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Sci. STKE, 31 July 2001
Vol. 2001, Issue 93, p. re1
[DOI: 10.1126/stke.2001.93.re1]

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Stressed to Death: Regulation of Apoptotic Signaling Pathways by the Heat Shock Proteins

Helen M. Beere

The author is in the La Jolla Institute for Allergy and Immunology, 10355 Science Center Drive, San Diego, CA 92121, USA. E-mail: helenb{at}liai.org

Gloss: All the cells in our body are able to die by a process known as apoptosis. Apoptosis, sometimes called cellular suicide, is characterized by distinct changes in the appearance of the cell, including alterations in the nucleus and changes to the cell membrane. These changes are brought about by a group of proteases, called caspases, which precisely cleave specific proteins in the cell to activate or to inactivate them. This biochemical process can be engaged by a number of different stimuli or "stresses," including DNA damage, cellular starvation, heat, or anticancer agents. The connection between these stresses and the activation of the biochemical machinery to destroy the cell is mediated by signaling proteins. These proteins communicate with one another to form a signaling pathway that brings about changes in the cell--in this case, the activation of the caspase proteases following damage to the cell. Cells can also activate a protective mechanism that allows them to recover from some types of damage. This mechanism of protection is mediated by heat shock proteins (Hsps). These proteins protect cells by inhibiting apoptosis. This review discusses how we think the Hsps maintain the survival of cells by regulating the signaling pathways that lead to the activation of apoptosis.

Citation: H. M. Beere, Stressed to Death: Regulation of Apoptotic Signaling Pathways by the Heat Shock Proteins. Sci. STKE 2001, re1 (2001).


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