
3289-3303
Language
English
PMID
23201771
DOI
10.1016/j.bbagen.2012.11.020
Web of Science Id
WOS:000317797600011
Abstract
BACKGROUND:
With increasing evidence that hydroperoxides are not only toxic but rather exert essential physiological functions, also hydroperoxide removing enzymes have to be re-viewed. In mammals, the peroxidases inter alia comprise the 8 glutathione peroxidases (GPx1-GPx8) so far identified.
SCOPE OF THE REVIEW:
Since GPxs have recently been reviewed under various aspects, we here focus on novel findings considering their diverse physiological roles exceeding an antioxidant activity.
MAJOR CONCLUSIONS:
GPxs are involved in balancing the H2O2 homeostasis in signalling cascades, e.g. in the insulin signalling pathway by GPx1; GPx2 plays a dual role in carcinogenesis depending on the mode of initiation and cancer stage; GPx3 is membrane associated possibly explaining a peroxidatic function despite low plasma concentrations of GSH; GPx4 has novel roles in the regulation of apoptosis and, together with GPx5, in male fertility. Functions of GPx6 are still unknown, and the proposed involvement of GPx7 and GPx8 in protein folding awaits elucidation.
GENERAL SIGNIFICANCE:
Collectively, selenium-containing GPxs (GPx1-4 and 6) as well as their non-selenium congeners (GPx5, 7 and 8) became key players in important biological contexts far beyond the detoxification of hydroperoxides. This article is part of a Special Issue entitled Cellular functions of glutathione.
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