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First published online May 28, 2004
doi: 10.1242/10.1242/jcs.01284


Journal of Cell Science 117, 2641-2651 (2004)
Published by The Company of Biologists 2004
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`The stress of dying': the role of heat shock proteins in the regulation of apoptosis

Helen M. Beere

La Jolla Institute for Allergy and Immunology, 10355 Science Center Drive, San Diego, CA 92121, USA




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Fig. 1. Events regulated by Hsps in the mitochondrial or `intrinsic' apoptotic pathway. Extracellular signals or stresses converge to regulate the mitochondria-mediated pathway to caspase activation and cell death. Heat shock proteins intervene at multiple points within this pathway both upstream (A) and downstream (B) of the associated mitochondrial changes to regulate the engagement and/or progression of apoptotic events. Hsp-mediated inhibition is indicated (T-bars) and Hsp-mediated potentiation of a signaling pathway is depicted as a direct interaction between the Hsp and its target (+).

 


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Fig. 2. Events regulated by Hsps in the death receptor mediated or `extrinsic' pathway to apoptosis. Ligation of cell surface death receptors, e.g. Fas and TNFR1, by the appropriate ligand engages multiple intracellular signals leading to caspase activation and cell death or NF-{kappa}B-mediated survival. Many elements of these pathways are regulated by the activities of Hsps to help maintain cellular survival following death receptor ligation. Hsp-mediated inhibition is indicated (T-bars) and Hsp-mediated potentiation of a signaling pathway is depicted as a direct interaction between the Hsp and its target (+).

 





© The Company of Biologists Ltd 2004