Small heat shock proteins and protection against injury.
The small heat shock proteins alpha B crystallin and HSP27 exert a protective effect in response to simulated ischemia. A model is proposed whereby proteins not in their final folding state bind to the outside of the large oligomeric small heat shock protein complexes thus finding a safe haven during ischemia. After the ischemia is resolved, these proteins may be released and, with the help of HSP70, are shuttled to a productive refolding pathway resulting in proteins in their final folding state, which can assume their normal activity in cells recovered from ischemic injury.
Department of Medicine, University of California, San Diego, La Jolla 92093, USA. wdillmann@ucsd.edu
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D000818:Animals; D003459:Crystallins / Q000502:physiology*; D055551:HSP27 Heat-Shock Proteins; D006321:Heart / Q000503:physiopathology*; D006360:Heat-Shock Proteins; D006801:Humans; D018832:Molecular Chaperones; D017202:Myocardial Ischemia / Q000473:pathology / Q000503:physiopathology*; D009363:Neoplasm Proteins / Q000502:physiology*
D003459:Crystallins; D055551:HSP27 Heat-Shock Proteins; C057725:HSPB1 protein, human; D006360:Heat-Shock Proteins; D018832:Molecular Chaperones; D009363:Neoplasm Proteins