Okada Y, Nagase H, Harris E D
J Rheumatol. 1987 May;14 Spec No:41-2.
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.
已从培养的类风湿性滑膜贴壁细胞中分离并纯化出一种中性金属蛋白酶。这种蛋白酶名为基质金属蛋白酶3（MMP - 3），可降解明胶、蛋白聚糖、纤连蛋白、IV型胶原、层粘连蛋白以及I型前胶原的N端前肽。它可以与MMP - 2（一种强效明胶酶）和MMP - 1（一种间质胶原酶）分离。MMP - 3以55 kDa的酶原形式从细胞中释放出来。经胰蛋白酶或有机汞激活后产生45 kDa和28 kDa的两种活性形式。该酶含有锌作为固有成分，并且需要钙来维持构象稳定性。协同作用时，活性MMP - 1、 - 2和 - 3可破坏关节结构的所有重要结构蛋白。
