Generic placeholder image

Current Chemical Biology

Author(s): Chiranjib Bhattacharjee and Lokesh Deb*

DOI: 10.2174/2212796814666200122114833

DownloadDownload PDF Flyer Cite As
The Role of Heat Shock Protein -90 (HSP-90) in Inflammatory Disorders

Page: [30 - 37] Pages: 8

  • * (Excluding Mailing and Handling)

Abstract

In human cells, Heat Shock Protein-90 (HSP-90) is present in the cytosol, nucleoplasm, endoplasmic reticulum, and mitochondria. The eukaryotic HSP-90 is multifunctionary and essential for cell viability, signal transduction, cell-cycle control as well as transcriptional regulation. The intracellular environment does not restrict HSP-90. It has a vital role in all types of inflammatory disorders, including cancer, autoimmune diseases, infectious inflammatory conditions. Hence, pharmacological inhibition of HSP-90 is currently a choice of therapeutic target for the treatment of autoimmune diseases, cancer, and infectious diseases. Based on the biology of HSP-90, several COOH-terminal ATPase sites of HSP-90, NH2-terminal ATPase sites of HSP-90, and Histone deacetylase inhibitors are evaluated and classified under various groups. For the treatment of different inflammatory disorders, HSP-90 identified as a promising therapeutic target. The present review may guide researchers for evaluating the HSP-90 targeted pathway as a useful therapeutic target for inflammatory diseases, including cancers.

Keywords: Heat shock protein-90 (HSP-90), autoimmune diseases, cancer, HSP inhibitor, viral HSP-90, fungal HSP-90.

Graphical Abstract

[1]
Ponta A, Akter S, Bae Y. Degradable cross-linked nanoassemblies as drug carriers for heat shock protein 90 inhibitor 17-N-Allylamino-17-demethoxy-geldanamycin. Pharmaceuticals (Basel) 2011; 4(10): 1281-92.
[http://dx.doi.org/10.3390/ph4101281] [PMID: 27721325]
[2]
Tukaj S, Węgrzyn G. Anti-Hsp90 therapy in autoimmune and inflammatory diseases: a review of preclinical studies. Cell Stress Chaperones 2016; 21(2): 213-8.
[http://dx.doi.org/10.1007/s12192-016-0670-z] [PMID: 26786410]
[3]
Sidera K, Patsavoudi E. HSP90 inhibitors: current development and potential in cancer therapy. Recent Patents Anticancer Drug Discov 2014; 9(1): 1-20.
[http://dx.doi.org/10.2174/15748928113089990031] [PMID: 23312026]
[4]
Soga S, Akinaga S, Shiotsu Y. Hsp90 inhibitors as anti-cancer agents, from basic discoveries to clinical development. Curr Pharm Des 2013; 19(3): 366-76.
[http://dx.doi.org/10.2174/138161213804143617] [PMID: 22920907]
[5]
Byrd JC. HSP90 inhibition without heat shock response. Blood 2018; 132(3): 241-2.
[http://dx.doi.org/10.1182/blood-2018-05-850271] [PMID: 30026301]
[6]
Tutar L, Coskun AK, Tutar Y. New generation cancer drug studies: Hsp90 inhibitors. Single Cell Biol 2016., 5e124
[http://dx.doi.org/10.4172/2168-9431.1000e124]
[7]
Moser C, Lang SA, Stoeltzing O. Heat-shock protein 90 (Hsp90) as a molecular target for therapy of gastrointestinal cancer. Anticancer Res 2009; 29(6): 2031-42.
[PMID: 19528462]
[8]
Sevin M, Girodon F, Garrido C, de Thonel A. HSP90 and HSP70: Implication in inflammation processes and therapeutic approaches for myeloproliferative neoplasms. Mediators Inflamm 2015; 2015:970242
[http://dx.doi.org/10.1155/2015/970242]
[9]
Madrigal-Matute J, López-Franco O, Blanco-Colio LM, et al. Heat shock protein 90 inhibitors attenuate inflammatory responses in atherosclerosis. Cardiovasc Res 2010; 86(2): 330-7.
[http://dx.doi.org/10.1093/cvr/cvq046] [PMID: 20154064]
[10]
Zagouri F, Bournakis E, Koutsoukos K, Papadimitriou CA. Heat shock protein 90 (hsp90) expression and breast cancer. Pharmaceuticals (Basel) 2012; 5(9): 1008-20.
[http://dx.doi.org/10.3390/ph5091008] [PMID: 24280702]
[11]
Weber H, Valbuena JR, Barbhuiya MA, et al. Small molecule inhibitor screening identifified HSP90 inhibitor 17-AAG as potential therapeutic agent for gallbladder cancer. Oncotarget 2017; 8(16): 26169-84.
[http://dx.doi.org/10.18632/oncotarget.15410] [PMID: 28412732]
[12]
Qin J-H, Wang K, Fu X-L, et al. Hsp90 inhibitor induces KG-1a cell differentiation and apoptosis via Akt/NF-κB signaling. Oncol Rep 2017; 38: 1517-24.
[http://dx.doi.org/10.3892/or.2017.5797] [PMID: 28713903]
[13]
Ho N, Li A, Li S, Zhang H. Heat shock protein 90 and role of its chemical inhibitors in treatment of hematologic malignancies. Pharmaceuticals (Basel) 2012; 5(8): 779-801.
[http://dx.doi.org/10.3390/ph5080779] [PMID: 24280675]
[14]
Rong B, Yang S. Molecular mechanism and targeted therapy of Hsp90 involved in lung cancer: New discoveries and developments (Review). Int J Oncol 2018; 52(2): 321-36.
[PMID: 29207057] [http://dx.doi.org/10.3892/ijo.2017.4214]
[15]
Chatterjee S, Bhattacharya S, Socinski MA, Burns TF. HSP90 inhibitors in lung cancer: promise still unfulfilled. Clin Adv Hematol Oncol 2016; 14(5): 346-56.
[PMID: 27379696]
[16]
Jiao Y, Ou W, Meng F, Zhou H, Wang A. Targeting HSP90 in ovarian cancers with multiple receptor tyrosine kinase coactivation. Mol Cancer 2011; 10: 125.
[http://dx.doi.org/10.1186/1476-4598-10-125] [PMID: 21962244]
[17]
Abbasi F, Marchion D, Xiong Y, et al. HSP90 inhibition decreases ovarian cancer cell proliferation and potentiates platinum sensitivity. Gynecol Oncol 2014; 133: 122-3.
[http://dx.doi.org/10.1016/j.ygyno.2014.03.321]
[18]
Wang X, Zhang J, Wu H, Li Y, Conti PS, Chen K. PET imaging of Hsp90 expression in pancreatic cancer using a new 64Cu-labeled dimeric Sansalvamide A decapeptide. Amino Acids 2018; 50(7): 897-907.
[http://dx.doi.org/10.1007/s00726-018-2566-y] [PMID: 29691700]
[19]
Ghadban T, Dibbern JL, Reeh M, et al. HSP90 is a promising target in gemcitabine and 5-fluorouracil resistant pancreatic cancer. Apoptosis 2017; 22(3): 369-80.
[http://dx.doi.org/10.1007/s10495-016-1332-4] [PMID: 27878398]
[20]
Routray S, Sunkavalli A, Swain N, Shankar AA. Emphasizing on heat shock protein 90's utility in head and neck squamous cell carcinoma treatment. J Cancer Res Ther 2013; 9(4): 583-6.
[http://dx.doi.org/10.4103/0973-1482.126451] [PMID: 24518700]
[21]
McLaughlin M, Barker HE, Khan AA, et al. HSP90 inhibition sensitizes head and neck cancer to platin-based chemoradiotherapy by modulation of the DNA damage response resulting in chromosomal fragmentation. BMC Cancer 2017; 17(1): 86.
[http://dx.doi.org/10.1186/s12885-017-3084-0] [PMID: 28143445]
[22]
Geller R, Taguwa S, Frydman J. Broad action of Hsp90 as a host chaperone required for viral replication. Biochim Biophys Acta 2012; 1823(3): 698-706.
[http://dx.doi.org/10.1016/j.bbamcr.2011.11.007] [PMID: 22154817]
[23]
Matthews R, Burnie J. The role of hsp90 in fungal infection. Immunol Today 1992; 13(9): 345-8.
[http://dx.doi.org/10.1016/0167-5699(92)90169-8] [PMID: 1466751]