Journal Article

Control of Cell Fate by Hsp70: More than an Evanescent Meeting

Nobuhiro Morishima

in The Journal of Biochemistry

Published on behalf of The Japanese Biochemical Society

Volume 137, issue 4, pages 449-453
Published in print April 2005 | ISSN: 0021-924X
Published online April 2005 | e-ISSN: 1756-2651 | DOI: http://dx.doi.org/10.1093/jb/mvi057
Control of Cell Fate by Hsp70: More than an Evanescent Meeting

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During their lifetime, proteins inevitably expose hydrophobic segments within the polypeptide chains on a molecule’s surface, which may be otherwise buried inside the molecules in the proper conformation. This potentially dangerous situation is managed with the aid of the 70-kDa heat shock proteins (Hsp70s) and other molecular chaperones. Although a major function of Hsp70 is assisting in efficient folding of anonymous proteins in unfolded states, recent studies have revealed that Hsp70 plays a variety of specific roles, sometimes deciding the cell fate. These multiple activities are based on the specific binding of Hsp70 to proteins in native states, which regulate cell growth and/or death. It is now well recognized that unfolding of some proteins may cause serious diseases, especially those associated with neurodegeneration, such as Alzheimer’s disease. It is suggested that Hsp70 might be a potential drug against these diseases, but caution should be taken because Hsp70 exerts multiple effects by binding to specific proteins.

Keywords: apoptosis; chaperone; Hsp70; neurodegeneration; SceI

Journal Article.  3981 words.  Illustrated.

Subjects: Biochemistry

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