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Small Stress Proteins as Novel Regulators of Apoptosis
Open accessAbstract
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 alphaB-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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Nagata, S., & Golstein, P. (1995) · Science · doi:10.1126/science.7533326 · Cited by 3,979
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Rajasekaran, N. S., Connell, P., Christians, E. S., Yan, L.-J., Taylor, R. P., Orosz, A., Zhang, X. Q., Stevenson, T. J., Peshock, R. M., Leopold, J. A., et al. (2007) · Cell · doi:10.1016/j.cell.2007.06.044 · Cited by 437
Expression profiles of multiple genes in single neurons of Alzheimer’s disease
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Metadata
- Authors
- Mehlen, P., Schulze-Osthoff, K., & Arrigo, A.-P.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1996-07
- Volume
- 271
- Issue
- 28
- Pages
- 16510-16514
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2008343355
- Cited by
- 607
- References
- 1
- FWCI
- 11.87
- Type
- journal article
- Language
- en
- Open access
- hybrid
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