MOLECULAR CHARACTERIZATION OF HUMAN AND BOVINE ENDOTHELIN-CONVERTING ENZYME (ECE-1)

被引：177

作者：

SCHMIDT, M ^{[1
]}

KROGER, B ^{[1
]}

JACOB, E ^{[1
]}

SEULBERGER, H ^{[1
]}

SUBKOWSKI, T ^{[1
]}

OTTER, R ^{[1
]}

MEYER, T ^{[1
]}

SCHMALZING, G ^{[1
]}

HILLEN, H ^{[1
]}

机构：

[1] MAX PLANCK INST BIOPHYS,D-60528 FRANKFURT,GERMANY

来源：

FEBS LETTERS | 1994年 / 356卷 / 2-3期

关键词：

ENDOTHELIN-1; ENDOTHELIN CONVERTING ENZYME;

D O I：

10.1016/0014-5793(94)01277-6

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：

A membrane-bound protease activity that specifically converts Big endothelin-1 has been purified from bovine endothelial cells (FBHE). The enzyme was cleaved with trypsin and the peptide sequencing analysis confirmed it to be a zinc chelating metalloprotease containing the typical HEXXH (HELTH) motif. RT-PCR and cDNA screens were employed to isolate the complete cDNAs of the bovine and human enzymes. This human metalloprotease was expressed heterologously in cell culture and oocytes. The catalytic activity of the recombinant enzyme is the same as that determined for the natural enzyme. The data suggest that the characterized enzyme represents the functional human endothelin converting enzyme ECE-1.

引用

页码：238 / 243

页数：6

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