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Heat Shock Protein 72 Modulates Pathways of Stress-induced Apoptosis
Open accessAbstract
The resistance to stress-induced apoptosis conferred by the thermotolerant state or by exogenous expression of HSP72 was measured in mouse embryo fibroblasts. The induction of thermotolerance protects cells from heat, tumor necrosis factor alpha (TNFalpha), and ceramide-induced apoptosis but not from ionizing radiation. Because the development of thermotolerance is associated with increased levels of heat shock proteins, we determined whether constitutive expression of one of the major inducible heat shock proteins, HSP72, could also protect cells from stress-induced apoptosis. Cells expressing constitutive HSP72 were shown to have significantly reduced levels of apoptosis after heat, TNFalpha, and ceramide but not after ionizing radiation. Activation of stress-activated protein kinase/c-Jun N-terminal kinase (SAPK/JNK) was found to be strongly inhibited in thermotolerant cells after heat shock but not after other stresses. Cells that constitutively express HSP72 did not demonstrate decreased SAPK/JNK activation after any of these stresses. Thus, factors other than HSP72 that are induced in the thermotolerant state are able to reduce activation of SAPK/JNK after heat stress. Notably, the level of activation of SAPK/JNK did not correlate with the amount of apoptosis detected after different stresses. Constitutive HSP72 expression inhibited poly(ADP-ribose) polymerase cleavage in cells after heat shock and TNFalpha but not after ceramide or ionizing radiation. The results suggest either that SAPK/JNK activation is not required for apoptosis in mouse embryo fibroblasts or that HSP72 acts downstream of SAPK/JNK. Furthermore, the data support the concept that caspase activity, which can be down-regulated by HSP72, is a crucial step in stress-induced apoptosis. Based on data presented here and elsewhere, we propose that the heat shock protein family can be classified as a class of anti-apoptotic genes, in addition to the Bcl-2 and inhibitor of apoptosis protein families of genes.
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Cited by
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Jolly, C. (2000) · Journal of the National Cancer Institute · doi:10.1093/jnci/92.19.1564 · Cited by 1,048
The Chaperone Function of hsp70 Is Required for Protection against Stress-Induced Apoptosis
Mosser, D. D., Caron, A. W., Bourget, L., Meriin, A. B., Sherman, M. Y., Morimoto, R. I., & Massie, B. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.19.7146-7159.2000 · Cited by 731
Intracellular and extracellular functions of heat shock proteins: repercussions in cancer therapy
Schmitt, E., Gehrmann, M., Brunet, M., Multhoff, G., & Garrido, C. (2007) · Journal of Leukocyte Biology · doi:10.1189/jlb.0306167 · Cited by 573
Molecular chaperones and the stress of oncogenesis
Mosser, D. D., & Morimoto, R. I. (2004) · Oncogene · doi:10.1038/sj.onc.1207529 · Cited by 502
Hsp72 functions as a natural inhibitory protein of c-Jun N-terminal kinase
Park, H.-S. (2001) · The EMBO Journal · doi:10.1093/emboj/20.3.446 · Cited by 317
Metadata
- Authors
- Buzzard, K. A., Giaccia, A. J., Killender, M., & Anderson, R. L.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1998-07
- Volume
- 273
- Issue
- 27
- Pages
- 17147-17153
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2013751209
- Cited by
- 281
- References
- 2
- FWCI
- 8.10
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Buzzard, K. A., Giaccia, A. J., Killender, M., & Anderson, R. L. (1998). Heat Shock Protein 72 Modulates Pathways of Stress-induced Apoptosis. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.273.27.17147
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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