The DOI matches its Crossref record; 27 of the 27 references it cites were found in a registry or an index.
The Epitopes Targeted by the Rheumatoid Arthritis-Associated Antifilaggrin Autoantibodies are Posttranslationally Generated on Various Sites of (Pro)Filaggrin by Deimination of Arginine Residues
Abstract
Antifilaggrin autoantibodies (AFA) are a population of IgG autoantibodies associated to rheumatoid arthritis (RA), which includes the so-called “antikeratin” Abs and antiperinuclear factor. AFA are the most specific serological markers of RA. We previously showed that they recognize human epidermal filaggrin and other profilaggrin-related proteins of various epithelial tissues. Here, we report further characterization of the protein Ags and epitopes targeted by AFA. All the Ags that exhibit numerous neutral/acidic isoelectric variants were immunochemically demonstrated to be deiminated proteins. In vitro deimination of a recombinant human filaggrin by a peptidylarginine deiminase generated AFA epitopes on the protein. Moreover, two of three filaggrin-derived synthetic peptides with a citrulline in the central position were specifically and widely recognized by AFA affinity-purified from a series of RA sera. These results indicate that citrulline residues are constitutive of the AFA epitopes, but only in the context of specific amino acid sequences of filaggrin. In competition experiments, the two peptides abolished the AFA reactivity of RA sera, showing that they present major AFA epitopes. These data should help in the identification of a putative deiminated AFA-inducing or cross-reactive articular autoantigen and provide new insights into the pathogenesis of RA. They could also open the way toward specific immunosuppressive and/or preventive therapy of RA.
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New Serum Factor in Patients with Rheumatoid Arthritis: The Antiperinuclear Factor
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Protein Unfolding by Peptidylarginine Deiminase
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Self-citationAnti-keratin antibodies in rheumatoid arthritis.
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Almost all about citrulline in mammals
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Metadata
- Authors
- Girbal-Neuhauser, E., Durieux, J.-J., Arnaud, M., Dalbon, P., Sebbag, M., Vincent, C., Simon, M., Senshu, T., Masson-Bessière, C., Jolivet-Reynaud, C., Jolivet, M., & Serre, G.
- Venue
- The Journal of Immunology
- Publisher
- Oxford University Press (OUP)
- Published
- 1999-01-01
- Volume
- 162
- Issue
- 1
- Pages
- 585-594
- ISSN
- 0022-1767 (ISSN-L)
- 1550-6606
- OpenAlex
- W1582204239
- Cited by
- 485
- References
- 27
- FWCI
- 12.16
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: The Epitopes Targeted by the Rheumatoid Arthritis-Associated Antifilaggrin Autoantibodies are Posttranslationally Generated on Various Sites of (Pro)Filaggrin by Deimination of Arginine Residues. https://app.cochat.ai/papers/10.4049/jimmunol.162.1.585
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- Girbal-Neuhauser, E., Durieux, J.-J., Arnaud, M., Dalbon, P., Sebbag, M., Vincent, C., Simon, M., Senshu, T., Masson-Bessière, C., Jolivet-Reynaud, C., Jolivet, M., & Serre, G. (1999). The Epitopes Targeted by the Rheumatoid Arthritis-Associated Antifilaggrin Autoantibodies are Posttranslationally Generated on Various Sites of (Pro)Filaggrin by Deimination of Arginine Residues. The Journal of Immunology. https://doi.org/10.4049/jimmunol.162.1.585
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
