Go to JCI Insight
  • About
  • Editors
  • Consulting Editors
  • For authors
  • Publication ethics
  • Alerts
  • Advertising
  • Job board
  • Subscribe
  • Contact
  • Current issue
  • Past issues
  • By specialty
    • COVID-19
    • Cardiology
    • Gastroenterology
    • Immunology
    • Metabolism
    • Nephrology
    • Neuroscience
    • Oncology
    • Pulmonology
    • Vascular biology
    • All ...
  • Videos
    • Conversations with Giants in Medicine
    • Author's Takes
  • Reviews
    • View all reviews ...
    • Aging (Jul 2022)
    • Next-Generation Sequencing in Medicine (Jun 2022)
    • New Therapeutic Targets in Cardiovascular Diseases (Mar 2022)
    • Immunometabolism (Jan 2022)
    • Circadian Rhythm (Oct 2021)
    • Gut-Brain Axis (Jul 2021)
    • Tumor Microenvironment (Mar 2021)
    • View all review series ...
  • Viewpoint
  • Collections
    • In-Press Preview
    • Commentaries
    • Concise Communication
    • Editorials
    • Viewpoint
    • Top read articles
  • Clinical Medicine
  • JCI This Month
    • Current issue
    • Past issues

  • Current issue
  • Past issues
  • Specialties
  • Reviews
  • Review series
  • Conversations with Giants in Medicine
  • Author's Takes
  • In-Press Preview
  • Commentaries
  • Concise Communication
  • Editorials
  • Viewpoint
  • Top read articles
  • About
  • Editors
  • Consulting Editors
  • For authors
  • Publication ethics
  • Alerts
  • Advertising
  • Job board
  • Subscribe
  • Contact
Top
  • View PDF
  • Download citation information
  • Send a comment
  • Share this article
  • Terms of use
  • Standard abbreviations
  • Need help? Email the journal
  • Top
  • Abstract
  • Version history
  • Article usage
  • Citations to this article

Advertisement

Research Article Free access | 10.1172/JCI116713

The cytokeratin filament-aggregating protein filaggrin is the target of the so-called "antikeratin antibodies," autoantibodies specific for rheumatoid arthritis.

M Simon, E Girbal, M Sebbag, V Gomès-Daudrix, C Vincent, G Salama, and G Serre

Department of Biology and Pathology of the Cell, Toulouse-Purpan School of Medicine, University of Toulouse III, France.

Find articles by Simon, M. in: JCI | PubMed | Google Scholar

Department of Biology and Pathology of the Cell, Toulouse-Purpan School of Medicine, University of Toulouse III, France.

Find articles by Girbal, E. in: JCI | PubMed | Google Scholar

Department of Biology and Pathology of the Cell, Toulouse-Purpan School of Medicine, University of Toulouse III, France.

Find articles by Sebbag, M. in: JCI | PubMed | Google Scholar

Department of Biology and Pathology of the Cell, Toulouse-Purpan School of Medicine, University of Toulouse III, France.

Find articles by Gomès-Daudrix, V. in: JCI | PubMed | Google Scholar

Department of Biology and Pathology of the Cell, Toulouse-Purpan School of Medicine, University of Toulouse III, France.

Find articles by Vincent, C. in: JCI | PubMed | Google Scholar

Department of Biology and Pathology of the Cell, Toulouse-Purpan School of Medicine, University of Toulouse III, France.

Find articles by Salama, G. in: JCI | PubMed | Google Scholar

Department of Biology and Pathology of the Cell, Toulouse-Purpan School of Medicine, University of Toulouse III, France.

Find articles by Serre, G. in: JCI | PubMed | Google Scholar

Published September 1, 1993 - More info

Published in Volume 92, Issue 3 on September 1, 1993
J Clin Invest. 1993;92(3):1387–1393. https://doi.org/10.1172/JCI116713.
© 1993 The American Society for Clinical Investigation
Published September 1, 1993 - Version history
View PDF
Abstract

In rheumatoid arthritis (RA), the high diagnostic value of serum antibodies to the stratum corneum of rat esophagus epithelium has been widely reported. These so-called "antikeratin antibodies," detected by indirect immunofluorescence, were found to be autoantibodies since they also labeled human epidermis. Despite their name, the actual target of these autoantibodies was not known. In this study, a 40-kD protein (designated as 40K), extracted from human epidermis and specifically immunodetected by 75% of RA sera, was purified and identified as a neutral/acidic isoform of basic filaggrin, a cytokeratin filament-aggregating protein, by peptide mapping studies and by the following evidences: (a) mAbs specific for filaggrin reacted with the 40K protein; (b) the autoantibodies, affinity-purified from RA sera on the 40K protein, immunodetected purified filaggrin; (c) the reactivity of RA sera to the 40K protein was abolished after immunoadsorption with purified filaggrin; (d) the 40K protein and filaggrin had similar amino acid compositions. Furthermore, autoantibodies against the 40K protein and the so-called "antikeratin antibodies" were shown, by immunoadsorption experiments, to be largely the same. The identification of filaggrin as a RA-specific autoantigen could contribute to the understanding of the pathogenesis of this disease and, ultimately, to the development of methods for preventing the autoimmune response.

Images.

Browse pages

Click on an image below to see the page. View PDF of the complete article

icon of scanned page 1387
page 1387
icon of scanned page 1388
page 1388
icon of scanned page 1389
page 1389
icon of scanned page 1390
page 1390
icon of scanned page 1391
page 1391
icon of scanned page 1392
page 1392
icon of scanned page 1393
page 1393
Version history
  • Version 1 (September 1, 1993): No description

Article tools

  • View PDF
  • Download citation information
  • Send a comment
  • Share this article
  • Terms of use
  • Standard abbreviations
  • Need help? Email the journal

Metrics

  • Article usage
  • Citations to this article

Go to

  • Top
  • Abstract
  • Version history
Advertisement
Advertisement

Copyright © 2022 American Society for Clinical Investigation
ISSN: 0021-9738 (print), 1558-8238 (online)

Sign up for email alerts