Cloning and expression of novel mosaic serine proteases with and without a transmembrane domain from human lung

被引：50

作者：

Kim, DR ^{[1
]}

Sharmin, S ^{[1
]}

Inoue, M ^{[1
]}

Kido, H ^{[1
]}

机构：

[1] Univ Tokushima, Inst Enzyme Res, Div Enzyme Chem, Tokushima 7708503, Japan

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-GENE STRUCTURE AND EXPRESSION | 2001年 / 1518卷 / 1-2期

基金：

日本学术振兴会;

关键词：

serine protease; transmembrane domain; mosaic protein; cDNA sequence; human lung; expression;

D O I：

10.1016/S0167-4781(01)00184-1

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Two cDNAs encoding novel mosaic proteins with a serine protease domain and potential regulatory modules, consisting of a protein kinase substrate and a low-density lipoprotein receptor, were cloned from a human lung cDNA library by PCR. One with a transmembrane domain (MSPL) and the other without one (MSPS) comprise 581 and 537 amino acids, respectively. Except for the C-terminal ends, the two isoforms had an identical serine protease domain exhibiting 42, 39 and 43% identity with those of plasma kallikrein, hepsin and transmembrane protease serine 2, respectively. Both genes were predominantly expressed in human lung, placenta, pancreas and prostate. (C) 2001 Elsevier Science B.V. All rights reserved.

引用

页码：204 / 209

页数：6

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