Endothelial nitric oxide synthase in the microcirculation

被引：0
作者：
Xiaohong Shu
T. C. Stevenson Keller
Daniela Begandt
Joshua T. Butcher
Lauren Biwer
Alexander S. Keller
Linda Columbus
Brant E. Isakson
机构：
[1] Dalian Medical University,College of Pharmacy
[2] University of Virginia School of Medicine,Robert M. Berne Cardiovascular Research Center
[3] University of Virginia School of Medicine,Department of Molecular Physiology and Biophysics
[4] University of Virginia School of Medicine,Department of Pharmacology
[5] University of Virginia,Department of Chemistry
来源：
Cellular and Molecular Life Sciences | 2015年 / 72卷
关键词：
Endothelial nitric oxide synthase; Nitric oxide; Endothelium; Microcirculation;
D O I：
暂无
中图分类号：
学科分类号：
摘要：
Endothelial nitric oxide synthase (eNOS, NOS3) is responsible for producing nitric oxide (NO)—a key molecule that can directly (or indirectly) act as a vasodilator and anti-inflammatory mediator. In this review, we examine the structural effects of regulation of the eNOS enzyme, including post-translational modifications and subcellular localization. After production, NO diffuses to surrounding cells with a variety of effects. We focus on the physiological role of NO and NO-derived molecules, including microvascular effects on vessel tone and immune response. Regulation of eNOS and NO action is complicated; we address endogenous and exogenous mechanisms of NO regulation with a discussion of pharmacological agents used in clinical and laboratory settings and a proposed role for eNOS in circulating red blood cells.
引用
收藏
页码：4561 / 4575
页数：14
相关论文
共 951 条
[1]  
Roman LJ(2002)Intrinsic and extrinsic modulation of nitric oxide synthase activity Chem Rev 102 1179-1190
[2]  
Martásek P(2014)Holoenzyme structures of endothelial nitric oxide synthase—an allosteric role for calmodulin in pivoting the FMN domain for electron transfer J Struct Biol 188 46-54
[3]  
Masters BS(2014)Solution structure of calmodulin bound to the target peptide of endothelial nitric oxide synthase phosphorylated at Thr495 Biochemistry 53 1241-1249
[4]  
Volkmann N(1998)Structure of nitric oxide synthase oxygenase dimer with pterin and substrate Science 279 2121-2126
[5]  
Martásek P(1994)Cysteine 184 of endothelial nitric oxide synthase is involved in heme coordination and catalytic activity J Biol Chem 269 25062-25066
[6]  
Roman LJ(1995)Cysteine 99 of endothelial nitric oxide synthase (NOS-III) is critical for tetrahydrobiopterin-dependent NOS-III stability and activity Biochem Biophys Res Commun 215 1119-1129
[7]  
Xu XP(1999)Structural characterization of nitric oxide synthase isoforms reveals striking active-site conservation Nat Struct Biol 6 233-242
[8]  
Page C(1997)Calmodulin promotes dimerization of the oxygenase domain of human endothelial nitric-oxide synthase J Biol Chem 272 12030-12034
[9]  
Swift M(2000)The autoinhibitory control element and calmodulin conspire to provide physiological modulation of endothelial and neuronal nitric oxide synthase activity Acta Physiol Scand 168 53-63
[10]  
Hanein D(2002)Disabling a C-terminal autoinhibitory control element in endothelial nitric-oxide synthase by phosphorylation provides a molecular explanation for activation of vascular NO synthesis by diverse physiological stimuli J Biol Chem 277 19087-19094
12345678910