Barnes K, Turner A J
Department of Biochemistry and Molecular Biology, University of Leeds, United Kingdom.
Neurochem Res. 1997 Aug;22(8):1033-40. doi: 10.1023/a:1022435111928.
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). In 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.
生物活性血管活性肽——内皮素（ETs），是由无活性的中间体大内皮素，通过锌金属蛋白酶——内皮素转化酶（ECE）催化的独特加工过程产生的。在本综述中，我们研究了内皮素在大脑中的作用，并重点关注ECE的结构和细胞定位。讨论了ET-1、ET-2和ET-3在大脑中的异质性分布与其血液动力学、促有丝分裂和增殖特性以及它们作为神经递质的可能作用。将ECE在神经元和神经胶质细胞中的细胞和亚细胞定位与其他脑细胞膜金属蛋白酶——中性内肽酶-24.11（脑啡肽酶）、血管紧张素转换酶和氨肽酶N进行了比较，这些酶均参与神经肽的加工和代谢。与这些外切酶不同，ECE在细胞中表现出双重定位，存在于质膜上，并且在某些情况下，集中在核周区域。这种差异定位可能反映了不同ECE同工型——ECE-1α、ECE-1β和ECE-2的不同靶向作用。
