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  • Title: Matrix metalloproteinases 1, 2, and 3 from rheumatoid synovial cells are sufficient to destroy joints.
    Author: Okada Y, Nagase H, Harris ED.
    Journal: J Rheumatol; 1987 May; 14 Spec No():41-2. PubMed ID: 3305938.
    Abstract:
    A neutral metalloproteinase has been isolated and purified from adherent rheumatoid synovial cells in culture. This protease, named matrix metalloproteinase 3, (MMP-3) degrades gelatin, proteoglycan, fibronectin, type IV collagen, laminin, and the N propeptide of type I procollagen. It can be separated from MMP-2 (a potent gelatinase), and MMP-1, an interstitial collagenase. MMP-3 is released from cells as a proenzyme of 55 Kda. Activation by trypsin or organic mercurials produces 2 active species of 45 Kda and 28 Kda. The enzyme contains zinc as an intrinsic component and requires calcium for conformational stability. In concert, active MMP-1, -2, and -3 can destroy all significant structural proteins of joint structures.
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