Nitric oxide synthase 1 (neuronal), also known as NOS1, is an enzyme that in humans is encoded by the NOS1 gene.[5][6]
Quick Facts Available structures, PDB ...
NOS1 |
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![](//upload.wikimedia.org/wikipedia/commons/thumb/f/f0/PDB_1b8q_EBI.jpg/250px-PDB_1b8q_EBI.jpg) |
Available structures |
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PDB | Ortholog search: PDBe RCSB |
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List of PDB id codes |
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4D1N, 4UCH, 4UH5, 4UH6, 4V3U, 5ADF, 5ADG, 5ADI, 5FVX, 5FVW, 5FVU, 5FVV |
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Identifiers |
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Aliases | NOS1, IHPS1, N-NOS, NC-NOS, NOS, bNOS, nNOS, nitric oxide synthase 1 |
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External IDs | OMIM: 163731; MGI: 97360; HomoloGene: 37327; GeneCards: NOS1; OMA:NOS1 - orthologs |
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RNA expression pattern |
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Bgee | Human | Mouse (ortholog) |
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Top expressed in | - body of tongue
- biceps brachii
- Skeletal muscle tissue of biceps brachii
- Skeletal muscle tissue of rectus abdominis
- muscle of thigh
- pons
- gastrocnemius muscle
- spinal ganglia
- buccal mucosa cell
- vastus lateralis muscle
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| Top expressed in | - anterior amygdaloid area
- pontine nuclei
- subiculum
- digastric muscle
- temporal muscle
- mammillary body
- dorsal tegmental nucleus
- ventromedial nucleus
- lateral hypothalamus
- sternocleidomastoid muscle
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| More reference expression data |
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BioGPS | |
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Wikidata |
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Nitric oxide synthases (EC 1.14.13.39) (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.[7] 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.[8]
It has been implicated in asthma,[9][10] schizophrenia,[11][12] restless leg syndrome,[13] and psychostimulant neurotoxicity. It has also been investigated with respect to bipolar disorder[14] and air pollution exposure.[15]
NOS1 has been shown to interact with DLG4[16][17] and NOS1AP.[16]
Kishimoto J, Spurr N, Liao M, Lizhi L, Emson P, Xu W (November 1992). "Localization of brain nitric oxide synthase (NOS) to human chromosome 12". Genomics. 14 (3): 802–4. doi:10.1016/S0888-7543(05)80192-2. PMID 1385308. Reif A, Herterich S, Strobel A, Ehlis AC, Saur D, Jacob CP, Wienker T, Töpner T, Fritzen S, Walter U, Schmitt A, Fallgatter AJ, Lesch KP (March 2006). "A neuronal nitric oxide synthase (NOS-I) haplotype associated with schizophrenia modifies prefrontal cortex function". Mol. Psychiatry. 11 (3): 286–300. doi:10.1038/sj.mp.4001779. PMID 16389274. Winkelmann J, Lichtner P, Schormair B, Uhr M, Hauk S, Stiasny-Kolster K, Trenkwalder C, Paulus W, Peglau I, Eisensehr I, Illig T, Wichmann HE, Pfister H, Golic J, Bettecken T, Pütz B, Holsboer F, Meitinger T, Müller-Myhsok B (February 2008). "Variants in the neuronal nitric oxide synthase (nNOS, NOS1) gene are associated with restless legs syndrome". Mov. Disord. 23 (3): 350–8. doi:10.1002/mds.21647. PMID 18058820. S2CID 42425890. Buttenschön HN, Mors O, Ewald H, McQuillin A, Kalsi G, Lawrence J, Gurling H, Kruse TA (January 2004). "No association between a neuronal nitric oxide synthase (NOS1) gene polymorphism on chromosome 12q24 and bipolar disorder". Am. J. Med. Genet. B Neuropsychiatr. Genet. 124B (1): 73–5. doi:10.1002/ajmg.b.20040. PMID 14681919. S2CID 45596789. Brenman JE, Chao DS, Gee SH, McGee AW, Craven SE, Santillano DR, Wu Z, Huang F, Xia H, Peters MF, Froehner SC, Bredt DS (March 1996). "Interaction of nitric oxide synthase with the postsynaptic density protein PSD-95 and alpha1-syntrophin mediated by PDZ domains". Cell. 84 (5): 757–67. doi:10.1016/S0092-8674(00)81053-3. PMID 8625413. S2CID 15834673.
This article incorporates text from the United States National Library of Medicine, which is in the public domain.