Membrane type 1 matrix metalloproteinase and gelatinase A synergistically degrade type 1 collagen in a cell model
Membrane type 1 matrix metalloproteinase and gelatinase A synergistically degrade type 1 collagen in a cell model
复制标题
DOI：
10.1016/s0014-5793(01)02204-9
复制
发表时间：
2001-03-02
期刊：
影响因子：
3.5
通讯作者：
Murphy, G
中科院分区：
文献类型：
--
作者：
Atkinson, SJ;Patterson, ML;Murphy, G
转染基质金属蛋白酶MT1 MMP的纤维肉瘤细胞系显示出增强的降解c -14标记的胶原膜的能力。如前所述，对于proMMP 2的激活，timp1是一种无效的胶原溶解过程抑制剂，而timp2是有效的，完全阻止胶原降解。在钙离子载体、离子霉素的存在下，MT1 MMP的蛋白水解加工受到限制，没有发生胶原溶解，表明63 kDa形式的酶不是功能性胶原酶。MT1 MMP的胶原溶解活性被证明通过添加proMMP 2增强，但TIMP I的抑制作用相对于TIMP 2仍然较差。该研究表明，两种非传统胶原酶之间的协同作用有效地降解了不溶性细胞周围胶原。由于MTI MMP的膜定位，这可能以高度局部的方式发生。(C) 2001欧洲生化学会联合会，Elsevier Science B.V.出版，版权所有。
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.