A COMPARISON OF THE PROPERTIES AND ENZYMATIC-ACTIVITIES OF 3 ANGIOTENSIN PROCESSING ENZYMES - ANGIOTENSIN-CONVERTING ENZYME, PROLYL ENDOPEPTIDASE AND NEUTRAL ENDOPEPTIDASE 24.11

被引：250

作者：

WELCHES, WR ^{[1
]}

BROSNIHAN, KB ^{[1
]}

FERRARIO, CM ^{[1
]}

机构：

[1] BOWMAN GRAY SCH MED, CTR HYPERTENS, DEPT SURG SCI, WINSTON SALEM, NC 27157 USA

来源：

LIFE SCIENCES | 1993年 / 52卷 / 18期

关键词：

D O I：

10.1016/0024-3205(93)90108-F

中图分类号：

R-3 [医学研究方法]; R3 [基础医学];

学科分类号：

1001 ;

摘要：

The discovery of angiotensin-(1-7) [Ang-(1-7)] as a bioactive Ang II fragment of the renin-angiotensin system (RAS) alters the current understanding of the enzymatic components that comprise the RAS cascade. Two neutral endopeptidases, prolyl endopeptidase (E.C. 3.4.21.26) and neutral endopeptidase 24.11 (E.C. 3.4.24.11), are capable of forming Ang-(1-7) from Ang I and have been implicated in the in vivo processing of Ang I. This makes them putative Ang processing enzymes and part of the RAS cascade. This review summarizes the physical characteristics and distribution of angiotensin converting enzyme (E.C. 3.4.15.1), a known Ang I processing enzyme, and compares its features to what is known of prolyl endopeptidase and neutral endopeptidase 24.11.

引用

页码：1461 / 1480

页数：20

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