The DOI matches its Crossref record; 49 of the 49 references it cites were found in a registry or an index.
Dual Role of Heat Shock Proteins as Regulators of Apoptosis and Innate Immunity
Abstract
Stress or heat shock proteins (HSPs) 70 and 90 are powerful chaperones whose expression is induced in response to a wide variety of physiological and environmental insults. These proteins have different functions depending on their intracellular or extracellular location. Intracellular HSPs have a protective function. They allow the cells to survive potentially lethal conditions. The cytoprotective functions of HSPs can largely be explained by their anti-apoptotic properties. HSP70 and HSP90 can directly interact with different proteins of the tightly regulated programmed cell death machinery and thereby block the apoptotic process at distinct key points. In cancer cells, where the expression of HSP70 and/or HSP90 is frequently abnormally high, they participate in oncogenesis and in resistance to chemotherapy. Therefore, the inhibition of HSPs has become an interesting strategy in cancer therapy. In contrast to intracellular HSPs, extracellularly located or membrane-bound HSPs mediate immunological functions. They can elicit an immune response providing a link between innate and adaptive immune systems. In cancer, most immunotherapeutical approaches based on extracellular HSPs exploit their carrier function for immunogenic peptides. This review will focus on the roles of HSP70 and HSP90 in apoptosis and in innate immunity and how these functions are being exploited in cancer therapy.
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1 retracted
Extracellular Heat Shock Proteins in Cell Signaling and Immunity
CALDERWOOD, S. K., MAMBULA, S. S., & GRAY, P. J. (2007) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1391.019 · Cited by 227
RetractedRegulation of Cell Death Protease Caspase-9 by Phosphorylation
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Novel Signal Transduction Pathway Utilized by Extracellular HSP70
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Self-citationHeat-shock protein 70 antagonizes apoptosis-inducing factor
Ravagnan, L., Gurbuxani, S., Susin, S. A., Maisse, C., Daugas, E., Zamzami, N., Mak, T., Jäättelä, M., Penninger, J. M., Garrido, C., et al. (2001) · Nature Cell Biology · doi:10.1038/ncb0901-839 · Cited by 858
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Heat Shock Protein 70 Promotes Cell Survival by Inhibiting Lysosomal Membrane Permeabilization
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Cited by
The Biology of Aging and Cancer: A Brief Overview of Shared and Divergent Molecular Hallmarks
Aunan, J. R., Cho, W. C., & Søreide, K. (2017) · Aging and disease · doi:10.14336/ad.2017.0103 · Cited by 373
Heat Shock Proteins: Agents of Cancer Development and Therapeutic Targets in Anti-Cancer Therapy
Yun, C. W., Kim, H. J., Lim, J. H., & Lee, S. H. (2019) · Cells · doi:10.3390/cells9010060 · Cited by 284
HSP27, 70 and 90, anti-apoptotic proteins, in clinical cancer therapy
WANG, X., CHEN, M., ZHOU, J., & ZHANG, X. (2014) · International Journal of Oncology · doi:10.3892/ijo.2014.2399 · Cited by 269
Hulina, A., Grdić Rajković, M., Jakšić Despot, D., Jelić, D., Dojder, A., Čepelak, I., & Rumora, L. (2018) · Cell Stress and Chaperones · doi:10.1007/s12192-017-0847-0 · Cited by 92
Jego, G., Lanneau, D., De Thonel, A., Berthenet, K., Hazoumé, A., Droin, N., Hamman, A., Girodon, F., Bellaye, P.-S., Wettstein, G., et al. (2014) · Leukemia · doi:10.1038/leu.2014.63 · Cited by 42
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Metadata
- Authors
- Joly, A.-L., Wettstein, G., Mignot, G., Ghiringhelli, F., & Garrido, C.
- Venue
- Journal of Innate Immunity
- Publisher
- S. Karger AG
- Published
- 2010
- Volume
- 2
- Issue
- 3
- Pages
- 238-247
- ISSN
- 1662-811X (ISSN-L)
- 1662-8128
- OpenAlex
- W2020942835
- Cited by
- 301
- References
- 49
- FWCI
- 8.51
- Type
- journal article
- Language
- en
- Open access
- closed
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