INACTIVATION OF TISSUE INHIBITOR OF METALLOPROTEINASES BY NEUTROPHIL ELASTASE AND OTHER SERINE PROTEINASES
INACTIVATION OF TISSUE INHIBITOR OF METALLOPROTEINASES BY NEUTROPHIL ELASTASE AND OTHER SERINE PROTEINASES
复制标题
DOI：
10.1016/0014-5793(88)80817-2
复制
发表时间：
1988-02-29
期刊：
影响因子：
3.5
通讯作者：
NAGASE, H
中科院分区：
文献类型：
--
作者：
OKADA, Y;WATANABE, S;NAGASE, H
从培养的牛牙髓中提取的金属蛋白酶组织抑制剂（TIMP）抑制人类风湿滑膜基质金属蛋白酶3 (MMP-3)，其摩尔化学计量比为1:1。在所检测的丝氨酸蛋白酶中，人中性粒细胞弹性蛋白酶、胰蛋白酶和α-凝乳胰蛋白酶通过将抑制剂分子降解成小片段来破坏TIMP对MMP-3的抑制活性。而组织蛋白酶G、胰弹性酶和纤溶酶对TIMP的抑制作用没有显著降低。这些数据表明，在各种炎症条件下浸润组织的中性粒细胞可能通过中性粒细胞弹性酶的作用在体内调节TIMP活性中发挥重要作用。
Tissue inhibitor of metalloproteinases (TIMP) from cultured bovine dental pulp inhibits human rheumatoid synovial matrix metalloproteinase 3 (MMP-3) with a stoichiometry of 1:1 on a molar basis. Among the serine proteinases examined, human neutrophil elastase, trypsin and α-chymotrypsin destroyed the inhibitory activity of TIMP against MMP-3 by degrading the inhibitor molecule into small fragments. In contrast, the inhibitory activity of TIMP was not significantly reduced by the actions of cathepsin G, pancreatic elastase and plasmin. These data indicate that neutrophils which infiltrate tissues in various inflammatory conditions may play an important role in regulating TIMP activity in vivo through the action of neutrophil elastase.