HSP90 as a new therapeutic target for cancer therapy: the story unfolds

Maloney, Alison; Workman, Paul

doi:10.1517/14712598.2.1.3

Cited by 531Heat shock proteins researchUbiquitin and proteasome pathwaysCancer Mechanisms and Therapy

HSP90 as a new therapeutic target for cancer therapy: the story unfolds

Maloney, Alison, Workman, Paul·2002·Expert Opinion on Biological Therapy

DOI 10.1517/14712598.2.1.3

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Abstract

Current anticancer drug development strategies involve identifying novel molecular targets which are crucial for tumourigenesis. The molecular chaperone heat shock protein (HSP) 90 is of interest as an anticancer drug target because of its importance in maintaining the conformation, stability and function of key oncogenic client proteins involved in signal transduction pathways leading to proliferation, cell cycle progression and apoptosis, as well as other features of the malignant phenotype such as invasion, angiogenesis and metastasis. The natural product HSP90 inhibitors geldanamycin and radicicol exert their antitumour effect by inhibiting the intrinsic ATPase activity of HSP90, resulting in degradation of HSP90 client proteins via the ubiquitin proteosome pathway. Anticancer selectivity may derive from the simultaneous combinatorial effects of HSP90 inhibitors on multiple cancer targets and pathways. 17-allylamino, 17-demethoxygeldanamycin (17AAG), a geldanamycin derivative, showed good activity and cancer selectivity in preclinical models and has now progressed to Phase I clinical trial in cancer patients with encouraging initial results. Phase II trials including combination studies with cytotoxic agents are now being planned and these should allow the therapeutic activity of 17AAG to be determined. Second generation HSP90 inhibitors may be designed to overcome some of the drawbacks of 17AAG, including limited oral bioavailability and solubility. They could also be engineered to target specific functions of HSP90, which may not only provide greater molecular selectivity and clinical benefit but may also increase understanding of the complex functions of this molecular chaperone. HSP90 inhibitors provide proof of concept for drugs directed at HSP90 and protein folding and this principle may be applicable to other medical conditions involving protein aggregation and stability.

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HSP90 is involved in the maturation of several oncogenic client proteins, the degradation of which could abrogate cell growth and induce apoptosis.
“HSP90 is involved in the maturation of several oncogenic client proteins, the degradation of which could abrogate cell growth and induce apoptosis (Maloney and Workman, 2002).”
From A novel small molecule hydroxamate preferentially inhibits HDAC6 activity and tumour growth (2013) · cites this paper as Maloney and Workman, 2002

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Authors: Maloney, A., & Workman, P.
Affiliations: Institute of Cancer Research (GB)
ORCID: Maloney, Alison
Workman, Paul
Venue: Expert Opinion on Biological Therapy
Publisher: Informa Healthcare
Published: 2002-01
Volume: 2
Issue: 1
Pages: 3-24
ISSN: 1471-2598 (ISSN-L)
1744-7682
DOI: 10.1517/14712598.2.1.3
OpenAlex: W2111187586
Cited by: 531
References: 134
Citations by year: 2026: 6 · 2025: 8 · 2024: 6 · 2023: 11 · 2022: 9 · 2021: 10 · 2020: 15 · 2019: 15 · 2018: 6 · 2017: 6 · 2016: 11 · 2015: 17 · 2014: 26 · 2013: 26 · 2012: 20
FWCI: 3.16
Type: journal article
Language: en
Open access: closed
Locations: Expert Opinion on Biological Therapy (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
Health Sciences › Medicine › Pathology and Forensic Medicine › Cancer Mechanisms and Therapy
Keywords: HSP90, Hsp90 inhibitors, cancer therapy, molecular chaperones, geldanamycin, radicicol, 17-AAG, Hsp90 client proteins, ubiquitin-proteasome degradation, anticancer drug targets, combination therapy, protein folding, drug selectivity
MeSH terms: Animals, Antineoplastic Agents, Humans, Benzoquinones, Apoptosis, Rifabutin, HSP90 Heat-Shock Proteins, Lactams, Macrocyclic

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