Hsp27 (HspB1) and alphaB-crystallin (HspB5) as therapeutic targets

FEBS Letters

 

 

Volume 581, Issue 19, 31 July 2007, Pages 3665-3674
Cellular Stress

Copyright © 2007 Federation of European Biochemical Societies Published by Elsevier B.V.

André-Patrick Arrigoa,, Stéphanie Simona, b, Benjamin Giberta, Carole Kretz-Remya, Mathieu Nivona, Anna Czekallaa, Dominique Guilleta, Maryline Moulina, Chantal Diaz-Latouda and Patrick Vicartb

aLaboratoire Stress, Chaperons et Mort Cellulaire, CNRS, UMR5534, Centre de Génétique Moléculaire et Cellulaire, Université Lyon 1, Bat. Gregor Mendel, 16 Rue Dubois, F-69622, Villeurbanne Cedex, France

bEA 300 Stress et Pathologies du Cytosquelette, UFR de Biochimie, Université Paris 7, Paris, France

Received 16 February 2007; 
revised 11 April 2007; 
accepted 15 April 2007. 
Available online 24 April 2007.


Abstract

Hsp27 and αB-crystallin are molecular chaperones that are constitutively expressed in several mammalian cells, particularly in pathological conditions. These proteins share functions as diverse as protection against toxicity mediated by aberrantly folded proteins or oxidative-inflammation conditions. In addition, these proteins share anti-apoptotic properties and are tumorigenic when expressed in cancer cells. This review summarizes the current knowledge about Hsp27 and αB-crystallin and the implications, either positive or deleterious, of these proteins in pathologies such as neurodegenerative diseases, myopathies, asthma, cataracts and cancers. Approaches towards therapeutic strategies aimed at modulating the expression and/or the activities of Hsp27 and αB-crystallin are presented.

 

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