Linked Life Data

17098212

Source:http://linkedlifedata.com/resource/pubmed/id/17098212

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
2007-3-27
pubmed:abstractText
Glutathione (GSH) provides a major source of thiol homeostasis critical to the maintenance of a reduced cellular environment that is conducive to cell survival. Mammals have accumulated a significant cadre of sulfur containing proteins, the interactive significance of which has become clear in recent times. Glutathione transferases (GST) are prevalent in eukaryotes and have been ascribed catalytic functions that involve detoxification of electrophiles through thioether bond formation with the cysteine thiol of GSH. The neutralizing impact of these reactions on products of reactive oxygen has contributed to the significant evolutionary conservation and adaptive functional redundancy of the multifaceted GSH system. Amongst the GSTs, GSTP has been implicated in tumorigenesis and in anticancer drug resistance. Emerging studies indicate that GSTP has ligand binding properties and contributes in the regulation of signaling kinases through direct protein:protein interactions. Furthermore, S-glutathionylation is a post-translational modification of low pK(a) cysteine residues in target proteins. The forward rate of the S-glutathionylation reaction can be influenced by GSTP, whereas the reverse rate is affected by a number of redox sensitive proteins including glutaredoxin, thioredoxin and sulfiredoxin. The functional importance of these reactions in governing how cells respond to oxidative or nitrosative stress exemplifies the broad importance of GSH/GST homeostasis in conditions such as cancer, ageing and neurodegenerative diseases. GSTP has also provided a platform for therapeutic drug development where some agents have completed preclinical testing and are in clinical trial for the management of cancer.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0006-2952
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
73
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1257-69
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Redox in redux: Emergent roles for glutathione S-transferase P (GSTP) in regulation of cell signaling and S-glutathionylation.
pubmed:affiliation
Department of Cell and Molecular Pharmacology and Experimental Therapeutics, Medical University of South Carolina, 173 Ashley Avenue, P.O. Box 250505, Charleston, SC 29425, United States. tewk@musc.edu
pubmed:publicationType
Journal Article