The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Members of the heat-shock protein 70 family promote cancer cell growth by distinct mechanisms
Open accessAbstract
Whereas the stress-inducible heat-shock protein 70 (Hsp70) has gained plenty of attention as a putative target for tumor therapy, little is known about the role of other Hsp70 proteins in cancer. Here we present the first thorough analysis of the expression and function of the cytosolic Hsp70 proteins in human cancer cells and identify Hsp70-2, a protein essential for spermatogenesis, as an important regulator of cancer cell growth. Targeted knock-down of the individual family members by RNA interference revealed that both Hsp70 and Hsp70-2 were required for cancer cell growth, whereas the survival of tumorigenic as well as nontumorigenic cells depended on Hsc70. Cancer cells depleted for Hsp70 and Hsp70-2 displayed strikingly different morphologies (detached and round vs. flat senescent-like), cell cycle distributions (G2/M vs. G1 arrest) and gene expression profiles. Only Hsp70-2 depletion induced the expression of macrophage inhibitory cytokine-1 that was identified as a target of P53 tumor-suppressor protein and a mediator of the G1 arrest and the senescent phenotype. Importantly, concomitant depletion of Hsp70 and Hsp70-2 had a synergistic antiproliferative effect on cancer cells. Thus, highly homologous Hsp70 proteins bring about nonoverlapping functions essential for cell growth and survival.
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“The minimal molecular changes required for the infinite growth of human epithelial cells in culture have been identified recently and include the activation of telomerase and the inhibition of the retinoblastoma/p16 pathway (Kiyono et al. 1998).”
BackgroundHeat Shock Protein 70 Promotes Cell Survival by Inhibiting Lysosomal Membrane Permeabilization
Nylandsted, J., Gyrd-Hansen, M., Danielewicz, A., Fehrenbacher, N., Lademann, U., Høyer-Hansen, M., Weber, E., Multhoff, G., Rohde, M., & Jäättelä, M. (2004) · The Journal of Experimental Medicine · doi:10.1084/jem.20040531 · Cited by 545
Self-citationHsiao, E. C., Koniaris, L. G., Zimmers-Koniaris, T., Sebald, S. M., Huynh, T. V., & Lee, S.-J. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.10.3742-3751.2000 · Cited by 302
Li, P.-X., Wong, J., Ayed, A., Ngo, D., Brade, A. M., Arrowsmith, C., Austin, R. C., & Klamut, H. J. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m909580199 · Cited by 254
Cited by
HSP90 and the chaperoning of cancer
Whitesell, L., & Lindquist, S. L. (2005) · Nature Reviews Cancer · doi:10.1038/nrc1716 · Cited by 2,502
Control of Macroautophagy by Calcium, Calmodulin-Dependent Kinase Kinase-β, and Bcl-2
Høyer-Hansen, M., Bastholm, L., Szyniarowski, P., Campanella, M., Szabadkai, G., Farkas, T., Bianchi, K., Fehrenbacher, N., Elling, F., Rizzuto, R., et al. (2007) · Molecular Cell · doi:10.1016/j.molcel.2006.12.009 · Cited by 1,072
Self-citationHsp70 stabilizes lysosomes and reverts Niemann–Pick disease-associated lysosomal pathology
Kirkegaard, T., Roth, A. G., Petersen, N. H. T., Mahalka, A. K., Olsen, O. D., Moilanen, I., Zylicz, A., Knudsen, J., Sandhoff, K., Arenz, C., et al. (2010) · Nature · doi:10.1038/nature08710 · Cited by 519
Self-citationA Small Molecule Inhibitor of Inducible Heat Shock Protein 70
Leu, J. I.-J., Pimkina, J., Frank, A., Murphy, M. E., & George, D. L. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.09.023 · Cited by 441
Massey, A. J., Williamson, D. S., Browne, H., Murray, J. B., Dokurno, P., Shaw, T., Macias, A. T., Daniels, Z., Geoffroy, S., Dopson, M., et al. (2010) · Cancer Chemotherapy and Pharmacology · doi:10.1007/s00280-009-1194-3 · Cited by 313
Metadata
- Authors
- Rohde, M., Daugaard, M., Jensen, M. H., Helin, K., Nylandsted, J., & Jäättelä, M.
- Venue
- Genes & Development
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2005-03-01
- Volume
- 19
- Issue
- 5
- Pages
- 570-582
- ISSN
- 0890-9369 (ISSN-L)
- 1549-5477
- OpenAlex
- W2025743107
- Cited by
- 413
- References
- 4
- Type
- posted content
- Language
- en
- Open access
- diamond
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- Rohde, M., Daugaard, M., Jensen, M. H., Helin, K., Nylandsted, J., & Jäättelä, M. (2005). Members of the heat-shock protein 70 family promote cancer cell growth by distinct mechanisms. Genes & Development. https://doi.org/10.1101/gad.305405
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