Hsp27: novel regulator of intracellular redox state.
Small stress proteins are molecular chaperones that modulate the ability of cells to respond to several types of injuries. In this regard, a protection generated by the expression of mammalian small stress proteins against the cell death induced by oxidative stress has been described. This review summarizes the current knowledge of the protective mechanism generated by the expression of the major mammalian small stress protein Hsp27 in cells exposed to oxidative stress. A possible role of this chaperone protein in the presentation of oxidized proteins to the proteasome degradation machinery is proposed.
Arrigo
A P
AP
Centre de Génétique Moléculaire et Cellulaire, CNRS UMR5534, Université Claude Bernard Lyon-I, Villeurbanne, France. arrigo@univ-lyon1.fr
D000818:Animals; D016923:Cell Death; D018833:Chaperonins / Q000378:metabolism; D055551:HSP27 Heat-Shock Proteins; D006360:Heat-Shock Proteins; D006801:Humans; D008954:Models, Biological; D018832:Molecular Chaperones; D009363:Neoplasm Proteins / Q000737:chemistry* / Q000378:metabolism*; D010084:Oxidation-Reduction; D018384:Oxidative Stress
D055551:HSP27 Heat-Shock Proteins; C057725:HSPB1 protein, human; D006360:Heat-Shock Proteins; D018832:Molecular Chaperones; D009363:Neoplasm Proteins; D018833:Chaperonins