Inhibition of interleukin-1α-induced cartilage oligomeric matrix protein degradation in bovine articular cartilage by matrix metalloproteinase inhibitors: Potential role for matrix metalloproteinases in the generation of cartilage oligomeric matrix protein fragments in arthritic synovial fluid
✍ Scribed by Vishwas Ganu; Ronald Goldberg; Jane Peppard; John Rediske; Richard Melton; Shou-Ih Hu; Weigwang Wang; Charlotte Duvander; Dick Heinegård
- Publisher
- John Wiley and Sons
- Year
- 1998
- Tongue
- English
- Weight
- 918 KB
- Volume
- 41
- Category
- Article
- ISSN
- 0004-3591
No coin nor oath required. For personal study only.
✦ Synopsis
Objective. To determine whether matrix metalloproteinases (MMPs) degrade cartilage oligomeric matrix protein (COMP) to produce fragments similar to those found in synovial fluid (SF) from patients with arthritis.
Methods. COMP fragments were generated in vitro by treating (a) bovine articular cartilage with interleukin-la (IL-la), (b) purified bovine COMP with MMPs, and (c) articular cartilage with MMPs. The fragments generated in each case were analyzed by Western blot, using an antibody to the C-terminal heptadecapeptide of COMP.
Results. IL-la stimulation of cartilage resulted in a fragmentation of COMP, which was inhibited by MMP inhibitors CGS 27023A and BE-94. Isolated, recombinant MMPs rapidly degraded purified COMP, as well as COMP residing in cartilage. Several COMP fragments produced in vitro had similar electrophoretic mobility to those in SF of patients with arthritis.
ConcZusion. MMPs may contribute to the COMP fragments found in vivo.