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Molecular Aspects of the Stress Response: Chaperones, Membranes and Networks pp 14–26Cite as

The Cellular “Networking” of Mammalian Hsp27 and Its Functions in the Control of Protein Folding, Redox State and Apoptosis

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Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 594))

Abstract

Cells possess effective mechanisms to cope with chronic or acute disturbance of homeo-stasis. Key roles in maintaining or restoring homeostasis are played by the various heat shock or stress proteins (Hsps). Among the Hsps, the group of proteins characterized by low molecular masses (between 20 to 30 kDa) and homology to α-crystallin are called small stress proteins (denoted sHsps). The present chapter summarizes the actual knowledge of the protective mechanisms generated by the expression of mammalian Hsp27 (also denoted HspB1 in human) against the cytotoxicity induced by heat shock and oxidative stress. It also describes the anti-apoptotic properties of Hsp27 and their putative consequences in different pathological conditions.

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Authors and Affiliations

  1. Laboratoire Stress Oxydant, Chaperons et Apoptose, CNRS UMR 5534, Centre de Génétique Moléculaire et Cellulaire, Université Claude Bernard, 16 rue Dubois, 69622, Villeurbanne Cedex, France

    André-Patrick Arrigo

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  1. André-Patrick Arrigo
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Editors and Affiliations

  1. Department of Medical Chemistry, Semmelweis University, Budapest, Hungary

    Peter Csermely

  2. Institute of Biochemistry, Biological Research Center of the Hungarian Academy of Sciences, Szeged, Hungary

    László Vígh

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© 2007 Landes Bioscience and Springer Science+Business Media

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Arrigo, AP. (2007). The Cellular “Networking” of Mammalian Hsp27 and Its Functions in the Control of Protein Folding, Redox State and Apoptosis. In: Csermely, P., Vígh, L. (eds) Molecular Aspects of the Stress Response: Chaperones, Membranes and Networks. Advances in Experimental Medicine and Biology, vol 594. Springer, New York, NY. https://doi.org/10.1007/978-0-387-39975-1_2

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