The influence of alpha1-acid glycoprotein on collagenase-3 activity in early rheumatoid arthritis.

Abstract

The concentration and glycosylation of alpha(1)-acid glycoprotein (AGP) alter significantly during inflammation. A definitive physiological role for AGP remains elusive and is the subject of extensive investigation. This study investigated the influence of AGP on the activity of collagenase-3, an important mediator of cartilage destruction in rheumatoid arthritis. AGP was isolated from normal and rheumatoid plasma. Fucosylation was determined by high pH anion-exchange chromatography; sialylation was assessed following enzymatic digest. Rheumatoid AGP displayed elevated fucosylation and sialylation compared with normal. The influence of each sample on collagenase-3 activity was measured fluorometrically. AGP influenced collagenase-3 catalysis and collagen binding, with catalytic activity correlating with fucosylation. Rheumatoid AGP exhibited less efficient inhibition than normal plasma AGP. It is hypothesized that AGP within rheumatoid synovial fluid may be inadequate to prevent excessive cartilage destruction and hence may exacerbate the disease process.

• Authors: J Louise Haston, Oliver FitzGerald, David Kane, Kevin D Smith
• Journal: Biomedical chromatography : BMC (Biomed Chromatogr) Vol. 17 Issue 6 Pg. 361-4 (Sep 2003) ISSN: 0269-3879 [Print] England
• PMID: 13680845 (Publication Type: Journal Article)
• Copyright: Copyright 2003 John Wiley & Sons, Ltd.

Chemical References

• Orosomucoid
• Recombinant Proteins
• Collagenases
• MMP13 protein, human
• Matrix Metalloproteinase 13

Topics

• Arthritis, Rheumatoid (enzymology, metabolism)
• Chromatography, Ion Exchange
• Collagenases (metabolism)
• Humans
• Hydrogen-Ion Concentration
• Matrix Metalloproteinase 13
• Orosomucoid (metabolism)
• Recombinant Proteins (metabolism)