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Rheumatology Advance Access originally published online on April 21, 2006
Rheumatology 2006 45(11):1364-1369; doi:10.1093/rheumatology/kel113
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© The Author 2006. Published by Oxford University Press on behalf of the British Society for Rheumatology. All rights reserved. For Permissions, please email: journals.permissions@oxfordjournals.org

Inhibitory characteristics of citrullinated telopeptides of type I and II collagens for autoantibody binding in patients with rheumatoid arthritis

M.-K. Koivula, S. Åman1, E. Alasaarela1, A. Karjalainen1, M. Hakala2 and J. Risteli

Department of Clinical Chemistry, 1Division of Rheumatology, Department of Internal Medicine, University of Oulu, Oulu and 2Rheumatism Foundation Hospital, Heinola, Finland.

Correspondence to: Juha Risteli, MD, PhD, Professor of Clinical Chemistry, University of Oulu, PL 5000, FI-90014 Oulun yliopisto, Finland. E-mail: juha.risteli{at}oulu.fi

Objective. To study how soluble citrullinated telopeptides of type I and II collagens inhibit the binding of autoantibodies to the respective antigens immobilized onto solid phase, and to use modifications of previous methods to re-analyse rheumatoid arthritis (RA) and control serum samples.

Methods. Autoantibody binding was inhibited with normal or citrullinated carboxytelopeptides using enzyme-linked immunosorbent assay (ELISA) methods. Serum samples were available from 120 patients with RA and 81 controls.

Results. Autoantibodies that bind normal C-telopeptides were not inhibited with soluble normal or citrullinated telopeptides. However, the antibodies that bind only citrullinated telopeptides could be inhibited with corresponding citrullinated telopeptides. Thus, it is not necessary to study the binding of autoantibodies to normal collagens if the specificity of their binding is assessed by immunological inhibition. For type I telopeptide, there are two arginines, the latter of which, when citrullinated, is important for binding. For type II telopeptide, there is one arginine, which is important when citrullinated. The other amino acids, e.g. the last alanine, have only a slight effect on binding. These improved methods differentiate better between RA patients, who have specific citrullinated autoantibodies, and controls than previous ELISA methods.

Conclusions. Based on inhibition assay, it is possible to measure the autoantibodies binding specifically to citrullinated telopeptides of type I and II collagens. When only one assay is involved, variance is decreased and the overall performance is easier than before.

KEY WORDS: Anti-CCP antibodies, Autoantibodies, Citrullination, Rheumatoid arthritis, Telopeptide, Type I collagen, Type II collagen


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M.-K. Koivula, E. Savolainen, O. Kaipiainen-Seppanen, H. Kautiainen, R. Luosujarvi, M. Hakala, and J. Risteli
Sensitivity and specificity of autoantibodies binding to citrullinated carboxyterminal telopeptides of types I and II collagens in an early arthritis series
Rheumatology, May 1, 2008; 47(5): 656 - 659.
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