Display Settings:

Format

Send to:

Choose Destination
Antioxid Redox Signal. 2005 Mar-Apr;7(3-4):414-22.

Hsp27 consolidates intracellular redox homeostasis by upholding glutathione in its reduced form and by decreasing iron intracellular levels.

Author information

  • 1Laboratoire 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

Abstract

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.

PMID:
15706088
[PubMed - indexed for MEDLINE]
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Icon for Mary Ann Liebert, Inc.
    Loading ...
    Write to the Help Desk