The Role of Heat Shock Protein 70 kDa in Asthma

References

• Lambrecht BN, Hammad H. The immunology of asthma. Nat Immunol. 2015;16(1):45–56. doi:10.1038/ni.304925521684
   PubMed Web of Science ®Google Scholar
• Kuruvilla ME, Lee FE-H, Lee GB. Understanding asthma phenotypes, endotypes, and mechanisms of disease. Clin Rev Allergy Immunol. 2019;56(2):219–233. doi:10.1007/s12016-018-8712-130206782
   PubMed Web of Science ®Google Scholar
• Boonpiyathad T, Sozener ZC, Satitsuksanoa P, Akdis CA. Immunologic mechanisms in asthma. Semin Immunol. 2019;46:101333. doi:10.1016/j.smim.2019.10133331703832
   PubMed Web of Science ®Google Scholar
• Lambrecht BN, Hammad H, Fahy JV. The cytokine of asthma. Immunity. 2019;50(4):975–991. doi:10.1016/j.immuni.2019.03.01830995510
   PubMed Web of Science ®Google Scholar
• Huang XL, Tan XY, Liang Y, et al. Differential DAMP release was observed in the sputum of COPD, asthma and asthma-COPD overlap (ACO) patients. Sci Rep. 2019;9:19241. doi:10.1038/s41598-019-55502-231848359
   PubMed Web of Science ®Google Scholar
• Radons J. The human HSP70 family of chaperones: where do we stand? Cell Stress Chaperones. 2016;21(3):379–404.26865365
   PubMed Web of Science ®Google Scholar
• Kampinga HH, Hageman J, Vos MJ, et al. Guidelines for the nomenclature of the human heat shock proteins. Cell Stress Chaperones. 2009;14(1):105–111. doi:10.1007/s12192-008-0068-718663603
   PubMed Web of Science ®Google Scholar
• Hou C, Zhao H, Li W, et al. Erratum to: increased heat shock protein 70 levels in induced sputum and plasma correlate with severity of asthma patients. Cell Stress Chaperones. 2011;16(6):663–671. doi:10.1007/s12192-011-0278-221643870
   PubMed Web of Science ®Google Scholar
• Shevchenko MA, Troyanova NI, Servuli EA, Bolkhovitina EL, Fedorina AS, Sapozhnikov AM. Study of immunomodulatory effects of extracellular HSP70 in a mouse model of allergic airway inflammation. Biochemistry (Mosc). 2016;81(11):1384–1395. doi:10.1134/S000629791611015827914463
   PubMed Web of Science ®Google Scholar
• Borges TJ, Wieten L, van Herwijnen MJ, et al. The anti-inflammatory mechanisms of Hsp70. Front Immunol. 2012;3:95. doi:10.3389/fimmu.2012.0009522566973
   PubMed Web of Science ®Google Scholar
• De Maio A. Extracellular Hsp70: export and function. Curr Protein Pept Sci. 2014;15(3):225–231. doi:10.2174/138920371566614033111305724694368
   PubMed Web of Science ®Google Scholar
• Satoh M, Shimoda Y, Akatsu T, Ishikawa Y, Minami Y, Nakamura M. Elevated circulating levels of heat shock protein 70 are related to systemic inflammatory reaction through monocyte toll signal in patients with heart failure after acute myocardial infarction. Eur J Heart Fail. 2006;8(8):810–815. doi:10.1016/j.ejheart.2006.03.00416714144
   PubMed Web of Science ®Google Scholar
• Stocki P, Dickinson AM. The immunosuppressive activity of heat shock protein 70. Autoimmune Dis. 2012;2012:617213. doi:10.1155/2012/61721323326648
   PubMedGoogle Scholar
• Wallin RP, Lundqvist A, More SH, von Bonin A, Kiessling R, Ljunggren HG. Heat-shock proteins as activators of the innate immune system. Trends Immunol. 2002;23(3):130–135. doi:10.1016/S1471-4906(01)02168-811864840
   PubMed Web of Science ®Google Scholar
• Cantillo JF, Puerta L, Puchalska P, Lafosse-Marin S, Subiza JL, Fernandez-Caldas E. Allergenome characterization of the mosquito aedes aegypti. Allergy. 2017;72(10):1499–1509. doi:10.1111/all.1315028235135
   PubMed Web of Science ®Google Scholar
• Radauer C, Bublin M, Wagner S, Mari A, Breiteneder H. Allergens are distributed into few protein families and possess a restricted number of biochemical functions. J Allergy Clin Immunol. 2008;121(4):847–852.e7. doi:10.1016/j.jaci.2008.01.02518395549
   PubMed Web of Science ®Google Scholar
• Xie ZJ, Yin J. Chinese birch pollen allergy and immunotherapy in Mice. Inflammation. 2019;42(3):961–972. doi:10.1007/s10753-019-00957-830715691
   PubMed Web of Science ®Google Scholar
• Yang M, Wu T, Cheng L, Wang F, Wei Q, Tanguay RM. Plasma antibodies against heat shock protein 70 correlate with the incidence and severity of asthma in a Chinese population. Respir Res. 2005;6(1):18. doi:10.1186/1465-9921-6-1815710045
   PubMed Web of Science ®Google Scholar
• Hosseini SA, Zilaee M, Shoushtari MH, Dehcheshmeh MG. An evaluation of the effect of saffron supplementation on the antibody titer to heat-shock protein (HSP) 70, hsCRP and spirometry test in patients with mild and moderate persistent allergic asthma: a triple-blind, randomized placebo-controlled trial. Respir Med. 2018;145:28–34. doi:10.1016/j.rmed.2018.10.01630509713
   PubMed Web of Science ®Google Scholar
• Andersson A, Rasool O, Schmidt M, et al. Cloning, expression and characterization of two new IgE-binding proteins from the yeast Malassezia sympodialis with sequence similarities to heat shock proteins and manganese superoxide dismutase. Eur J Biochem. 2004;271(10):1885–1894. doi:10.1111/j.1432-1033.2004.04098.x15128298
   PubMedGoogle Scholar
• Vignola AM, Chanez P, Polla BS, Vic P, Godard P, Bousquet J. Increased expression of heat-shock-protein-70 on airway cells in asthma and chronic-bronchitis. Am J Respir Cell Mol Biol. 1995;13(6):683–691. doi:10.1165/ajrcmb.13.6.75767067576706
   PubMed Web of Science ®Google Scholar
• Tong WC, Luo WC. Heat shock proteins mRNA expressions by peripheral blood mononuclear cells in asthma and chronic bronchitis. Chin Med J. 2000;113(2):175–177.11775547
   PubMed Web of Science ®Google Scholar
• Prado N, Marazuela EG, Segura E, et al. Exosomes from bronchoalveolar fluid of tolerized mice prevent allergic reaction. J Immunol. 2008;181(2):1519–1525. doi:10.4049/jimmunol.181.2.151918606707
   PubMed Web of Science ®Google Scholar
• Asea A, Kraeft SK, Kurt-Jones EA, et al. Hsp70 stimulates cytokine production via a CD14-dependent pathway: a “chaperokine”. Cell Stress Chaperones. 2000;5(5):491.
   Web of Science ®Google Scholar
• Li CJ, Ning W, Matthay MA, Feghali-Bostwick CA, Choi AMK. MAPK pathway mediates EGR-1-HSP70-dependent cigarette smoke-induced chemokine production. Am J Physiol Lung Cell Mol Physiol. 2007;292(5):L1297–L1303. doi:10.1152/ajplung.00194.200617494953
   PubMed Web of Science ®Google Scholar
• Chase MA, Wheeler DS, Lierl KM, Hughes VS, Wong HR, Page K. Hsp72 induces inflammation and regulates cytokine production in airway epithelium through a TLR4- and NF-kappa B-dependent mechanism. J Immunol. 2007;179(9):6318–6324. doi:10.4049/jimmunol.179.9.631817947709
   PubMed Web of Science ®Google Scholar
• Wheeler DS, Chase MA, Senft AP, Poynter SE, Wong HR, Page K. Extracellular Hsp72, an endogenous DAMP, is released by virally infected airway epithelial cells and activates neutrophils via Toll-like receptor (TLR)-4. Respir Res. 2009;10(1):31. doi:10.1186/1465-9921-10-3119405961
   PubMed Web of Science ®Google Scholar
• Hulina A, Rajkovic MG, Despot DJ, et al. Extracellular Hsp70 induces inflammation and modulates LPS/LTA-stimulated inflammatory response in THP-1 cells. Cell Stress Chaperones. 2018;23(3):373–384. doi:10.1007/s12192-017-0847-029067554
   PubMed Web of Science ®Google Scholar
• Hulina-Tomaskovic A, Rajkovic MG, Jelic D, et al. Pro-inflammatory effects of extracellular Hsp70 on NCI-H292 human bronchial epithelial cell line. Int J Exp Pathol. 2019;100(5–6):320–329. doi:10.1111/iep.1233531828837
   PubMed Web of Science ®Google Scholar
• Mac Sharry J, Shalaby KH, Marchica C, et al. Concomitant exposure to ovalbumin and endotoxin augments airway inflammation but not airway hyperresponsiveness in a murine model of asthma. PLoS One. 2014;9(6):e98648. doi:10.1371/journal.pone.009864824968337
   PubMed Web of Science ®Google Scholar
• Yombo D, Mentik-Kane MM, Wilson MS, Wynn TA, Madala SK. Hsp70 is a positive regulator of airway inflammation and mucus hypersecretion through the increase of type 2 cytokine production by activated T cells in allergic asthma. Am J Respir Crit Care Med. 2019;199:A1053.
   Web of Science ®Google Scholar
• Singleton KD, Wischmeyer PE. Effects of HSP70.1/3 gene knockout on acute respiratory distress syndrome and the inflammatory response following sepsis. Am J Physiol Lung Cell Mol Physiol. 2006;290(5):L956–L961. doi:10.1152/ajplung.00466.200516361353
   PubMed Web of Science ®Google Scholar
• Fujibayashi T, Hashimoto N, Jijiwa M, Hasegawa Y, Kojima T, Ishiguro N. Protective effect of geranylgeranylacetone, an inducer of heat shock protein 70, against drug-induced lung injury/fibrosis in an animal model. BMC Pulm Med. 2009;9:45. doi:10.1186/1471-2466-9-4519758434
   PubMedGoogle Scholar
• Tanaka K, Tanaka Y, Namba T, Azuma A, Mizushima T. Heat shock protein 70 protects against bleomycin-induced pulmonary fibrosis in mice. Biochem Pharmacol. 2010;80(6):920–931. doi:10.1016/j.bcp.2010.05.02520513440
   PubMed Web of Science ®Google Scholar
• Calderwood SK, Theriault J, Gray PJ, Gong J. Cell surface receptors for molecular chaperones. Methods. 2007;43(3):199–206. doi:10.1016/j.ymeth.2007.06.00817920516
   PubMed Web of Science ®Google Scholar
• Basu S, Binder RJ, Ramalingam T, Srivastava PK. CD91 is a common receptor for heat shock proteins gp96, hsp90, hsp70, and calreticulin. Immunity. 2001;14(3):303–313. doi:10.1016/S1074-7613(01)00111-X11290339
   PubMed Web of Science ®Google Scholar
• Fong JJ, Sreedhara K, Deng LW, et al. Immunomodulatory activity of extracellular Hsp70 mediated via paired receptors siglec-5 and siglec-14. EMBO J. 2015;34(22):2775–2788. doi:10.15252/embj.20159140726459514
   PubMed Web of Science ®Google Scholar
• Murshid A, Borges TJ, Bonorino C, Lang BJ, Calderwood SK. Immunological outcomes mediated upon binding of heat shock proteins to scavenger receptors SCARF1 and LOX-1, and endocytosis by mononuclear phagocytes. Front Immunol. 2020;10:3035. doi:10.3389/fimmu.2019.0303531998315
   PubMed Web of Science ®Google Scholar
• Asea A, Rehli M, Kabingu E, et al. Novel signal transduction pathway utilized by extracellular HSP70 - role of toll-like receptor (TLR) 2 AND TLR4. J Biol Chem. 2002;277(17):15028–15034. doi:10.1074/jbc.M20049720011836257
   PubMed Web of Science ®Google Scholar
• Murshid A, Borges TJ, Lang BJ, Calderwood SK. The scavenger receptor SREC-I cooperates with toll-like receptors to trigger inflammatory innate immune responses. Front Immunol. 2016;7:226. doi:10.3389/fimmu.2016.0022627379091
   PubMed Web of Science ®Google Scholar
• Grunwald MS, Ligabue-Braun R, Souza CS, et al. Putative model for heat shock protein 70 complexation with receptor of advanced glycation end products through fluorescence proximity assays and normal mode analyses. Cell Stress Chaperones. 2017;22(1):99–111. doi:10.1007/s12192-016-0746-927858225
   PubMed Web of Science ®Google Scholar
• Oczypok EA, Perkins TN, Oury TD. All the “RAGE” in lung disease: the receptor for advanced glycation endproducts (RAGE) is a major mediator of pulmonary inflammatory responses. Paediatr Respir Rev. 2017;23:40–49. doi:10.1016/j.prrv.2017.03.01228416135
   PubMed Web of Science ®Google Scholar
• Shang LQ, Wang L, Shi XL, et al. HMGB1 was negatively regulated by HSF1 and mediated the TLR4/MyD88/NF-kappa B signal pathway in asthma. Life Sci. 2020;241:117120. doi:10.1016/j.lfs.2019.11712031825792
   PubMed Web of Science ®Google Scholar
• Cappelletti M, Presicce P, Calcaterra F, Mavilio D, Della Bella S. Bright expression of CD91 identifies highly activated human dendritic cells that can be expanded by defensins. Immunology. 2015;144(4):661–667. doi:10.1111/imm.1241825351513
   PubMed Web of Science ®Google Scholar
• Mishra A, Yao XL, Saxena A, et al. Low-density lipoprotein receptor-related protein 1 attenuates house dust mite-induced eosinophilic airway inflammation by suppressing dendritic cell-mediated adaptive immune responses. J Allergy Clin Immunol. 2018;142(4):1066–1079.e6. doi:10.1016/j.jaci.2017.10.04429274414
   PubMed Web of Science ®Google Scholar
• Hadebe S, Brombacher F, Brown GD. C-type lectin receptors in asthma. Front Immunol. 2018;9:733. doi:10.3389/fimmu.2018.0073329696023
   PubMed Web of Science ®Google Scholar
• Patten DA, Shetty S. More than just a removal service: scavenger receptors in leukocyte trafficking. Front Immunol. 2018;9:2904.30631321
   PubMed Web of Science ®Google Scholar
• Chen Z, Bai FF, Han L, et al. Targeting neutrophils in severe asthma via siglec-9. Int Arch Allergy Immunol. 2018;175(1–2):5–15. doi:10.1159/00048487329306942
   PubMed Web of Science ®Google Scholar
• Macauley MS, Crocker PR, Paulson JC. Siglec-mediated regulation of immune cell function in disease. Nat Rev Immunol. 2014;14(10):653–666. doi:10.1038/nri373725234143
   PubMed Web of Science ®Google Scholar
• Schleimer RP, Schnaar RL, Bochner BS. Regulation of airway inflammation by siglec-8 and siglec-9 sialoglycan ligand expression. Curr Opin Allergy Clin Immunol. 2016;16(1):24–30. doi:10.1097/ACI.000000000000023426694037
   PubMed Web of Science ®Google Scholar
• Zakeri A, Russo M. Dual role of toll-like receptors in human and experimental asthma models. Front Immunol. 2018;9:1027. doi:10.3389/fimmu.2018.0102729867994
   PubMed Web of Science ®Google Scholar
• Pooe OJ, Kollisch G, Heine H, Shonhai A. Plasmodium falciparum heat shock protein 70 lacks immune modulatory activity. Protein Pept Lett. 2017;24(6):503–510. doi:10.2174/092986652466617021414190928201964
   PubMed Web of Science ®Google Scholar
• Ferat-Osorio E, Sanchez-Anaya A, Gutierrez-Mendoza M, et al. Heat shock protein 70 down-regulates the production of toll-like receptor-induced pro-inflammatory cytokines by a heat shock factor-1/constitutive heat shock element-binding factor-dependent mechanism. J Inflamm (Lond). 2014;11(1):19. doi:10.1186/1476-9255-11-1925053922
   PubMed Web of Science ®Google Scholar
• Bauer AK, Rondini EA, Hummel KA, et al. Identification of candidate genes downstream of TLR4 signaling after ozone exposure in mice: a role for heat-shock protein 70. Environ Health Perspect. 2011;119(8):1091–1097. doi:10.1289/ehp.100332621543283
   PubMed Web of Science ®Google Scholar
• Gorska MM. Natural killer cells in asthma. Curr Opin Allergy Clin Immunol. 2017;17(1):50–54. doi:10.1097/ACI.000000000000032727841766
   PubMed Web of Science ®Google Scholar
• Farhadi N, Lambert L, Triulzi C, Openshaw PJM, Guerra N, Culley FJ. Natural killer cell NKG2D and granzyme B are critical for allergic pulmonary inflammation. J Allergy Clin Immunol. 2014;133(3):827–835.e3. doi:10.1016/j.jaci.2013.09.04824290277
   PubMed Web of Science ®Google Scholar
• Ray A, Kolls JK. Neutrophilic inflammation in asthma and association with disease severity. Trends Immunol. 2017;38(12):942–954. doi:10.1016/j.it.2017.07.00328784414
   PubMed Web of Science ®Google Scholar
• Lommatzsch M, Julius P, Kuepper M, et al. The course of allergen-induced leukocyte infiltration in human and experimental asthma. J Allergy Clin Immunol. 2006;118(1):91–97. doi:10.1016/j.jaci.2006.02.03416815143
   PubMed Web of Science ®Google Scholar
• Lutfi R, Lewkowich IP, Zhou P, Ledford JR, Page K. The role of protease-activated receptor-2 on pulmonary neutrophils in the innate immune response to cockroach allergen. J Inflamm (Lond). 2012;9(1):32. doi:10.1186/1476-9255-9-3222954301
   PubMed Web of Science ®Google Scholar
• Patel DF, Piero T, Bruno N, et al. Neutrophil restrain allergic airway inflammation by limiting ILC2 function and monocyte-dendritic cell antigen presentation. Sci Immunol. 2019;4(41):eaax7006. doi:10.1126/sciimmunol.aax700631704734
   PubMed Web of Science ®Google Scholar
• Ortega E, Hinchado MD, Martin-Cordero L, Asea A. The effect of stress-inducible extracellular Hsp72 on human neutrophil chemotaxis: a role during acute intense exercise. Stress. 2009;12(3):240–249. doi:10.1080/1025389080230985318850491
   PubMed Web of Science ®Google Scholar
• Assimon VA, Gillies AT, Rauch JN, Gestwicki JE. Hsp70 protein complexes as drug targets. Curr Pharm Des. 2013;19(3):404–417. doi:10.2174/13816121380414369922920901
   PubMed Web of Science ®Google Scholar
• Fan GH, Yang W, Sai J, Richmond A. Hsc/Hsp70 interacting protein (hip) associates with CXCR2 and regulates the receptor signaling and trafficking. J Biol Chem. 2002;277(8):6590–6597. doi:10.1074/jbc.M11058820011751889
   PubMed Web of Science ®Google Scholar
• Ciepiela O, Ostafin M, Demkow U. Neutrophils in asthma–a review. Respir Physiol Neurobiol. 2015;209:13–16. doi:10.1016/j.resp.2014.12.00425511380
   PubMed Web of Science ®Google Scholar
• Dworski R, Simon HU, Hoskins A, Yousefi S. Eosinophil and neutrophil extracellular DNA traps in human allergic asthmatic airways. J Allergy Clin Immunol. 2011;127(5):1260–1266. doi:10.1016/j.jaci.2010.12.110321315435
   PubMed Web of Science ®Google Scholar
• Fox S, Leitch AE, Duffin R, Haslett C, Rossi AG. Neutrophil apoptosis: relevance to the innate immune response and inflammatory disease. J Innate Immun. 2010;2(3):216–227. doi:10.1159/00028436720375550
   PubMed Web of Science ®Google Scholar
• Troyanova NI, Shevchenko MA, Boyko AA, et al. Modulating effect of extracellular HSP70 on generation of reactive oxigen species in populations of phagocytes. Russ J Bioorg Chem. 2015;41(3):271–279. doi:10.1134/S1068162015030097
   Web of Science ®Google Scholar
• Yurinskaya MM, Evgen’ev MB, Antonova OY, Vinokurov MG. Exogenous heat shock protein HSP70 suppresses bacterial pathogen-induced activation of human neutrophils. Dokl Biochem Biophys. 2010;435:316–319. doi:10.1134/S160767291006009821184302
   PubMed Web of Science ®Google Scholar
• Sofoluwe A, Bacchetta M, Badaoui M, Kwak BR, Chanson M. ATP amplifies NADPH-dependent and -independent neutrophil extracellular trap formation. Sci Rep. 2019;9(1):16556. doi:10.1038/s41598-019-53058-931719610
   PubMed Web of Science ®Google Scholar
• Woytschak J, Keller N, Krieg C, et al. Type 2 interleukin-4 receptor signaling in neutrophils antagonizes their expansion and migration during infection and inflammation. Immunity. 2016;45(1):172–184. doi:10.1016/j.immuni.2016.06.02527438770
   PubMed Web of Science ®Google Scholar
• Li Y, Shi XL, Cheng ZY, Li GP, Zhong S, Chen Z. HSP70/CD80 DNA vaccine inhibits airway remodeling by regulating the transcription factors T-bet and GATA-3 in a murine model of chronic asthma. Arch Med Sci. 2013;9(5):906–915. doi:10.5114/aoms.2013.3318024273578
   PubMed Web of Science ®Google Scholar
• Roche PA, Furuta K. The ins and outs of MHC class II-mediated antigen processing and presentation. Nat Rev Immunol. 2015;15(4):203–216. doi:10.1038/nri381825720354
   PubMed Web of Science ®Google Scholar
• Afshar R, Medoff BD, Luster AD. Allergic asthma: a tale of many T cells. Clin Exp Allergy. 2008;38(12):1847–1857. doi:10.1111/j.1365-2222.2008.03119.x19037961
   PubMed Web of Science ®Google Scholar
• Lambrecht BN. Dendritic cells and the regulation of the allergic immune response. Allergy. 2005;60(3):271–282. doi:10.1111/j.1398-9995.2005.00708.x15679711
   PubMed Web of Science ®Google Scholar
• Srivastava P. Roles of heat-shock proteins in innate and adaptive immunity. Nat Rev Immunol. 2002;2(3):185–194. doi:10.1038/nri74911913069
   PubMed Web of Science ®Google Scholar
• Multhoff G. Heat shock protein 70 (Hsp70): membrane location, export and immunological relevance. Methods. 2007;43(3):229–237. doi:10.1016/j.ymeth.2007.06.00617920520
   PubMed Web of Science ®Google Scholar
• Shevtsov M, Multhoff G. Heat shock protein-peptide and HSP-based immunotherapies for the treatment of cancer. Front Immunol. 2016;7:171. doi:10.3389/fimmu.2016.0017127199993
   PubMed Web of Science ®Google Scholar
• Motta A, Schmitz C, Rodrigues L, et al. Mycobacterium tuberculosis heat-shock protein 70 impairs maturation of dendritic cells from bone marrow precursors, induces interleukin-10 production and inhibits T-cell proliferation in vitro. Immunology. 2007;121(4):462–472. doi:10.1111/j.1365-2567.2007.02564.x17346283
   PubMed Web of Science ®Google Scholar
• Rohrer KM, Haug M, Schworer D, Kalbacher H, Holzer U. Mutations in the substrate binding site of human heat-shock protein 70 indicate specific interaction with HLA-DR outside the peptide binding groove. Immunology. 2014;142(2):237–247. doi:10.1111/imm.1224924428437
   PubMed Web of Science ®Google Scholar
• Stocki P, Morris NJ, Preisinger C, et al. Identification of potential HLA class I and class II epitope precursors associated with heat shock protein 70 (HSPA). Cell Stress Chaperones. 2010;15(5):729–741. doi:10.1007/s12192-010-0184-z20358320
   PubMed Web of Science ®Google Scholar
• Berings M, Karaaslan C, Altunbulakli C, et al. Advances and highlights in allergen immunotherapy: on the way to sustained clinical and immunologic tolerance. J Allergy Clin Immunol. 2017;140(5):1250–1267. doi:10.1016/j.jaci.2017.08.02528941667
   PubMed Web of Science ®Google Scholar
• Wambre E, DeLong JH, James EA, et al. Specific immunotherapy modifies allergen-specific CD4(+) T-cell responses in an epitope-dependent manner. J Allergy Clin Immunol. 2014;133(3):872–879.e7. doi:10.1016/j.jaci.2013.10.05424373351
   PubMed Web of Science ®Google Scholar
• Brenu EW, Staines DR, Tajouri L, Huth T, Ashton KJ, Marshall-Gradisnik SM. Heat shock proteins and regulatory T cells. Autoimmune Dis. 2013;2013:813256. doi:10.1155/2013/81325623573417
   PubMedGoogle Scholar
• Wieten L, van der Zee R, Spiering R, et al. A novel heat-shock protein coinducer boosts stress protein Hsp70 to activate T cell regulation of inflammation in autoimmune arthritis. Arthritis Rheum. 2010;62(4):1026–1035. doi:10.1002/art.2734420131272
   PubMed Web of Science ®Google Scholar
• Mantel PY, Kuipers H, Boyman O, et al. GATA3-driven Th2 responses inhibit TGF-beta1-induced FOXP3 expression and the formation of regulatory T cells. PLoS Biol. 2007;5(12):e329. doi:10.1371/journal.pbio.005032918162042
   PubMed Web of Science ®Google Scholar
• Joly AL, Wettstein G, Mignot G, Ghiringhelli F, Garrido C. Dual role of heat shock proteins as regulators of apoptosis and innate immunity. J Innate Immun. 2010;2(3):238–247. doi:10.1159/00029650820375559
   PubMed Web of Science ®Google Scholar
• Kampinga HH, Craig EA. The HSP70 chaperone machinery: J proteins as drivers of functional specificity. Nat Rev Mol Cell Biol. 2010;11(8):579–592. doi:10.1038/nrm294120651708
   PubMed Web of Science ®Google Scholar
• Rosenzweig R, Nillegoda NB, Mayer MP, Bukau B. The Hsp70 chaperone network. Nat Rev Mol Cell Biol. 2019;20(11):665–680. doi:10.1038/s41580-019-0133-331253954
   PubMed Web of Science ®Google Scholar
• Terrab L, Wipf P. Hsp70 and the unfolded protein response as a challenging drug target and an inspiration for probe molecule development. ACS Med Chem Lett. 2020;11(3):232–236. doi:10.1021/acsmedchemlett.9b0058332184949
   PubMed Web of Science ®Google Scholar
• Osorio F, Lambrecht B, Janssens S. The UPR and lung disease. Semin Immunopathol. 2013;35:293–306. doi:10.1007/s00281-013-0368-623536202
   PubMed Web of Science ®Google Scholar
• Miao K, Zhang L, Pan T, Wang Y. Update on the role of endoplasmic reticulum stress in asthma. Am J Transl Res. 2020;12(4):1168–1183.32355534
   PubMed Web of Science ®Google Scholar
• Kim SR, Kim DI, Kang MR, et al. Endoplasmic reticulum stress influences bronchial asthma pathogenesis by modulating nuclear factor κB activation. J Allergy Clin Immunol. 2013;132(6):1397–1408. doi:10.1016/j.jaci.2013.08.04124161747
   PubMed Web of Science ®Google Scholar
• Zeki AA, Yeganeh B, Kenyon NJ, Post M, Ghavami S. Autophagy in airway diseases: a new frontier in human asthma? Allergy. 2016;71(1):5–14. doi:10.1111/all.1276126335713
   PubMed Web of Science ®Google Scholar
• Fernández-Fernández MR, Gragera M, Ochoa-Ibarrola L, Quintana-Gallardo L, Valpuesta JM. Hsp70 - a master regulator in protein degradation. FEBS Lett. 2017;591(17):2648–2660. doi:10.1002/1873-3468.1275128696498
   PubMed Web of Science ®Google Scholar
• Lukaszewicz A, Niechoda A, Zarzecki M, Cwiklinska M, Holownia A. Co-expression of Hsp70 protein and autophagy marker protein LC3 in A549 cells and THP1 cells exposed to nanoparticles of air pollution. Adv Exp Med Biol. 2020;1271:61–68.31925751
   PubMed Web of Science ®Google Scholar
• Ornatowski W, Lu Q, Yegambaram M, et al. Complex interplay between autophagy and oxidative stress in the development of pulmonary disease. Redox Biol. 2020;36:101679. doi:10.1016/j.redox.2020.10167932818797
   PubMed Web of Science ®Google Scholar
• McAlinden KD, Deshpande DA, Ghavami S, et al. Autophagy activation in asthma airways remodeling. Am J Respir Cell Mol Biol. 2019;60(5):541–553. doi:10.1165/rcmb.2018-0169OC30383396
   PubMed Web of Science ®Google Scholar
• Liu JN, Suh DH, Trinh HK, Chwae YJ, Park HS, Shin YS. The role of autophagy in allergic inflammation: a new target for severe asthma. Exp Mol Med. 2016;48(7):e243. doi:10.1038/emm.2016.3827364893
   PubMed Web of Science ®Google Scholar
• Menoret A. Purification of recombinant and endogenous HSP70s. Methods. 2004;32(1):7–12. doi:10.1016/S1046-2023(03)00180-414624870
   PubMed Web of Science ®Google Scholar
• Hurley JH. The sugar kinase/heat shock protein 70/actin super family: implications of conserved structure for mechanism. Annu Rev Biophys Biomol Struct. 1996;25:137–162. doi:10.1146/annurev.bb.25.060196.0010338800467
   PubMedGoogle Scholar
• Vogel M, Bukau B, Mayer MP. Allosteric regulation of Hsp70 chaperones by a proline switch. Mol Cell. 2006;21(3):359–367. doi:10.1016/j.molcel.2005.12.01716455491
   PubMed Web of Science ®Google Scholar
• Theyssen H, Schuster HP, Packschies L, Bukau B, Reinstein J. The second step of ATP binding to DnaK induces peptide release. J Mol Biol. 1996;263(5):657–670. doi:10.1006/jmbi.1996.06068947566
   PubMed Web of Science ®Google Scholar
• Kityk R, Kopp J, Sinning I, Mayer MP. Structure and dynamics of the ATP-bound open conformation of Hsp70 chaperones. Mol Cell. 2012;48(6):863–874. doi:10.1016/j.molcel.2012.09.02323123194
   PubMed Web of Science ®Google Scholar
• Kepp O, Loos F, Liu P, Kroemer G. Extracellular nucleosides and nucleotides as immunomodulators. Immunol Rev. 2017;280(1):83–92. doi:10.1111/imr.1257129027229
   PubMed Web of Science ®Google Scholar
• Willart MA, Lambrecht BN. The danger within: endogenous danger signals, atopy and asthma. Clin Exp Allergy. 2009;39(1):12–19. doi:10.1111/j.1365-2222.2008.03118.x19016800
   PubMed Web of Science ®Google Scholar
• Idzko M, Hammad H, van Nimwegen M, et al. Extracellular ATP triggers and maintains asthmatic airway inflammation by activating dendritic cells. Nat Med. 2007;13(8):913–919. doi:10.1038/nm161717632526
   PubMed Web of Science ®Google Scholar
• Gorini S, Gatta L, Pontecorvo L, Vitiello L, la Sala A. Regulation of innate immunity by extracellular nucleotides. Am J Blood Res. 2013;3(1):14–28.23358447
   PubMedGoogle Scholar
• Yegutkin GG. Nucleotide- and nucleoside-converting ectoenzymes: important modulators of purinergic signalling cascade. Biochim Biophys Acta. 2008;1783(5):673–694. doi:10.1016/j.bbamcr.2008.01.02418302942
   PubMed Web of Science ®Google Scholar
• Zimmermann H, Zebisch M, Strater N. Cellular function and molecular structure of ecto-nucleotidases. Purinergic Signal. 2012;8(3):437–502.22555564
   PubMed Web of Science ®Google Scholar
• Vitiello L, Gorini S, Rosano G, la Sala A. Immunoregulation through extracellular nucleotides. Blood. 2012;120(3):511–518. doi:10.1182/blood-2012-01-40649622661701
   PubMed Web of Science ®Google Scholar
• Bolkhovitina EL, Sapozhnikov AM, Shevchenko MA. Effect of heat shock protein 70 on ATP-induced dendritic cell chemotaxis. Russ J Immunol. 2013;7((16)(2–3)):342–343.
   Google Scholar
• Goloudina AR, Demidov ON, Garrido C. Inhibition of HSP70: a challenging anti-cancer strategy. Cancer Lett. 2012;325(2):117–124. doi:10.1016/j.canlet.2012.06.00322750096
   PubMed Web of Science ®Google Scholar
• Breitenbach M, Simon-Nobbe B. The allergens of Cladosporium herbarum and Alternaria alternata. Chem Immunol. 2002;81:48–72.12102004
   PubMedGoogle Scholar
• Shen HD, Au LC, Lin WL, Liaw SF, Tsai JJ, Han SH. Molecular cloning and expression of a Penicillium citrinum allergen with sequence homology and antigenic crossreactivity to a hsp 70 human heat shock protein. Clin Exp Allergy. 1997;27(6):682–690. doi:10.1111/j.1365-2222.1997.tb01197.x9208190
   PubMed Web of Science ®Google Scholar
• Aki T, Fujikawa A, Wada T, et al. Cloning and expression of cDNA coding for a new allergen from the house dust mite, dermatophagoides farinae: homology with human heat shock cognate proteins in the heat shock protein 70 family. J Biochem. 1994;115(3):435–440. doi:10.1093/oxfordjournals.jbchem.a1243568056755
   PubMed Web of Science ®Google Scholar
• An S, Chen LL, Long CB, et al. Dermatophagoides farinae allergens diversity identification by proteomics. Mol Cell Proteomics. 2013;12(7):1818–1828. doi:10.1074/mcp.M112.02713623481662
   PubMed Web of Science ®Google Scholar
• Liu XY, Yang KY, Wang MQ, et al. High-quality assembly of Dermatophagoides pteronyssinus genome and transcriptome reveals a wide range of novel allergens. J Allergy Clin Immunol. 2018;141(6):2268–2271. doi:10.1016/j.jaci.2017.11.03829305317
   PubMed Web of Science ®Google Scholar
• Cui Y, Yu L, Teng F, et al. Transcriptomic/proteomic identification of allergens in the mite Tyrophagus putrescentiae. Allergy. 2016;71(11):1635–1639. doi:10.1111/all.1299927496383
   PubMed Web of Science ®Google Scholar
• Gruehn S, Suphioglu C, O’Hehir RE, Volkmann D. Molecular cloning and characterization of hazel pollen protein (70 kD) as a luminal binding protein (BiP): a novel cross-reactive plant allergen. Int Arch Allergy Immunol. 2003;131(2):91–100. doi:10.1159/00007092412811017
   PubMed Web of Science ®Google Scholar
• Zhang L, Muradia G, De Vouge MW, Rode H, Vijay HM. An allergenic polypeptide representing a variable region of hsp 70 cloned from a cDNA library of Cladosporium herbarum. Clin Exp Allergy. 1996;26(1):88–95. doi:10.1111/j.1365-2222.1996.tb00060.x8789547
   PubMed Web of Science ®Google Scholar
• Simon-Nobbe B, Denk U, Poll V, Rid R, Breitenbach M. The spectrum of fungal allergy. Int Arch Allergy Immunol. 2008;145(1):58–86. doi:10.1159/00010757817709917
   PubMed Web of Science ®Google Scholar