the fine specificity of igm anti-citrullinated protein antibodies (acpa) is different from that of igg acpaigm anti-citrullinated蛋白特异性的抗体(acpa)是不同于免疫球蛋白acpa.pdfVIP

Suwannalai et al. Arthritis Research Therapy 2011, 13:R195 /content/13/6/R195 RESEARCH ARTICLE Open Access The fine specificity of IgM anti-citrullinated protein antibodies (ACPA) is different from that of IgG ACPA 1 1 1 1 1 Parawee Suwannalai , Annemiek Willemze , Linda van Toorn , Gerrie Stoeken-Rijsbergen , Nivine Levarht , 2 1 1 1* Jan Wouter Drijfhout , Tom W J Huizinga , Rene E M Toes and Leendert A Trouw Abstract Introduction: The antigen recognition pattern of immunoglobulin M (IgM) could, when directed against protein antigens, provide an indication of the antigenic moieties triggering new B cells. The half-life of IgM is short and memory B cells against T-cell-dependent protein antigens typically produce IgG and not IgM antibodies. In this study, we analyzed whether a difference exists between the fine specificity of IgM versus IgG anti-citrullinated protein antibodies (ACPAs). Methods: We determined the fine specificity of IgM and IgG ACPAs in 113 ACPA-positive rheumatoid arthritis patients with IgM cyclic citrullinated peptide 2 (CCP2) levels above 100 AU/ml. Fine specificity was assessed by performing ELISA using citrullinated peptides derived from vimentin, fibrinogen-b, fibrinogen-a and a-enolase, as well as citrullinated proteins fibrinogen and myelin basic protein. The arginine counterparts were used as controls. Results: Recognition of defined citrullinated antigens by IgM ACPA was confined to samples that also displayed recognition by IgG ACPA. However, the IgM ACPA response displayed a more restricted antigen recognition profile than IgG ACPA (OR = 0.26, P 0.0001).