The endothelin system and endothelin-converting enzyme in the brain: Molecular and cellular studies

被引：42

作者：

Barnes, K ^{[1
]}

Turner, AJ ^{[1
]}

机构：

[1] UNIV LEEDS,DEPT BIOCHEM & MOL BIOL,LEEDS LS2 9JT,W YORKSHIRE,ENGLAND

来源：

NEUROCHEMICAL RESEARCH | 1997年 / 22卷 / 08期

基金：

英国医学研究理事会;

关键词：

endothelin; endothelin converting enzyme; metalloprotease; neutral endopeptidase; aminopeptidases;

D O I：

10.1023/A:1022435111928

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：

The biologically active vasoactive peptides, the endothelins (ETs), are generated from inactive intermediates, the big endothelins, by a unique processing event catalysed by the zinc metalloprotease, endothelin converting enzyme (ECE). Zn this overview we examine the actions of endothelins in the brain, and focus on the structure and cellular locations of ECE. The heterogeneous distribution in the brain of ET-1, ET-2, and ET-3 is discussed in relation to their hemodynamic, mitogenic and proliferative properties as well as their possible roles as neurotransmitters. The cellular and subcellular localization of ECE in neuronal and in glial cells is compared with that of other brain membrane metalloproteases, neutral endopeptidase-24.11 (neprilysin), angiotensin converting enzyme and aminopeptidase N, which all function in neuropeptide processing and metabolism. Unlike these ectoenzymes, ECE exhibits a dual localisation in the cell, being present on the plasma membrane and also, in some instances, being concentrated in a perinuclear region. This differential localization may reflect distinct targeting of different ECE isoforms, ECE-1 alpha, ECE-1 beta, and ECE-2.

引用

页码：1033 / 1040

页数：8

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