大鼠肠道、脑膜及血清中肠抑素的代谢：脯氨酸特异性肽酶的不同作用

Metabolism of enterostatin in rat intestine, brain membranes, and serum: differential involvement of proline-specific peptidases.

作者信息

Bouras M, Huneau J F, Luengo C, Erlanson-Albertsson C, Tomé D

机构信息

INRA, Unité de nutrition Humaine et Physiologie Intestinale, Faculté de Pharmacie, Paris, France.

出版信息

Peptides. 1995;16(3):399-405. doi: 10.1016/0196-9781(94)00213-p.

DOI:10.1016/0196-9781(94)00213-p

PMID:7651891

Abstract

The degradation of enterostatin (VPDPR), a potent inhibitor of food intake, by intestinal brush-border membranes, brain membranes, and rat serum has been investigated in the presence of specific inhibitors. Hydrolysis by intestinal membranes was found to be 10 and 100 times faster than in serum and brain membranes, respectively. Enterostatin hydrolysis by intestinal and brain membranes involves the removal of C-terminal arginine by carboxypeptidase P, leading to the production of des-Arg-enterostatin, and the splitting of the Pro2-Asp3 bond by dipeptidyl aminopeptidase IV (DPP IV). A small amount of the potent anorectic peptide Pro2-Asp3-Pro4 was released during hydrolysis of des-Arg-enterostatin by brain membranes and rat serum. In rat serum, enterostatin degradation was mainly due to DPP IV.

摘要

在存在特异性抑制剂的情况下，对肠道刷状缘膜、脑膜和大鼠血清对强效食欲抑制剂肠抑素（VPDPR）的降解情况进行了研究。发现肠膜的水解速度分别比血清和脑膜快10倍和100倍。肠膜和脑膜对肠抑素的水解涉及羧肽酶P去除C末端精氨酸，产生去精氨酸肠抑素，以及二肽基氨基肽酶IV（DPP IV）裂解Pro2-Asp3键。在脑膜和大鼠血清对去精氨酸肠抑素的水解过程中，释放出少量强效的食欲抑制肽Pro2-Asp3-Pro4。在大鼠血清中，肠抑素的降解主要归因于DPP IV。