CONVERSION OF BIG ENDOTHELIN ISOPEPTIDES TO MATURE ENDOTHELIN ISOPEPTIDES BY CULTURED BOVINE ENDOTHELIAL-CELLS

被引:8
作者
OHNAKA, K
TAKAYANAGI, R
OHASHI, M
NAWATA, H
机构
[1] The Third Department of Internal Medicine, Faculty of Medicine, Kyushu University, Fukuoka
关键词
ENDOTHELIN; BIG ENDOTHELIN; ENDOTHELIN-CONVERTING ENZYME; ENDOTHELIAL CELLS;
D O I
10.1097/00005344-199100177-00006
中图分类号
R5 [内科学];
学科分类号
1002 ; 100201 ;
摘要
Both the soluble and membrane fractions prepared from cultured bovine endothelial cells (ECs) possessed the converting activities to metabolize big endothelin-1 (big ET-1) to endothelin-1 (ET-1) at neutral pH. Metal chelators inhibited the activities of both fractions, whereas phosphoramidon, a metalloprotease inhibitor, strongly inhibited only the activity of the membrane fraction. Phosphoramidon reduced the secretion of ET-1 and concomitantly enhanced the release of big ET-1 from cultured ECs. The incubations of big ET-1, big ET-2, and big ET-3 with cultured ECs resulted in their conversions to mature ETs. Phosphoramidon also abolished these conversions. These results indicate that vascular endothelium can convert not only endogenous big ET-1 but also exogenous big ET isopeptides to their mature ETs through a phosphoramidon-sensitive neutral metalloprotease.
引用
收藏
页码:S17 / S19
页数:3
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