NOS1

Also known as IHPS1, N-NOS, NC-NOS, NOS, bNOS, nNOS, nitric oxide synthase 1

Nitric oxide synthase 1 (neuronal), also known as NOS1, is an enzyme that in humans is encoded by the NOS1 gene.

Gene data

NOS1

Name: nitric oxide synthase 1
Type: protein-coding
Position: 117,208,142–117,452,170 (−)
Aliases: IHPS1, N-NOS, NC-NOS, NOS, bNOS, nNOS
Ensembl: ENSG00000089250
RefSeq RNA: NM_000620.5, NM_001204213.2, NM_001204214.2, NM_001204218.2
RefSeq protein: NP_000611.1, NP_001191142.1, NP_001191143.1, NP_001191147.1

The protein encoded by this gene belongs to the family of nitric oxide synthases, which synthesize nitric oxide from L-arginine. Nitric oxide is a reactive free radical, which acts as a biologic mediator in several processes, including neurotransmission, and antimicrobial and antitumoral activities. In the brain and peripheral nervous system, nitric oxide displays many properties of a neurotransmitter, and has been implicated in neurotoxicity associated with stroke and neurodegenerative diseases, neural regulation of smooth muscle, including peristalsis, and penile erection. This protein is ubiquitously expressed, with high level of expression in skeletal muscle. Multiple transcript variants that differ in the 5' UTR have been described for this gene but the full-length nature of these transcripts is not known. Additionally, alternatively spliced transcript variants encoding different isoforms (some testis-specific) have been found for this gene.[provided by RefSeq, Feb 2011].

Article

6 sections

Contents

Function
Clinical significance
Interactions
See also
References
Further reading

Nitric oxide synthase 1 (neuronal), also known as NOS1, is an enzyme that in humans is encoded by the NOS1 gene.

== Function == Nitric oxide synthases () (NOSs) are a family of synthases that catalyze the production of nitric oxide (NO) from L-arginine. NO is a chemical messenger with diverse functions throughout the body depending on its enzymatic source and tissue localization. In the brain and peripheral nervous system, where NOS1 is largely present, NO displays many properties of a neurotransmitter and may be involved in long term potentiation. It is implicated in neurotoxicity associated with stroke and neurodegenerative diseases, neural regulation of smooth muscle, including peristalsis and sphincter relaxation, and penile erection. NO is also responsible for endothelium-derived relaxing factor activity regulating blood pressure as produced from its related enzyme NOS3. In macrophages, NO mediates tumoricidal and bactericidal actions, as produced from its related enzyme NOS2. Various pharmacological inhibitors of NO synthases (NOS) block these effects, but further distinction of their function has been elucidated by animal models in which these specific genes have been inactivated. Neuronal NOS (NOS1), Endothelial NOS (NOS3), and Inducible NOS macrophage NOS are distinct isoforms. Both the neuronal and the macrophage forms are unusual among oxidative enzymes in requiring several electron donors: flavin adenine dinucleotide (FAD), flavin mononucleotide (FMN), NADPH, and tetrahydrobiopterin.