Cloning and characterization of the cDNA for human airway trypsin-like protease
Cloning and characterization of the cDNA for human airway trypsin-like protease
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DOI：
10.1074/jbc.273.19.11895
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发表时间：
1998-05-08
影响因子：
4.8
通讯作者：
Yasuoka, S
中科院分区：
文献类型：
--
作者：
Yamaoka, K;Masuda, K;Yasuoka, S
以前我们从慢性气道疾病患者的痰中分离出一种胰蛋白酶样酶，称为人气道胰蛋白酶样蛋白酶。本文介绍了cDNA的克隆、由cDNA推断出的初级蛋白结构的特征，以及该酶在人体各种组织中的基因表达。我们获得了全长1517个碱基对的cDNA序列，其中一个开放阅读框编码了一个含有418个氨基酸残基的多肽。该多肽由一个232个残基的催化区和一个186个残基的非催化区组成，在NH2末端附近有一个推测为疏水的跨膜结构域。该多肽被认为是一种II型完整膜蛋白，其中cooh末端催化区位于细胞外。因此，该蛋白被认为是作为一种膜结合前体合成的，并通过有限的蛋白水解成熟为一种可溶的活性蛋白酶。在催化区序列上，它与人的hepsin、enterop肽酶、acrosin和肥大细胞胰蛋白酶的同源性为29-38%。非催化区与其他已知的蛋白质几乎没有相似之处。在Northern blot分析中，在17个被检查的人体组织中，在气管中检测到1.9千碱基的转录本最为显著。
Previously we isolated a trypsin-like enzyme designated human airway trypsin-like protease from the sputum of patients with chronic airway diseases. This paper describes the cDNA cloning, characterization of the primary protein structure deduced from the cDNA, and gene expression of this enzyme in various human tissues. We obtained an entire 1517-base pair sequence of cDNA with an open reading frame encoding a polypeptide with 418-amino acid residues. The polypeptide consisted of a 232-residue catalytic region and a 186-residue noncatalytic region with a hydrophobic putative transmembrane domain near the NH2 terminus. The polypeptide was suggested to be a type II integral membrane protein in which the COOH-terminal catalytic region is extracellular. Therefore, this protein is thought to be synthesized as a membrane-bound precursor and to mature to a soluble and active protease by limited proteolysis, It showed 29-38% identity in the sequence of the catalytic region with human hepsin, enteropeptidase, acrosin, and mast cell tryptase. The noncatalytic region had little similarity to other known proteins. In Northern blot analysis a transcript of 1.9 kilobases was detectable most prominently in the trachea among 17 human tissues examined.