期刊
FEBS LETTERS
卷 491, 期 3, 页码 222-226出版社
WILEY
DOI: 10.1016/S0014-5793(01)02204-9
关键词
MT1 MMP; MMP 2; TIMP; collagen; proteolysis
A fibrosarcoma cell line transfected with the matrix metalloproteinase MT1 MMP showed an enhanced ability to degrade C-14-labelled collagen films. As previously shown for proMMP 2 activation, TIMP 1 was an ineffective inhibitor of the process of collagenolysis whereas TIMP 2 was efficient and completely prevented collagen degradation. In the presence of the calcium ionophore, ionomycin, proteolytic processing of MT1 MMP was restricted and collagenolysis did not occur indicating that the 63 kDa form of the enzyme is not a functional collagenase, The collagenolytic activity of MT1 MMP was shown to be enhanced by the addition of proMMP 2, but TIMP I inhibition remained poor relative to that of TIMP 2, The study demonstrated that synergy between two non-conventional collagenases effectively degrades insoluble pericellular collagen, Due to the membrane localisation of MTI MMP, this could potentially occur in a highly localised manner. (C) 2001 Federation of European Biochemical Societies, Published by Elsevier Science B.V. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据