Activation of a recombinant membrane type 1-matrix metalloproteinase (MT1-MMP) by furin and its interaction with tissue inhibitor of metalloproteinases (TIMP)-2
Activation of a recombinant membrane type 1-matrix metalloproteinase (MT1-MMP) by furin and its interaction with tissue inhibitor of metalloproteinases (TIMP)-2
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DOI：
10.1016/0014-5793(96)00861-7
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发表时间：
1996-09-09
期刊：
影响因子：
3.5
通讯作者：
Seiki, M
中科院分区：
文献类型：
--
作者：
Sato, H;Kinoshita, T;Seiki, M
膜1型基质金属蛋白酶（MT 1-MMP）通过切割Asn（66）-Leu肽键启动酶原明胶酶A/72-kDa IV型胶原酶的活化。我们先前指出MT 1-MMP具有独特的氨基酸序列Arg-Arg-Lys-Arg（111），该序列是弗林蛋白酶样蛋白酶的潜在识别序列（Nature，370（1994）61-65），在此，使用在大肠杆菌中表达的重组MT 1-MMP，我们证明弗林蛋白酶在体外特异性地切割Arg（111）-Tyr之间的MT 1-MMP，这导致对明胶酶A激活功能的刺激，金属蛋白酶组织抑制剂（TIMP）-2通过与活化的MT 1-MMP形成稳定的复合物来抑制明胶酶A的活化。
Membrane type 1-matrix metalloproteinase (MT1-MMP) initiates the activation of the zymogen progelatinase A/72-kDa type IV collagenase by cleavage of the Asn(66)-Leu peptide bond, We previously pointed out that MT1-MMP possesses a unique amino acid sequence Arg-Arg-Lys-Arg(111) which is a potential recognition sequence for furin-like proteases (Nature, 370 (1994) 61-65), Here, using a recombinant MT1-MMP expressed in Escherichia coli we demonstrated that furin specifically cleaves MT1-MMP between Arg(111)-Tyr in vitro, which resulted in a stimulation of progelatinase A-activation function, Tissue inhibitor of metalloproteinases (TIMP)-2 inhibited activation of progelatinase A by forming a stable complex with activated MT1-MMP.