Citrullination: a small change for a protein with great consequences for rheumatoid arthritis

A new autoantibody activity, which is almost 100% specific for rheumatoid arthritis (RA), has been found. The essential part of the B-cell epitope is a modified form of arginine (ie citrulline). The conversion of protein-contained arginine to citrulline is an enzymatic process that is carried out by...

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Detalles Bibliográficos
Autores principales: van Venrooij, Walther J, Pruijn, Ger J M
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2000
Materias:
Commentary
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC130012/
https://www.ncbi.nlm.nih.gov/pubmed/11094435
http://dx.doi.org/10.1186/ar95
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author van Venrooij, Walther J
Pruijn, Ger J M
author_facet van Venrooij, Walther J
Pruijn, Ger J M
author_sort van Venrooij, Walther J
collection PubMed
description A new autoantibody activity, which is almost 100% specific for rheumatoid arthritis (RA), has been found. The essential part of the B-cell epitope is a modified form of arginine (ie citrulline). The conversion of protein-contained arginine to citrulline is an enzymatic process that is carried out by peptidylarginine deiminase (PAD), an enzyme that appears to be hormonally controlled. Because of its remarkable specificity, citrullination and related processes might open new possibilities for studying the aetiology of RA.
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spelling pubmed-1300122002-10-28 Citrullination: a small change for a protein with great consequences for rheumatoid arthritis van Venrooij, Walther J Pruijn, Ger J M Arthritis Res Commentary A new autoantibody activity, which is almost 100% specific for rheumatoid arthritis (RA), has been found. The essential part of the B-cell epitope is a modified form of arginine (ie citrulline). The conversion of protein-contained arginine to citrulline is an enzymatic process that is carried out by peptidylarginine deiminase (PAD), an enzyme that appears to be hormonally controlled. Because of its remarkable specificity, citrullination and related processes might open new possibilities for studying the aetiology of RA. BioMed Central 2000 2000-05-24 /pmc/articles/PMC130012/ /pubmed/11094435 http://dx.doi.org/10.1186/ar95 Text en Copyright © 2000 Current Science Ltd
spellingShingle Commentary
van Venrooij, Walther J
Pruijn, Ger J M
Citrullination: a small change for a protein with great consequences for rheumatoid arthritis
title Citrullination: a small change for a protein with great consequences for rheumatoid arthritis
title_full Citrullination: a small change for a protein with great consequences for rheumatoid arthritis
title_fullStr Citrullination: a small change for a protein with great consequences for rheumatoid arthritis
title_full_unstemmed Citrullination: a small change for a protein with great consequences for rheumatoid arthritis
title_short Citrullination: a small change for a protein with great consequences for rheumatoid arthritis
title_sort citrullination: a small change for a protein with great consequences for rheumatoid arthritis
topic Commentary
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC130012/
https://www.ncbi.nlm.nih.gov/pubmed/11094435
http://dx.doi.org/10.1186/ar95
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