Nagase H
Department of Biochemistry and Molecular Biology, University of Kansas Medical Center, Kansas City 66160, USA.
Biol Chem. 1997 Mar-Apr;378(3-4):151-60.
Matrix metalloproteinases (MMPs), also called matrixins, function in the turnover of extracellular matrix components. These enzymes are considered to play important roles in embryo development, morphogenesis and tissue remodeling, and in diseases such as arthritis, periodontitis, glomerulonephritis, atherosclerosis, tissue ulceration, and in cancer cell invasion and metastasis. All MMPs are synthesized as preproenzymes and most of them are secreted from the cells as proenzymes. Thus, the activation of these proenzymes is one of the critical steps that leads to extracellular matrix breakdown. This review describes recent progress made to elucidate the activation mechanisms of pro-matrixins which include extracellular stepwise activation common to most proMMPs, cell surface activation of progelatinase A and procollagenase 3, and intracellular activation of prostromelysin 3 and pro-membrane-type-1 MMP.
基质金属蛋白酶（MMPs），也称为基质溶素，在细胞外基质成分的周转中发挥作用。这些酶被认为在胚胎发育、形态发生和组织重塑中以及在诸如关节炎、牙周炎、肾小球肾炎、动脉粥样硬化、组织溃疡等疾病以及癌细胞侵袭和转移中发挥重要作用。所有MMPs均以前体酶的形式合成，并且它们中的大多数作为酶原从细胞中分泌出来。因此，这些酶原的激活是导致细胞外基质分解的关键步骤之一。本综述描述了在阐明前基质溶素激活机制方面取得的最新进展，这些机制包括大多数前MMPs共有的细胞外逐步激活、前明胶酶A和前胶原酶3的细胞表面激活以及前基质溶解素3和前膜型1 MMP的细胞内激活。
