Meeting abstract
Open Access
Volume 6 Supplement 1
24th European Workshop for Rheumatology Research
Antifilaggrin antibodies in serum and synovial fluid samples of patients with rheumatoid arthritis show similar reactivity pattern towards citrulline containing peptides
Received: 16 January 2004
Published: 24 February 2004
Background
Antifilaggrin antibodies are highly specific serological markers of rheumatoid arthritis (RA). They have been shown to comprise a heterogeneous population of antibodies directed at citrullinated peptides. Recent studies suggest that the site of the initial antigenic trigger where these autoantibodies are produced can be localized to the synovial tissue.
Objective
The aim of this study was to compare the recognition patterns of antibodies in paired serum and synovial fluid samples of RA patients toward citrullinated peptide sequences to investigate whether or not they comprise the same antibody population.
Methods
Arginine-rich peptide sequence corresponding to human profilaggrin (amino acid residues 306–324) and sequences with citrulline substitution at different positions were synthesized by mutipin peptide synthesis on solid support. Completely citrullinated variant of the 19-mer peptide and shortened sequences were also produced. The reactivity of these peptides with paired sera and synovial fluid samples of RA patients were determined (n = 25). Results were evaluated statistically using the paired t test.
Results and Conclusion
The results (Table 1) show that the 12–19 amino acid long epitopes are recognized by homogeneous antibody population present in serum and synovial fluid, whereas the reactivities toward short citrullinated sequences differs significantly.
Table 1
Comparison of the reactivities of antibodies in paired serum and synovial fluid samples
Sequence | P value | Sequence | P value |
|---|---|---|---|
SHQESTXGXSXGXSGXSGS | 0.754 | TXGRSRGRSGRSG | 0.598 |
SHQESTXGXSXGXSGRSGS | 0.382 | TXGRSRGRSGRS | 0.129 |
SHQESTXGXSXGRSGRSGS | 0.09 | TXGRSRGRSGR | 0.04* |
SHQESTRGXSXGXSGXSGS | 0.081 | TXGRSRGRSG | 0.122 |
SHQESTRGRSXGXSGXSGS | 0.143 | TXGRSRGRS | 0.128 |
SHQESTRGRSRGXSGXSGS | 0.192 | TXGRSRGR | 0.039* |
TXGRSRG | 0.019* | ||
TXGRSR | 0.003* | ||
TXGRS | 0.003* | ||
TXGR | 0.011* |
Declarations
Acknowledgement
This work was supported by the Hungarian grant: OTKA T037876.
Authors’ Affiliations
(1)
National Institute of Rheumatology
(2)
Peptide Chemistry Research Group, Eötvös Lóránd University, Academy of Science
Copyright
© The Author(s) 2004
