Human lactase-phlorizin hydrolase is not processed by furin, PC1/PC3, PC2, PACE4 and PC5/PC6A of the family of subtilisin-like proprotein processing proteases.
Human lactase-phlorizin hydrolase is not processed by furin, PC1/PC3, PC2, PACE4 and PC5/PC6A of the family of subtilisin-like proprotein processing proteases.
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人乳糖酶-根皮苷水解酶不被枯草杆菌蛋白酶样前蛋白加工蛋白酶家族的弗林蛋白酶、PC1/PC3、PC2、PACE4 和 PC5/PC6A 加工。
DOI：
10.1016/0167-4889(96)00007-9
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发表时间：
1996
期刊：
影响因子：
--
通讯作者：
Sterchi,EE
中科院分区：
文献类型：
--
作者：
Wüthrich,M;Creemers,JW;vandeVen,WJ;Sterchi,EE
人乳糖酶-根皮苷水解酶（LPH，EC 3.2.1.23/62）是一种相对分子质量略高于200 kDa的单链前体糖蛋白（pro-LPH）。成熟为成熟酶（m-LPH，160 kDa）发生在pro-LPH通过高尔基复合体之后，并且涉及849个氨基酸的前肽的蛋白水解去除。这种前肽的作用以及其去除尚未完全了解，并且涉及的蛋白水解酶或酶未知。我们使用基于牛痘病毒的共表达系统在猪肾PK（15）细胞中研究了枯草杆菌蛋白酶样前蛋白加工蛋白酶家族的五个不同成员在人LPH成熟过程中的潜在作用。感染/转染的PK（15）细胞表达全长pro-LPH，但未观察到成熟为m-LPH。人pro-LPH与人弗林蛋白酶、人PC 1/PC 3、人PC 2、人PACE 4和小鼠PC 6A在PK（15）细胞中的共表达没有导致酶的成熟。使用血管性血友病因子前体（pro-vWF）的切割和分泌作为阳性对照。所测试的五种前蛋白加工蛋白酶中没有一种能够切割人pro-LPH，这强烈表明它们不参与该酶的成熟。
Human lactase-phlorizin hydrolase (LPH, EC 3.2.1.23/62) is synthesized as a single-chain precursor glycoprotein (pro-LPH) with a relative molecular mass of just over 200 kDa. Maturation to the mature enzyme (m-LPH, 160 kDa) occurs after passage of pro-LPH through the Golgi complex and involves the proteolytic removal of a 849 amino acid propeptide. The role of this propeptide as well as its removal is not fully understood and the proteolytic enzyme or enzymes involved are unknown. We studied the potential role of five different members of the family of subtilisin-like proprotein processing proteases in the maturation process of human LPH using a vaccinia virus based coexpression system in pig kidney PK(15) cells. Infected/transfected PK(15) cells expressed full-length pro-LPH but no maturation to m-LPH was observed. Coexpression of human pro-LPH with human furin, human PC1/PC3, human PC2, human PACE4 and mouse PC6A in PK(15) cells did not result in maturation of the enzyme. Cleavage and secretion of von Willebrand factor precursor (pro-vWF) was used as a positive control. None of the five proprotein processing proteases tested were capable of cleaving human pro-LPH, strongly suggesting that they are not involved in the maturation of this enzyme.