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Review Article

The Haywain:炎性疾病患者的抗合成酶抗体:针对单核细胞还是中性粒细胞?

卷 27, 期 17, 2020

页: [2863 - 2871] 页: 9

弟呕挨: 10.2174/0929867326666191128141215

价格: $65

Open Access Journals Promotions 2
摘要

抗氨酰基转递核糖核酸（tRNA）合成酶的自身抗生素在患有多种自身免疫性疾病和炎症性疾病的患者中被发现。最近的数据表明，这些抗体是针对拼接变异的合成酶基因，即所谓的催化零。后一种分子具有类似细胞因子的功能，参与调节淋巴细胞、单核细胞和粒细胞的激活。抗合成酶抗体作为诊断工具和治疗干预的目标的潜在作用被讨论。

关键词: 抗合成酶，皮肌炎，多发性肌炎，肺间质性疾病，氨酰基tRNA，炎症性疾病。

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[1]
Fritzler, M.J. Choosing wisely: Review and commentary on anti-nuclear antibody (ANA) testing. Autoimmun. Rev., 2016, 15(3), 272-280.
[http://dx.doi.org/10.1016/j.autrev.2015.12.002] [PMID: 26687321]
[2]
Cooper, G.S.; Stroehla, B.C. The epidemiology of autoimmune diseases. Autoimmun. Rev., 2003, 2(3), 119-125.
[http://dx.doi.org/10.1016/S1568-9972(03)00006-5] [PMID: 12848952]
[3]
Gaubitz, M. Epidemiology of connective tissue disorders. Rheumatology (Oxford), 2006, 45(Suppl. 3), iii3-iii4.
[http://dx.doi.org/10.1093/rheumatology/kel282] [PMID: 16987829]
[4]
Chan, E.K.; Damoiseaux, J.; Carballo, O.G.; Conrad, K.; de Melo Cruvinel, W.; Francescantonio, P.L.; Fritzler, M.J.; Garcia-De La Torre, I.; Herold, M.; Mimori, T.; Satoh, M.; von Mühlen, C.A.; Andrade, L.E. Report of the first international consensus on standardized nomenclature of antinuclear antibody HEp-2 cell patterns 2014-2015. Front. Immunol., 2015, 6, 412.
[http://dx.doi.org/10.3389/fimmu.2015.00412] [PMID: 26347739]
[5]
Selmi, C.; Ceribelli, A.; Generali, E.; Scirè, C.A.; Alborghetti, F.; Colloredo, G.; Porrati, L.; Achenza, M.I.; De Santis, M.; Cavaciocchi, F.; Massarotti, M.; Isailovic, N.; Paleari, V.; Invernizzi, P.; Matthias, T.; Zucchi, A.; Meroni, P.L. Serum antinuclear and extractable nuclear antigen antibody prevalence and associated morbidity and mortality in the general population over 15 years. Autoimmun. Rev., 2016, 15(2), 162-166.
[http://dx.doi.org/10.1016/j.autrev.2015.10.007] [PMID: 26524640]
[6]
Fang, P.; Guo, M. Structural characterization of human aminoacyl-tRNA synthetases for translational and nontranslational functions. Methods, 2017, 113, 83-90.
[http://dx.doi.org/10.1016/j.ymeth.2016.11.014] [PMID: 27887987]
[7]
Nishikai, M.; Reichlin, M. Heterogeneity of precipitating antibodies in polymyositis and dermatomyositis. Characterization of the Jo-1 antibody system. Arthritis Rheum., 1980, 23(8), 881-888.
[http://dx.doi.org/10.1002/art.1780230802] [PMID: 7406938]
[8]
Mathews, M.B.; Reichlin, M.; Hughes, G.R.; Bernstein, R.M. Anti-threonyl-tRNA synthetase, a second myositis-related autoantibody. J. Exp. Med., 1984, 160(2), 420-434.
[http://dx.doi.org/10.1084/jem.160.2.420] [PMID: 6206177]
[9]
Targoff, I.N. Autoantibodies to aminoacyl-transfer RNA synthetases for isoleucine and glycine. Two additional synthetases are antigenic in myositis. J. Immunol., 1990, 144(5), 1737-1743.
[PMID: 2307838]
[10]
Satoh, M.; Tanaka, S.; Ceribelli, A.; Calise, S.J.; Chan, E.K. A comprehensive overview on myositis-specific antibodies: new and old biomarkers in idiopathic inflammatory myopathy. Clin. Rev. Allergy Immunol., 2017, 52(1), 1-19.
[http://dx.doi.org/10.1007/s12016-015-8510-y] [PMID: 26424665]
[11]
Lega, J.C.; Fabien, N.; Reynaud, Q.; Durieu, I.; Durupt, S.; Dutertre, M.; Cordier, J.F.; Cottin, V. The clinical phenotype associated with myositis-specific and associated autoantibodies: a meta-analysis revisiting the so-called antisynthetase syndrome. Autoimmun. Rev., 2014, 13(9), 883-891.
[http://dx.doi.org/10.1016/j.autrev.2014.03.004] [PMID: 24704867]
[12]
Ghirardello, A.; Bassi, N.; Palma, L.; Borella, E.; Domeneghetti, M.; Punzi, L.; Doria, A. Autoantibodies in polymyositis and dermatomyositis. Curr. Rheumatol. Rep., 2013, 15(6), 335.
[http://dx.doi.org/10.1007/s11926-013-0335-1] [PMID: 23591825]
[13]
Hamaguchi, Y.; Fujimoto, M.; Matsushita, T.; Kaji, K.; Komura, K.; Hasegawa, M.; Kodera, M.; Muroi, E.; Fujikawa, K.; Seishima, M.; Yamada, H.; Yamada, R.; Sato, S.; Takehara, K.; Kuwana, M. Common and distinct clinical features in adult patients with anti-aminoacyl-tRNA synthetase antibodies: heterogeneity within the syndrome. PLoS One, 2013, 8(4) e60442
[http://dx.doi.org/10.1371/journal.pone.0060442] [PMID: 23573256]
[14]
Bohan, A.; Peter, J.B. Polymyositis and dermatomyositis (first of two parts). N. Engl. J. Med., 1975, 292(7), 344-347.
[http://dx.doi.org/10.1056/NEJM197502132920706] [PMID: 1090839]
[15]
Bohan, A.; Peter, J.B. Polymyositis and dermatomyositis (second of two parts). N. Engl. J. Med., 1975, 292(8), 403-407.
[http://dx.doi.org/10.1056/NEJM197502202920807] [PMID: 1089199]
[16]
Findlay, A.R.; Goyal, N.A.; Mozaffar, T. An overview of polymyositis and dermatomyositis. Muscle Nerve, 2015, 51(5), 638-656.
[http://dx.doi.org/10.1002/mus.24566] [PMID: 25641317]
[17]
Hozumi, H.; Fujisawa, T.; Nakashima, R.; Johkoh, T.; Sumikawa, H.; Murakami, A.; Enomoto, N.; Inui, N.; Nakamura, Y.; Hosono, Y.; Imura, Y.; Mimori, T.; Suda, T. Comprehensive assessment of myositis-specific autoantibodies in polymyositis/dermatomyositis-associated interstitial lung disease. Respir. Med., 2016, 121, 91-99.
[http://dx.doi.org/10.1016/j.rmed.2016.10.019] [PMID: 27888997]
[18]
Chatterjee, S.; Prayson, R.; Farver, C. Antisynthetase syndrome: not just an inflammatory myopathy. Cleve. Clin. J. Med., 2013, 80(10), 655-666.
[http://dx.doi.org/10.3949/ccjm.80a.12171] [PMID: 24085811]
[19]
Yura, H.; Sakamoto, N.; Satoh, M.; Ishimoto, H.; Hanaka, T.; Ito, C.; Hasegawa, T.; Tanaka, S.; Miyamura, T.; Nakashima, S.; Hara, A.; Kakugawa, T.; Oda, K.; Kido, T.; Obase, Y.; Ishimatsu, Y.; Yatera, K.; Kawakami, A.; Mukae, H. Clinical characteristics of patients with anti-aminoacyl-tRNA synthetase antibody positive idiopathic interstitial pneumonia. Respir. Med., 2017, 132, 189-194.
[http://dx.doi.org/10.1016/j.rmed.2017.10.020] [PMID: 29229096]
[20]
Pinal-Fernandez, I.; Casal-Dominguez, M.; Huapaya, J.A.; Albayda, J.; Paik, J.J.; Johnson, C.; Silhan, L.; Christopher-Stine, L.; Mammen, A.L.; Danoff, S.K. A longitudinal cohort study of the anti-synthetase syndrome: increased severity of interstitial lung disease in black patients and patients with anti-PL7 and anti-PL12 autoantibodies. Rheumatology (Oxford), 2017, 56(6), 999-1007.
[http://dx.doi.org/10.1093/rheumatology/kex021] [PMID: 28339994]
[21]
Saketkoo, L.A.; Mittoo, S.; Frankel, S.; LeSage, D.; Sarver, C.; Phillips, K.; Strand, V.; Matteson, E.L. Reconciling healthcare professional and patient perspectives in the development of disease activity and response criteria in connective tissue disease-related interstitial lung diseases. J. Rheumatol., 2014, 41(4), 792-798.
[http://dx.doi.org/10.3899/jrheum.131251] [PMID: 24488412]
[22]
Debray, M.P.; Borie, R.; Revel, M.P.; Naccache, J.M.; Khalil, A.; Toper, C.; Israel-Biet, D.; Estellat, C.; Brillet, P.Y. Interstitial lung disease in anti-synthetase syndrome: initial and follow-up CT findings. Eur. J. Radiol., 2015, 84(3), 516-523.
[http://dx.doi.org/10.1016/j.ejrad.2014.11.026] [PMID: 25541020]
[23]
Strek, M.E.; Costabel, U. Interstitial pneumonia with autoimmune features: a critical appraisal of the new definition. Curr. Opin. Pulm. Med., 2016, 22(5), 442-449.
[http://dx.doi.org/10.1097/MCP.0000000000000298] [PMID: 27379968]
[24]
Fischer, A.; Antoniou, K.M.; Brown, K.K.; Cadranel, J.; Corte, T.J.; du Bois, R.M.; Lee, J.S.; Leslie, K.O.; Lynch, D.A.; Matteson, E.L.; Mosca, M.; Noth, I.; Richeldi, L.; Strek, M.E.; Swigris, J.J.; Wells, A.U.; West, S.G.; Collard, H.R.; Cottin, V. An official European Respiratory Society/American Thoracic Society research statement: interstitial pneumonia with autoimmune features. Eur. Respir. J., 2015, 46(4), 976-987.
[http://dx.doi.org/10.1183/13993003.00150-2015] [PMID: 26160873]
[25]
Fischer, A.; du Bois, R. Interstitial lung disease in connective tissue disorders. Lancet, 2012, 380(9842), 689-698.
[http://dx.doi.org/10.1016/S0140-6736(12)61079-4] [PMID: 22901890]
[26]
Tzelepis, G.E.; Toya, S.P.; Moutsopoulos, H.M. Occult connective tissue diseases mimicking idiopathic interstitial pneumonias. Eur. Respir. J., 2008, 31(1), 11-20.
[http://dx.doi.org/10.1183/09031936.00060107] [PMID: 18166591]
[27]
Mittoo, S.; Gelber, A.C.; Christopher-Stine, L.; Horton, M.R.; Lechtzin, N.; Danoff, S.K. Ascertainment of collagen vascular disease in patients presenting with interstitial lung disease. Respir. Med., 2009, 103(8), 1152-1158.
[http://dx.doi.org/10.1016/j.rmed.2009.02.009] [PMID: 19304475]
[28]
Castelino, F.V.; Varga, J. Interstitial lung disease in connective tissue diseases: evolving concepts of pathogenesis and management. Arthritis Res. Ther., 2010, 12(4), 213.
[http://dx.doi.org/10.1186/ar3097] [PMID: 20735863]
[29]
Lo, W.S.; Gardiner, E.; Xu, Z.; Lau, C.F.; Wang, F.; Zhou, J.J.; Mendlein, J.D.; Nangle, L.A.; Chiang, K.P.; Yang, X.L.; Au, K.F.; Wong, W.H.; Guo, M.; Zhang, M.; Schimmel, P. Human tRNA synthetase catalytic nulls with diverse functions. Science, 2014, 345(6194), 328-332.
[http://dx.doi.org/10.1126/science.1252943] [PMID: 25035493]
[30]
Zhou, J.J.; Wang, F.; Xu, Z.; Lo, W.S.; Lau, C.F.; Chiang, K.P.; Nangle, L.A.; Ashlock, M.A.; Mendlein, J.D.; Yang, X.L.; Zhang, M.; Schimmel, P. Secreted histidyl-tRNA synthetase splice variants elaborate major epitopes for autoantibodies in inflammatory myositis. J. Biol. Chem., 2014, 289(28), 19269-19275.
[http://dx.doi.org/10.1074/jbc.C114.571026] [PMID: 24898250]
[31]
Schimmel, P. The emerging complexity of the tRNA world: mammalian tRNAs beyond protein synthesis. Nat. Rev. Mol. Cell Biol., 2018, 19(1), 45-58.
[http://dx.doi.org/10.1038/nrm.2017.77] [PMID: 28875994]
[32]
Wakasugi, K.; Schimmel, P. Two distinct cytokines released from a human aminoacyl-tRNA synthetase. Science, 1999, 284(5411), 147-151.
[http://dx.doi.org/10.1126/science.284.5411.147] [PMID: 10102815]
[33]
Howard, O.M.; Dong, H.F.; Yang, D.; Raben, N.; Nagaraju, K.; Rosen, A.; Casciola-Rosen, L.; Härtlein, M.; Kron, M.; Yang, D.; Yiadom, K.; Dwivedi, S.; Plotz, P.H.; Oppenheim, J.J. Histidyl-tRNA synthetase and asparaginyl-tRNA synthetase, autoantigens in myositis, activate chemokine receptors on T lymphocytes and immature dendritic cells. J. Exp. Med., 2002, 196(6), 781-791.
[http://dx.doi.org/10.1084/jem.20020186] [PMID: 12235211]
[34]
Park, S.G.; Schimmel, P.; Kim, S. Aminoacyl tRNA synthetases and their connections to disease. Proc. Natl. Acad. Sci. USA, 2008, 105(32), 11043-11049.
[http://dx.doi.org/10.1073/pnas.0802862105] [PMID: 18682559]
[35]
Sajish, M.; Schimmel, P. A human tRNA synthetase is a potent PARP1-activating effector target for resveratrol. Nature, 2015, 519(7543), 370-373.
[http://dx.doi.org/10.1038/nature14028] [PMID: 25533949]
[36]
Mammen, A.L. Autoimmune myopathies: autoantibodies, phenotypes and pathogenesis. Nat. Rev. Neurol., 2011, 7(6), 343-354.
[http://dx.doi.org/10.1038/nrneurol.2011.63] [PMID: 21654717]
[37]
Mathews, M.B.; Bernstein, R.M. Myositis autoantibody inhibits histidyl-tRNA synthetase: a model for autoimmunity. Nature, 1983, 304(5922), 177-179.
[http://dx.doi.org/10.1038/304177a0] [PMID: 6866113]
[38]
Martin, A.; Shulman, M.J.; Tsui, F.W. Epitope studies indicate that histidyl-tRNA synthetase is a stimulating antigen in idiopathic myositis. FASEB J., 1995, 9(12), 1226-1233.
[http://dx.doi.org/10.1096/fasebj.9.12.7672516] [PMID: 7672516]
[39]
Raben, N.; Nichols, R.; Dohlman, J.; McPhie, P.; Sridhar, V.; Hyde, C.; Leff, R.; Plotz, P. A motif in human histidyl-tRNA synthetase which is shared among several aminoacyl-tRNA synthetases is a coiled-coil that is essential for enzymatic activity and contains the major autoantigenic epitope. J. Biol. Chem., 1994, 269(39), 24277-24283.
[PMID: 7523371]
[40]
Miller, F.W.; Twitty, S.A.; Biswas, T.; Plotz, P.H. Origin and regulation of a disease-specific autoantibody response. Antigenic epitopes, spectrotype stability, and isotype restriction of anti-Jo-1 autoantibodies. J. Clin. Invest., 1990, 85(2), 468-475.
[http://dx.doi.org/10.1172/JCI114461] [PMID: 1688885]
[41]
Xu, Z.; Wei, Z.; Zhou, J.J.; Ye, F.; Lo, W.S.; Wang, F.; Lau, C.F.; Wu, J.; Nangle, L.A.; Chiang, K.P.; Yang, X.L.; Zhang, M.; Schimmel, P. Internally deleted human tRNA synthetase suggests evolutionary pressure for repurposing. Structure, 2012, 20(9), 1470-1477.
[http://dx.doi.org/10.1016/j.str.2012.08.001] [PMID: 22958643]
[42]
Porto, B.N.; Stein, R.T. Neutrophil extracellular traps in pulmonary diseases: too much of a good thing? Front. Immunol., 2016, 7, 311.
[http://dx.doi.org/10.3389/fimmu.2016.00311] [PMID: 27574522]
[43]
Zhang, S.; Shu, X.; Tian, X.; Chen, F.; Lu, X.; Wang, G. Enhanced formation and impaired degradation of neutrophil extracellular traps in dermatomyositis and polymyositis: a potential contributor to interstitial lung disease complications. Clin. Exp. Immunol., 2014, 177(1), 134-141.
[http://dx.doi.org/10.1111/cei.12319] [PMID: 24611519]
[44]
Ascherman, D.P. Role of Jo-1 in the immunopathogenesis of the anti-synthetase syndrome. Curr. Rheumatol. Rep., 2015, 17(9), 56.
[http://dx.doi.org/10.1007/s11926-015-0532-1] [PMID: 26210509]
[45]
Williamson, D.A.; Carter, G.P.; Howden, B.P. Current and emerging topical antibacterials and antiseptics: agents, action, and resistance patterns. Clin. Microbiol. Rev., 2017, 30(3), 827-860.
[http://dx.doi.org/10.1128/CMR.00112-16] [PMID: 28592405]
[46]
Yao, P.; Fox, P.L. Aminoacyl-tRNA synthetases in medicine and disease. EMBO Mol. Med., 2013, 5(3), 332-343.
[http://dx.doi.org/10.1002/emmm.201100626] [PMID: 23427196]
[47]
Saunders, J.; Maki, K.; Koski, R.; Nybo, S.E. Tavaborole, Efinaconazole, and Luliconazole: Three new antimycotic agents for the treatment of dermatophytic fungi. J. Pharm. Pract., 2017, 30(6), 621-630.
[http://dx.doi.org/10.1177/0897190016660487] [PMID: 27488125]
[48]
Luo, Y.; Xie, X.; Luo, D.; Wang, Y.; Gao, Y. The role of halofuginone in fibrosis: more to be explored? J. Leukoc. Biol., 2017, 102(6), 1333-1345.
[http://dx.doi.org/10.1189/jlb.3RU0417-148RR] [PMID: 28986385]
[49]
Shibata, A.; Kuno, M.; Adachi, R.; Sato, Y.; Hattori, H.; Matsuda, A.; Okuzono, Y.; Igaki, K.; Tominari, Y.; Takagi, T.; Yabuki, M.; Okaniwa, M. Discovery and pharmacological characterization of a new class of prolyl-tRNA synthetase inhibitor for anti-fibrosis therapy. PLoS One, 2017, 12(10) e0186587
[http://dx.doi.org/10.1371/journal.pone.0186587] [PMID: 29065190]
[50]
Nangle, L.A.; Tong, Y.; Crampton, S.P.; Adams, R.A.; Chiang, K.P.; Mertsching, E.; Taylor, K.; Ogilvie, K.M.; McKew, J.C.; Ashlock, M.A.; Schimmel, P. The resokine pathway is implicated in the pathology of interstitial lung disease. Am. J. Respir. Crit. Care Med., 2017, 195, A7068.
[51]
Ogilvie, K.M.; Do, M.T.; Chiang, K.P.; Adams, R.A.; Crampton, S.P.; Nangle, L.A.; Cubitt, A.B.; McKew, J.C.; Ashlock, M.A.; Mendlein, J.D. Resokine modulates immune cell infiltration into the lung and provides therapeutic activity in a bleomycin-induced lung fibrosis model. Am. J. Respir. Crit. Care Med., 2017, 195, A6428.
[52]
Evaluation of the safety, tolerability, immunogenicity, pharmacokinetics and pharmacodynamics of intravenous ATYR1923 in healthy volunteers. Australian New Zealand Clinical trials registry, 2019. Available at:. https://www. anzctr.org.au/Trial/Registration/TrialReview.aspx?id=373652 (Accessed Date: November 2, 2019).
[53]
McElvaney, O.J.; Horan, D.; Franciosi, A.N.; Gunaratnam, C.; McElvaney, N.G. Pulmonary alveolar proteinosis. QJM, 2018, 111(3), 185-186.
[http://dx.doi.org/10.1093/qjmed/hcx235] [PMID: 29240908]
[54]
Nishimura, M.; Yamaguchi, E.; Takahashi, A.; Asai, N.; Katsuda, E.; Ohta, T.; Ohtsuka, Y.; Kosaka, K.; Matsubara, A.; Tanaka, H.; Yokoe, N.; Kubo, A.; Konno, S.; Baba, K. Clinical significance of serum anti-GM-CSF autoantibody levels in autoimmune pulmonary alveolar proteinosis. Biomarkers Med., 2018, 12(2), 151-159.
[http://dx.doi.org/10.2217/bmm-2017-0362] [PMID: 29202602]
[55]
The haywain. Museo del Prado. Available at:. http://boschproject.org/#/artworks/The_Haywain_Prado (Accessed Date : October 2019.).

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