Skip to main content
Top
Published in: Discover Oncology 1/2024

Open Access 01-12-2024 | Shock | Review

Hsp90α and cell death in cancers: a review

Authors: Bin Liu, Daohai Qian

Published in: Discover Oncology | Issue 1/2024

Login to get access

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.
Literature
1.
go back to reference Calderwood SK, Khaleque MA, Sawyer DB, et al. Heat shock proteins in cancer: chaperones of tumorigenesis. Trends Biochem Sci. 2006;31(3):164–72.PubMedCrossRef Calderwood SK, Khaleque MA, Sawyer DB, et al. Heat shock proteins in cancer: chaperones of tumorigenesis. Trends Biochem Sci. 2006;31(3):164–72.PubMedCrossRef
2.
go back to reference Eustace BK, Sakurai T, Stewart JK, et al. Functional proteomic screens reveal an essential extracellular role for hsp90 alpha in cancer cell invasiveness. Nat Cell Biol. 2004;6(6):507–14.PubMedCrossRef Eustace BK, Sakurai T, Stewart JK, et al. Functional proteomic screens reveal an essential extracellular role for hsp90 alpha in cancer cell invasiveness. Nat Cell Biol. 2004;6(6):507–14.PubMedCrossRef
3.
go back to reference Hoter A, El-Sabban ME, Naim HY. The HSP90 family: structure, regulation, function, and implications in health and disease. Int J Mol Sci. 2018;19(9):2560.PubMedPubMedCentralCrossRef Hoter A, El-Sabban ME, Naim HY. The HSP90 family: structure, regulation, function, and implications in health and disease. Int J Mol Sci. 2018;19(9):2560.PubMedPubMedCentralCrossRef
7.
go back to reference Lavery LA, Partridge JR, Ramelot TA, et al. Structural asymmetry in the closed state of mitochondrial Hsp90 (TRAP1) supports a two-step ATP hydrolysis mechanism. Mol Cell. 2014;53(2):330–43.PubMedPubMedCentralCrossRef Lavery LA, Partridge JR, Ramelot TA, et al. Structural asymmetry in the closed state of mitochondrial Hsp90 (TRAP1) supports a two-step ATP hydrolysis mechanism. Mol Cell. 2014;53(2):330–43.PubMedPubMedCentralCrossRef
8.
go back to reference Sreedhar AS, Kalmár E, Csermely P, et al. Hsp90 isoforms: functions, expression and clinical importance. FEBS Lett. 2004;562(1–3):11–5.PubMedCrossRef Sreedhar AS, Kalmár E, Csermely P, et al. Hsp90 isoforms: functions, expression and clinical importance. FEBS Lett. 2004;562(1–3):11–5.PubMedCrossRef
9.
go back to reference Taiyab A, Rao ChM. HSP90 modulates actin dynamics: inhibition of HSP90 leads to decreased cell motility and impairs invasion. Biochim Biophys Acta. 2011;1813(1):213–21.PubMedCrossRef Taiyab A, Rao ChM. HSP90 modulates actin dynamics: inhibition of HSP90 leads to decreased cell motility and impairs invasion. Biochim Biophys Acta. 2011;1813(1):213–21.PubMedCrossRef
10.
go back to reference Walerych D, Kudla G, Gutkowska M, et al. Hsp90 chaperones wild-type p53 tumor suppressor protein. J Biol Chem. 2004;279(47):48836–45.PubMedCrossRef Walerych D, Kudla G, Gutkowska M, et al. Hsp90 chaperones wild-type p53 tumor suppressor protein. J Biol Chem. 2004;279(47):48836–45.PubMedCrossRef
11.
go back to reference Whitesell L, Lindquist SL. HSP90 and the chaperoning of cancer. Nat Rev Cancer. 2005;5(10):761–72.PubMedCrossRef Whitesell L, Lindquist SL. HSP90 and the chaperoning of cancer. Nat Rev Cancer. 2005;5(10):761–72.PubMedCrossRef
12.
go back to reference Suzuki R, Kikuchi S, Harada T, et al. Combination of a selective HSP90α/β inhibitor and a RAS-RAF-MEK-ERK signaling pathway inhibitor triggers synergistic cytotoxicity in multiple myeloma cells. PLoS ONE. 2015;10(12): e0143847.PubMedPubMedCentralCrossRef Suzuki R, Kikuchi S, Harada T, et al. Combination of a selective HSP90α/β inhibitor and a RAS-RAF-MEK-ERK signaling pathway inhibitor triggers synergistic cytotoxicity in multiple myeloma cells. PLoS ONE. 2015;10(12): e0143847.PubMedPubMedCentralCrossRef
13.
go back to reference Zhang J, Zhong W, Liu Y, et al. Extracellular HSP90α interacts with ER stress to promote fibroblasts activation through PI3K/AKT pathway in pulmonary fibrosis. Front Pharmacol. 2021;12: 708462.PubMedPubMedCentralCrossRef Zhang J, Zhong W, Liu Y, et al. Extracellular HSP90α interacts with ER stress to promote fibroblasts activation through PI3K/AKT pathway in pulmonary fibrosis. Front Pharmacol. 2021;12: 708462.PubMedPubMedCentralCrossRef
14.
go back to reference Bohonowych JE, Hance MW, Nolan KD, et al. Extracellular Hsp90 mediates an NF-κB dependent inflammatory stromal program: implications for the prostate tumor microenvironment. Prostate. 2014;74(4):395–407.PubMedCrossRef Bohonowych JE, Hance MW, Nolan KD, et al. Extracellular Hsp90 mediates an NF-κB dependent inflammatory stromal program: implications for the prostate tumor microenvironment. Prostate. 2014;74(4):395–407.PubMedCrossRef
15.
go back to reference Kroemer G, Galluzzi L, Vandenabeele P, et al. Classification of cell death: recommendations of the Nomenclature Committee on Cell Death 2009. Cell Death Differ. 2009;16(1):3–11.PubMedCrossRef Kroemer G, Galluzzi L, Vandenabeele P, et al. Classification of cell death: recommendations of the Nomenclature Committee on Cell Death 2009. Cell Death Differ. 2009;16(1):3–11.PubMedCrossRef
16.
go back to reference Yan J, Wan P, Choksi S, Liu ZG. Necroptosis and tumor progression. Trends Cancer. 2022;8(1):21–7.PubMedCrossRef Yan J, Wan P, Choksi S, Liu ZG. Necroptosis and tumor progression. Trends Cancer. 2022;8(1):21–7.PubMedCrossRef
17.
go back to reference Marunouchi T, Nishiumi C, Iinuma S, et al. Effects of Hsp90 inhibitor on the RIP1-RIP3-MLKL pathway during the development of heart failure in mice. Eur J Pharmacol. 2021;898: 173987.PubMedCrossRef Marunouchi T, Nishiumi C, Iinuma S, et al. Effects of Hsp90 inhibitor on the RIP1-RIP3-MLKL pathway during the development of heart failure in mice. Eur J Pharmacol. 2021;898: 173987.PubMedCrossRef
18.
go back to reference Liu YH, Liu XM, Wang PC, et al. Heat shock protein 90α couples with the MAPK-signaling pathway to determine meiotic maturation of porcine oocytes. J Anim Sci. 2018;96(8):3358–69.PubMedPubMedCentralCrossRef Liu YH, Liu XM, Wang PC, et al. Heat shock protein 90α couples with the MAPK-signaling pathway to determine meiotic maturation of porcine oocytes. J Anim Sci. 2018;96(8):3358–69.PubMedPubMedCentralCrossRef
19.
go back to reference Bruckheimer EM, Cho SH, Sarkiss M, et al. The Bcl-2 gene family and apoptosis. Adv Biochem Eng Biotechnol. 1998;62:75–105.PubMed Bruckheimer EM, Cho SH, Sarkiss M, et al. The Bcl-2 gene family and apoptosis. Adv Biochem Eng Biotechnol. 1998;62:75–105.PubMed
20.
go back to reference Zhou X, Wen Y, Tian Y, et al. Heat shock protein 90α-dependent B-cell-2-associated transcription factor 1 promotes hepatocellular carcinoma proliferation by regulating MYC proto-oncogene c-MYC mRNA stability. Hepatology. 2019;69(4):1564–81.PubMedCrossRef Zhou X, Wen Y, Tian Y, et al. Heat shock protein 90α-dependent B-cell-2-associated transcription factor 1 promotes hepatocellular carcinoma proliferation by regulating MYC proto-oncogene c-MYC mRNA stability. Hepatology. 2019;69(4):1564–81.PubMedCrossRef
21.
go back to reference Islam A, Lv YJ, Abdelnasir A, et al. The role of Hsp90α in heat-induced apoptosis and cell damage in primary myocardial cell cultures of neonatal rats. Genet Mol Res. 2013;12(4):6080–91.PubMedCrossRef Islam A, Lv YJ, Abdelnasir A, et al. The role of Hsp90α in heat-induced apoptosis and cell damage in primary myocardial cell cultures of neonatal rats. Genet Mol Res. 2013;12(4):6080–91.PubMedCrossRef
22.
go back to reference Kliková K, Štefaniková A, Pilchová I, et al. Differential impact of bortezomib on HL-60 and K562 cells. Gen Physiol Biophys. 2015;34(1):33–42.PubMedCrossRef Kliková K, Štefaniková A, Pilchová I, et al. Differential impact of bortezomib on HL-60 and K562 cells. Gen Physiol Biophys. 2015;34(1):33–42.PubMedCrossRef
23.
go back to reference Wang N, Chen S, Zhang B, et al. 8u, a pro-apoptosis/cell cycle arrest compound, suppresses invasion and metastasis through HSP90α downregulating and PI3K/Akt inactivation in hepatocellular carcinoma cells. Sci Rep. 2018;8(1):309.PubMedPubMedCentralCrossRef Wang N, Chen S, Zhang B, et al. 8u, a pro-apoptosis/cell cycle arrest compound, suppresses invasion and metastasis through HSP90α downregulating and PI3K/Akt inactivation in hepatocellular carcinoma cells. Sci Rep. 2018;8(1):309.PubMedPubMedCentralCrossRef
24.
go back to reference Zeng D, Gao M, Zheng R, et al. The HSP90 inhibitor KW-2478 depletes the malignancy of BCR/ABL and overcomes the imatinib-resistance caused by BCR/ABL amplification. Exp Hematol Oncol. 2022;11(1):33.PubMedPubMedCentralCrossRef Zeng D, Gao M, Zheng R, et al. The HSP90 inhibitor KW-2478 depletes the malignancy of BCR/ABL and overcomes the imatinib-resistance caused by BCR/ABL amplification. Exp Hematol Oncol. 2022;11(1):33.PubMedPubMedCentralCrossRef
25.
go back to reference Chatterjee M, Jain S, Stühmer T, et al. STAT3 and MAPK signaling maintain overexpression of heat shock proteins 90alpha and beta in multiple myeloma cells, which critically contribute to tumor-cell survival. Blood. 2007;109(2):720–8.PubMedCrossRef Chatterjee M, Jain S, Stühmer T, et al. STAT3 and MAPK signaling maintain overexpression of heat shock proteins 90alpha and beta in multiple myeloma cells, which critically contribute to tumor-cell survival. Blood. 2007;109(2):720–8.PubMedCrossRef
26.
go back to reference Chua KV, Fan CS, Chen CC, et al. Octyl gallate induces pancreatic ductal adenocarcinoma cell apoptosis and suppresses endothelial-mesenchymal transition-promoted M2-macrophages, HSP90α secretion, and tumor growth. Cells. 2019;9(1):91.PubMedPubMedCentralCrossRef Chua KV, Fan CS, Chen CC, et al. Octyl gallate induces pancreatic ductal adenocarcinoma cell apoptosis and suppresses endothelial-mesenchymal transition-promoted M2-macrophages, HSP90α secretion, and tumor growth. Cells. 2019;9(1):91.PubMedPubMedCentralCrossRef
27.
go back to reference Chen JJ, Yan QL, Bai M, et al. Deoxyelephantopin, a germacrane-type sesquiterpene lactone from Elephantopus scaber, induces mitochondrial apoptosis of hepatocarcinoma cells by targeting Hsp90α in vitro and in vivo. Phytother Res. 2023;37(2):702–16.PubMedCrossRef Chen JJ, Yan QL, Bai M, et al. Deoxyelephantopin, a germacrane-type sesquiterpene lactone from Elephantopus scaber, induces mitochondrial apoptosis of hepatocarcinoma cells by targeting Hsp90α in vitro and in vivo. Phytother Res. 2023;37(2):702–16.PubMedCrossRef
28.
go back to reference Tao W, Cheng X, Sun D, et al. Synthesis of multi-branched Au nanocomposites with distinct plasmon resonance in NIR-II window and controlled CRISPR-Cas9 delivery for synergistic gene-photothermal therapy. Biomaterials. 2022;287: 121621.PubMedCrossRef Tao W, Cheng X, Sun D, et al. Synthesis of multi-branched Au nanocomposites with distinct plasmon resonance in NIR-II window and controlled CRISPR-Cas9 delivery for synergistic gene-photothermal therapy. Biomaterials. 2022;287: 121621.PubMedCrossRef
29.
go back to reference Fan R, Chen C, Hu J, et al. Multifunctional gold nanorods in low-temperature photothermal interactions for combined tumor starvation and RNA interference therapy. Acta Biomater. 2023;159:324–37.PubMedCrossRef Fan R, Chen C, Hu J, et al. Multifunctional gold nanorods in low-temperature photothermal interactions for combined tumor starvation and RNA interference therapy. Acta Biomater. 2023;159:324–37.PubMedCrossRef
31.
go back to reference Vanden Berghe T, Kalai M, van Loo G, Declercq W, Vandenabeele P. Disruption of HSP90 function reverts tumor necrosis factor-induced necrosis to apoptosis. J Biol Chem. 2003;278(8):5622–9.PubMedCrossRef Vanden Berghe T, Kalai M, van Loo G, Declercq W, Vandenabeele P. Disruption of HSP90 function reverts tumor necrosis factor-induced necrosis to apoptosis. J Biol Chem. 2003;278(8):5622–9.PubMedCrossRef
32.
go back to reference Chen T, Tao YN, Wu Y, et al. HSP70 attenuates neuronal necroptosis through the HSP90α-RIPK3 pathway following neuronal trauma. Mol Biol Rep. 2023;50(9):7237–44.PubMedCrossRef Chen T, Tao YN, Wu Y, et al. HSP70 attenuates neuronal necroptosis through the HSP90α-RIPK3 pathway following neuronal trauma. Mol Biol Rep. 2023;50(9):7237–44.PubMedCrossRef
33.
go back to reference Ocaña GJ, Pérez L, Guindon L, et al. Inflammatory stress of pancreatic beta cells drives release of extracellular heat-shock protein 90α. Immunology. 2017;151(2):198–210.PubMedPubMedCentralCrossRef Ocaña GJ, Pérez L, Guindon L, et al. Inflammatory stress of pancreatic beta cells drives release of extracellular heat-shock protein 90α. Immunology. 2017;151(2):198–210.PubMedPubMedCentralCrossRef
34.
go back to reference Liao Y, Yang Y, Pan D, et al. HSP90α mediates sorafenib resistance in human hepatocellular carcinoma by necroptosis inhibition under hypoxia. Cancers. 2021;13(2):243.PubMedPubMedCentralCrossRef Liao Y, Yang Y, Pan D, et al. HSP90α mediates sorafenib resistance in human hepatocellular carcinoma by necroptosis inhibition under hypoxia. Cancers. 2021;13(2):243.PubMedPubMedCentralCrossRef
35.
go back to reference Wang Z, Guo LM, Wang Y, et al. Inhibition of HSP90α protects cultured neurons from oxygen-glucose deprivation induced necroptosis by decreasing RIP3 expression. J Cell Physiol. 2018;233(6):4864–84.PubMedCrossRef Wang Z, Guo LM, Wang Y, et al. Inhibition of HSP90α protects cultured neurons from oxygen-glucose deprivation induced necroptosis by decreasing RIP3 expression. J Cell Physiol. 2018;233(6):4864–84.PubMedCrossRef
36.
go back to reference Sato A, Hiramoto A, Uchikubo Y, et al. Gene expression profiles of necrosis and apoptosis induced by 5-fluoro-2′-deoxyuridine. Genomics. 2008;92(1):9–17.PubMedCrossRef Sato A, Hiramoto A, Uchikubo Y, et al. Gene expression profiles of necrosis and apoptosis induced by 5-fluoro-2′-deoxyuridine. Genomics. 2008;92(1):9–17.PubMedCrossRef
37.
go back to reference Fan CS, Chen CC, Chen LL, et al. Extracellular HSP90α induces MyD88-IRAK complex-associated IKKα/β-NF-κB/IRF3 and JAK2/TYK2-STAT-3 signaling in macrophages for tumor-promoting M2-polarization. Cells. 2022;11(2):229.PubMedPubMedCentralCrossRef Fan CS, Chen CC, Chen LL, et al. Extracellular HSP90α induces MyD88-IRAK complex-associated IKKα/β-NF-κB/IRF3 and JAK2/TYK2-STAT-3 signaling in macrophages for tumor-promoting M2-polarization. Cells. 2022;11(2):229.PubMedPubMedCentralCrossRef
39.
go back to reference Wang B, Chen Z, Yu F, et al. Hsp90 regulates autophagy and plays a role in cancertherapy. Tumour Biol. 2016;37(1):1–6.PubMedCrossRef Wang B, Chen Z, Yu F, et al. Hsp90 regulates autophagy and plays a role in cancertherapy. Tumour Biol. 2016;37(1):1–6.PubMedCrossRef
41.
go back to reference Xu Z, Han X, Ou D, et al. Targeting PI3K/AKT/mTOR-mediated autophagy for tumortherapy. Appl Microbiol Biotechnol. 2020;104(2):1–13.CrossRef Xu Z, Han X, Ou D, et al. Targeting PI3K/AKT/mTOR-mediated autophagy for tumortherapy. Appl Microbiol Biotechnol. 2020;104(2):1–13.CrossRef
42.
go back to reference Chen F, Bao H, Xie H, et al. Heat shock protein expression and autophagy after incomplete thermal ablation and their correlation. Int J Hyperth. 2019;36(1):95–103.CrossRef Chen F, Bao H, Xie H, et al. Heat shock protein expression and autophagy after incomplete thermal ablation and their correlation. Int J Hyperth. 2019;36(1):95–103.CrossRef
43.
go back to reference Cruickshanks N, Shervington L, Patel R, et al. Can hsp90alpha-targeted siRNA combined with TMZ be a future therapy for glioma? Cancer Invest. 2010;28(6):608–14.PubMedCrossRef Cruickshanks N, Shervington L, Patel R, et al. Can hsp90alpha-targeted siRNA combined with TMZ be a future therapy for glioma? Cancer Invest. 2010;28(6):608–14.PubMedCrossRef
44.
go back to reference Sun Y, Chen P, Zhai B, et al. The emerging role of ferroptosis in inflammation. Biomed Pharmacother. 2020;127: 110108.PubMedCrossRef Sun Y, Chen P, Zhai B, et al. The emerging role of ferroptosis in inflammation. Biomed Pharmacother. 2020;127: 110108.PubMedCrossRef
45.
go back to reference Lewerenz J, Ates G, Methner A, et al. Oxytosis/ferroptosis-(Re-) emerging roles for oxidative stress-dependent non-apoptotic cell death in diseases of the central nervous system. Front Neurosci. 2018;12:214.PubMedPubMedCentralCrossRef Lewerenz J, Ates G, Methner A, et al. Oxytosis/ferroptosis-(Re-) emerging roles for oxidative stress-dependent non-apoptotic cell death in diseases of the central nervous system. Front Neurosci. 2018;12:214.PubMedPubMedCentralCrossRef
47.
go back to reference Chen X, Kang R, Kroemer G, et al. Broadening horizons: the role of ferroptosis in cancer. Nat Rev Clin Oncol. 2021;18(5):280–96.PubMedCrossRef Chen X, Kang R, Kroemer G, et al. Broadening horizons: the role of ferroptosis in cancer. Nat Rev Clin Oncol. 2021;18(5):280–96.PubMedCrossRef
48.
go back to reference Dixon SJ, Patel DN, Welsch M, et al. Pharmacological inhibition of cystine-glutamate exchange induces endoplasmic reticulum stress and ferroptosis. Elife. 2014;3: e02523.PubMedPubMedCentralCrossRef Dixon SJ, Patel DN, Welsch M, et al. Pharmacological inhibition of cystine-glutamate exchange induces endoplasmic reticulum stress and ferroptosis. Elife. 2014;3: e02523.PubMedPubMedCentralCrossRef
49.
50.
go back to reference Zhou C, Yu T, Zhu R, et al. Timosaponin AIII promotes non-small-cell lung cancer ferroptosis through targeting and facilitating HSP90 mediated GPX4 ubiquitination and degradation. Int J Biol Sci. 2023;19(5):1471–89.PubMedPubMedCentralCrossRef Zhou C, Yu T, Zhu R, et al. Timosaponin AIII promotes non-small-cell lung cancer ferroptosis through targeting and facilitating HSP90 mediated GPX4 ubiquitination and degradation. Int J Biol Sci. 2023;19(5):1471–89.PubMedPubMedCentralCrossRef
51.
go back to reference Chen C, Wang D, Yu Y, et al. Legumain promotes tubular ferroptosis by facilitating chaperone-mediated autophagy of GPX4 in AKI. Cell Death Dis. 2021;12(1):65.PubMedPubMedCentralCrossRef Chen C, Wang D, Yu Y, et al. Legumain promotes tubular ferroptosis by facilitating chaperone-mediated autophagy of GPX4 in AKI. Cell Death Dis. 2021;12(1):65.PubMedPubMedCentralCrossRef
53.
54.
go back to reference Suk FM, Lin SY, Lin RJ, et al. Bortezomib inhibits Burkitt’s lymphoma cell proliferation by downregulating sumoylated hnRNP K and c-Myc expression. Oncotarget. 2015;6(28):25988–6001.PubMedPubMedCentralCrossRef Suk FM, Lin SY, Lin RJ, et al. Bortezomib inhibits Burkitt’s lymphoma cell proliferation by downregulating sumoylated hnRNP K and c-Myc expression. Oncotarget. 2015;6(28):25988–6001.PubMedPubMedCentralCrossRef
56.
go back to reference Song X, Wang X, Zhuo W, et al. The regulatory mechanism of extracellular Hsp90{alpha} on matrix metalloproteinase-2 processing and tumor angiogenesis. J Biol Chem. 2010;285(51):40039–49.PubMedPubMedCentralCrossRef Song X, Wang X, Zhuo W, et al. The regulatory mechanism of extracellular Hsp90{alpha} on matrix metalloproteinase-2 processing and tumor angiogenesis. J Biol Chem. 2010;285(51):40039–49.PubMedPubMedCentralCrossRef
57.
go back to reference Barginear MF, Van Poznak C, Rosen N, et al. The heat shock protein 90 chaperone complex: an evolving therapeutic target. Curr Cancer Drug Targets. 2008;8(6):522–32.PubMedCrossRef Barginear MF, Van Poznak C, Rosen N, et al. The heat shock protein 90 chaperone complex: an evolving therapeutic target. Curr Cancer Drug Targets. 2008;8(6):522–32.PubMedCrossRef
58.
go back to reference Lee SJ, Lee I, Lee J, et al. Statins, 3-hydroxy-3-methylglutaryl coenzyme A reductase inhibitors, potentiate the anti-angiogenic effects of bevacizumab by suppressing angiopoietin2, BiP, and Hsp90α in human colorectal cancer. Br J Cancer. 2014;111(3):497–505.PubMedPubMedCentralCrossRef Lee SJ, Lee I, Lee J, et al. Statins, 3-hydroxy-3-methylglutaryl coenzyme A reductase inhibitors, potentiate the anti-angiogenic effects of bevacizumab by suppressing angiopoietin2, BiP, and Hsp90α in human colorectal cancer. Br J Cancer. 2014;111(3):497–505.PubMedPubMedCentralCrossRef
60.
go back to reference Dernovšek J, Tomašič T. Following the design path of isoform-selective Hsp90 inhibitors: small differences, great opportunities. Pharmacol Ther. 2023;245: 108396.PubMedCrossRef Dernovšek J, Tomašič T. Following the design path of isoform-selective Hsp90 inhibitors: small differences, great opportunities. Pharmacol Ther. 2023;245: 108396.PubMedCrossRef
61.
go back to reference Zhang Y, Ware MB, Zaidi MY, et al. Heat shock protein-90 inhibition alters activation of pancreatic stellate cells and enhances the efficacy of PD-1 blockade in pancreatic cancer. Mol Cancer Ther. 2021;20(1):150–60.PubMedCrossRef Zhang Y, Ware MB, Zaidi MY, et al. Heat shock protein-90 inhibition alters activation of pancreatic stellate cells and enhances the efficacy of PD-1 blockade in pancreatic cancer. Mol Cancer Ther. 2021;20(1):150–60.PubMedCrossRef
62.
go back to reference Liu L, Deng Y, Zheng Z, et al. Hsp90 inhibitor STA9090 sensitizes hepatocellular carcinoma to hyperthermia-induced DNA damage by suppressing DNA-PKcs protein stability and mRNA transcription. Mol Cancer Ther. 2021;20(10):1880–92.PubMedPubMedCentralCrossRef Liu L, Deng Y, Zheng Z, et al. Hsp90 inhibitor STA9090 sensitizes hepatocellular carcinoma to hyperthermia-induced DNA damage by suppressing DNA-PKcs protein stability and mRNA transcription. Mol Cancer Ther. 2021;20(10):1880–92.PubMedPubMedCentralCrossRef
63.
go back to reference Liu W, Li J, Zhang P, et al. A novel pan-cancer biomarker plasma heat shock protein 90alpha and its diagnosis determinants in clinic. Cancer Sci. 2019;110(9):2941–59.PubMedPubMedCentralCrossRef Liu W, Li J, Zhang P, et al. A novel pan-cancer biomarker plasma heat shock protein 90alpha and its diagnosis determinants in clinic. Cancer Sci. 2019;110(9):2941–59.PubMedPubMedCentralCrossRef
64.
go back to reference Zuo DS, Dai J, Bo AH, et al. Significance of expression of heat shock protein90alpha in human gastric cancer. World J Gastroenterol. 2003;9(11):2616–8.PubMedPubMedCentralCrossRef Zuo DS, Dai J, Bo AH, et al. Significance of expression of heat shock protein90alpha in human gastric cancer. World J Gastroenterol. 2003;9(11):2616–8.PubMedPubMedCentralCrossRef
65.
go back to reference Lee HW, Kim KM. Clinical significance of heat shock protein 90α expression as a biomarker of prognosis in patients with gastric cancer. Niger J Clin Pract. 2019;22(12):1698–705.PubMedCrossRef Lee HW, Kim KM. Clinical significance of heat shock protein 90α expression as a biomarker of prognosis in patients with gastric cancer. Niger J Clin Pract. 2019;22(12):1698–705.PubMedCrossRef
66.
go back to reference Liang XQ, Li KZ, Li Z, et al. Diagnostic and prognostic value of plasma heat shock protein 90alpha in gastric cancer. Int Immunopharmacol. 2021;90: 107145.PubMedCrossRef Liang XQ, Li KZ, Li Z, et al. Diagnostic and prognostic value of plasma heat shock protein 90alpha in gastric cancer. Int Immunopharmacol. 2021;90: 107145.PubMedCrossRef
67.
go back to reference Pan T, Yu Z, Jin Z, et al. Tumor suppressor lnc-CTSLP4 inhibits EMT and metastasis of gastric cancer by attenuating HNRNPAB-dependent Snail transcription. Mol Ther Nucleic Acids. 2021;23:1288–303.PubMedPubMedCentralCrossRef Pan T, Yu Z, Jin Z, et al. Tumor suppressor lnc-CTSLP4 inhibits EMT and metastasis of gastric cancer by attenuating HNRNPAB-dependent Snail transcription. Mol Ther Nucleic Acids. 2021;23:1288–303.PubMedPubMedCentralCrossRef
68.
go back to reference Ni TW, Duan XC, Wang M, et al. Alkaloid derivative ION-31a inhibits breast cancer metastasis and angiogenesis by targeting HSP90α. Bioorg Chem. 2021;115: 105201.PubMedCrossRef Ni TW, Duan XC, Wang M, et al. Alkaloid derivative ION-31a inhibits breast cancer metastasis and angiogenesis by targeting HSP90α. Bioorg Chem. 2021;115: 105201.PubMedCrossRef
69.
go back to reference Liu XY, Wang YM, Zhang XY, et al. Alkaloid derivative (Z)-3β-ethylamino-Pregn-17(20)-en inhibits triple-negative breast cancer metastasis and angiogenesis by targeting HSP90α. Molecules. 2022;27(20):7132.PubMedPubMedCentralCrossRef Liu XY, Wang YM, Zhang XY, et al. Alkaloid derivative (Z)-3β-ethylamino-Pregn-17(20)-en inhibits triple-negative breast cancer metastasis and angiogenesis by targeting HSP90α. Molecules. 2022;27(20):7132.PubMedPubMedCentralCrossRef
70.
go back to reference Hou Q, Chen S, An Q, et al. Extracellular Hsp90α promotes tumor lymphangiogenesis and lymph node metastasis in breast cancer. Int J Mol Sci. 2021;22(14):7747.PubMedPubMedCentralCrossRef Hou Q, Chen S, An Q, et al. Extracellular Hsp90α promotes tumor lymphangiogenesis and lymph node metastasis in breast cancer. Int J Mol Sci. 2021;22(14):7747.PubMedPubMedCentralCrossRef
71.
go back to reference Tian Y, Wang C, Chen S, et al. Extracellular Hsp90α and clusterin synergistically promote breast cancer epithelial-to-mesenchymal transition and metastasis via LRP1. J Cell Sci. 2019;132(15): jcs228213.PubMedCrossRef Tian Y, Wang C, Chen S, et al. Extracellular Hsp90α and clusterin synergistically promote breast cancer epithelial-to-mesenchymal transition and metastasis via LRP1. J Cell Sci. 2019;132(15): jcs228213.PubMedCrossRef
72.
go back to reference Tibatan MA, Önay UE. Long non-coding RNA NKILA regulates expression of HSP90α, NF-κB and β-catenin proteins in the MCF-7 breast cancer cell line. Mol Biol Rep. 2021;48(5):4563–71.PubMedCrossRef Tibatan MA, Önay UE. Long non-coding RNA NKILA regulates expression of HSP90α, NF-κB and β-catenin proteins in the MCF-7 breast cancer cell line. Mol Biol Rep. 2021;48(5):4563–71.PubMedCrossRef
73.
go back to reference Chang C, Tang X, Mosallaei D, et al. LRP-1 receptor combines EGFR signalling and eHsp90α autocrine to support constitutive breast cancer cell motility in absence of blood supply. Sci Rep. 2022;12(1):12006.PubMedPubMedCentralCrossRef Chang C, Tang X, Mosallaei D, et al. LRP-1 receptor combines EGFR signalling and eHsp90α autocrine to support constitutive breast cancer cell motility in absence of blood supply. Sci Rep. 2022;12(1):12006.PubMedPubMedCentralCrossRef
75.
go back to reference Alsaeed SA, Toss M, Alsaleem M, et al. Prognostic significance of heat shock protein 90AA1 (HSP90α) in invasive breast cancer. J Clin Pathol. 2022;75(4):263–9.PubMedCrossRef Alsaeed SA, Toss M, Alsaleem M, et al. Prognostic significance of heat shock protein 90AA1 (HSP90α) in invasive breast cancer. J Clin Pathol. 2022;75(4):263–9.PubMedCrossRef
76.
go back to reference Xue N, Du T, Lai F, et al. Secreted HSP90α-LRP1 signaling promotes tumor metastasis and chemoresistance in pancreatic cancer. Int J Mol Sci. 2022;23(10):5532.PubMedPubMedCentralCrossRef Xue N, Du T, Lai F, et al. Secreted HSP90α-LRP1 signaling promotes tumor metastasis and chemoresistance in pancreatic cancer. Int J Mol Sci. 2022;23(10):5532.PubMedPubMedCentralCrossRef
77.
go back to reference Chen CC, Chen LL, Li CP, et al. Myeloid-derived macrophages and secreted HSP90α induce pancreatic ductal adenocarcinoma development. Oncoimmunology. 2018;7(5): e1424612.PubMedPubMedCentralCrossRef Chen CC, Chen LL, Li CP, et al. Myeloid-derived macrophages and secreted HSP90α induce pancreatic ductal adenocarcinoma development. Oncoimmunology. 2018;7(5): e1424612.PubMedPubMedCentralCrossRef
78.
go back to reference Mayer P, Harjung A, Breinig M, et al. Expression and therapeutic relevance of heat-shock protein 90 in pancreatic endocrine tumors. Endocr Relat Cancer. 2012;19(3):217–32.PubMedCrossRef Mayer P, Harjung A, Breinig M, et al. Expression and therapeutic relevance of heat-shock protein 90 in pancreatic endocrine tumors. Endocr Relat Cancer. 2012;19(3):217–32.PubMedCrossRef
79.
go back to reference Xue N, Lai F, Du T, et al. Chaperone-mediated autophagy degradation of IGF-1Rβ induced by NVP-AUY922 in pancreatic cancer. Cell Mol Life Sci. 2019;76(17):3433–47.PubMedCrossRef Xue N, Lai F, Du T, et al. Chaperone-mediated autophagy degradation of IGF-1Rβ induced by NVP-AUY922 in pancreatic cancer. Cell Mol Life Sci. 2019;76(17):3433–47.PubMedCrossRef
80.
go back to reference Wang Y, Zhang T, Zhang H, et al. Bovine hemoglobin derived peptide Asn-Phe-Gly-Lys inhibits pancreatic cancer cells metastasis by targeting secreted Hsp90α. J Food Sci. 2017;82(12):3005–12.PubMedCrossRef Wang Y, Zhang T, Zhang H, et al. Bovine hemoglobin derived peptide Asn-Phe-Gly-Lys inhibits pancreatic cancer cells metastasis by targeting secreted Hsp90α. J Food Sci. 2017;82(12):3005–12.PubMedCrossRef
81.
go back to reference Jiang H, Duan B, He C, et al. Cytoplasmic HSP90α expression is associated with perineural invasion in pancreatic cancer. Int J Clin Exp Pathol. 2014;7(6):3305–11.PubMedPubMedCentral Jiang H, Duan B, He C, et al. Cytoplasmic HSP90α expression is associated with perineural invasion in pancreatic cancer. Int J Clin Exp Pathol. 2014;7(6):3305–11.PubMedPubMedCentral
82.
go back to reference Mao M, Wang X, Sheng H, et al. Heat shock protein 90α provides an effective and novel diagnosis strategy for nasopharyngeal carcinoma. Adv Ther. 2021;38(1):413–22.PubMedCrossRef Mao M, Wang X, Sheng H, et al. Heat shock protein 90α provides an effective and novel diagnosis strategy for nasopharyngeal carcinoma. Adv Ther. 2021;38(1):413–22.PubMedCrossRef
83.
go back to reference Ye Q, Guo J, Chen Y, et al. Performance of plasma HSP90α, serum EBV VCA IgA antibody and plasma EBV DNA for the diagnosis and prognosis prediction of nasopharyngeal carcinoma. Cancer Manag Res. 2021;13:5793–802.PubMedPubMedCentralCrossRef Ye Q, Guo J, Chen Y, et al. Performance of plasma HSP90α, serum EBV VCA IgA antibody and plasma EBV DNA for the diagnosis and prognosis prediction of nasopharyngeal carcinoma. Cancer Manag Res. 2021;13:5793–802.PubMedPubMedCentralCrossRef
84.
go back to reference Han S, Cheng Z, Zhao X, et al. Diagnostic value of heat shock protein 90α and squamous cell carcinoma antigen in detection of cervical cancer. J Int Med Res. 2019;47(11):5518–25.PubMedPubMedCentralCrossRef Han S, Cheng Z, Zhao X, et al. Diagnostic value of heat shock protein 90α and squamous cell carcinoma antigen in detection of cervical cancer. J Int Med Res. 2019;47(11):5518–25.PubMedPubMedCentralCrossRef
85.
go back to reference Thanner J, Bekos C, Veraar C, et al. Heat shock protein 90α in thymic epithelial tumors and non-thymomatous myasthenia gravis. Oncoimmunology. 2020;9(1):1756130.PubMedPubMedCentralCrossRef Thanner J, Bekos C, Veraar C, et al. Heat shock protein 90α in thymic epithelial tumors and non-thymomatous myasthenia gravis. Oncoimmunology. 2020;9(1):1756130.PubMedPubMedCentralCrossRef
86.
go back to reference Huang B, Pan J, Liu H, et al. High expression of plasma extracellular HSP90α is associated with the poor efficacy of chemotherapy and prognosis in small cell lung cancer. Front Mol Biosci. 2022;9: 913043.PubMedPubMedCentralCrossRef Huang B, Pan J, Liu H, et al. High expression of plasma extracellular HSP90α is associated with the poor efficacy of chemotherapy and prognosis in small cell lung cancer. Front Mol Biosci. 2022;9: 913043.PubMedPubMedCentralCrossRef
87.
go back to reference Liu K, Xu SH, Chen Z, et al. TRPM7 overexpression enhances the cancer stem cell-like and metastatic phenotypes of lung cancer through modulation of the Hsp90α/uPA/MMP2 signaling pathway. BMC Cancer. 2018;18(1):1167.PubMedPubMedCentralCrossRef Liu K, Xu SH, Chen Z, et al. TRPM7 overexpression enhances the cancer stem cell-like and metastatic phenotypes of lung cancer through modulation of the Hsp90α/uPA/MMP2 signaling pathway. BMC Cancer. 2018;18(1):1167.PubMedPubMedCentralCrossRef
88.
go back to reference Li X, Tong X, Liu B, et al. Potential predictive value of plasma heat shock protein 90α in lung cancer. J Int Med Res. 2021;49(12):3000605211064393.PubMedCrossRef Li X, Tong X, Liu B, et al. Potential predictive value of plasma heat shock protein 90α in lung cancer. J Int Med Res. 2021;49(12):3000605211064393.PubMedCrossRef
89.
go back to reference Chen S, Yu Q, Zhou S. Plasmatic levels of HSP90α at diagnosis: a novel prognostic indicator of clinical outcome in advanced lung cancer patients treated with PD-1/PD-L1 inhibitors plus chemotherapy. Front Oncol. 2021;11: 765115.PubMedPubMedCentralCrossRef Chen S, Yu Q, Zhou S. Plasmatic levels of HSP90α at diagnosis: a novel prognostic indicator of clinical outcome in advanced lung cancer patients treated with PD-1/PD-L1 inhibitors plus chemotherapy. Front Oncol. 2021;11: 765115.PubMedPubMedCentralCrossRef
90.
go back to reference Arkhypov I, Özbay Kurt FG, Bitsch R, et al. HSP90α induces immunosuppressive myeloid cells in melanoma via TLR4 signaling. J Immunother Cancer. 2022;10(9): e005551.PubMedPubMedCentralCrossRef Arkhypov I, Özbay Kurt FG, Bitsch R, et al. HSP90α induces immunosuppressive myeloid cells in melanoma via TLR4 signaling. J Immunother Cancer. 2022;10(9): e005551.PubMedPubMedCentralCrossRef
91.
go back to reference Zhang T, Li Q, Zhang Y, et al. Diagnostic and prognostic value of heat shock protein 90α in malignant melanoma. Melanoma Res. 2021;31(2):152–61.PubMedCrossRef Zhang T, Li Q, Zhang Y, et al. Diagnostic and prognostic value of heat shock protein 90α in malignant melanoma. Melanoma Res. 2021;31(2):152–61.PubMedCrossRef
92.
go back to reference Chen WS, Lee CC, Hsu YM, et al. Identification of heat shock protein 90α as an IMH-2 epitope-associated protein and correlation of its mRNA overexpression with colorectal cancer metastasis and poor prognosis. Int J Colorectal Dis. 2011;26(8):1009–17.PubMedCrossRef Chen WS, Lee CC, Hsu YM, et al. Identification of heat shock protein 90α as an IMH-2 epitope-associated protein and correlation of its mRNA overexpression with colorectal cancer metastasis and poor prognosis. Int J Colorectal Dis. 2011;26(8):1009–17.PubMedCrossRef
93.
go back to reference Nam HY, Lee HW. Relationship between 18F-FDG uptake and heat shock protein 90α expression in colorectal cancer. Hell J Nucl Med. 2021;24(1):10–7.PubMed Nam HY, Lee HW. Relationship between 18F-FDG uptake and heat shock protein 90α expression in colorectal cancer. Hell J Nucl Med. 2021;24(1):10–7.PubMed
94.
go back to reference Chen WS, Chen CC, Chen LL, et al. Secreted heat shock protein 90α (HSP90α) induces nuclear factor-κB-mediated TCF12 protein expression to down-regulate E-cadherin and to enhance colorectal cancer cell migration and invasion. J Biol Chem. 2013;288(13):9001–10.PubMedPubMedCentralCrossRef Chen WS, Chen CC, Chen LL, et al. Secreted heat shock protein 90α (HSP90α) induces nuclear factor-κB-mediated TCF12 protein expression to down-regulate E-cadherin and to enhance colorectal cancer cell migration and invasion. J Biol Chem. 2013;288(13):9001–10.PubMedPubMedCentralCrossRef
95.
go back to reference Chen JS, Hsu YM, Chen CC, et al. Secreted heat shock protein 90alpha induces colorectal cancer cell invasion through CD91/LRP-1 and NF-kappaB-mediated integrin alphaV expression. J Biol Chem. 2010;285(33):25458–66.PubMedPubMedCentralCrossRef Chen JS, Hsu YM, Chen CC, et al. Secreted heat shock protein 90alpha induces colorectal cancer cell invasion through CD91/LRP-1 and NF-kappaB-mediated integrin alphaV expression. J Biol Chem. 2010;285(33):25458–66.PubMedPubMedCentralCrossRef
96.
go back to reference Elzakra N, Cui L, Liu T, et al. Mass spectrometric analysis of SOX11-binding proteins in head and neck cancer cells demonstrates the interaction of SOX11 and HSP90α. J Proteome Res. 2017;16(11):3961–8.PubMedCrossRef Elzakra N, Cui L, Liu T, et al. Mass spectrometric analysis of SOX11-binding proteins in head and neck cancer cells demonstrates the interaction of SOX11 and HSP90α. J Proteome Res. 2017;16(11):3961–8.PubMedCrossRef
97.
go back to reference Ono K, Sogawa C, Kawai H, et al. Triple knockdown of CDC37, HSP90-alpha and HSP90-beta diminishes extracellular vesicles-driven malignancy events and macrophage M2 polarization in oral cancer. J Extracell Vesicles. 2020;9(1):1769373.PubMedPubMedCentralCrossRef Ono K, Sogawa C, Kawai H, et al. Triple knockdown of CDC37, HSP90-alpha and HSP90-beta diminishes extracellular vesicles-driven malignancy events and macrophage M2 polarization in oral cancer. J Extracell Vesicles. 2020;9(1):1769373.PubMedPubMedCentralCrossRef
98.
go back to reference Usman M, Ilyas A, Syed B, Hashim Z, et al. Serum HSP90-alpha and oral squamous cell carcinoma: a prospective biomarker. Protein Pept Lett. 2021;28(10):1157–63.PubMedCrossRef Usman M, Ilyas A, Syed B, Hashim Z, et al. Serum HSP90-alpha and oral squamous cell carcinoma: a prospective biomarker. Protein Pept Lett. 2021;28(10):1157–63.PubMedCrossRef
Metadata
Title
Hsp90α and cell death in cancers: a review
Authors
Bin Liu
Daohai Qian
Publication date
01-12-2024
Publisher
Springer US
Keywords
Shock
Shock
Published in
Discover Oncology / Issue 1/2024
Print ISSN: 1868-8497
Electronic ISSN: 2730-6011
DOI
https://doi.org/10.1007/s12672-024-01021-0

Other articles of this Issue 1/2024

Discover Oncology 1/2024 Go to the issue
Live Webinar | 27-06-2024 | 18:00 (CEST)

Keynote webinar | Spotlight on medication adherence

Live: Thursday 27th June 2024, 18:00-19:30 (CEST)

WHO estimates that half of all patients worldwide are non-adherent to their prescribed medication. The consequences of poor adherence can be catastrophic, on both the individual and population level.

Join our expert panel to discover why you need to understand the drivers of non-adherence in your patients, and how you can optimize medication adherence in your clinics to drastically improve patient outcomes.

Prof. Kevin Dolgin
Prof. Florian Limbourg
Prof. Anoop Chauhan
Developed by: Springer Medicine
Obesity Clinical Trial Summary

At a glance: The STEP trials

A round-up of the STEP phase 3 clinical trials evaluating semaglutide for weight loss in people with overweight or obesity.

Developed by: Springer Medicine