Linked Life Data

15706088

Source:http://linkedlifedata.com/resource/pubmed/id/15706088

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3-4
pubmed:dateCreated
2005-2-11
pubmed:abstractText
Small stress proteins [small heat shock proteins (sHsps)] are molecular chaperones that modulate the ability of cells to respond to oxidative stress. The current knowledge concerning the protective mechanism generated by the expression of mammalian heat shock protein-27 (Hsp27) that allows cells to increase their resistance to oxidative stress is presented. We describe the effects mediated by Hsp27 expression toward crucial enzymes such as glucose-6-phosphate dehydrogenase and glutathione reductase that uphold glutathione in its reduced form. New data are presented showing that the expression of sHsps correlates with a drastic decrease in the intracellular level of iron, a catalyzer of hydroxyl radical (OH( . )) generation. A decreased ability of sHsps expressing cells to concentrate iron will therefore end up in a decreased level of oxidized proteins. In addition, we propose a role of Hsp27 in the presentation of oxidized proteins to the proteasome degradation machinery. We also present an analysis of several Hsp27 mutants that suggests that the C-terminal part of this stress protein is essential for its protective activity against oxidative stress.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1523-0864
pubmed:author
pubmed:issnType
Print
pubmed:volume
7
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
414-22
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:articleTitle
Hsp27 consolidates intracellular redox homeostasis by upholding glutathione in its reduced form and by decreasing iron intracellular levels.
pubmed:affiliation
Laboratoire stress oxydant, chaperons et apoptose, Centre de Génétique Moléculaire et Cellulaire, CNRS UMR-5534, Université Claude Bernard, Lyon-I, Bât. Gregor Mendel, 16 rue Dubois, 69622 Villeurbanne Cédex, France. arrigo@univ-lyon1.fr
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't