Matrix metalloproteinase-3 (MMP-3) in synovial fluid with temporomandibular joint disorders

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Matrix metalloproteinase-3 (MMP-3, stromelysin) is known to degrade certain matrix components, including proteoglycans, fibronectin, laminin and collagens. We investigated the early signs of cartilage degradation by assaying MMP-3 in the synovial fluid of human temporomandibular joints with internal derangement (ID) or osteoarthritis (OA). Synovial fluid was collected from the upper joint space by direct aspiration (nondiluted synovial fluid) or by pumping with lidocaine (diluted synovial fluid). MMP-3 was visualized by casein enzymography and measured by one-step sandwich enzyme immunoassay using an anti-human MMP-3 antibody that recognizes both active enzyme and inactive proenzyme. The concentration of MMP-3 with ID in both diluted and non-diluted synovial fluid was significantly greater than that with OA or in the asymptomatic controls (p<0.001). Enzymatically active components were detected in the non-diluted synovial fluid, but not in the diluted synovial fluid. Active MMP-3 was detected only in the nondiluted synovial fluid with OA, while inactive MMP-3 was observed in the non-diluted synovial fluid both with ID and with OA. These results indicate that MMP-3 may be released as proenzyme into the synovial fluid during the early stages of degenerative changes in the TMJ. Subsequently, progressive TMJ destruction may induce the release of active MMP-3. We concluded that MMP-3 assay using synovial fluid may be a useful marker for the diagnosis of TMJ disorders. (J Osaka Dent Univ 2003; 37: 123-127.)
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Matrix metalloproteinase-3 (MMP-3) in synovial fluid with temporomandibular joint disorders

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