去亮氨酸血管紧张素I：生物合成与饮水反应

Des-Leu angiotensin I: biosynthesis and drinking response.

作者信息

Changaris D G, Porter J L, Miller J J, Levy R S

机构信息

University of Louisville School of Medicine, Health Sciences Center, KY 40292.

出版信息

Regul Pept. 1988 Apr;20(4):273-80. doi: 10.1016/0167-0115(88)90062-6.

DOI:10.1016/0167-0115(88)90062-6

PMID:3285377

Abstract

The crude rat and bovine synaptosomal lysate from brain can hydrolyze angiotensin I (AI) to des-Leu angiotensin I (AI-dL) and no further. This cytosolic enzyme has a specificity for angiotensin-related sequences, R-His-Pro-Phe-His-Leu and therefore named angiotensin-related carboxypeptidase (ARC). These studies led to the biosynthesis and purification of AI-dL in order to determine if it can provoke a drinking response. This nonapeptide is a potent dipsogen when injected into the cerebroventricles of rats. The drinking response probably requires a second hydrolysis to angiotensin II (AII) since both captopril and saralasin can inhibit this response.

摘要

来自大鼠和牛脑的粗制突触体裂解物可将血管紧张素I（AI）水解为去亮氨酸血管紧张素I（AI-dL），且不能进一步水解。这种胞质酶对血管紧张素相关序列R-His-Pro-Phe-His-Leu具有特异性，因此被命名为血管紧张素相关羧肽酶（ARC）。这些研究促使人们对AI-dL进行生物合成和纯化，以确定它是否能引发饮水反应。当将这种九肽注射到大鼠脑室中时，它是一种有效的致渴剂。由于卡托普利和沙拉新都能抑制这种反应，因此饮水反应可能需要进一步水解为血管紧张素II（AII）。