Generic placeholder image

Current Pharmaceutical Design

Editor-in-Chief

ISSN (Print): 1381-6128
ISSN (Online): 1873-4286

General Review Article

The Role of Heat Shock Protein 27 in Carcinogenesis and Treatment of Colorectal Cancer

Author(s): Fereshteh Asgharzadeh, Reyhaneh Moradi-Marjaneh* and Mahdi Moradi Marjaneh*

Volume 28, Issue 32, 2022

Published on: 08 September, 2022

Page: [2677 - 2685] Pages: 9

DOI: 10.2174/1381612828666220427140640

open access plus

Abstract

The incidence of colorectal cancer (CRC) has significantly increased in recent decades, which has made this disease an important global health issue. Despite many efforts, there is no useful prognostic or diagnostic biomarker for CRC. Heat shock protein 27 (Hsp27) is one of the most studied members of the Hsp family. It has attracted particular attention in CRC pathogenesis since it is involved in fundamental cell functions for cell survival. Evidence shows that Hsp27 plays important role in CRC progression and metastasis. Hsp27 overexpression has been observed in CRC and is suggested to be associated with CRC’s poor prognosis. In the present review, we focus on the current knowledge of the role of Hsp27 in CRC carcinogenesis and the underlying mechanisms. In addition, we discuss the value of targeting Hsp27 in CRC treatment.

Keywords: Carcinogenesis, colorectal cancer, heat shock protein 27, anticancer agents, chemotherapeutic agents, biomarker.

« Previous
[1]
Moradi Marjaneh R, Khazaei M, Ferns GA, Avan A, Aghaee-Bakhtiari SH. MicroRNAs as potential therapeutic targets to predict responses to oxaliplatin in colorectal cancer: From basic evidence to therapeutic implication. IUBMB Life 2019; 71(10): 1428-41.
[http://dx.doi.org/10.1002/iub.2108] [PMID: 31322820]
[2]
Moradi Marjaneh R, Hassanian SM, Ghobadi N, et al. Targeting the death receptor signaling pathway as a potential therapeutic target in the treatment of colorectal cancer. J Cell Physiol 2018; 233(10): 6538-49.
[http://dx.doi.org/10.1002/jcp.26640] [PMID: 29741789]
[3]
Singh MK, Sharma B, Tiwari PK. The small heat shock protein Hsp27: Present understanding and future prospects. J Therm Biol 2017; 69: 149-54.
[http://dx.doi.org/10.1016/j.jtherbio.2017.06.004] [PMID: 29037376]
[4]
Choi S-K, Kam H, Kim K-Y, Park SI, Lee Y-S. Targeting heat shock protein 27 in cancer: A druggable target for cancer treatment? Cancers (Basel) 2019; 11(8): 1195.
[http://dx.doi.org/10.3390/cancers11081195] [PMID: 31426426]
[5]
Vidyasagar A, Wilson NA, Djamali A. Heat shock protein 27 (HSP27): Biomarker of disease and therapeutic target. Fibrogenesis Tissue Repair 2012; 5(1): 7.
[http://dx.doi.org/10.1186/1755-1536-5-7] [PMID: 22564335]
[6]
Bakthisaran R, Tangirala R, Rao ChM. Small heat shock proteins: Role in cellular functions and pathology. Biochim Biophys Acta 2015; 1854(4): 291-319.
[http://dx.doi.org/10.1016/j.bbapap.2014.12.019] [PMID: 25556000]
[7]
Konishi H, Matsuzaki H, Tanaka M, et al. Activation of protein kinase B (Akt/RAC-protein kinase) by cellular stress and its association with heat shock protein Hsp27. FEBS Lett 1997; 410(2-3): 493-8.
[http://dx.doi.org/10.1016/S0014-5793(97)00541-3] [PMID: 9237690]
[8]
Arrigo A-P, Virot S, Chaufour S, Firdaus W, Kretz-Remy C, Diaz-Latoud C. Hsp27 consolidates intracellular redox homeostasis by upholding glutathione in its reduced form and by decreasing iron intracellular levels. Antioxid Redox Signal 2005; 7(3-4): 414-22.
[http://dx.doi.org/10.1089/ars.2005.7.414] [PMID: 15706088]
[9]
Concannon CG, Orrenius S, Samali A. Hsp27 inhibits cytochrome c-mediated caspase activation by sequestering both pro-caspase-3 and cytochrome c. Gene Expr 2001; 9(4-5): 195-201.
[http://dx.doi.org/10.3727/000000001783992605] [PMID: 11444529]
[10]
Giordano G, Febbraro A, Tomaselli E, et al. Cancer-related CD15/FUT4 overexpression decreases benefit to agents targeting EGFR or VEGF acting as a novel RAF-MEK-ERK kinase downstream regulator in metastatic colorectal cancer. J Exp Clin Cancer Res 2015; 34(1): 108.
[http://dx.doi.org/10.1186/s13046-015-0225-7] [PMID: 26427914]
[11]
Rogalla T, Ehrnsperger M, Preville X, et al. Regulation of Hsp27 oligomerization, chaperone function, and protective activity against oxidative stress/tumor necrosis factor α by phosphorylation. J Biol Chem 1999; 274(27): 18947-56.
[http://dx.doi.org/10.1074/jbc.274.27.18947] [PMID: 10383393]
[12]
Wyttenbach A, Sauvageot O, Carmichael J, Diaz-Latoud C, Arrigo A-P, Rubinsztein DC. Heat shock protein 27 prevents cellular polyglutamine toxicity and suppresses the increase of reactive oxygen species caused by huntingtin. Hum Mol Genet 2002; 11(9): 1137-51.
[http://dx.doi.org/10.1093/hmg/11.9.1137] [PMID: 11978772]
[13]
Freilich R, Betegon M, Tse E, et al. Competing protein-protein interactions regulate binding of Hsp27 to its client protein tau. Nat Commun 2018; 9(1): 4563.
[http://dx.doi.org/10.1038/s41467-018-07012-4] [PMID: 30385828]
[14]
Jovcevski B, Kelly MA, Rote AP, et al. Phosphomimics destabilize Hsp27 oligomeric assemblies and enhance chaperone activity. Chem Biol 2015; 22(2): 186-95.
[http://dx.doi.org/10.1016/j.chembiol.2015.01.001] [PMID: 25699602]
[15]
Katsogiannou M, Andrieu C, Rocchi P. Heat shock protein 27 phosphorylation state is associated with cancer progression. Front Genet 2014; 5: 346.
[http://dx.doi.org/10.3389/fgene.2014.00346] [PMID: 25339975]
[16]
Kostenko S, Moens U. Heat shock protein 27 phosphorylation: Kinases, phosphatases, functions and pathology. Cell Mol Life Sci 2009; 66(20): 3289-307.
[http://dx.doi.org/10.1007/s00018-009-0086-3] [PMID: 19593530]
[17]
Stope MB, Weiss M, Preuss M, et al. Immediate and transient phosphorylation of the heat shock protein 27 initiates chemoresistance in prostate cancer cells. Oncol Rep 2014; 32(6): 2380-6.
[http://dx.doi.org/10.3892/or.2014.3492] [PMID: 25231055]
[18]
Garrido C, Fromentin A, Bonnotte B, et al. Heat shock protein 27 enhances the tumorigenicity of immunogenic rat colon carcinoma cell clones. Cancer Res 1998; 58(23): 5495-9.
[PMID: 9850085]
[19]
Liu W, Ma Y, Huang L, et al. Identification of HSP27 as a potential tumor marker for colorectal cancer by the two-dimensional polyacrylamide gel electrophoresis. Mol Biol Rep 2010; 37(7): 3207-16.
[http://dx.doi.org/10.1007/s11033-009-9903-x] [PMID: 19842058]
[20]
Yu Z, Zhi J, Peng X, Zhong X, Xu A. Clinical significance of HSP27 expression in colorectal cancer. Mol Med Rep 2010; 3(6): 953-8.
[PMID: 21472339]
[21]
Wang F, Zhang P, Shi C, Yang Y, Qin H. Immunohistochemical detection of HSP27 and hnRNP K as prognostic and predictive biomarkers for colorectal cancer. Med Oncol 2012; 29(3): 1780-8.
[http://dx.doi.org/10.1007/s12032-011-0037-3] [PMID: 21861207]
[22]
Garrido C, Ottavi P, Fromentin A, et al. HSP27 as a mediator of confluence-dependent resistance to cell death induced by anticancer drugs. Cancer Res 1997; 57(13): 2661-7.
[PMID: 9205074]
[23]
Choi DH, Ha JS, Lee WH, et al. Heat shock protein 27 is associated with irinotecan resistance in human colorectal cancer cells. FEBS Lett 2007; 581(8): 1649-56.
[http://dx.doi.org/10.1016/j.febslet.2007.02.075] [PMID: 17395183]
[24]
Tsuruta M, Nishibori H, Hasegawa H, et al. Heat shock protein 27, a novel regulator of 5-fluorouracil resistance in colon cancer. Oncol Rep 2008; 20(5): 1165-72.
[PMID: 18949417]
[25]
Hayashi R, Ishii Y, Ochiai H, et al. Suppression of heat shock protein 27 expression promotes 5-fluorouracil sensitivity in colon cancer cells in a xenograft model. Oncol Rep 2012; 28(4): 1269-74.
[http://dx.doi.org/10.3892/or.2012.1935] [PMID: 22842517]
[26]
Chatterjee S, Burns TF. Targeting heat shock proteins in cancer: A promising therapeutic approach. Int J Mol Sci 2017; 18(9): 1978.
[http://dx.doi.org/10.3390/ijms18091978] [PMID: 28914774]
[27]
Zhao L, Liu L, Wang S, Zhang YF, Yu L, Ding YQ. Differential proteomic analysis of human colorectal carcinoma cell lines metastasis-associated proteins. J Cancer Res Clin Oncol 2007; 133(10): 771-82.
[http://dx.doi.org/10.1007/s00432-007-0222-0] [PMID: 17503081]
[28]
Han L, Jiang Y, Han D, Tan W. Hsp27 regulates epithelial mesenchymal transition, metastasis and proliferation in colorectal carcinoma. Oncol Lett 2018; 16(4): 5309-16.
[http://dx.doi.org/10.3892/ol.2018.9286] [PMID: 30250600]
[29]
Diepenbruck M, Christofori G. Epithelial-mesenchymal transition (EMT) and metastasis: Yes, no, maybe? Curr Opin Cell Biol 2016; 43: 7-13.
[http://dx.doi.org/10.1016/j.ceb.2016.06.002] [PMID: 27371787]
[30]
Gurzu S, Silveanu C, Fetyko A, Butiurca V, Kovacs Z, Jung I. Systematic review of the old and new concepts in the epithelial-mesenchymal transition of colorectal cancer. World J Gastroenterol 2016; 22(30): 6764-75.
[http://dx.doi.org/10.3748/wjg.v22.i30.6764] [PMID: 27570416]
[31]
Cordonnier T, Bishop JL, Shiota M, et al. Hsp27 regulates EGF/β-catenin mediated epithelial to mesenchymal transition in prostate cancer. Int J Cancer 2015; 136(6): E496-507.
[http://dx.doi.org/10.1002/ijc.29122] [PMID: 25130271]
[32]
Amerizadeh F, Rezaei N, Rahmani F, et al. Crocin synergistically enhances the antiproliferative activity of 5-flurouracil through Wnt/PI3K pathway in a mouse model of colitis-associated colorectal cancer. J Cell Biochem 2018; 119(12): 10250-61.
[http://dx.doi.org/10.1002/jcb.27367] [PMID: 30129057]
[33]
Wei L, Liu T-T, Wang H-H, et al. Hsp27 participates in the maintenance of breast cancer stem cells through regulation of epithelial-mesenchymal transition and nuclear factor-κB. Breast Cancer Res 2011; 13(5): R101.
[http://dx.doi.org/10.1186/bcr3042] [PMID: 22023707]
[34]
Ghosh A, Lai C, McDonald S, et al. HSP27 expression in primary colorectal cancers is dependent on mutation of KRAS and PI3K/AKT activation status and is independent of TP53. Exp Mol Pathol 2013; 94(1): 103-8.
[http://dx.doi.org/10.1016/j.yexmp.2012.09.001] [PMID: 22982087]
[35]
Berridge MJ, Bootman MD, Roderick HL. Calcium signalling: Dynamics, homeostasis and remodelling. Nat Rev Mol Cell Biol 2003; 4(7): 517-29.
[http://dx.doi.org/10.1038/nrm1155] [PMID: 12838335]
[36]
Srivats S, Balasuriya D, Pasche M, et al. Sigma1 receptors inhibit store-operated Ca2+ entry by attenuating coupling of STIM1 to Orai1. J Cell Biol 2016; 213(1): 65-79.
[http://dx.doi.org/10.1083/jcb.201506022] [PMID: 27069021]
[37]
Zhou Y, Srinivasan P, Razavi S, et al. Initial activation of STIM1, the regulator of store-operated calcium entry. Nat Struct Mol Biol 2013; 20(8): 973-81.
[http://dx.doi.org/10.1038/nsmb.2625] [PMID: 23851458]
[38]
Zhou Y, Meraner P, Kwon HT, et al. STIM1 gates the store-operated calcium channel ORAI1 in vitro. Nat Struct Mol Biol 2010; 17(1): 112-6.
[http://dx.doi.org/10.1038/nsmb.1724] [PMID: 20037597]
[39]
Wong HS-C, Chang W-C. Correlation of clinical features and genetic profiles of stromal interaction molecule 1 (STIM1) in colorectal cancers. Oncotarget 2015; 6(39): 42169-82.
[http://dx.doi.org/10.18632/oncotarget.5888] [PMID: 26543234]
[40]
Chen Y-F, Chen Y-T, Chiu W-T, Shen M-R. Remodeling of calcium signaling in tumor progression. J Biomed Sci 2013; 20(1): 23.
[http://dx.doi.org/10.1186/1423-0127-20-23] [PMID: 23594099]
[41]
Jardin I, Rosado JA. STIM and calcium channel complexes in cancer. Biochim Biophys Acta 2016; 1863(6): 1418-26.
[42]
Umemura M, Balijinnyam E, Feske S, De Lorenzo MS, Xie L-H, Ishikawa Y, et al. Store-operated Ca2+ entry (SOCE) regulates melanoma proliferation and cell migration. PLoS One 2014; 9(2)e89292
[43]
Yang N, Tang Y, Wang F, et al. Blockade of store-operated Ca2+ entry inhibits hepatocarcinoma cell migration and invasion by regulating focal adhesion turnover. Cancer Lett 2013; 330(2): 163-9.
[http://dx.doi.org/10.1016/j.canlet.2012.11.040] [PMID: 23211538]
[44]
Yang S, Zhang JJ, Huang X-Y. Orai1 and STIM1 are critical for breast tumor cell migration and metastasis. Cancer Cell 2009; 15(2): 124-34.
[http://dx.doi.org/10.1016/j.ccr.2008.12.019] [PMID: 19185847]
[45]
Zhang Z, Liu X, Feng B, et al. STIM1, a direct target of microRNA-185, promotes tumor metastasis and is associated with poor prognosis in colorectal cancer. Oncogene 2015; 34(37): 4808-20.
[http://dx.doi.org/10.1038/onc.2014.404] [PMID: 25531324]
[46]
Vashisht A, Trebak M, Motiani RK. STIM and Orai proteins as novel targets for cancer therapy. A Review in the Theme: Cell and Molecular Processes in Cancer Metastasis. Am J Physiol Cell Physiol 2015; 309(7): C457-69.
[http://dx.doi.org/10.1152/ajpcell.00064.2015] [PMID: 26017146]
[47]
Huang C-Y, Wei P-L, Chen W-Y, Chang W-C, Chang Y-J. Silencing heat shock protein 27 inhibits the progression and metastasis of Colorectal Cancer (CRC) by maintaining the Stability of Stromal Interaction Molecule 1 (STIM1) proteins. Cells 2018; 7(12): 262.
[http://dx.doi.org/10.3390/cells7120262] [PMID: 30544747]
[48]
Sherr CJ, Roberts JM. CDK inhibitors: Positive and negative regulators of G1-phase progression. Genes Dev 1999; 13(12): 1501-12.
[http://dx.doi.org/10.1101/gad.13.12.1501] [PMID: 10385618]
[49]
Schwartz GK, Shah MA. Targeting the cell cycle: A new approach to cancer therapy. J Clin Oncol 2005; 23(36): 9408-21.
[http://dx.doi.org/10.1200/JCO.2005.01.5594] [PMID: 16361640]
[50]
Zhou B-BS, Elledge SJ. The DNA damage response: Putting checkpoints in perspective. Nature 2000; 408(6811): 433-9.
[http://dx.doi.org/10.1038/35044005] [PMID: 11100718]
[51]
Thuringer D, Jego G, Wettstein G, et al. Extracellular HSP27 mediates angiogenesis through Toll-like receptor 3. FASEB J 2013; 27(10): 4169-83.
[http://dx.doi.org/10.1096/fj.12-226977] [PMID: 23804239]
[52]
Paone A, Galli R, Gabellini C, et al. Toll-like receptor 3 regulates angiogenesis and apoptosis in prostate cancer cell lines through hypoxia-inducible factor 1 α. Neoplasia 2010; 12(7): 539-49.
[http://dx.doi.org/10.1593/neo.92106] [PMID: 20651983]
[53]
De Veirman K, Rao L, De Bruyne E, et al. Cancer associated fibroblasts and tumor growth: Focus on multiple myeloma. Cancers (Basel) 2014; 6(3): 1363-81.
[http://dx.doi.org/10.3390/cancers6031363] [PMID: 24978438]
[54]
Hirano S, Shelden EA, Gilmont RR. HSP27 regulates fibroblast adhesion, motility, and matrix contraction. Cell Stress Chaperones 2004; 9(1): 29-37.
[http://dx.doi.org/10.1379/1466-1268(2004)009<0029:HRFAMA>2.0.CO;2] [PMID: 15270075]
[55]
Suarez E, Syed F, Alonso-Rasgado T, Mandal P, Bayat A. Up-regulation of tension-related proteins in keloids: Knockdown of Hsp27, α2β1-integrin, and PAI-2 shows convincing reduction of extracellular matrix production. Plast Reconstr Surg 2013; 131(2): 158e-73e.
[http://dx.doi.org/10.1097/PRS.0b013e3182789b2b] [PMID: 23358011]
[56]
Schweiger T, Nikolowsky C, Starlinger P, et al. Stromal expression of heat-shock protein 27 is associated with worse clinical outcome in patients with colorectal cancer lung metastases. PLoS One 2015; 10(3)e0120724
[http://dx.doi.org/10.1371/journal.pone.0120724] [PMID: 25793600]
[57]
Jacquemin G, Granci V, Gallouet AS, et al. Quercetin-mediated Mcl-1 and survivin downregulation restores TRAIL-induced apoptosis in non-Hodgkin’s lymphoma B cells. Haematologica 2012; 97(1): 38-46.
[http://dx.doi.org/10.3324/haematol.2011.046466] [PMID: 21933852]
[58]
Knowles LM, Zigrossi DA, Tauber RA, Hightower C, Milner JA. Flavonoids suppress androgen-independent human prostate tumor proliferation. Nutr Cancer 2000; 38(1): 116-22.
[http://dx.doi.org/10.1207/S15327914NC381_16] [PMID: 11341036]
[59]
Elattar TM, Virji AS. The inhibitory effect of curcumin, genistein, quercetin and cisplatin on the growth of oral cancer cells in vitro. Anticancer Res 2000; 20(3A): 1733-8.
[PMID: 10928101]
[60]
Russo M, Milito A, Spagnuolo C, et al. CK2 and PI3K are direct molecular targets of quercetin in chronic lymphocytic leukaemia. Oncotarget 2017; 8(26): 42571-87.
[http://dx.doi.org/10.18632/oncotarget.17246] [PMID: 28489572]
[61]
Fu WM, Zhang JF, Wang H, et al. Heat shock protein 27 mediates the effect of 1,3,5-trihydroxy-13,13-dimethyl-2H-pyran [7,6-b] xanthone on mitochondrial apoptosis in hepatocellular carcinoma. J Proteomics 2012; 75(15): 4833-43.
[http://dx.doi.org/10.1016/j.jprot.2012.05.032] [PMID: 22677112]
[62]
Heinrich J-C, Tuukkanen A, Schroeder M, Fahrig T, Fahrig R. RP101 (brivudine) binds to heat shock protein HSP27 (HSPB1) and enhances survival in animals and pancreatic cancer patients. J Cancer Res Clin Oncol 2011; 137(9): 1349-61.
[http://dx.doi.org/10.1007/s00432-011-1005-1] [PMID: 21833720]
[63]
Heinrich JC, Donakonda S, Haupt VJ, Lennig P, Zhang Y, Schroeder M. New HSP27 inhibitors efficiently suppress drug resistance development in cancer cells. Oncotarget 2016; 7(42): 68156-69.
[http://dx.doi.org/10.18632/oncotarget.11905] [PMID: 27626687]
[64]
Choi S-H, Lee Y-J, Seo WD, Lee H-J, Nam J-W, Lee YJ, et al. Altered cross-linking of Hsp27 by zerumbone as a novel strategy for overcoming Hsp27-mediated radioresistance. Int J Radiat Oncol Biol Phys 2011; 79(4): 1196-205.
[http://dx.doi.org/10.1016/j.ijrobp.2010.10.025]
[65]
Choi B, Choi S-K, Park YN, et al. Sensitization of lung cancer cells by altered dimerization of HSP27. Oncotarget 2017; 8(62): 105372-82.
[http://dx.doi.org/10.18632/oncotarget.22192] [PMID: 29285257]
[66]
Kim JH, Jung YJ, Choi B, et al. Overcoming HSP27-mediated resistance by altered dimerization of HSP27 using small molecules. Oncotarget 2016; 7(33): 53178-90.
[http://dx.doi.org/10.18632/oncotarget.10629] [PMID: 27449291]
[67]
Kim J-Y, An Y-M, Yoo BR, et al. HSP27 inhibitor attenuates radiation-induced pulmonary inflammation. Sci Rep 2018; 8(1): 4189.
[http://dx.doi.org/10.1038/s41598-018-22635-9] [PMID: 29520071]
[68]
Crooke ST, Liang XH, Crooke RM, Baker BF, Geary RS. Antisense drug discovery and development technology considered in a pharmacological context. Biochem Pharmacol 2021; 189114196
[http://dx.doi.org/10.1016/j.bcp.2020.114196] [PMID: 32800852]
[69]
Chi KN, Yu EY, Jacobs C, et al. A phase I dose-escalation study of apatorsen (OGX-427), an antisense inhibitor targeting heat shock protein 27 (Hsp27), in patients with castration-resistant prostate cancer and other advanced cancers. Ann Oncol 2016; 27(6): 1116-22.
[http://dx.doi.org/10.1093/annonc/mdw068] [PMID: 27022067]
[70]
Yu EY, Ellard SL, Hotte SJ, et al. A randomized phase 2 study of a HSP27 targeting antisense, apatorsen with prednisone versus prednisone alone, in patients with metastatic castration resistant prostate cancer. Invest New Drugs 2018; 36(2): 278-87.
[http://dx.doi.org/10.1007/s10637-017-0553-x] [PMID: 29250742]
[71]
Spigel DR, Shipley DL, Waterhouse DM, et al. A randomized, double-blinded, phase II trial of carboplatin and pemetrexed with or without Apatorsen (OGX-427) in patients with previously untreated stage IV non-squamous-non-small-cell lung cancer: The SPRUCE trial. Oncologist 2019; 24(12): e1409-16.
[http://dx.doi.org/10.1634/theoncologist.2018-0518] [PMID: 31420467]
[72]
Seigneuric R, Gobbo J, Colas P, Garrido C. Targeting cancer with peptide aptamers. Oncotarget 2011; 2(7): 557-61.
[http://dx.doi.org/10.18632/oncotarget.297] [PMID: 21709317]
[73]
Gibert B, Hadchity E, Czekalla A, et al. Inhibition of heat shock protein 27 (HspB1) tumorigenic functions by peptide aptamers. Oncogene 2011; 30(34): 3672-81.
[http://dx.doi.org/10.1038/onc.2011.73] [PMID: 21423207]
[74]
McConnell JR, McAlpine SR. Heat shock proteins 27, 40, and 70 as combinational and dual therapeutic cancer targets. Bioorg Med Chem Lett 2013; 23(7): 1923-8.
[http://dx.doi.org/10.1016/j.bmcl.2013.02.014] [PMID: 23453837]
[75]
Dai S, Jia Y, Wu S-L, et al. Comprehensive characterization of heat shock protein 27 phosphorylation in human endothelial cells stimulated by the microbial dithiole thiolutin. J Proteome Res 2008; 7(10): 4384-95.
[http://dx.doi.org/10.1021/pr800376w] [PMID: 18720982]
[76]
Jia Y, Wu S-L, Isenberg JS, et al. Thiolutin inhibits endothelial cell adhesion by perturbing Hsp27 interactions with components of the actin and intermediate filament cytoskeleton. Cell Stress Chaperones 2010; 15(2): 165-81.
[http://dx.doi.org/10.1007/s12192-009-0130-0] [PMID: 19579057]
[77]
Söderström HK, Kauppi JT, Oksala N, et al. Overexpression of HSP27 and HSP70 is associated with decreased survival among patients with esophageal adenocarcinoma. World J Clin Cases 2019; 7(3): 260-9.
[http://dx.doi.org/10.12998/wjcc.v7.i3.260] [PMID: 30746368]
[78]
Mittal S, Rajala MS. Heat shock proteins as biomarkers of lung cancer. Cancer Biol Ther 2020; 21(6): 477-85.
[http://dx.doi.org/10.1080/15384047.2020.1736482] [PMID: 32228356]

© 2024 Bentham Science Publishers | Privacy Policy