Linked Life Data

8325038

Source:http://linkedlifedata.com/resource/pubmed/id/8325038

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1993-8-6
pubmed:abstractText
The current knowledge about the structure of GST genes and the molecular mechanisms involved in regulation of their expression are reviewed. Information derived from the study of rat and mouse GST Alpha-class, Ya genes, and a rat GST Pi-class gene seems to indicate that a single cis-regulatory element, composed of two adjacent AP-1-like binding sites in the 5'-flanking region of these GST genes, is responsible for their basal and xenobiotic-inducible activity. The identification of Fos/Jun (AP-1) complex as the trans-acting factor that binds to this element and mediates the basal and inducible expression of GST genes offers a basis for an understanding of the molecular processes involved in GST regulation. The induction of expression of Fos and Jun transcriptional regulatory proteins by a variety of extracellular stimuli is known to mediate the activation of target genes via the AP-1 binding sites. The modulation of the AP-1 activity may account for the changes induced by growth factors, hormones, chemical carcinogens, transforming oncogenes, and cellular stress-inducing agents in the pattern of GST expression. Recent observations implying reactive oxygen as the transduction signal that mediates activation of c-fos and c-jun genes are presently considered to provide an explanation for the induction of GST gene expression by chemical agents of diverse structure. The possibility that these agents may all induce conditions of oxidative stress by various pathways to activate expression of GST genes that are regulated by the AP-1 complex is discussed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1040-9238
pubmed:author
pubmed:issnType
Print
pubmed:volume
28
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
173-207
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Glutathione S-transferases: gene structure and regulation of expression.
pubmed:affiliation
Department of Biochemistry, Weizmann Institute of Science, Rehovot, Israel.
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't