Matrix metalloproteinases 1, 2, and 3 from rheumatoid synovial cells are sufficient to destroy joints.
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.
Okada
Y
Y
Nagase
H
H
Harris
E D
ED
D001172:Arthritis, Rheumatoid / Q000201:enzymology* / Q000209:etiology; D010450:Endopeptidases / Q000378:metabolism*; D005109:Extracellular Matrix / Q000201:enzymology; D006801:Humans; D008666:Metalloendopeptidases; D013583:Synovial Membrane / Q000201:enzymology*
D010450:Endopeptidases; D008666:Metalloendopeptidases