Accession Number : AD1028490

Title :   Citrullinated Chemokines in Rheumatoid Arthritis

Descriptive Note : Technical Report,30 Sep 2013,29 Sep 2016

Corporate Author : Regents of the University of Michigan Ann Arbor United States

Personal Author(s) : Fox,David A

Full Text :

Report Date : 01 Dec 2016

Pagination or Media Count : 39

Abstract : Citrullination, catalysed by peptidylarginine deiminase (PAD), is a post-translational modification of arginine to citrulline, which contributes to the pathogenesis of rheumatoid arthritis (RA). We show that citrullinated epithelial-derived neutrophil-activating peptide78/CXCL5 (cit-ENA-78/CXCL5) is significantly higher in RA synovial fluids (SFs) compared to osteoarthritis (OA) and other inflammatory rheumatic diseases (OD) SFs, and its concentration correlates with RA disease activity. Citrullinated chemokine concentrations were measured by enzyme linked immunosorbent assay (ELISA) in RA and normal (NL) sera and in RA, osteoarthritis(OA), and other inflammatory rheumatic disease (OD) synovial fluids (SFs). The correlation between the citrullinated chemokine levels and clinical data was analyzed. A strong correlation was found between the amounts of citENA-78/CXCL5 and C-reactive protein orerythrocyte sedimentation rate (ESR) in RA SFs. These results indicate that citENA-78/CXCL5 may have novel inflammatory properties inRA pathogenesis.

Descriptors :   ARTHRITIS , immunology , stem cells , proteins , biological factors , peptides , immunoproteins , amino acids , liquid chromatography , proteomics , cell physiological processes , blood , chemotactic factors , joints (anatomy) , albumins , inflammation

Distribution Statement : APPROVED FOR PUBLIC RELEASE