CLONING AND FUNCTIONAL EXPRESSION OF HUMAN ENDOTHELIN-CONVERTING ENZYME CDNA

被引：119

作者：

SHIMADA, K ^{[1
]}

MATSUSHITA, Y ^{[1
]}

WAKABAYASHI, K ^{[1
]}

TAKAHASHI, M ^{[1
]}

MATSUBARA, A ^{[1
]}

IIJIMA, Y ^{[1
]}

TANZAWA, K ^{[1
]}

机构：

[1] SANKYO CO LTD,PHARMACOL & MOLEC BIOL RES LABS,SHINJUKU KU,TOKYO 140,JAPAN

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1995年 / 207卷 / 02期

关键词：

D O I：

10.1006/bbrc.1995.1258

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：

Endothelin (ET) is a 21-residue potent vasoconstrictive peptide produced by vascular endothelial cells and formed from its precursor, big endothelin (big ET), by endothelin-converting enzyme (ECE). This paper describes the cloning and functional expression of a cDNA encoding a human ECE from human umbilical vein endothelial cells (HUVEC). Human ECE consists of 758 amino acid residues and has high homology to rat and bovine ECE. Immunoblot analysis using a monoclonal antibody risen against rat lung ECE showed the presence of immunoreactive protein in membrane fraction prepared from both HUVEC and COS-1 cells transfected with human ECE cDNA. Both COS-1 cells expressing human ECE and its membrane fraction converted big ET-1 most efficiently among big ETs. (C) 1995 Academic Press, Inc.

引用

页码：807 / 812

页数：6

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