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.
Dillmann
W H
WH
Department of Medicine, University of California, San Diego, La Jolla 92093, USA. wdillmann@ucsd.edu
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