Journal
FREE RADICAL BIOLOGY AND MEDICINE
Volume 51, Issue 2, Pages 299-313Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.freeradbiomed.2011.04.013
Keywords
Glutathione; Glutathione S-transferase; c-jun NH2 kinase; S-glutathionylation; Signaling pathways; Post-translational modification; Bone marrow; Myeloproliferation; Cancer drug development; Cancer; Genetic polymorphisms
Funding
- NCI NIH HHS [R01 CA085660, R01 CA085660-14, T32 CA075266, T32 CA075266-05] Funding Source: Medline
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Glutathione S-transferase P is abundantly expressed in some mammalian tissues, particularly those associated with malignancies. While the enzyme can catalyze thioether bond formation between some electrophilic chemicals and GSH, novel nondetoxification functions are now ascribed to it. This review summarizes recent material that implicates GSTP in mediating S-glutathionylation of specific clusters of target proteins and in reactions that define a negative regulatory role in some kinase pathways through ligand or protein:protein interactions. It is becoming apparent that GSTP participates in the maintenance of cellular redox homeostasis through a number of convergent and divergent mechanisms. Moreover, drug platforms that have GSTP as a target have produced some interesting preclinical and clinical candidates. (C) 2011 Elsevier Inc. All rights reserved.
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