Collagenase-like (CL) peptidase activity in synovial fluid from patients with rheumatoid arthritis.

Abstract

We found the presence of collagenase-like (CL) peptidase in synovial fluid by a highly sensitive fluorescence assay using (succinyl-Gly-Pro-Leu-Gly-Pro)-4-methyl-coumaryl-7-amide (Suc-GPLGP-MCA) as a substrate. Suc-GPLGP-MCA is hydrolyzed at the Leu-Gly bond by CL-peptidase. The CL-peptidase activity in synovial fluid was significantly higher in patients with rheumatoid arthritis (RA) than in patients with osteoarthritis (OA) and in arthropathy-free controls. No significant difference in CL-peptidase activity in synovial fluid was found between patients with OA and arthropathy-free controls.

• Authors: A Ito, M Hagihara, T Nagatsu, H Iwata, T Miura
• Journal: Clinica chimica acta; international journal of clinical chemistry (Clin Chim Acta) Vol. 170 Issue 2-3 Pg. 291-6 (Dec 1987) ISSN: 0009-8981 [Print] Netherlands
• PMID: 2830060 (Publication Type: Journal Article)

Chemical References

• Coumarins
• Oligopeptides
• succinylglycyl-prolyl-leucyl-glycyl-prolyl-4-methylcoumaryl-7-amide
• Microbial Collagenase

Topics

• Arthritis, Rheumatoid (enzymology)
• Coumarins (metabolism)
• Fluorescence
• Humans
• Microbial Collagenase (analysis)
• Oligopeptides
• Osteoarthritis (enzymology)
• Synovial Fluid (enzymology)