PMID- 17662654
OWN - NLM
STAT- MEDLINE
DCOM- 20071108
LR  - 20131121
IS  - 1471-4892 (Print)
IS  - 1471-4892 (Linking)
VI  - 7
IP  - 4
DP  - 2007 Aug
TI  - Mechanisms of reversible protein glutathionylation in redox signaling and 
      oxidative stress.
PG  - 381-91
AB  - Reversible protein S-glutathionylation (protein-SSG) is an important 
      post-translational modification, providing protection of protein cysteines from 
      irreversible oxidation and serving to transduce redox signals. Analogous to 
      phosphatases, glutaredoxin (GRx) enzymes catalyze deglutathionylation of 
      proteins, regulating diverse intracellular signaling pathways. Recently, other 
      enzymes have been reported to exhibit deglutathionylating activity, but their 
      contribution to intracellular protein deglutathionylation is uncertain. 
      Currently, no enzyme has been shown to serve as a catalyst of S-glutathionylation 
      in situ, although potential prototypes are reported, including human GRx1 and the 
      pi isoform of glutathione-S-transferase (GSTpi). Further insight into cellular 
      mechanisms of protein glutathionylation and deglutathionylation will enrich our 
      understanding of redox signal transduction and potentially identify new 
      therapeutic targets for diseases in which oxidative stress perturbs normal redox 
      signaling. Accordingly, this review focuses primarily on mechanisms of catalysis 
      in mammalian systems.
FAU - Gallogly, Molly M
AU  - Gallogly MM
AD  - Department of Pharmacology, School of Medicine, Case Western Reserve University, 
      10900 Euclid Avenue, and the Louis Stokes Cleveland Veterans Affairs Medical 
      Research Center, Cleveland, OH 44106-4965, United States.
FAU - Mieyal, John J
AU  - Mieyal JJ
LA  - eng
GR  - 1F30AG029687/AG/NIA NIH HHS/United States
GR  - P01 AG 15885/AG/NIA NIH HHS/United States
GR  - R01 AG 024413/AG/NIA NIH HHS/United States
GR  - T32 GM008803/GM/NIGMS NIH HHS/United States
GR  - T32 GM07250/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
PT  - Research Support, U.S. Gov't, Non-P.H.S.
PT  - Review
DEP - 20070726
PL  - England
TA  - Curr Opin Pharmacol
JT  - Current opinion in pharmacology
JID - 100966133
RN  - 0 (GLRX protein, human)
RN  - 0 (Glutaredoxins)
RN  - 0 (Sulfhydryl Compounds)
RN  - EC 1.- (Oxidoreductases)
RN  - GAN16C9B8O (Glutathione)
RN  - K848JZ4886 (Cysteine)
SB  - IM
MH  - Animals
MH  - Catalysis
MH  - Cysteine/chemistry/*metabolism
MH  - Glutaredoxins
MH  - Glutathione/chemistry/*metabolism
MH  - Humans
MH  - Oxidation-Reduction
MH  - *Oxidative Stress
MH  - Oxidoreductases/metabolism
MH  - *Protein Processing, Post-Translational
MH  - Signal Transduction
MH  - Sulfhydryl Compounds/chemistry/metabolism
RF  - 106
EDAT- 2007/07/31 09:00
MHDA- 2007/11/09 09:00
CRDT- 2007/07/31 09:00
PHST- 2007/04/12 00:00 [received]
PHST- 2007/05/29 00:00 [revised]
PHST- 2007/06/07 00:00 [accepted]
PHST- 2007/07/31 09:00 [pubmed]
PHST- 2007/11/09 09:00 [medline]
PHST- 2007/07/31 09:00 [entrez]
AID - S1471-4892(07)00103-8 [pii]
AID - 10.1016/j.coph.2007.06.003 [doi]
PST - ppublish
SO  - Curr Opin Pharmacol. 2007 Aug;7(4):381-91. doi: 10.1016/j.coph.2007.06.003. Epub 
      2007 Jul 26.