The DOI matches its Crossref record; 10 of the 10 references it cites were found in a registry or an index.
`The stress of dying': the role of heat shock proteins in the regulation of apoptosis
Abstract
Heat shock proteins (Hsps) are a family of highly homologous chaperone proteins that are induced in response to environmental, physical and chemical stresses and that limit the consequences of damage and facilitate cellular recovery. The underlying ability of Hsps to maintain cell survival correlates with an inhibition of caspase activation and apoptosis that can, but does not always, depend upon their chaperoning activities. Several mechanisms proposed to account for these observations impact on both the `intrinsic', mitochondria-dependent and the `extrinsic', death-receptor-mediated pathways to apoptosis. Hsps can inhibit the activity of pro-apoptotic Bcl-2 proteins to prevent permeabilization of the outer mitochondrial membrane and release of apoptogenic factors. The disruption of apoptosome formation represents another mechanism by which Hsps can prevent caspase activation and induction of apoptosis. Several signaling cascades involved in the regulation of key elements within the apoptotic cascade are also subject to modulation by Hsps, including those involving JNK, NF-κB and AKT. The coordinated activities of the Hsps thus modulate multiple events within apoptotic pathways to help sustain cell survival following damaging stimuli.
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Cites
Cellular survival: a play in three Akts
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Molecular characterization of mitochondrial apoptosis-inducing factor
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Direct Activation of Bax by p53 Mediates Mitochondrial Membrane Permeabilization and Apoptosis
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“JNK phosphorylates c-Myc and p53 (Fuchs et al., 1998a; Fuchs et al., 1998b; Noguchi et al., 1999), both of which have been implicated in the release of cytochrome c (Chipuk et al., 2003; Chipuk et al., 2004; Juin et al., 1999; Schuler et al., 2000).”
BackgroundIAP proteins: blocking the road to death's door
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“Regardless of this, JNK activation is potently suppressed by Hsp70 (Gabai et al., 1997; Meriin et al., 1998; Mosser et al., 1997; Mosser et al., 2000; Park et al., 2001).”
Background
Cited by
Finka, A., Cuendet, A. F. H., Maathuis, F. J. M., Saidi, Y., & Goloubinoff, P. (2012) · The Plant Cell · doi:10.1105/tpc.112.095844 · Cited by 367
Apoptosis: mechanisms and relevance in cancer
Vermeulen, K., Van Bockstaele, D. R., & Berneman, Z. N. (2005) · Annals of Hematology · doi:10.1007/s00277-005-1065-x · Cited by 344
Cauwe, B., & Opdenakker, G. (2010) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2010.501783 · Cited by 299
Upadhya, R., Zingg, W., Shetty, S., & Shetty, A. K. (2020) · Journal of Controlled Release · doi:10.1016/j.jconrel.2020.04.017 · Cited by 282
THE PROTEASOME AND PROTEASOME INHIBITORS IN CANCER THERAPY
Voorhees, P. M., & Orlowski, R. Z. (2006) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.46.120604.141300 · Cited by 247
Metadata
- Authors
- Beere, H. M.
- Venue
- Journal of Cell Science
- Publisher
- The Company of Biologists
- Published
- 2004-06-01
- Volume
- 117
- Issue
- 13
- Pages
- 2641-2651
- ISSN
- 0021-9533 (ISSN-L)
- 1477-9137
- OpenAlex
- W2065861852
- Cited by
- 639
- References
- 10
- FWCI
- 12.46
- Type
- journal article
- Language
- en
- Open access
- closed
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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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