Cell Biology and Metabolism
Small Stress Proteins as Novel Regulators of Apoptosis: HEAT SHOCK PROTEIN 27 BLOCKs FAS/APO-1- AND STAUROSPORINE-INDUCED CELL DEATH*

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Small stress protein expression enhances the survival of mammalian cells exposed to numerous injuries that induce necrotic cell death. The cell surface receptor Fas/APO-1 and its ligand have been recently identified as important mediators of apoptosis. Here, we show that constitutive expression of human heat shock protein (hsp)27 in murine L929 cells blocks Fas/APO-1-mediated cell death. Expression of human hsp27 prevented anti-APO-1-induced DNA fragmentation and morphological changes. These results strongly suggest that human hsp27 acts as a cellular inhibitor of Fas/APO-1-induced apoptosis. We also report that the expression of small stress proteins from different species, such as human hsp27, Drosophila Dhsp27, or human αB-crystallin, confers resistance to apoptotic cell death induced by staurosporine, a protein kinase C inhibitor. Hence, small stress proteins are novel regulators that are able to block apoptosis induced by different pathways.

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This work was supported by Grants 6011 from the Association pour la Recherche sur le Cancer, 91.C.388 from the Ministère de la Recherche et de la Technologie, 930.501 from the Institut National pour la Santé et la Recherche Médicale (INSERM), CHRX-CT 93-0260 from the European Economic Community (Human Capital and Mobility), the CNRS, and the Région Rhône-Alpes (to A.-P. A). The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked “advertisement” in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

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Supported by a postdoctoral fellowship from the Ecole Normale Supérieure.