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PMID: 15270699 Published · ppublish English Comment Journal Article Review

Protein kinase function and glutathionylation.

The Biochemical journal ·Vol. 381 ·No. Pt 3 ·2004-08-01 ·Pages e1-2

Anselmo AN, Cobb MH

Abstract

Intracellular reactive oxygen species are generated as a by-product of normal metabolic processes and can both damage cellular constituents and function as important signalling species. This signalling often involves changes in the thiol redox balance. As an antioxidant, glutathione serves in maintaining the reduced state of cellular protein thiol groups. The paper by Cross and Templeton appearing in this issue of the Biochemical Journal describes a mechanism by which glutathionylation plays a key role in the regulation of the kinase activity of MEKK1 [MAP (mitogen-activated protein kinase)/ERK (extracellular-signal-regulated kinase) kinase kinase; MAP3K] in response to oxidative stresses. This type of post-translational-modification glutathionylation may represent a general mechanism by which protein kinase function can be regulated.

MeSH Terms
Glutathione/chemistry Protein Kinases/chemistry,physiology
Chemicals
Protein Kinases Glutathione
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Anselmo Anthony N
Department of Pharmacology, The University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390-9041, USA.
Cobb Melanie H
References (11)
11 references, click to expand
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
1470-8728
Published
2004-08-01
Pages
e1-2
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1133907
Subset
IM
Corrections
CommentOn
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