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Review
. 1999 Dec;80(6):291-303.
doi: 10.1046/j.1365-2613.1999.00137.x.

Endothelial nitric oxide in humans in health and disease

P Vallance  1 , A Hingorani
Affiliations
Review

Endothelial nitric oxide in humans in health and disease

P Vallance et al. Int J Exp Pathol. 1999 Dec.
No abstract available

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Figures

Figure 1
Figure 1
Nitric oxide (NO) is synthesized from l-arginine and oxygen by the action of nitric oxide synthase. This process can be inhibited by NG monomethyl-l-arginine (L-NMMA). Once synthesized, the NO duffuses to target cells. In the process of diffusion it may be destroyed or stablised by interaction with other molecules (x). The major physiological target enzyme for NO is guanylyl cyclase (GC). This enzyme is activated when NO binds to its haem moiety. GC converts guanosine triphosphate (GTP) to cyclic guanosine monophosphate (cGMP).
Figure 2
Figure 2
Basal nitric oxide generation in the human forearm. L-NMMA produces a dose-dependent fall in resting forearm blood flow. L-NMMA (1, 2 and 4 μmol/min) was infused into the brachial artery of one arm and blood flow measured in both arms. Local inhibition of nitric oxide synthesis leads to a substantial fall in resting flow and an increase in peripheral resistance in the infused arm (▪), with no change in flow in the control arm (□).
Figure 3
Figure 3
Polymorphisms of the human endothelial nitric oxide synthase gene (NOS 3). (a) illustrates the gene structure intron/exon arrangement and polymorphisms of the human NOS. 3 gene. Single nucleotide bi-allelic polymorphisms are shown above the gene. The variable number tandem repeat (VNTR) polymorphism in intron 4 is also bi-allelic with individuals having 4 or 5 repeats of a 27-bp sequence element. The multiallelic CA repeat polymorphism in intron 13 is highly polymorphic with allele sizes ranging from 18 to 36 CA repeats (Reproduced with permission from Hingorani 1997).
Figure 4
Figure 4
Synthesis and metabolism of ADMA. l-arginine is converted to nitric oxide by nitric oxide synthase. However, it can also be converted to the inhibitor ADMA. The precise synthetic route is not clear but probably involves methylation of arginine residues in proteins. Free ADMA is metabolized to citrulline by the action of dimethylarginine dimethylaminohydrolase (DDAH). Citrulline is subsequently recycled to arginine.
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