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Surface-bound immune complexes containing antibodies to collagen type II induce production of TNF-α, IL-1β and IL-8 from monocytes via FcγRII

Authors
Journal
Arthritis Research & Therapy
1478-6354
Publisher
Springer (Biomed Central Ltd.)
Publication Date
Volume
6
Identifiers
DOI: 10.1186/ar1044
Keywords
  • Meeting Abstract
Disciplines
  • Biology

Abstract

S1 Available online http://arthritis-research.com/supplements/6/S1 Autoantibodies and autoantigens 1 Differential antibody recognition of the 349–364aa B-cell epitope of human La/SSB protein and its phosphorylated analogue AG Terzoglou, JG Routsias, HM Moutsopoulos, AG Tzioufas Department of Pathophysiology, School of Medicine, University of Athens, Athens, Greece Arthritis Res Ther 2004 6(Suppl 1):1 (DOI 10.1186/ar1043) Background La/SSB is a phosphoprotein that associates with various small RNA molecules. It has been found that the primary phosphorylation site of the molecule during various physiological processes is in Ser366. Objectives To determine whether the phosphorylation state of Ser366 could affect the antigenicity and the recognition of the protein by anti- bodies from patients with primary Sjögren’s syndrome (pSS). Methods Peptides 349–368aa and phos349–368aa (with the Ser366 residue phosphorylated) were synthesized. Sera with anti-La specificity from 30 patients with pSS and sera from 19 normal individuals were examined against the two synthetic peptides in ELISA. The antibody specificity against the epitopes was tested with homologous and het- erologous inhibition assays. Results Of pSS sera 23% reacted against the 349–368aa peptide. Sera binding to unphosphorylated peptide reacted also with phos349–368aa. Although the same sera gave a positive reaction against both peptides, the optical density values received from antibod- ies to phos349–368aa were higher, indicating a higher concentration or stronger affinity. When phos349–368aa was used as soluble inhibitor, in homologous inhibition the reactivity was almost completely abolished (92%). In contrast, when the unphosphorylated peptide was used as inhibitor, the reactivity of sera against phos349–368aa was only partially reduced (35%), indicating that sera from these patients possess two distinct groups of antibodies: one against the unphospho- rylated and one against the phosphorylated epitope. Conclusion The phosphor

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