MATRIX METALLOPROTEINASE-2 IS AN INTERSTITIAL COLLAGENASE - INHIBITOR-FREE ENZYME CATALYZES THE CLEAVAGE OF COLLAGEN FIBRILS AND SOLUBLE NATIVE TYPE-I COLLAGEN GENERATING THE SPECIFIC 3/4-LENGTH AND 1/4-LENGTH FRAGMENTS
MATRIX METALLOPROTEINASE-2 IS AN INTERSTITIAL COLLAGENASE - INHIBITOR-FREE ENZYME CATALYZES THE CLEAVAGE OF COLLAGEN FIBRILS AND SOLUBLE NATIVE TYPE-I COLLAGEN GENERATING THE SPECIFIC 3/4-LENGTH AND 1/4-LENGTH FRAGMENTS
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DOI：
10.1074/jbc.270.11.5872
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发表时间：
1995-03-17
影响因子：
4.8
通讯作者：
QUIGLEY, JP
中科院分区：
文献类型：
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作者：
AIMES, RT;QUIGLEY, JP
72-kDa明胶酶/IV型胶原酶（MMP-2）是酶的基质金属蛋白酶（MMP）家族的成员。已知这种酶切割IV型胶原蛋白以及降解变性胶原蛋白。然而，据报道天然间质胶原对MMP-2具有抗性，并且被认为仅对间质胶原酶MMP-1和MMP-8敏感。在这项研究中，我们报告了人和鸡MMP-8，不含金属蛋白酶组织抑制剂（TIMP），能够切割可溶性三螺旋I型胶原，产生脊椎动物间质胶原酶特征的3/4和1/4长度的胶原片段，MMP-2在胶原α链中与间质胶原酶相同的Gly-Ile/Leu键处切割，k（cat）和K-m值与MMP-1相似。MMP-2也能够降解重构的I型胶原原纤维。密切相关的92-kDa明胶酶/IV型胶原酶（MMP-9）在相同条件下不能切割可溶性或纤维状胶原，表明MMP-8的特异性胶原溶解活性不是明胶酶的一般性质。MMP-2是一种有效的明胶酶，也可以切割纤维状胶原蛋白，这为细胞侵入期间基质胶原蛋白的完全溶解需要两种酶（间质胶原酶和明胶酶）的提议提供了替代方案。
The 72-kDa gelatinase/type IV collagenase (MMP-2) is a member of the matrix metalloproteinase (MMP) family of enzymes. This enzyme is known to cleave type IV collagen as well as degrade denatured collagens. However, native interstitial collagens are reportedly resistant to MMP-2 and are thought to be susceptible only to the interstitial collagenases MMP-1 and MMP-8. In this study we report that both human and chicken MMP-8, free of tissue inhibitors of metalloproteinases (TIMPs) are capable of cleaving soluble, triple helical type I collagen generating the 3/4- and 1/4-length collagen fragments characteristic of vertebrate interstitial collagenases, MMP-2 cleaves at the same Gly-Ile/Leu bond in the collagen alpha chains as interstitial collagenases with k(cat) and K-m values similar to that of MMP-1. MMP-2 also is capable of degrading reconstituted type I collagen fibrils, The closely related 92-kDa gelatinase/type IV collagenase (MMP-9) is unable to cleave soluble or fibrillar collagen under identical conditions indicating that the specific collagenolytic activity of MMP-8 is not a general property of gelatinases. That MMP-2, a potent gelatinase, also can cleave fibrillar collagen provides an alternative to the proposal that two enzymes, an interstitial collagenase and a gelatinase, are required for the complete dissolution of stromal collagen during cellular invasion.