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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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  1. Calderwood SK, Khaleque MA, Sawyer DB, et al. Heat shock proteins in cancer: chaperones of tumorigenesis. Trends Biochem Sci. 2006;31(3):164–72. · DOI
  2. 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. · DOI
  3. Dubey A, Prajapati KS, Swamy M, et al. Heat shock proteins: a therapeutic target worth to consider. Vet World. 2015;8(1):46–51. · DOI
  4. Lindquist S, Craig EA. The heat-shock proteins. Annu Rev Genet. 1988;22:631–77. · DOI
  5. Jackson SE. Hsp90: structure and function. Top Curr Chem. 2013;328:155–240. · DOI
  6. 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. · DOI
  7. Sreedhar AS, Kalmár E, Csermely P, et al. Hsp90 isoforms: functions, expression and clinical importance. FEBS Lett. 2004;562(1–3):11–5. · DOI
  8. 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. · DOI
  9. Walerych D, Kudla G, Gutkowska M, et al. Hsp90 chaperones wild-type p53 tumor suppressor protein. J Biol Chem. 2004;279(47):48836–45. · DOI
  10. Whitesell L, Lindquist SL. HSP90 and the chaperoning of cancer. Nat Rev Cancer. 2005;5(10):761–72. · DOI · Paper page
  11. 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. · DOI
  12. 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. · DOI
  13. 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. · DOI
  14. 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. · DOI · Paper page
  15. Yan J, Wan P, Choksi S, Liu ZG. Necroptosis and tumor progression. Trends Cancer. 2022;8(1):21–7. · DOI
  16. 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. · DOI
  17. 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. · DOI
  18. Bruckheimer EM, Cho SH, Sarkiss M, et al. The Bcl-2 gene family and apoptosis. Adv Biochem Eng Biotechnol. 1998;62:75–105.
  19. 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. · DOI
  20. 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. · DOI
  21. 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. · DOI
  22. 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. · DOI
  23. 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. · DOI
  24. 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. · DOI
  25. 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. · DOI
  26. 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. · DOI
  27. 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. · DOI
  28. 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. · DOI
  29. 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. · DOI
  30. 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. · DOI
  31. 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. · DOI
  32. 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. · DOI
  33. 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. · DOI
  34. 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. · DOI
  35. 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. · DOI
  36. Green DR, Llambi F. Cell death signaling. Cold Spring Harb Perspect Biol. 2015;7(12): a006080. · DOI
  37. Wang B, Chen Z, Yu F, et al. Hsp90 regulates autophagy and plays a role in cancertherapy. Tumour Biol. 2016;37(1):1–6. · DOI
  38. Xiao X, Wang W, Li Y, et al. HSP90AA1-mediated autophagy promotes drug resistancein osteosarcoma. J Exp Clin Cancer Res. 2018;37(1):201. · DOI
  39. Xu Z, Han X, Ou D, et al. Targeting PI3K/AKT/mTOR-mediated autophagy for tumortherapy. Appl Microbiol Biotechnol. 2020;104(2):1–13. · DOI
  40. 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. · DOI
  41. 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. · DOI
  42. 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. · DOI
  43. Liu J, Dai E, Kang R, et al. The dark side of ferroptosis in pancreatic cancer. Oncoimmunology. 2021;10(1):1868691. · DOI
  44. 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. · DOI
  45. Dixon SJ, Patel DN, Welsch M, et al. Pharmacological inhibition of cystine-glutamate exchange induces endoplasmic reticulum stress and ferroptosis. Elife. 2014;3: e02523. · DOI · Paper page
  46. Miao Z, Tian W, Ye Y, et al. Hsp90 induces Acsl4-dependent glioma ferroptosis via dephosphorylating Ser637 at Drp1. Cell Death Dis. 2022;13(6):548. · DOI
  47. 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. · DOI
  48. 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. · DOI
  49. Birbo B, Madu EE, Madu CO, et al. Role of HSP90 in cancer. Int J Mol Sci. 2021;22(19):10317. · DOI
  50. Nakai A, Ishikawa T. Cell cycle transition under stress conditions controlled by vertebrate heat shock factors. EMBO J. 2001;20(11):2885–95. · DOI
  51. 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. · DOI
  52. Zuehlke AD, Beebe K, Neckers L, et al. Regulation and function of the human HSP90AA1 gene. Gene. 2015;570(1):8–16. · DOI
  53. 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. · DOI
  54. 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. · DOI
  55. 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. · DOI
  56. Maiti S, Picard D. Cytosolic Hsp90 isoform-specific functions and clinical significance. Biomolecules. 2022;12(9):1166. · DOI
  57. Dernovšek J, Tomašič T. Following the design path of isoform-selective Hsp90 inhibitors: small differences, great opportunities. Pharmacol Ther. 2023;245: 108396. · DOI
  58. 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. · DOI
  59. 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. · DOI
  60. 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. · DOI
  61. 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. · DOI
  62. 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. · DOI
  63. 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. · DOI
  64. 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. · DOI
  65. 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. · DOI
  66. 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. · DOI
  67. 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. · DOI
  68. 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. · DOI
  69. 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. · DOI
  70. 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. · DOI
  71. Wang YY, Liu C, Chen X, et al. Heat shock protein 90α in nipple discharge as a potential tumor marker for breast cancer. Chin J Physiol. 2021;64(5):251–6. https://doi.org/10.4103/cjp.cjp_72_21. · DOI
  72. 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. · DOI
  73. 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. · DOI
  74. Chen CC, Chen LL, Li CP, et al. Myeloid-derived macrophages and secreted HSP90α induce pancreatic ductal adenocarcinoma development. Oncoimmunology. 2018;7(5): e1424612. · DOI
  75. 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. · DOI
  76. 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. · DOI
  77. 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. · DOI
  78. 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.
  79. 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. · DOI
  80. 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. · DOI
  81. 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. · DOI
  82. 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. · DOI
  83. 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. · DOI
  84. 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. · DOI
  85. 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. · DOI
  86. 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. · DOI
  87. 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. · DOI
  88. 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. · DOI
  89. 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. · DOI
  90. 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.
  91. 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. · DOI
  92. 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. · DOI
  93. 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. · DOI
  94. 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. · DOI
  95. 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. · DOI

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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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Liu, B., & Qian, D. (2024). Hsp90α and cell death in cancers: a review. Discover Oncology. https://doi.org/10.1007/s12672-024-01021-0

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