Anti-citrullinated protein antibodies as biomarkers in rheumatoid arthritis

References

• Smolen JS, Aletaha D, Barton A, et al. Rheumatoid arthritis. Nat Rev Dis Primers. 2018;8(4):18001. doi: 10.1038/nrdp.2018.1
   Google Scholar
• McInnes IB, Schett G. Pathogenetic insights from the treatment of rheumatoid arthritis. Lancet. 2017;389(10086):2328–2337. doi: 10.1016/S0140-6736(17)31472-1
   PubMed Web of Science ®Google Scholar
• Aletaha D, Neogi T, Silman AJ, et al. 2010 rheumatoid arthritis classification criteria: an American College of Rheumatology/European League against rheumatism collaborative initiative. Ann Rheum Dis. 2010;69(9):1580–1588. doi: 10.1136/ard.2010.138461
   PubMed Web of Science ®Google Scholar
• Toes RE, van der Woude D. ACPA (anti-citrullinated protein antibodies) and rheumatoid arthritis. Acta Reumatol Port. 2011;36(3):205–207.
   PubMed Web of Science ®Google Scholar
• Ärlestig L, Mullazehi M, Kokkonen H, et al. Antibodies against cyclic citrullinated peptides of IgG, IgA and IgM isotype and rheumatoid factor of IgM and IgA isotype are increased in unaffected members of multicase rheumatoid arthritis families from northern Sweden. Ann Rheum Dis. 2012;71(6):825–829. doi: 10.1136/annrheumdis-2011-200668.
   PubMed Web of Science ®Google Scholar
• Bas S, Genevay S, Meyer O, et al. Anti-cyclic citrullinated peptide antibodies, IgM and IgA rheumatoid factors in the diagnosis and prognosis of rheumatoid arthritis. Rheumatology. 2003;42(5):677–680. doi: 10.1093/rheumatology/keg184.
   PubMed Web of Science ®Google Scholar
• Schellekens GA, de Jong BA, van de Putte LB, et al. Citrulline is an essential constituent of antigenic determinants recognized by rheumatoid arthritis-specific autoantibodies. J Clin Investig. 1998;101(1):273–281. doi: 10.1172/JCI1316
   PubMed Web of Science ®Google Scholar
• Girbal-Neuhauser E, Durieux JJ, Arnaud M, et al. The epitopes targeted by the rheumatoid arthritis-associated antifilaggrin autoantibodies are posttranslationally generated on various sites of (pro)filaggrin by deimination of arginine residues.J Immunol. J Immunol. 1999;162(1):585–594. doi: 10.4049/jimmunol.162.1.585
   PubMed Web of Science ®Google Scholar
• Harre U, Georgess D, Bang H, et al. Induction of osteoclastogenesis and bone loss by human autoantibodies against citrullinated vimentin. J Clin Invest. 2012;122(5):1791–1802. doi: 10.1172/JCI60975
   PubMed Web of Science ®Google Scholar
• Kuhn KA, Kulik L, Tomooka B, et al. Antibodies against citrullinated proteins enhance tissue injury in experimental autoimmune arthritis. J Clin Invest. 2006;116(4):961‐973. doi: 10.1172/JCI25422
   PubMed Web of Science ®Google Scholar
• Khandpur R, Carmona-Rivera C, Vivekanandan-Giri A, et al. Nets are a source of citrullinated autoantigens and stimulate inflammatory responses in rheumatoid arthritis. Sci Transl Med. 2013;5(178):178ra40. doi: 10.1126/scitranslmed.3005580
   PubMed Web of Science ®Google Scholar
• Mouterde G, Lukas C, Goupille P, et al. Association of anticyclic citrullinated peptide antibodies and/or rheumatoid factor status and clinical presentation in early arthritis: results from the ESPOIR cohort. J Rheumatol. 2014;41(8):1614–1622. doi: 10.3899/jrheum.130884.
   PubMed Web of Science ®Google Scholar
• Rantapaa-Dahlqvist S, de Jong BA, Berglin E, et al. Antibodies against cyclic citrullinated peptide and IgA rheumatoid factor predict the development of rheumatoid arthritis. Arthritis Rheum. 2003;48(10):2741–2749. doi: 10.1002/art.11223
   PubMedGoogle Scholar
• Janke K, Kiefer C, McGauran N, et al. A systematic comparison of different composite measures (DAS 28, CDAI, SDAI, and Boolean approach) for determining treatment effects on low disease activity and remission in rheumatoid arthritis. BMC Rheumatol. 2022;6(1):82. doi: 10.1186/s41927-022-00314-7
   PubMedGoogle Scholar
• Satis S. New inflammatory marker associated with disease activity in rheumatoid arthritis: the systemic immune-inflammation index. Curr Health Sci J. 2021;47(4):553–557. doi: 10.12865/CHSJ.47.04.11
   PubMedGoogle Scholar
• Giles JT. Extra-articular manifestations and comorbidity in rheumatoid arthritis: potential impact of pre–rheumatoid arthritis prevention. Clin Ther. 2019;41(7):1246–1255. doi: 10.1016/j.clinthera.2019.04.018
   PubMed Web of Science ®Google Scholar
• Ajeganova S, Humphreys JH, Verheul MK, et al. Anticitrullinated protein antibodies and rheumatoid factor are associated with increased mortality but with different causes of death in patients with rheumatoid arthritis: a longitudinal study in three European cohorts. Ann Rheum Dis. 2016;75(11):1924–1932. doi: 10.1136/annrheumdis-2015-208579
   PubMed Web of Science ®Google Scholar
• Stastny P. Mixed lymphocyte cultures in rheumatoid arthritis. J Clin Invest. 1976;57(5):1148–1157. doi: 10.1172/JCI108382
   PubMed Web of Science ®Google Scholar
• Stastny P. Association of the B-Cell alloantigen DRw4 with rheumatoid arthritis. N Engl J Med. 1978;298(16):869–871. doi: 10.1056/NEJM197804202981602.
   PubMed Web of Science ®Google Scholar
• Arleevskaya M, Takha E, Petrov S, et al. Interplay of environmental, individual and genetic factors in rheumatoid arthritis provocation. Int J Mol Sci. 2022;23(15):8140. doi: 10.3390/ijms23158140
   PubMed Web of Science ®Google Scholar
• Tuomi T, Heliovaara M, Palosuo T, et al. Smoking, lung function, and rheumatoid factors. Ann Rheum Dis. 1990;49(10):753–756. doi: 10.1136/ard.49.10.753
   PubMed Web of Science ®Google Scholar
• Suzuki A, Yamada R, Chang X, et al. Functional haplotypes of PADI4, encoding citrullinating enzyme peptidylarginine deiminase 4, are associated with rheumatoid arthritis. Nat Genet. 2003;34(4):395–402. doi: 10.1038/ng1206
   PubMed Web of Science ®Google Scholar
• Song GG, Bae SC, Le YH. Association between vitamin D intake and the risk of rheumatoid arthritis: a meta-analysis. Clin Rheumatol. 2012;31(12):1733–1739. doi: 10.1007/s10067-012-2080-7
   PubMed Web of Science ®Google Scholar
• Begovich AB, Carlton VE, Honigberg LA, et al. A missense single-nucleotide polymorphism in a gene encoding a protein tyrosine phos-phatase (PTPN22) is associated with rheumatoid arthritis. The American Journal Of Human Genetics. 2004;75(2):330–337. doi: 10.1086/422827
   PubMed Web of Science ®Google Scholar
• Hitchon CA, Chandad F, Ferucci ED, et al. Antibodies to porphyromonas gingivalis are associated with anticitrullinated protein antibodies in patients with rheumatoid arthritis and their relatives. J Rheumatol. 2010 Jun;37(6):1105–1112. doi: 10.3899/jrheum.091323
   PubMed Web of Science ®Google Scholar
• Houen G, Trier NH. Epstein-Barr virus and systemic autoimmune diseases. Front Immunol. 2021;11:587380.
   PubMed Web of Science ®Google Scholar
• Budlewski T, Sarnik J, Galita G, et al. SNP in PTPN22, PADI4, and STAT4 but not TRAF1 and CD40 increase the risk of rheumatoid arthritis in polish population. Int J Mol Sci. 2023;24(8):7586. doi: 10.3390/ijms24087586
   PubMed Web of Science ®Google Scholar
• Mouat I, Morse ZJ, Shanina I, et al. Elife. Latent gammaherpesvirus exacerbates arthritis through modification of age-associated B cells. 2021;10:e67024. doi:10.7554/eLife.67024
   Google Scholar
• Rönnelid J, Turesson C, Kastbom A. Autoantibodies in rheumatoid arthritis – laboratory and clinical perspectives. Front Immunol. 2021;12:685312. doi: 10.3389/fimmu.2021.685312
   PubMed Web of Science ®Google Scholar
• Van Hoovels L, Jacobs J, Vander Cruyssen B, et al. Performance characteristics of rheumatoid factor and anti-cyclic citrullinated peptide antibody assays may impact ACR/EULAR classification of rheumatoid arthritis. Ann Rheum Dis. 2018;77(5):667–677. doi: 10.1136/annrheumdis-2017-212365
   PubMed Web of Science ®Google Scholar
• Sebbag M, Simon M, Vincent C, et al. The antiperinuclear factor and the so-called antikeratin antibodies are the same rheumatoid arthritis-specific autoantibodies. J Clin Invest. 1995;95(6):2672–2679. doi: 10.1172/JCI117969
   PubMed Web of Science ®Google Scholar
• Hoet RM, Boerbooms AM, Arends M, et al. Antiperinuclear factor, a marker autoantibody for rheumatoid arthritis: Colocalisation of the perinuclear factor and profilaggrin. Ann Rheum Dis. 1991;50(9):611–618. doi: 10.1136/ard.50.9.611
   PubMed Web of Science ®Google Scholar
• Youinou P, Serre G. The antiperinuclear factor and antikeratin antibody systems. Int Arch Allergy Immunol. 1995;107(4):508–518. doi: 10.1159/000237093
   PubMed Web of Science ®Google Scholar
• Hoober KJ, Eggink LL. The discovery and function of filaggrin. Int J Mol Sci. 2022;23(3):1455. doi: 10.3390/ijms23031455
   PubMed Web of Science ®Google Scholar
• McLean WH. Filaggrin failure – from ichthyosis vulgaris to atopic eczema and beyond. Br J Dermatol. 2016;175 Suppl 2(Suppl Suppl 2):4–7. doi: 10.1111/bjd.14997
   PubMedGoogle Scholar
• Steffen U, Schett G, Bozec A. How autoantibodies regulate osteoclast induced bone loss in rheumatoid arhtiris. Front Immunol. 2019;10:1483. doi: 10.3389/fimmu.2019.01483
   PubMed Web of Science ®Google Scholar
• Clavel C, Nogueira L, Laurent L, et al. Induction of macrophage secretion of tumor necrosis factor alpha through Fcgamma receptor IIa engagement by rheumatoid arthritis-specific autoantibodies to citrullinated proteins complexed with fibrinogen. Arthritis Rheum. 2008;58(3):678–688. doi: 10.1002/art.23284
   PubMed Web of Science ®Google Scholar
• Engdahl C, Bang H, Dietel K, et al. Periarticular bone loss in arthritis is induced by autoantibodies against citrullinated vimentin. J Bone Mineral Res. 2017;32(8):1681‐1691. doi: 10.1002/jbmr.3158.
   PubMed Web of Science ®Google Scholar
• Petkova SB, Konstantinov KN, Sproule TJ, et al. Human antibodies induce arthritis in mice deficient in the low‐affinity inhibitory IgG receptor FcγRIIB. J Exp Med. 2006;203(2):275‐280. doi: 10.1084/jem.20051951
   PubMed Web of Science ®Google Scholar
• Uysal H, Bockermann R, Nandakumar KS, et al. Structure and pathogenicity of antibodies specific for citrullinated collagen type II in experimental arthritis. J Exp Med. 2009;206(2):449–462. doi: 10.1084/jem.20081862
   PubMed Web of Science ®Google Scholar
• Trouw LA, Haisma EM, Levarht EWN, et al. Anti–cyclic citrullinated peptide antibodies from rheumatoid arthritis patients activate complement via both the classical and alternative pathways. Arthritis Rheum. 2009;60(7):1923–1931. doi: 10.1002/art.24622
   PubMed Web of Science ®Google Scholar
• Bemis EA, Norris JM, Seifert J, et al. Complement and its environmental determinants in the progression of human rheumatoid arthritis. Mol Immunol. 2019;112:256–265. doi: 10.1016/j.molimm.2019.05.012
   PubMed Web of Science ®Google Scholar
• Carmona-Rivera C, Carlucci PM, Moore E, et al. Synovial fibroblast-neutrophil interactions promote pathogenic adaptive immunity in rheumatoid arthritis. Sci Immunol. 2017;2(10):eaag3358. doi: 10.1126/sciimmunol.aag3358
   PubMed Web of Science ®Google Scholar
• Chirivi RGS, van Rosmalen JWG, van der Linden M, et al. Therapeutic ACPA inhibits NET formation: a potential therapy for neutrophil-mediated inflammatory diseases. Cell Mol Immunol. 2020;18(6):1528–1544. doi: 10.1038/s41423-020-0381-3
   PubMed Web of Science ®Google Scholar
• He Y, Ge C, Moreno-Giró A, et al. A subset of antibodies targeting citrullinated proteins confers protection from rheumatoid arthritis. Nat Commun. 2023;14(1):691. doi: 10.1038/s41467-023-36257-x.
   PubMed Web of Science ®Google Scholar
• Wigerblad G, Bas DB, Fernades-Cerqueira C, et al. Autoantibodies to citrullinated proteins induce joint pain independent of inflammation via a chemokine-dependent mechanism. Ann Rheum Dis. 2016;75(4):730–738. doi: 10.1136/annrheumdis-2015-208094
   PubMed Web of Science ®Google Scholar
• van Steenbergen HW, Aletaha D, Beaart-van de Voorde LJ, et al. EULAR definition of arthralgia suspicious for progression to rheumatoid arthritis. Ann Rheum Dis. 2017;76(3):491–496. doi: 10.1136/annrheumdis-2016-209846
   PubMed Web of Science ®Google Scholar
• Baka Z, György B, Géher P, et al. Citrullination under physiological and pathological conditions. Jt Bone Spine. 2012;79(5):431–436. doi: 10.1016/j.jbspin.2012.01.008
   PubMed Web of Science ®Google Scholar
• Tarcsa E, Marekov LN, Mei G, et al. Protein unfolding by peptidylarginine deiminase. Substrate specificity and structural relationships of the natural substrates trichohyalin and filaggrin. J Biol Chem. 1996;271(48):30709–30716. doi: 10.1074/jbc.271.48.30709
   PubMed Web of Science ®Google Scholar
• Ordóñez A, Martínez-Martínez I, Corrales FJ, et al. Effect of citrullination on the function and conformation of antithrombin. FEBS J. 2009;276(22):6763–6772. doi: 10.1111/j.1742-4658.2009.07391.x
   PubMed Web of Science ®Google Scholar
• Curran AM, Girgis AA, Jang Y, et al. Citrullination modulates antigen processing and presentation by revealing cryptic epitopes in rheumatoid arthritis. Nat Commun. 2023;14(1):1061. doi: 10.1038/s41467-023-36620-y
   PubMed Web of Science ®Google Scholar
• Fujisaki M, Sugawara K. Properties of peptidylarginine deiminase from the epidermis of newborn rats. J Biochem. 1981 Jan;89(1):257–263. doi: 10.1093/oxfordjournals.jbchem.a133189
   PubMed Web of Science ®Google Scholar
• Foulquier C, Sebbag M, Clavel C, et al. Peptidyl arginine deiminase type 2 (PAD-2) and PAD-4 but not PAD-1, PAD-3 and PAD-6 are expressed in rheumatoid arthritis synovium in close association with tissue inflammation. Arthritis Rheum. 2007;56(11):3541–3553. doi: 10.1002/art.22983
   PubMed Web of Science ®Google Scholar
• Chang X, Xia Y, Pan J, et al. PADI2 is significantly associated with rheumatoid arthritis. PLoS One. 2013;8(12):e81259. doi: 10.1371/journal.pone.0081259
   PubMed Web of Science ®Google Scholar
• Damgaard D, Senolt L, Nielsen CH. Increased levels of peptidylarginine deiminase 2 in synovial fluid from anti-CCP-positive rheumatoid arthritis patients: association with disease activity and inflammatory markers. Rheumatology (Oxford). 2016;55(5):918–927. doi: 10.1093/rheumatology/kev440
   PubMed Web of Science ®Google Scholar
• Spengler J, Lugonja B, Ytterberg AJ, et al. Release of active peptidyl arginine deiminases by neutrophils can explain production of extracellular citrullinated autoantigens in rheumatoid arthritis synovial fluid. Arthritis & Rheumat. 2015;67(12):3135–3145. doi: 10.1002/art.39313
   PubMed Web of Science ®Google Scholar
• Corsiero E, Bombardieri M, Carlotti E, et al. Single cell cloning and recombinant monoclonal antibodies generation from RA synovial B cells reveal frequent targeting of citrullinated histones of NETs. Ann Rheum Dis. 2016;75(10):1866–1875. doi: 10.1136/annrheumdis-2015-208356
   PubMed Web of Science ®Google Scholar
• Matsuo K, Xiang Y, Nakamura H, et al. Identification of novel citrullinated autoantigens of synovium in rheumatoid arthritis using a proteomic approach. Arthritis Res Ther. 2006;8(6):R175. doi: 10.1186/ar2085
   PubMed Web of Science ®Google Scholar
• Baeten D, Peene I, Union A, et al. Specific presence of intracellular citrullinated proteins in rheumatoid arthritis synovium: relevance to antifilaggrin autoantibodies. Arthritis Rheum. 2001;44(10):2255–2262.
   PubMedGoogle Scholar
• Goëb V, Thomas-L’Otellier M, Daveau R, et al. Candidate autoantigens identified by mass spectrometry in early rheumatoid arthritis are chaperones and citrullinated glycolytic enzymes. Arthritis Res Ther. 2009;11(2):R38. doi: 10.1186/ar2644
   PubMed Web of Science ®Google Scholar
• Masson-Bessiere C, Sebbag M, Girbal-Neuhauser E, et al. The major synovial targets of the rheumatoid arthritis-specific antifilaggrin autoantibodies are deiminated forms of the alpha- and beta-chains of fibrin. J Immunol. 2001;166(6):4177–4184. doi: 10.4049/jimmunol.166.6.4177
   PubMed Web of Science ®Google Scholar
• Kinloch A, Tatzer V, Wait R, et al. Identification of citrullinated alpha-enolase as a candidate autoantigen in rheumatoid arthritis. Arthritis Res Ther. 2005;7(6):R1421–R1429. doi: 10.1186/ar1845
   PubMed Web of Science ®Google Scholar
• Vossenaar ER, Despres N, Lapointe E, et al. Rheumatoid arthritis specific anti-Sa antibodies target citrullinated vimentin. Arthritis Res Ther. 2004;6(2):R142–150. doi: 10.1186/ar1149
   PubMed Web of Science ®Google Scholar
• van Beers JJ, Willemze A, Stammen-Vogelzangs J, et al. Anti-citrullinated fibronectin antibodies in rheumatoid arthritis are associated with human leukocyte antigen-DRB1 shared epitope alleles. Arthritis Res Ther. 2012;14(1):R35. doi: 10.1186/ar3744
   PubMed Web of Science ®Google Scholar
• van Beers JJ, Schwarte CM, Stammen-Vogelzangs J, et al. The rheumatoid arthritis synovial fluid citrullinome reveals novel citrullinated epitopes in apolipoprotein E, myeloid nuclear differentiation antigen, and β-actin. Arthritis Rheum. 2013;65(1):69–80. doi: 10.1002/art.37720
   PubMed Web of Science ®Google Scholar
• Ge C, Xu B, Liang B, et al. Structural basis of cross-reactivity of anti-citrullinated protein antibodies. Arthritis & Rheumat. 2019;71(2):210–221. doi: 10.1002/art.40698
   PubMed Web of Science ®Google Scholar
• Pratesi F, Tommasi C, Anzilotti C, et al. Deiminated Epstein-Barr virus nuclear antigen 1 is a target of anti-citrullinated protein antibodies in rheumatoid arthritis. Arthritis Rheum. 2006;54(3):733–741. doi: 10.1002/art.21629
   PubMedGoogle Scholar
• Sebbag M, Moinard N, Auger I, et al. Epitopes of human fibrin recognized by the rheumatoid arthritis-specific autoantibodies to citrullinated proteins. Eur J Immunol. 2006;36(8):2250–2263. doi: 10.1002/eji.200535790
   PubMed Web of Science ®Google Scholar
• Chang X, Zhao Y, Wang Y, et al. Screening citrullinated proteins in synovial tissues of rheumatoid arthritis using 2-dimensional western blotting. J Rheumatol. 2013;40(3):219–227. doi: 10.3899/jrheum.120751
   PubMed Web of Science ®Google Scholar
• Lundberg K, Kinloch A, Fisher BA, et al. Antibodies to citrullinated alpha-enolase peptide 1 are specific for rheumatoid arthritis and cross-react with bacterial enolase. Arthritis Rheum. 2008;58(10):3009–3019. doi: 10.1002/art.23936
   PubMed Web of Science ®Google Scholar
• Pratesi F, Tommasi C, Anzilotti C, et al. Antibodies to a new viral citrullinated peptide, VCP2: fine specificity and correlation with anti-cyclic citrullinated peptide (CCP) and anti-VCP1 antibodies. Clin Exp Immunol. 2011;164(3):337–345. doi: 10.1111/j.1365-2249.2011.04378.x
   PubMed Web of Science ®Google Scholar
• Pratesi F, Dioni I, Tommasi C, et al. Antibodies from patients with rheumatoid arthritis target citrullinated histone 4 contained in neutrophils extracellular traps. Ann Rheum Dis. 2014;73(7):1414–1422. doi: 10.1136/annrheumdis-2012-202765
   PubMed Web of Science ®Google Scholar
• Umeda N, Matsumoto I, Ito I, et al. Anti-citrullinated glucose-6-phosphate isomerase peptide antibodies in patients with rheumatoid arthritis are associated with HLA-DRB1 shared epitope alleles and disease activity. Clin Exp Immunol. 2013;172(1):44–53. doi: 10.1111/cei.12033
   PubMed Web of Science ®Google Scholar
• Chang X, Yamada R, Suzuki A, et al. Citrullination of fibronectin in rheumatoid arthritis synovial tissue. Rheumatology (Oxford). 2005;44(11):1374–1382. doi: 10.1093/rheumatology/kei023
   PubMed Web of Science ®Google Scholar
• Koivula MK, Heliövaara M, Rissanen H, et al. Antibodies binding to citrullinated telopeptides of type I and type II collagens and to mutated citrullinated vimentin synergistically predict the development of seropositive rheumatoid arthritis. Ann Rheum Dis. 2012;71(10):1666–1670. doi: 10.1136/annrheumdis-2011-200848
   PubMed Web of Science ®Google Scholar
• Shoda H, Fujio K, Shibuya M, et al. Detection of autoantibodies to citrullinated BiP in rheumatoid arthritis patients and pro-inflammatory role of citrullinated BiP in collagen-induced arthritis. Arthritis Res Ther. 2011;13(6):R191. doi: 10.1186/ar3520
   PubMed Web of Science ®Google Scholar
• Dam C, Houen G, Trier N. The dependency on neighboring amino acids for reactivity of anti-citrullinated protein antibodies to citrullinated proteins. Scand J Clin Lab Invest. 2016;76(5):417–425. doi: 10.1080/00365513.2016.1200133
   PubMed Web of Science ®Google Scholar
• Trier NH, Holm BE, Slot O, et al. Application of synthetic peptides for detection of anti-citrullinated peptide antibodies. Peptides. 2016;76:87–95. doi: 10.1016/j.peptides.2016.01.005
   PubMed Web of Science ®Google Scholar
• Trier NH, Holm BE, Heiden J, et al. Antibodies to a strain-specific citrullinated Epstein-Barr virus peptide diagnoses rheumatoid arthritis. Sci Rep. 2018;8(1):3684. doi: 10.1038/s41598-018-22058-6
   PubMedGoogle Scholar
• Trier NH, Holm BE, Slot O, et al. Physical characteristics of a citrullinated pro-filaggrin epitope recognized by anti-citrullinated protein antibodies in rheumatoid arthritis sera. PLoS One. 2016;11(12):e0168542. doi: 10.1371/journal.pone.0168542
   PubMed Web of Science ®Google Scholar
• Meng X, Ezzati P, Smolik I, et al. Characterization of autoantigens targeted by anti-citrullinated protein antibodies in vivo: prominent role for epitopes derived from histone 4 proteins. PLoS One. 2016;11(10):e0165501. doi: 10.1371/journal.pone.0165501
   PubMed Web of Science ®Google Scholar
• Verpoort KN, Cheung K, Ioan-Facsinay A, et al. Fine specificity of the anti-citrullinated protein antibody response is influenced by the shared epitope alleles. Arthritis Rheum. 2007;56(12):3949–3952. doi: 10.1002/art.23127
   PubMedGoogle Scholar
• Hermansson M, Artemenko K, Ossipova E, et al. MS analysis of rheumatoid arthritic synovial tissue identifies specific citrullination sites on fibrinogen. Proteomics Clin Appl. 2010;4(5):511–518. doi: 10.1002/prca.200900088
   PubMed Web of Science ®Google Scholar
• Snir O, Widhe M, Hermansson M, et al. Antibodies to several citrullinated antigens are enriched in the joints of rheumatoid arthritis patients. Arthritis Rheum. 2010;62(1):44–52. doi: 10.1002/art.25036
   PubMedGoogle Scholar
• Fanelli I, Rovero P, Hansen PR, et al. Specificity of anti-citrullinated protein antibodies to citrullinated α-enolase peptides as a function of epitope structure and composition. Antibodies (Basel). 2021;10(3):27. doi: 10.3390/antib10030027
   PubMedGoogle Scholar
• Li Q, Li Y, Liang B, et al. Rheumatoid arthritis sera antibodies to citrullinated collagen type II bind to joint cartilage. Arthritis Res Ther. 2022;24(1):257. doi: 10.1186/s13075-022-02945-0
   PubMed Web of Science ®Google Scholar
• Iobagiu C, Magyar A, Nogueira L, et al. The antigen specificity of the rheumatoid arthritis-associated ACPA directed to citrullinated fibrin is very closely restricted. J Autoimmun. 2011;37(4):263–272. doi: 10.1016/j.jaut.2011.07.003
   PubMed Web of Science ®Google Scholar
• Trier N, Dam C, Olsen D, et al. Contribution of peptide backbone to anti-citrullinated peptide antibody reactivity. PLoS One. 2015;10(12):e0144707. doi: 10.1371/journal.pone.0144707
   PubMed Web of Science ®Google Scholar
• Ge C, Tong D, Liang B, et al. Anticitrullinated protein antibodies cause arthritis by cross-reactivity to joint cartilage. JCI Insight. 2017;2(13):e93688. doi: 10.1172/jci.insight.93688
   PubMed Web of Science ®Google Scholar
• Trier N, Leth M, Hansen P, et al. Cross-reactivity of a human IgG1 anticitrullinated fibrinogen monoclonal antibody to a citrullinated profilaggrin peptide. Protein Sci. 2012;21(12):1929–1941. doi: 10.1002/pro.2178
   PubMed Web of Science ®Google Scholar
• Fanelli I, Rovero P, Hansen PR, et al. Reactivity of rheumatoid arthritis-associated citrulline-dependent antibodies to Epstein-Barr virus nuclear antigen1-3. Antibodies (Basel). 2022;11(1):20. doi: 10.3390/antib11010020
   PubMedGoogle Scholar
• Ioan-Facsinay A, el-Bannoudi H, Scherer HU, et al. Anti-cyclic citrullinated peptide antibodies are a collection of anti-citrullinated protein antibodies and contain overlapping and non-overlapping reactivities. Ann Rheum Dis. 2011;70(1):188–193. doi: 10.1136/ard.2010.131102
   PubMed Web of Science ®Google Scholar
• Ge C, Holmdahl R. The structure, specificity and function of anti-citrullinated protein antibodies. Nat Rev Rheumatol. 2019;15(8):503–508. doi: 10.1038/s41584-019-0244-4
   PubMed Web of Science ®Google Scholar
• Kissel T, Ge C, Hafkenscheid L, et al. Surface Ig variable domain glycosylation affects autoantigen binding and acts as threshold for human autoreactive B cell activation. Sci Adv. 2022;8(6):eabm1759. doi: 10.1126/sciadv.abm1759
   PubMed Web of Science ®Google Scholar
• Wagner E, Skoumal M, Bayer PM, et al. Antibody against mutated citrullinated vimentin: a new sensitive marker in the diagnosis of rheumatoid arthritis. Rheumatol Int. 2009;29(11):1315–1321. doi: 10.1007/s00296-009-0854-2
   PubMed Web of Science ®Google Scholar
• Van Steendam K, Tilleman K, De Ceuleneer M, et al. Citrullinated vimentin as an important antigen in immune complexes from synovial fluid of rheumatoid arthritis patients with antibodies against citrullinated proteins. Arthritis Res Ther. 2010;12(4):R132. doi: 10.1186/ar3070
   PubMed Web of Science ®Google Scholar
• Shi J, Knevel R, Suwannalai P, et al. Autoantibodies recognizing carbamylated proteins are present in sera of patients with rheumatoid arthritis and predict joint damage. Proc Natl Acad Sci U S A. 2011;108(42):17372–17377. doi: 10.1073/pnas.1114465108
   PubMed Web of Science ®Google Scholar
• Reed E, Jiang X, Kharlamova N, et al. Antibodies to carbamylated α-enolase epitopes in rheumatoid arthritis also bind citrullinated epitopes and are largely indistinct from anti-citrullinated protein antibodies. Arthritis Res Ther. 2016;18(1):96. doi: 10.1186/s13075-016-1001-6
   PubMedGoogle Scholar
• Sahlström P, Hansson M, Steen J, et al. Different hierarchies of anti-modified protein autoantibody reactivities in rheumatoid arthritis. Arthritis & rheumat. 2020;72(10):1643–1657. doi: 10.1002/art.41385
   PubMed Web of Science ®Google Scholar
• Kissel T, Reijm S, Slot LM, et al. Antibodies and B cells recognising citrullinated proteins display a broad cross-reactivity towards other post-translational modifications. Ann Rheum Dis. 2020;79(4):472–480. doi: 10.1136/annrheumdis-2019-216499
   PubMed Web of Science ®Google Scholar
• Brevet P, Lattard C, Guillou C, et al. Anti-carbamylated fibrinogen antibodies might be associated with a specific rheumatoid phenotype and include a subset recognizing in vivo epitopes of its γ chain one of which is not cross reactive with anti-citrullinated protein antibodies. Front Immunol. 2021;12:733511. doi: 10.3389/fimmu.2021.733511
   PubMed Web of Science ®Google Scholar
• Wang TT. IgG Fc glycosylation in human immunity. Curr Top Microbiol Immunol. 2019;423:63–75.
   PubMed Web of Science ®Google Scholar
• Flevaris K, Kontoravdi C. Immunoglobulin G N-glycan biomarkers for autoimmune diseases: current state and a glycoinformatics perspective. Int J Mol Sci. 2022;23(9):5180. doi: 10.3390/ijms23095180
   PubMed Web of Science ®Google Scholar
• Kissel T, Toes REM, Huizinga TWJ, et al. Glycobiology of rheumatic diseases. Nat Rev Rheumatol. 2023;19(1):28–43. doi: 10.1038/s41584-022-00867-4
   PubMed Web of Science ®Google Scholar
• Maibom-Thomsen SL, Trier NH, Holm B, et al. Immunoglobulin G structure and rheumatoid factor epitopes. PLoS One. 2019;14(6):e0217624. doi: 10.1371/journal.pone.0217624
   PubMed Web of Science ®Google Scholar
• Hafkenscheid L, Bondt A, Scherer HU, et al. Structural analysis of variable domain glycosylation of anti-citrullinated protein antibodies in rheumatoid arthritis reveals the presence of highly sialylated glycans. Mol & Cell Proteomics. 2017;16(2):278–287. doi: 10.1074/mcp.M116.062919
   PubMed Web of Science ®Google Scholar
• Vergroesen RD, Slot LM, Hafkenscheid L, et al. B-cell receptor sequencing of anti-citrullinated protein antibody (ACPA) IgG-expressing B cells indicates a selective advantage for the introduction of N-glycosylation sites during somatic hypermutation. Ann Rheum Dis. 2018;77(6):956–958. doi: 10.1136/annrheumdis-2017-212052
   PubMed Web of Science ®Google Scholar
• Vergroesen RD, Slot LM, van Schaik BDC, et al. N-glycosylation site analysis of citrullinated antigen-specific B-cell receptors indicates alternative selection pathways during autoreactive B-cell development. Front Immunol. 2019;10:2092. doi: 10.3389/fimmu.2019.02092
   PubMed Web of Science ®Google Scholar
• Rombouts Y, Willemze A, van Beers JJ, et al. Extensive glycosylation of ACPA-IgG variable domains modulates binding to citrullinated antigens in rheumatoid arthritis. Ann Rheum Dis. 2016;75(3):578–585. doi: 10.1136/annrheumdis-2014-206598
   PubMed Web of Science ®Google Scholar
• Lloyd KA, Steen J, Amara K, et al. Variable domain N-linked glycosylation and negative surface charge are key features of monoclonal ACPA: implications for B-cell selection. Eur J Immunol. 2018;48(6):1030–1045. doi: 10.1002/eji.201747446
   PubMed Web of Science ®Google Scholar
• Kissel T, van Schie KA, Hafkenscheid L, et al. On the presence of HLA-SE alleles and ACPA-IgG variable domain glycosylation in the phase preceding the development of rheumatoid arthritis. Ann Rheum Dis. 2019;78(12):1616–1620. doi: 10.1136/annrheumdis-2019-215698
   PubMed Web of Science ®Google Scholar
• Lu MC, Hsieh SC, Lai NS, et al. Comparison of anti-agalactosyl IgG antibodies, rheumatoid factors, and anti-cyclic citrullinated peptide antibodies in the differential diagnosis of rheumatoid arthritis and its mimics. Clin Exp Rheumatol. 2007;25(5):716–721.
   PubMed Web of Science ®Google Scholar
• Ryu HJ, Takeuchi F, Kuwata S, et al. The diagnostic utilities of anti-agalactosyl IgG antibodies, anti-cyclic citrullinated peptide antibodies, and rheumatoid factors in rheumatoid arthritis. Rheumatol Int. 2011;31(3):315–319. doi: 10.1007/s00296-009-1260-5
   PubMed Web of Science ®Google Scholar
• Kaneko C, Kobayashi T, Ito S, et al. Association among periodontitis severity, anti-agalactosyl immunoglobulin G titer, and the disease activity of rheumatoid arthritis. J Periodontal Res. 2021;56(4):702–709. doi: 10.1111/jre.12867
   PubMed Web of Science ®Google Scholar
• Hayem G, ChazerainP P, Combe B, et al. Anti-Sa antibody is an accurate diagnostic and prognostic marker in adult rheumatoid arthritis. J Rheumatol. 1999;26(1):7–13.
   PubMed Web of Science ®Google Scholar
• Schellekens GA, Visser H, de Jong BA, et al. The diagnostic properties of rheumatoid arthritis antibodies recognizing a cyclic citrullinated peptide. Arthritis Rheum. 2000;43(1):155–163. doi: 10.1002/1529-0131(200001)43:1<155:AID-ANR20>3.0.CO;2-3
   PubMed Web of Science ®Google Scholar
• Nishimura K, Sugiyama D, Kogata Y, et al. Meta-analysis: diagnostic accuracy of anti-cyclic citrullinated peptide antibody and rheumatoid factor for rheumatoid arthritis. Ann Intern Med. 2007;146(11):797–808. doi: 10.7326/0003-4819-146-11-200706050-00008
   PubMed Web of Science ®Google Scholar
• Szekanecz Z, Szabo Z, Zeher M, et al. Superior performance of the CCP3.1 test compared to CCP2 and MCV in the rheumatoid factor-negative RA population. Immunol Res. 2013;56(2–3):439–443. doi: 10.1007/s12026-013-8425-8
   PubMed Web of Science ®Google Scholar
• Trier NH, Holm BE, Heiden J, et al. The use of synthetic peptides for detection of anti-citrullinated protein antibodies in rheumatoid arthritis. J Immunol Methods. 2018;454:6–14. doi: 10.1016/j.jim.2017.11.004
   PubMed Web of Science ®Google Scholar
• van Heemst J, Trouw LA, Nogueira L, et al. An investigation of the added value of an ACPA multiplex assay in an early rheumatoid arthritis setting. Arthritis Res Ther. 2015;17:276. doi: 10.1186/s13075-015-0786-z
   PubMed Web of Science ®Google Scholar
• Nicaise-Roland P, Nogueira L, Demattei C, et al. Antibodies to citrullinated fibrinogen compared with anti-MCV and anti-CCP2 antibodies in diagnosing rheumatoid arthritis at an early stage: data from the French ESPOIR cohort. Ann Rheum Dis. 2013;72(3):357–362. doi: 10.1136/annrheumdis-2011-201056
   PubMed Web of Science ®Google Scholar
• Demoruelle MK, Parish MC, Derber LA, et al. Performance of anti‐cyclic citrullinated peptide assays differs in subjects at increased risk of rheumatoid arthritis and subjects with established disease. Arthritis Rheum. 2013;65(9):2243‐2252. doi: 10.1002/art.38017
   Google Scholar
• Pruijn GJ, Wiik A, Van Venrooij WJ. The use of citrullinated peptides and proteins for the diagnosis of rheumatoid arthritis. Arthritis Res Ther. 2010;12(1):203. doi: 10.1186/ar2903
   PubMed Web of Science ®Google Scholar
• Van Gaalen FA, Linn‐Rasker SP, Van Venrooij WJ, et al. Autoantibodies to cyclic citrullinated peptides predict progression to rheumatoid arthritis in patients with undifferentiated arthritis: a prospective cohort study. Arthritis Rheum. 2004;50(3):709‐715. doi: 10.1002/art.20044
   Google Scholar
• Saigal R, Bhakal SS, Goyal L, et al. Seroprevalence of anti-citrullinated protein antibodies (ACPA) in patients with rheumatic diseases other than rheumatoid arthritis. J Assoc Physicians India. 2018;66(4):26–28.
   Google Scholar
• Heidari B, Firouzjahi A, Heidari P, et al. The prevalence and diagnostic performance of anti-cyclic citrullinated peptide antibody in rheumatoid arthritis: the predictive and discriminative ability of serum antibody level in recognizing rheumatoid arthritis. Ann Saudi Med. 2009;29(6):467–470. doi: 10.4103/0256-4947.57170
   PubMed Web of Science ®Google Scholar
• Van de Stadt L, de Koning M, van de Stadt R, et al. Development of the anti-citrullinated protein antibody repertoire prior to the onset of rheumatoid arthritis. Arthritis Rheum. 2011;63(11):3226–3233. doi: 10.1002/art.30537
   PubMedGoogle Scholar
• Ioan-Facsinay A, Willemze A, Robinson DB, et al. Marked differences in fine specificity and isotype usage of the anti-citrullinated protein antibody in health and disease. Arthritis Rheum. 2008;58(10):3000–3008. doi: 10.1002/art.23763
   PubMedGoogle Scholar
• Goldbach-Mansky R, Lee J, McCoy A, et al. Rheumatoid arthritis associated autoantibodies in patients with synovitis of recent onset. Arthritis Res Ther. 2000;2(3):236–243. doi: 10.1186/ar93
   Google Scholar
• Soós L, Szekanecz Z, Szabó Z, et al. Clinical evaluation of anti-mutated citrullinated vimentin by ELISA in rheumatoid arthritis. J Rheumatol. 2007;34(8):1658–1663.
   PubMed Web of Science ®Google Scholar
• Aggarwal R, Liao K, Nair, et al. Anti-citrullinated peptide antibody assays and their role in the diagnosis of rheumatoid arthritis. Arthritis Rheum. 2009;61(11):1472–1483. doi: 10.1002/art.24827
   PubMedGoogle Scholar
• Li Y, Zhang R, Han Y, et al. Proficiency testing for the detection of anti-citrullinated protein antibody in China. Clin Chim Acta. 2015;450:67–71. doi: 10.1016/j.cca.2015.07.020
   PubMed Web of Science ®Google Scholar
• Deng X, Zeng M, Wang X, et al. Preparation and characterization of cyclic citrullinated peptide-immobilized latex beads for measurement of anti-citrullinated protein antibody through latex particle-enhanced turbidimetric immunoassay. J Chromatogr A. 2021;12(1642):462000. doi: 10.1016/j.chroma.2021.462000
   Google Scholar
• Verpoort KN, Jol-van der Zijde CM, Papendrecht-van der Voort EM, et al. Isotype distribution of anti-cyclic citrullinated peptide antibodies in undifferentiated arthritis and rheumatoid arthritis reflects an ongoing immune response. Arthritis Rheum. 2006;54(12):3799–3808. doi: 10.1002/art.22279
   PubMedGoogle Scholar
• Willemze A, Böhringer S, Knevel R, et al. The ACPA recognition profile and subgrouping of ACPA-positive RA patients. Ann Rheum Dis. 2012;71(2):268–274. doi: 10.1136/annrheumdis-2011-200421
   PubMed Web of Science ®Google Scholar
• Sieghart D, Platzer A, Studenic P, et al. Determination of autoantibody isotypes increases the sensitivity of serodiagnostics in rheumatoid arthritis. Front Immunol. 2018;9:876. doi: 10.3389/fimmu.2018.00876
   PubMed Web of Science ®Google Scholar
• Suwannalai P, Willemze A, van Toorn L, et al. The fine specificity of IgM anti-citrullinated protein antibodies (ACPA) is different from that of IgG ACPA. Arthritis Res Ther. 2011;3(6):R195. doi: 10.1186/ar3524
   Google Scholar
• Padyukov L, Seielstad M, Ong RTH, et al. A genome-wide association study suggests contrasting associations in ACPA-positive versus ACPA-negative rheumatoid arthritis. Annals Of The Rheumatic Diseases query. 2011 Feb;70(2):259–265. doi: 10.1136/ard.2009.126821
   PubMed Web of Science ®Google Scholar
• López-Longo FJ, Oliver-Mi-Arro D, de la Torre I, et al. Association between anti-cyclic citrullinated peptide antibodies and ischemic heart disease in patients with rheumatoid arthritis. Arthritis Rheum. 2009;61(4):419–424. doi: 10.1002/art.24390
   PubMedGoogle Scholar
• Grosse J, Allado E, Roux C, et al. ACPA-positive versus ACPA-negative rheumatoid arthritis: two distinct erosive disease entities on radiography and ultrasonography. Rheumatol Int. 2020;40(4):615–624. doi: 10.1007/s00296-019-04492-5
   PubMed Web of Science ®Google Scholar
• Van der Helm-van Mil AHM, Huizinga TWJ. Advances in the genetics of rheumatoid arthritis point to subclassification into distinct disease subsets. Arthritis Res Ther. 2008;10(2):205. doi: 10.1186/ar2384
   PubMed Web of Science ®Google Scholar
• Nielen MM, van Schaardenburg D, Reesink HW, et al. Specific autoantibodies precede the symptoms of rheumatoid arthritis: a study of serial measurements in blood donors. Arthritis Rheum. 2004;50(2):380–386. doi: 10.1002/art.20018
   PubMed Web of Science ®Google Scholar
• Saraux A, Berthelot J, Devauchelle V, et al. Value of antibodies to citrulline-containing peptides for diagnosing early rheumatoid arthritis. J Rheumatol. 2003;30(12):2535–2539.
   PubMed Web of Science ®Google Scholar
• Vencovsky J, Machacek S, Sedova L, et al. Autoantibodies can be prognostic markers of an erosive disease in early rheumatoid arthritis. Ann Rheum Dis. 2003;62(5):427–430. doi: 10.1136/ard.62.5.427
   PubMed Web of Science ®Google Scholar
• Rönnelid J, Wick MC, Lampa J, et al. Longitudinal analysis of citrullinated protein/peptide antibodies (anti-CP) during 5 year follow up in early rheumatoid arthritis: anti-CP status predicts worse disease activity and greater radiological progression. Ann Rheum Dis. 2005;64(12):1744–1749. doi: 10.1136/ard.2004.033571
   PubMed Web of Science ®Google Scholar
• Krishnamurthy A, Joshua V, Haj Hensvold A, et al. Identification of a novel chemokine‐dependent molecular mechanism underlying rheumatoid arthritis‐associated autoantibody‐mediated bone loss. Ann Rheum Dis. 2016;75(4):721‐729. doi: 10.1136/annrheumdis-2015-208093
   Web of Science ®Google Scholar
• van den Broek M, Dirven L, Klarenbeek NB, et al. The association of treatment response and joint damage with ACPA-status in recent-onset RA: a subanalysis of the 8- year follow-up of the BeSt study. Ann Rheum Dis. 2012;71(2):245–248. doi: 10.1136/annrheumdis-2011-200379
   PubMed Web of Science ®Google Scholar
• Szodoray P, Szabó Z, Kapitány A, et al. Anti-citrullinated protein/peptide autoantibodies in association with genetic and environmental factors as indicators of disease outcome in rheumatoid arthritis. Autoimmun Rev. 2010;9(3):140–143. doi: 10.1016/j.autrev.2009.04.006.
   PubMed Web of Science ®Google Scholar
• Seegobin SD, Ma MHY, Dahanayake C, et al. ACPA-positive and ACPA-negative rheumatoid arthritis differ in their requirements for combination DMARDs and corticosteroids: secondary analysis of a randomized controlled trial. Arthritis Res Ther. 2014;16:R13.
   PubMed Web of Science ®Google Scholar
• Tyker A, Ventura IB, Lee CT, et al. High-titer rheumatoid factor seropositivity predicts mediastinal lymphadenopathy and mortality in rheumatoid arthritis-related interstitial lung disease. Sci Rep. 2021;11(1):22821. doi: 10.1038/s41598-021-02066-9
   PubMed Web of Science ®Google Scholar
• Berglin E, Johansson T, Sundin U, et al. Radiological outcome in rheumatoid arthritis is predicted by presence of antibodies against cyclic citrullinated peptide before and at disease onset, and by IgA-RF at disease onset. Ann Rheum Dis. 2006;65(4):453–458. doi: 10.1136/ard.2005.041376
   PubMed Web of Science ®Google Scholar
• Meyer O, Labarre C, Dougados M, et al. Anticitrullinated protein/peptide antibody assays in early rheumatoid arthritis for predicting five year radiographic damage. Ann Rheum Dis. 2003;62(2):120–126. doi: 10.1136/ard.62.2.120
   PubMed Web of Science ®Google Scholar
• Westerlind H, Kastbom A, Rönnelid J, et al. The association between autoantibodies and risk for venous thromboembolic events among patients with rheumatoid arthritis. Rheumatology (Oxford). 2022;62(6):e204–e204. doi: 10.1093/rheumatology/keac649
   Web of Science ®Google Scholar
• van Beers JJ, Willemze A, Jansen JJ, et al. ACPA fine-specificity profiles in early rheumatoid arthritis patients do not correlate with clinical features at baseline or with disease progression. Arthritis Res Ther. 2013;15:R140. doi: 10.1186/ar4322
   PubMed Web of Science ®Google Scholar
• Rombouts Y, Ewing E, van de Stadt LA, et al. Anti-citrullinated protein antibodies acquire a pro-inflammatory Fc glycosylation phenotype prior to the onset of rheumatoid arthritis. Ann Rheum Dis. 2015;74(1):234–241. doi: 10.1136/annrheumdis-2013-203565
   PubMed Web of Science ®Google Scholar
• Hafkenscheid L, de Moel E, Smolik I, et al. N-Linked glycans in the variable domain of IgG anti-citrullinated protein antibodies predict the development of rheumatoid arthritis. Arthritis & Rheumat. 2019;71(10):1626–1633. doi: 10.1002/art.40920
   PubMed Web of Science ®Google Scholar
• Sakkas LI, Bogdanos DP, Katsiari C, et al. Anti-citrullinated peptides as autoantigens in rheumatoid arthritis-relevance to treatment. Autoimmun Rev. 2014;13(11):1114–1120. doi: 10.1016/j.autrev.2014.08.012
   PubMed Web of Science ®Google Scholar
• Endo Y, Koga T, Kawashiri SY, et al. Anti-citrullinated protein antibody titre as a predictor of abatacept treatment persistence in patients with rheumatoid arthritis: a prospective cohort study in Japan. Scand J Rheumatol. 2020;49(1):13–17. doi: 10.1080/03009742.2019.1627411
   PubMed Web of Science ®Google Scholar
• Smolen JS, Landewé R, Bijlsma J, et al. EULAR recommendations for the management of rheumatoid arthritis with synthetic and biological disease-modifying antirheumatic drugs: 2016 update. Ann Rheum Dis. 2017;76(6):960–977. doi: 10.1136/annrheumdis-2016-210715
   PubMed Web of Science ®Google Scholar
• Fraenkel L, Bathon JM, England BR, et al. American College of Rheumatology guideline for the treatment of rheumatoid arthritis. Arthritis & Rheumat. 2021;73(7):1108–1123. doi: 10.1002/art.41752.
   PubMed Web of Science ®Google Scholar
• Slaughter L, Carson DA, Jensen FC, et al. In vitro effects of Epstein-Barr virus on peripheral blood mononuclear cells from patients with rheumatoid arthritis and normal subjects. J Exp Med. 1978;148(5):1429–1434. doi: 10.1084/jem.148.5.1429
   PubMed Web of Science ®Google Scholar
• Johnson PM, Faulk WP. Rheumatoid factor: its nature, specificity, and production in rheumatoid arthritis. Clin Immunol Immunopathol. 1976;6(3):414–430. doi: 10.1016/0090-1229(76)90094-5
   PubMedGoogle Scholar
• Mageed RA, Børretzen M, Moyes SP, et al. Rheumatoid factor autoantibodies in health and disease. Ann N Y Acad Sci. 1997;815(1 B–Lymphocytes):296–311. doi: 10.1111/j.1749-6632.1997.tb52071.x
   PubMedGoogle Scholar
• Gioud-Paquet M, Auvinet M, Raffin T, et al. IgM rheumatoid factor (RF), IgA RF, IgE RF, and IgG RF detected by ELISA in rheumatoid arthritis. Ann Rheum Dis. 1987;46(1):65–71. doi: 10.1136/ard.46.1.65
   PubMed Web of Science ®Google Scholar
• Schmerling RH, Delbanco TL. How useful is the rheumatoid factor? An analysis of sensitivity, specificity, and predictive value. Arch Intern Med. 1992;152(12):2417–2420. doi: 10.1001/archinte.1992.00400240041006
   PubMedGoogle Scholar
• Kallerup HE, Egeskjold EM, Graudal H. IgG-, IgM- and IgA-rheumatoid factors in healthy adults and rheumatoid patients determined by an indirect immunofluorescence method. Scand J Rheumatol. 1979;8(1):1–9. doi: 10.1080/03009747909105327
   PubMed Web of Science ®Google Scholar
• Scott DL, Smith C, Kingsley G. Joint damage and disability in rheumatoid arthritis: an updated systematic review. Clin Exp Rheumatol. 2003;21(5 Suppl 31):S20–27.
   PubMed Web of Science ®Google Scholar
• Aho K, Heliövaara M, Maatela J, et al. Rheumatoid factors antedating clinical rheumatoid arthritis. J Rheumatol. 1991;18(9):1282–1284.
   PubMed Web of Science ®Google Scholar
• Alessandri C, Bombardieri M, Papa N, et al. Decrease of anti-cyclic citrullinated peptide antibodies and rheumatoid factor following anti-TNFalpha therapy (infliximab) in rheumatoid arthritis is associated with clinical improvement. Ann Rheum Dis. 2004;63(10):1218–1221. doi: 10.1136/ard.2003.014647
   PubMed Web of Science ®Google Scholar
• Mikuls TR, O’Dell JR, Stoner JA, et al. Association of rheumatoid arthritis treatment response and disease duration with declines in serum levels of IgM rheumatoid factor and anti-cyclic citrullinated peptide antibody. Arthritis Rheum. 2004;50(12):3776–3782. doi: 10.1002/art.20659
   PubMedGoogle Scholar
• De Rycke L, Verhelst X, Kruithof E, et al. Rheumatoid factor, but not anti-cyclic citrullinated peptide antibodies, is modulated by infliximab treatment in rheumatoid arthritis. Ann Rheum Dis. 2005;64(2):299–302. doi: 10.1136/ard.2004.023523
   PubMed Web of Science ®Google Scholar
• Bobbio-Pallavicini F, Alpini C, Caporali R, et al. Autoantibody profile in rheumatoid arthritis during long-term infliximab treatment. Arthritis Res Ther. 2004;6(3):R264–272. doi: 10.1186/ar1173
   PubMed Web of Science ®Google Scholar
• Bobbio-Pallavicini F, Caporali R, Alpini C, et al. High IgA rheumatoid factor levels are associated with poor clinical response to tumour necrosis factor alpha inhibitors in rheumatoid arthritis. Ann Rheum Dis. 2007;66(3):302–307. doi: 10.1136/ard.2006.060608
   PubMed Web of Science ®Google Scholar
• Chen HA, Lin KC, Chen CH, et al. The effect of etanercept on anti-cyclic citrullinated peptide antibodies and rheumatoid factor in patients with rheumatoid arthritis. Ann Rheum Dis. 2006;65(1):35–39. doi: 10.1136/ard.2005.038851
   PubMed Web of Science ®Google Scholar
• van Tuyl LH, Lems WF, Kerstens PJ, et al. IgM-rheumatoid factor and anti-cyclic citrullinated peptide decrease by 50% during intensive treatment in early rheumatoid arthritis. Ann Rheum Dis. 2009;68(10):1652–1653. doi: 10.1136/ard.2008.103184
   PubMed Web of Science ®Google Scholar
• Vis M, Bos WH, Wolbink G, et al. IgM-rheumatoid factor, anti-cyclic citrullinated peptide, and anti-citrullinated human fibrinogen antibodies decrease during treatment with the tumor necrosis factor blocker infliximab in patients with rheumatoid arthritis. J Rheumatol. 2008;35(3):425–428.
   PubMed Web of Science ®Google Scholar
• Bos WH, Bartelds GM, Vis M, et al. Preferential decrease in IgG4 anti-citrullinated protein antibodies during treatment with tumour necrosis factor blocking agents in patients with rheumatoid arthritis. Ann Rheum Dis. 2009;68(4):558–563. doi: 10.1136/ard.2008.088401
   PubMed Web of Science ®Google Scholar
• Iannone F, Tampoia M, Giannini M, et al. Changes in anti-cyclic citrullinated peptide antibodies and rheumatoid factor isotypes serum levels in patients with rheumatoid arthritis following treatment with different biological drugs. Clin Exp Rheumatol. 2016;34(3):424–429.
   PubMed Web of Science ®Google Scholar
• Takeuchi T, Miyasaka N, Inui T, et al. High titers of both rheumatoid factor and anti-CCP antibodies at baseline in patients with rheumatoid arthritis are associated with increased circulating baseline TNF level, low drug levels, and reduced clinical responses: a post hoc analysis of the RISING study. Arthritis Res Ther. 2017;19(1):194.
   PubMedGoogle Scholar
• Engelmann R, Nekarda S, Kuthning D, et al. Decreased IgG4 ACPA levels in responders and increased CD1c+ classical dendritic cells in non-responders of patients with rheumatoid arthritis under therapy. Clin Rheumatol. 2018;37(7):1783–1790. doi: 10.1007/s10067-018-4053-y
   PubMed Web of Science ®Google Scholar
• Noguchi A, Yasuda S, Hisada R, et al. Anti-cyclic citrullinated peptide antibody titers decrease in rheumatoid arthritis patients treated with tocilizumab: a pilot study. Mod Rheumatol. 2020;30(2):276–281. doi: 10.1080/14397595.2019.1583784
   PubMed Web of Science ®Google Scholar
• Berzofsky JA, Cease KB, Cornette JL, et al. Protein antigenic structures recognized by T cells: potential applications to vaccine design. Immunol Rev. 1987;98(1):9–52. doi: 10.1111/j.1600-065X.1987.tb00518.x
   PubMedGoogle Scholar
• Sokolove J, Johnson DS, Lahey LJ, et al. Rheumatoid factor as a potentiator of anti-citrullinated protein antibody mediated inflammation in rheumatoid arthritis. Arthritis & rheumat. 2014;66(4):813–821. doi: 10.1002/art.38307
   PubMed Web of Science ®Google Scholar
• Derksen VF, Ajeganova S, Trouw LA, et al. Rheumatoid arthritis phenotype at presentation differs depending on the number of autoantibodies present. Ann Rheum Dis. 2017;76(4):716–720. doi: 10.1136/annrheumdis-2016-209794
   PubMed Web of Science ®Google Scholar
• Whittingham SF, Stockman A, Rowley MJ. Collagen autoantibodies and their relationship to CCP antibodies and rheumatoid factor in the progression of early rheumatoid arthritis. Antibodies (Basel). 2017;6(2):6. doi: 10.3390/antib6020006
   PubMedGoogle Scholar
• Berzofsky JA, Brett SJ, Streicher HZ, et al. Antigen processing for presentation to T lymphocytes: function, mechanisms, and implications for the T-cell repertoire. Immunol Rev. 1988;106(1):5–31. doi: 10.1111/j.1600-065X.1988.tb00771.x
   PubMedGoogle Scholar
• Auger I, Sebbag M, Vincent C, et al. Influence of HLA-DR genes on the production of rheumatoid arthritis-specific autoantibodies to citrullinated fibrinogen. Arthritis Rheum. 2005;52(11):3424–3432. doi: 10.1002/art.21391
   PubMedGoogle Scholar
• Feitsma AL, van der Voort EI, Franken KL, et al. Identification of citrullinated vimentin peptides as T cell epitopes in HLA-DR4-positive patients with rheumatoid arthritis. Arthritis Rheum. 2010;62(1):117–125. doi: 10.1002/art.25059
   PubMedGoogle Scholar
• von Delwig A, Locke J, Robinson JH, et al. Response of Th17 cells to a citrullinated arthritogenic aggrecan peptide in patients with rheumatoid arthritis. Arthritis Rheum. 2010;62(1):143–149. doi: 10.1002/art.25064
   PubMed Web of Science ®Google Scholar
• Law SC, Street S, Yu CH, et al. T-cell autoreactivity to citrullinated autoantigenic peptides in rheumatoid arthritis patients carrying HLA-DRB1 shared epitope alleles. Arthritis Res Ther. 2012;14(3):R118. doi: 10.1186/ar3848
   PubMed Web of Science ®Google Scholar
• Aggarwal A, Srivastava R, Agrawal S. T cell responses to citrullinated self-peptides in patients with rheumatoid arthritis. Rheumatol Int. 2013;33(9):2359–2363. doi: 10.1007/s00296-013-2731-2
   PubMed Web of Science ®Google Scholar
• Chemin K, Pollastro S, James E, et al. A novel HLA-DRB1*10: 01-restricted T cell epitope from citrullinated type II collagen relevant to rheumatoid arthritis. Arthritis & rheumat. 2016;68(5):1124–1135. doi: 10.1002/art.39553
   PubMed Web of Science ®Google Scholar
• Chen J, Song S, Liu Y, et al. Autoreactive T cells to citrullinated HSP90 are associated with interstitial lung disease in rheumatoid arthritis. Int J Rheum Dis. 2018;21(7):1398–1405. doi: 10.1111/1756-185X.13316
   PubMed Web of Science ®Google Scholar
• Pieper J, Dubnovitsky A, Gerstner C, et al. Memory T cells specific to citrullinated α-enolase are enriched in the rheumatic joint. J Autoimmun. 2018;92:47–56. doi: 10.1016/j.jaut.2018.04.004
   PubMed Web of Science ®Google Scholar
• Rims C, Uchtenhagen H, Kaplan MJ, et al. Citrullinated aggrecan epitopes as targets of autoreactive CD4+ T cells in patients with rheumatoid arthritis. Arthritis & Rheumat. 2019;71(4):518–528. doi: 10.1002/art.40768
   PubMed Web of Science ®Google Scholar
• Cianciotti BC, Ruggiero E, Campochiaro C, et al. CD4+ memory stem T cells recognizing citrullinated epitopes are expanded in patients with rheumatoid arthritis and sensitive to tumor necrosis factor blockade. Arthritis & Rheumat. 2020;72(4):565–575. doi: 10.1002/art.41157
   PubMed Web of Science ®Google Scholar
• Turcinov S, Af Klint E, Van Schoubroeck B, et al. Diversity and clonality of T cell receptor repertoire and antigen specificities in small joints of early rheumatoid arthritis. Arthritis & Rheumat. 2022;75(5):673–684. Epub ahead of print. doi: 10.1002/art.42407
   Web of Science ®Google Scholar
• Moon JS, Younis S, Ramadoss NS, et al. Cytotoxic CD8+ T cells target citrullinated antigens in rheumatoid arthritis. Nat Commun. 2023;14(1):319. doi: 10.1038/s41467-022-35264-8
   PubMed Web of Science ®Google Scholar
• Scally SW, Petersen J, Law SC, et al. A molecular basis for the association of the HLA-DRB1 locus, citrullination, and rheumatoid arthritis. J Exp Med. 2013;210(12):2569–2582. doi: 10.1084/jem.20131241
   PubMed Web of Science ®Google Scholar
• Ting YT, Petersen J, Ramarathinam SH, et al. The interplay between citrullination and HLA-DRB1 polymorphism in shaping peptide binding hierarchies in rheumatoid arthritis. J Biol Chem. 2018;293(9):3236–3251. doi: 10.1074/jbc.RA117.001013
   PubMed Web of Science ®Google Scholar
• Lim JJ, Jones CM, Loh TJ, et al. The shared susceptibility epitope of HLA-DR4 binds citrullinated self-antigens and the TCR. Sci Immunol. 2021;6(58):eabe0896. doi: 10.1126/sciimmunol.abe0896
   PubMed Web of Science ®Google Scholar
• Bas S, Perneger TV, Seitz M, et al. Diagnostic tests for rheumatoid arthritis: comparison of anti-cyclic citrullinated peptide antibodies, anti-keratin antibodies and IgM rheumatoid factors. Rheumatology (Oxford). 2002 Jul;41(7):809–814. doi: 10.1093/rheumatology/41.7.809
   PubMed Web of Science ®Google Scholar
• Vincent C, de Keyser F, Masson-Bessière C, et al. Anti-perinuclear factor compared with the so called “antikeratin” antibodies and antibodies to human epidermis filaggrin, in the diagnosis of arthritides. Ann Rheum Dis. 1999 Jan;58(1):42–48. doi: 10.1136/ard.58.1.42
   PubMed Web of Science ®Google Scholar
• Iwaszkiewicz C, Puszczewicz M, Białkowska-Puszczewicz G. Diagnostic value of the anti-Sa antibody compared with the anti-cyclic citrullinated peptide antibody in rheumatoid arthritis. Int J Rheum Dis. 2015;18(1):46–51. doi: 10.1111/1756-185X.12544
   PubMed Web of Science ®Google Scholar
• Li X, Wang Z, Yi H, et al. Meta-analysis: diagnostic accuracy of the citrullinated peptides derived from fibrinogen and vimentin in rheumatoid arthritis. Clin Rheumatol. 2020 Apr;39(4):1111–1120. doi: 10.1007/s10067-019-04845-2
   PubMed Web of Science ®Google Scholar
• Liang B, Ge C, Lönnblom E, et al. The autoantibody response to cyclic citrullinated collagen type II peptides in rheumatoid arthritis. Rheumatology (Oxford). 2019 Sep 1;58(9):1623–1633.
   PubMed Web of Science ®Google Scholar