The type II transmembrane serine protease Matriptase-2 - identification, structural features, enzymology, expression pattern and potential roles
The type II transmembrane serine protease Matriptase-2 - identification, structural features, enzymology, expression pattern and potential roles
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DOI：
10.2741/2702
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发表时间：
2008-01-01
影响因子：
3.1
通讯作者：
Hooper, John D.
中科院分区：
文献类型：
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作者：
Ramsay, Andrew J.;Reid, Janet C.;Hooper, John D.
间质蛋白酶-2（也称为TMPRSS 6）是最近鉴定的II型跨膜丝氨酸蛋白酶（TTSP）家族的成员。在结构上，这种酶含有短的胞质氨基末端尾，跨膜区，含有两个CUB结构域和三个LDL受体A类结构域的茎区，以及在羧基末端的胰蛋白酶样丝氨酸蛋白酶结构域。间质蛋白酶-2基因及其编码蛋白在哺乳动物中高度保守。在生物化学上，间质蛋白酶-2具有与结构上相关的蛋白质间质蛋白酶（也称为MT-SP1）相似的底物特异性。虽然间质蛋白酶-2的病理生理功能尚不清楚，但其在肝脏和几种癌症中的高mRNA表达表明，这种酶与其他TTSP类似，可能在正常和疾病状态下具有重要的细胞表面相关作用。本文综述了间质蛋白酶-2的鉴定，总结了其结构特征、生物化学、表达模式和疾病相关性，并讨论了其潜在的功能。
Matriptase-2 (also known as TMPRSS6) is a recently identified member of the type II transmembrane serine protease (TTSP) family. Structurally this enzyme contains a short cytoplasmic amino terminal tail, a transmembrane region, a stem region containing two CUB domains and three LDL receptor class A domains, and at the carboxy terminal a trypsin-like serine protease domain. The matriptase-2 gene and encoded protein are highly conserved in mammals. Biochemically matriptase-2 has substrate specificity similar to the structurally related protein matriptase (also known as MT-SP1). Although the patho-physiological functions of matriptase-2 are not known, its high mRNA expression in liver and several cancers indicate that this enzyme, similar to other TTSPs, will likely have important cell surface associated roles in normal and disease states. Here we overview the identification of matriptase-2, summarise its structural features, biochemistry, expression pattern and disease associations and discuss its potential functions.