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Hsp90α and cell death in cancers: a review

Liu, Bin, Qian, Daohai·2024·Discover Oncology
DOI 10.1007/s12672-024-01021-0PMC PMC11087423
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Abstract

Heat shock protein 90α (Hsp90α), an important molecular chaperone, plays a crucial role in regulating the activity of various intracellular signaling pathways and maintaining the stability of various signaling transduction proteins. In cancer, the expression level of Hsp90α is often significantly upregulated and is recognized as one of the key factors in cancer cell survival and proliferation. Cell death can help achieve numerous purposes, such as preventing aging, removing damaged or infected cells, facilitating embryonic development and tissue repair, and modulating immune response. The expression of Hsp90α is closely associated with specific modes of cell death including apoptosis, necrotic apoptosis, and autophagy-dependent cell death, etc. This review discusses the new results on the relationship between expression of Hsp90α and cell death in cancer. Hsp90α is frequently overexpressed in cancer and promotes cancer cell growth, survival, and resistance to treatment by regulating cell death, rendering it a promising target for cancer therapy.

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Fig. 1 The involvement of Hsp90α in cell death pathways
Fig. 1 The involvement of Hsp90α in cell death pathwaysCC BY · PubMed Central
Fig. 2 Increased expression of Hsp90α in various cancers
Fig. 2 Increased expression of Hsp90α in various cancersCC BY · PubMed Central

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Cited by

Metadata

Authors
Liu, B., & Qian, D.
Venue
Discover Oncology
Publisher
Springer Science and Business Media LLC
Published
2024-05-10
Volume
15
Issue
1
ISSN
2730-6011
DOI
10.1007/s12672-024-01021-0
PMC
PMC11087423
Cited by
20
References
3
Language
en
Licence
Funders
  • Anhui Provincial Key Research and Development Plan (202004j07020051)
  • Yijishan Hospital talent and peak project (YR202122, GF2019T03, GF2019G03)

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