HUMAN PROGELATINASE-A CAN BE ACTIVATED BY MATRILYSIN
HUMAN PROGELATINASE-A CAN BE ACTIVATED BY MATRILYSIN
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DOI：
10.1016/0014-5793(94)00412-9
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发表时间：
1994-05-23
期刊：
影响因子：
3.5
通讯作者：
DOCHERTY, A
中科院分区：
文献类型：
--
作者：
CRABBE, T;SMITH, B;DOCHERTY, A
其他基质金属蛋白酶的人β-弹性蛋白酶A的激活进行了研究，通过以下的损失，其N-末端前肽和伴随的增加的合成底物的水解速率。活化的基质溶解素1不能引起任何激活的明胶酶A超过缓慢发生的自溶，但8小时的温育与活化的基质溶解素能够产生64%的活性产生的温育与（4-氨基苯汞）乙酸（APMA）。野生型明胶酶A和突变体酶原，不能成为积极的都被裂解的基质溶解素的低分子量的物种，失去了前肽。这表明基质溶解素通过在不需要任何自溶裂解的过程中去除前肽来激活明胶酶A。
The activation of human progelatinase A by other matrix metalloproteinases was studied by following both the loss of its N-terminal propeptide and the accompanying increase in the rate of hydrolysis of a synthetic substrate. Activated stromelysin 1 was unable to cause any activation of progelatinase A beyond that slowly occuring by autolysis, but an 8 h incubation with activated matrilysin was able to produce 64% of the activity generated by incubation with (4-aminophenylmercuric)acetate (APMA). Wild-type progelatinase A and a mutant proenzyme that cannot become active were both cleaved by matrilysin to a lower molecular weight species that had lost the propeptide. This shows that matrilysin activates progelatinase A by removing the propeptide in a process that does not require any autolytic cleavages.