The cellular "networking" of mammalian Hsp27 and its functions in the control of protein folding, redox state and apoptosis.
Cells possess effective mechanisms to cope with chronic or acute disturbance of homeostasis. Key roles in maintaining or restoring homeostasis are played by the various heat shock or stress proteins (Hsps). Among the Hsps, the group of proteins characterized by low molecular masses (between 20 to 30 kDa) and homology to alpha-crystallin are called small stress proteins (denoted sHsps). The present chapter summarizes the actual knowledge of the protective mechanisms generated by the expression of mammalian Hsp27 (also denoted HspB1 in human) against the cytotoxicity induced by heat shock and oxidative stress. It also describes the anti-apoptotic properties of Hsp27 and their putative consequences in different pathological conditions.
Arrigo
André-Patrick
AP
Laboratoire Stress Oxydant, Chaperons et Apoptose, CNRS UMR 5534, Centre de Génétique Moléculaire et Cellulaire, Université Claude Bernard, 16 rue Dubois, 69622 Villeurbanne Cedex, France. arrigo@univ-lyon1.fr
D000818:Animals; D017209:Apoptosis; D006360:Heat-Shock Proteins / Q000737:chemistry / Q000378:metabolism*; D018869:Heat-Shock Response; D006801:Humans; D008928:Mitochondria / Q000378:metabolism; D010084:Oxidation-Reduction; D017510:Protein Folding
D006360:Heat-Shock Proteins