Skip Navigation



Rheumatology Advance Access published online on March 3, 2008
Rheumatology, doi:10.1093/rheumatology/ken014
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
47/5/567    most recent
ken014v2
ken014v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrowRequest Permissions
Right arrow Disclaimer
Google Scholar
Right arrow Articles by Eggleton, P.
Right arrow Articles by Winyard, P. G.
PubMed
Right arrow PubMed Citation
Right arrow Articles by Eggleton, P.
Right arrow Articles by Winyard, P. G.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© The Author 2008. Published by Oxford University Press on behalf of the British Society for Rheumatology. All rights reserved. For Permissions, please email: journals.permissions@oxfordjournals.org

Review

Consequence of neo-antigenicity of the ‘altered self’

P. Eggleton1, R. Haigh1,2 and P. G. Winyard1

1Musculoskeletal and Inflammation Research Group, Institute of Biomedical and Clinical Science, Peninsula College of Medicine and Dentistry, Universities of Exeter and Plymouth and 2Princess Elizabeth Orthopaedic Centre, Exeter, UK.

Correspondence to: P. G. Winyard, Peninsula College of Medicine and Dentistry, St Luke's Campus, Universities of Exeter and Plymouth, Exeter, Devon EX1 2LU, UK. E-mail: paul.winyard{at}pms.ac.uk


  Abstract

Post-translational modifications play a central role in determining the function of proteins. Such protein modifications come in a great variety of guises, and include phosphorylation, proteolysis, glycosylation, citrullination and oxidative modifications. In relation to inflammatory autoimmune diseases, some post-translational modifications appear to result in the generation of new antigens, and hence autoantibodies. Examples include: the induction of peptide immunogenicity by the spontaneous conversion of aspartic acid residues to isoaspartic acid; granzyme B-mediated cleavage of SLE autoantigens; the oxidative modification—on the surface of apoptotic cells—of lipids and proteins, rendering them immunogenic; and the presence of antibodies to oxidatively modified type II collagen and C1q in RA and SLE patients, respectively. The measurement of autoantibodies to citrullinated proteins has been verified as a very useful diagnostic tool in RA. Proteomics techniques, in principle, allow the detection of all types of in vivo protein modifications, and the increasing application of such technologies to the study of rheumatological diseases will further our understanding of autoantigenicity.

KEY WORDS: Post-translational modification, Protein oxidation, Citrullination, Oxidized low-density lipoprotein, Inflammation, Rheumatic diseases, Anti-phospholipid syndrome, Neo-antigenicity, Autoantibody, Apoptosis

Submitted 7 September 2007; revised version accepted 7 January 2008.
Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?




Disclaimer:
Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.