Arai H, Hosoda K, Shirakami G, Yoshimasa T, Nakao K
Department of Medicine, Kyoto University School of Medicine.
Nihon Rinsho. 1993 Jun;51(6):1530-9.
Endothelin (ET) was initially identified as a potent vasoconstrictor peptide with 21 amino-acid residues, produced by cultured porcine aortic endothelial cells. Cloning of the ET genes revealed the existence of three isopeptides, ET-1, ET-2 and ET-3, which are widely distributed in a variety of tissues and possess wide variety of pharmacological functions. Recently, two subtypes of ET receptor have been isolated by the expression cloning technique and the molecular characteristics of the receptors were elucidated. Subsequently, the structural organizations of the ET receptor genes have been investigated. This article discusses the structure, function and expression of ET ligands and receptors from the molecular biological aspect.
内皮素（ET）最初被鉴定为一种由培养的猪主动脉内皮细胞产生的、具有21个氨基酸残基的强效血管收缩肽。ET基因的克隆揭示了三种异肽的存在，即ET-1、ET-2和ET-3，它们广泛分布于多种组织中，并具有多种药理功能。最近，通过表达克隆技术分离出了两种ET受体亚型，并阐明了这些受体的分子特征。随后，对ET受体基因的结构组织进行了研究。本文从分子生物学角度探讨了ET配体和受体的结构、功能及表达。
