STRUCTURE AND FUNCTION OF NITRIC-OXIDE SYNTHASES

被引：42

作者：

HATTORI, R ^{[1
]}

SASE, K ^{[1
]}

EIZAWA, H ^{[1
]}

KOSUGA, K ^{[1
]}

AOYAMA, T ^{[1
]}

INOUE, R ^{[1
]}

SASAYAMA, S ^{[1
]}

KAWAI, C ^{[1
]}

YUI, Y ^{[1
]}

机构：

[1] KYOTO UNIV,FAC MED,DEPT INTERNAL MED,DIV 3,KYOTO 60601,JAPAN

来源：

INTERNATIONAL JOURNAL OF CARDIOLOGY | 1994年 / 47卷 / 01期

关键词：

NITRIC OXIDE; NITRIC OXIDE SYNTHASE; ISOFORMS;

D O I：

10.1016/0167-5273(94)90329-8

中图分类号：

R5 [内科学];

学科分类号：

1002 ; 100201 ;

摘要：

Nitric oxide (NO), which accounts for the biological activity of endothelium-derived relaxing factor, is now thought to play a variety of roles in the nervous system and in immunologic reactions. NO is synthesized from L-arginine by nitric oxide synthase (NOS). There are three isoforms of NOS; type I (neuronal), type II (inducible), and type III (endothelial). The fundamental structure of the three isoforms, which contain calmodulin-, FMN-, FAD-, and NADPH-binding domains, is the same. Calmodulin is already bound to inducible NOS without requiring Ca2+, while the others are Ca2+/calmodulin-dependent. Endothelial NOS is bound to membranes by N-myristoylation, while the other isoforms are soluble. The human endothelial NOS gene has been cloned. It has several highly repetitive regions which could provide potential sites for DNA polymorphism. It might be of interest to examine the relationship between such polymorphism and cardiovascular disorders.

引用

页码：S71 / S75

页数：5

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