Macrophage metalloelastase degrades matrix and myelin proteins and processes a tumour necrosis factor-alpha fusion protein
Macrophage metalloelastase degrades matrix and myelin proteins and processes a tumour necrosis factor-alpha fusion protein
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DOI：
10.1006/bbrc.1996.1677
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发表时间：
1996-11-12
影响因子：
3.1
通讯作者：
Wells, G
中科院分区：
文献类型：
--
作者：
Chandler, S;Cossins, J;Wells, G
基质金属蛋白酶（MMP）是一组具有降解细胞外基质能力的酶。它们还裂解非基质蛋白，例如髓磷脂碱性蛋白和 α(1)-抗胰蛋白酶，并且能够将肿瘤坏死因子-α (TNF) 加工成成熟形式。我们克隆、表达并纯化了人巨噬细胞金属弹性蛋白酶 (EC 3.4.24.65)，这是一种因其降解弹性蛋白能力而被认可的 MMP，但其底物特异性尚未确定。除 I 型胶原蛋白外，该酶降解所有测试的基质蛋白，即：IV 型胶原蛋白、I 型明胶、纤连蛋白、层粘连蛋白、玻连蛋白和蛋白聚糖。它还降解髓磷脂碱性蛋白、裂解 α(1)-抗胰蛋白酶并从前 TNF 融合蛋白中释放 TNF。因此，与其他几种 MMP 一样，巨噬细胞金属弹性酶具有广泛的底物范围，超出了单独的弹性蛋白的底物范围。 (C) 1996 学术出版社
The matrix metalloproteinases (MMPs) are a group of enzymes which have the ability to degrade extracellular matrix. They also cleave non-matrix proteins such as myelin basic protein and alpha(1)-antitrypsin and they are able to process tumour necrosis factor-alpha (TNF) to its mature form. We have cloned, expressed and purified human macrophage metalloelastase (EC 3.4.24.65), an MMP recognised for its ability to degrade elastin, but whose substrate specificity has not yet been defined. With the exception of type I collagen this enzyme degraded all matrix proteins tested, namely: type IV collagen, type I gelatin, fibronectin, laminin, vitronectin and proteoglycan. It also degraded myelin basic protein, cleaved alpha(1)-antitrypsin and released TNF from a pro-TNF fusion protein. Thus, in common with several other MMPs, macrophage metalloelastase has a broad substrate range which extends beyond that of elastin alone. (C) 1996 Academic Press, Inc.