Citrullinated Chemokines in Rheumatoid Arthritis
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 peptide 78/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 amount of citrullinated ENA-78/CXCL5 and C-reactive protein or erythrocyte sedimentation rate (ESR) in RA SFs. These results indicate that citrullinated ENA- 78/CXCL5 may have novel inflammatory properties in RA pathogenesis.
Document Details
- Document Type
- Technical Report
- Publication Date
- Oct 01, 2014
- Accession Number
- ADA611994
Entities
People
- David A. Fox
Organizations
- University of Michigan