Cited by 314Heat shock proteins researchCell death mechanisms and regulationUbiquitin and proteasome pathways

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Dual Targeting of HSC70 and HSP72 Inhibits HSP90 Function and Induces Tumor-Specific Apoptosis

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Powers, Marissa V., Clarke, Paul A., Workman, Paul·2008·Cancer Cell

DOI 10.1016/j.ccr.2008.08.002

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Abstract

Heat-shock protein 70 (HSP70) isoforms contribute to tumorigenesis through their well-documented antiapoptotic activity and via their role as cochaperones for the HSP90 molecular chaperone. HSP70 expression is induced following treatment with HSP90 inhibitors, which may attenuate the cell death effects of this class of inhibitor. Here we show that silencing either heat-shock cognate 70 (HSC70) or HSP72 expression in human cancer cell lines has no effect on HSP90 activity or cell proliferation. However, simultaneously reducing the expression of both of these isoforms induces proteasome-dependent degradation of HSP90 client proteins, G1 cell-cycle arrest, and extensive tumor-specific apoptosis. Importantly, simultaneous silencing of HSP70 isoforms in nontumorigenic cell lines does not result in comparable growth arrest or induction of apoptosis, indicating a potential therapeutic window.

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Authors: Powers, M. V., Clarke, P. A., & Workman, P.
Affiliations: Institute of Cancer Research (GB)
Corresponding author: Workman, Paul
ORCID: Powers, Marissa V.
Clarke, Paul A.
Workman, Paul
Venue: Cancer Cell
Publisher: Elsevier BV
Published: 2008-09
Volume: 14
Issue: 3
Pages: 250-262
ISSN: 1535-6108 (ISSN-L)
DOI: 10.1016/j.ccr.2008.08.002
OpenAlex: W2170573493
Cited by: 307
References: 36
Citations by year: 2026: 7 · 2025: 4 · 2024: 5 · 2023: 5 · 2022: 9 · 2021: 15 · 2020: 8 · 2019: 17 · 2018: 16 · 2017: 18 · 2016: 24 · 2015: 25 · 2014: 27 · 2013: 29 · 2012: 24
FWCI: 10.38
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 1780 d)
Locations: Cancer Cell (publishedVersion)
PubMed (publishedVersion)
Funders: Cancer Research UK (C309/A8274, C309/A2187)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
Keywords: Hsc70, HSP72, HSP90, Hsp90 inhibitors, proteasomal degradation, Hsp90 client proteins, G1 cell cycle arrest, heat shock proteins, cancer cell lines, therapeutic window, anti-apoptotic effects
MeSH terms: Bortezomib, Boronic Acids, Cell Cycle, Cell Line, Humans, Kinetics, Neoplasms, Poly(ADP-ribose) Polymerases, Protease Inhibitors, Pyrazines, Transfection, Benzoquinones, Apoptosis, HSP70 Heat-Shock Proteins, HSP90 Heat-Shock Proteins, Proto-Oncogene Proteins c-raf, Protein Isoforms, RNA, Small Interfering, HCT116 Cells, Cell Line, Tumor, Proteasome Endopeptidase Complex, Lactams, Macrocyclic, Cell Proliferation, HSC70 Heat-Shock Proteins, HSP72 Heat-Shock Proteins, Cyclin-Dependent Kinase 4, Ubiquitination, Proteasome Inhibitors

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Dual Targeting of HSC70 and HSP72 Inhibits HSP90 Function and Induces Tumor-Specific Apoptosis

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