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Scientifica
Volume 2012, Article ID 185641, 19 pages
http://dx.doi.org/10.6064/2012/185641
Review Article

Pathology-Dependent Effects Linked to Small Heat Shock Proteins Expression: An Update

Apoptosis Cancer and Development Laboratory, Lyon Cancer Research Center, INSERM U1052-CNRS UMR5286, Centre Léon Bérard, Claude Bernard University Lyon1, 28 Rue Laennec, 69008 Lyon, France

Received 13 August 2012; Accepted 17 September 2012

Academic Editors: M. Hikida, D. Jun, M. H. Manjili, and C. Ramos

Copyright © 2012 A.-P. Arrigo. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Abstract

Small heat shock proteins (small Hsps) are stress-induced molecular chaperones that act as holdases towards polypeptides that have lost their folding in stress conditions or consequently of mutations in their coding sequence. A cellular protection against the deleterious effects mediated by damaged proteins is thus provided to cells. These chaperones are also highly expressed in response to protein conformational and inflammatory diseases and cancer pathologies. Through specific and reversible modifications in their phospho-oligomeric organization, small Hsps can chaperone appropriate client proteins in order to provide cells with resistance to different types of injuries or pathological conditions. By helping cells to better cope with their pathological status, their expression can be either beneficial, such as in diseases characterized by pathological cell degeneration, or deleterious when they are required for tumor cell survival. Moreover, small Hsps are actively released by cells and can act as immunogenic molecules that have dual effects depending on the pathology. The cellular consequences linked to their expression levels and relationships with other Hsps as well as therapeutic strategies are discussed in view of their dynamic structural organization required to interact with specific client polypeptides.