ENDOTHELIN-CONVERTING ENZYME-ACTIVITY IN HUMAN SERUM-LIPOPROTEIN FRACTION

被引：8

作者：

OHWAKI, T ^{[1
]}

SAKAI, H ^{[1
]}

HIRATA, Y ^{[1
]}

机构：

[1] TOKYO MED & DENT UNIV,DEPT INTERNAL MED 2,BUNKYO KU,TOKYO 113,JAPAN

来源：

FEBS LETTERS | 1993年 / 320卷 / 02期

关键词：

ENDOTHELIN; LIPOPROTEIN; ENDOTHELIN CONVERTING ENZYME;

D O I：

10.1016/0014-5793(93)80084-8

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-1 (ET-1)-converting enzyme (ECE) activity in the human serum lipoprotein fraction was studied using a sensitive enzyme immunoassay and reverse-phase high performance liquid chromatography. The ECE activity of cleaving synthetic human big ET-1 into ET-1 by the serum lipoprotein fraction was about 14-times greater than that by whole serum, and the activity was closely associated with lipoprotein itself. The lipoprotein ECE activity, which was optimal at pH 7.0, was inhibited by EDTA, o-phenanthroline, phosphoramidon, thiorphan, phenylmethane-sulfonyl fluoride and chymostatin, but not by cysteine or aspartic proteinase inhibitors, suggesting metalloproteinase- and chymotrypsin-like properties. These results suggest that the serum lipoprotein ECE may be involved in the processing of big ET-1 to ET-1 in the circulatory system.

引用

页码：165 / 168

页数：4

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