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人类风湿性滑膜细胞产生的基质金属蛋白酶3(基质溶解素)对IX型胶原蛋白的降解作用。

Degradation of type IX collagen by matrix metalloproteinase 3 (stromelysin) from human rheumatoid synovial cells.

作者信息

Okada Y, Konomi H, Yada T, Kimata K, Nagase H

机构信息

Department of Pathology, School of Medicine, Kanazawa University, Ishikawa, Japan.

出版信息

FEBS Lett. 1989 Feb 27;244(2):473-6. doi: 10.1016/0014-5793(89)80586-1.

Abstract

The degradation of type IX collagen, a minor collagen in cartilage, was examined by treatment with three different types of matrix metalloproteinases (MMPs) purified from the culture medium of rheumatoid synovial cells. Neither MMP-1 (collagenase) nor MMP-2 (so-called 'gelatinase') could digest type IX collagen, but MMP-3 (stromelysin) readily degraded it into smaller fragments. This suggests that MMP-3 may be responsible for the pathological degradation and/or normal turnover of type IX collagen.

摘要

通过用从类风湿性滑膜细胞培养基中纯化的三种不同类型的基质金属蛋白酶(MMP)处理,研究了软骨中的次要胶原蛋白IX型胶原蛋白的降解情况。MMP-1(胶原酶)和MMP-2(所谓的“明胶酶”)都不能消化IX型胶原蛋白,但MMP-3(基质溶素)很容易将其降解成更小的片段。这表明MMP-3可能是IX型胶原蛋白病理降解和/或正常周转的原因。

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