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Hsp27 (HspB1) and αB‐crystallin (HspB5) as therapeutic targets
Author(s) -
Arrigo André-Patrick,
Simon Stéphanie,
Gibert Benjamin,
Kretz-Remy Carole,
Nivon Mathieu,
Czekalla Anna,
Guillet Dominique,
Moulin Maryline,
Diaz-Latoud Chantal,
Vicart Patrick
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.04.033
Subject(s) - hsp27 , crystallin , heat shock protein , cataracts , cancer research , biology , microbiology and biotechnology , hsp70 , chemistry , biochemistry , genetics , gene
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.