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| Nitric-oxide synthase | |||||||||
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Human inducible nitric oxide synthase. PDB 1nsi
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| Identifiers | |||||||||
| EC number | 1.14.13.39 | ||||||||
| CAS number | 125978-95-2 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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| Nitric oxide synthase, oxygenase domain | |||||||||
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Structure of endothelial nitric oxide synthase heme domain.[1]
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| Identifiers | |||||||||
| Symbol | NO_synthase | ||||||||
| Pfam | PF02898 | ||||||||
| InterPro | IPR004030 | ||||||||
| SCOP | 1nos | ||||||||
| SUPERFAMILY | 1nos | ||||||||
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Nitric oxide synthases (EC 1.14.13.39) (NOSs) are a family of enzymes catalyzing the production of nitric oxide (NO) from L-arginine. NO is an important cellular signaling molecule. It helps modulate vascular tone, insulin secretion, airway tone, and peristalsis, and is involved in angiogenesis and neural development. It may function as a retrograde neurotransmitter. Nitric oxide is mediated in mammals by the calcium-calmodulin controlled isoenzymes eNOS (endothelial NOS) and nNOS (neuronal NOS). The inducible isoform, iNOS, is involved in immune response, binds calmodulin at physiologically relevant concentrations, and produces NO as an immune defense mechanism, as NO is a free radical with an unpaired electron. It is the proximate cause of septic shock and may function in autoimmune disease.
NOS catalyzes the reaction:[2]
- 2 L-arginine + 3 NADPH + 3 H+ + 4 O2 2 citrulline +2 nitric oxide + 4 H2O + 3 NADP+
NOS isoforms catalyze other leak and side reactions, such as superoxide production at the expense of NADPH. As such, this stoichiometry is not generally observed, and reflects the three electrons supplied per NO by NADPH.
NOSs are unusual in that they require five cofactors. Eukaryotic NOS isozymes are catalytically self-sufficient. The electron flow in the NO synthase reaction is: NADPH → FAD → FMN → heme → O2. Tetrahydrobiopterin provides an additional electron during the catalytic cycle which is replaced during turnover. NOS is the only known enzyme that binds flavin adenine dinucleotide (FAD), flavin mononucleotide (FMN), heme, tetrahydrobiopterin (BH4) and calmodulin.[citation needed]
Contents
- 1 Species distribution
- 2 Function
- 3 Classification
- 3.1 nNOS
- 3.2 iNOS
- 3.3 eNOS
- 3.4 bNOS
- 4 Chemical reaction
- 5 Structure
- 6 Inhibitors
- 7 See also
- 8 References
- 9 External links
Species distribution
Arginine-derived NO synthesis has been identified in mammals, fish, birds, invertebrates, and bacteria.[3] Best studied are mammals, where three distinct genes encode NOS isozymes: neuronal (nNOS or NOS-1), cytokine-inducible (iNOS or NOS-2) and endothelial (eNOS or NOS-3).[2] iNOS and nNOS are soluble and found predominantly in the cytosol, while eNOS is membrane associated. Evidence has been found for NO signaling in plants, but plant genomes are devoid of homologs to the superfamily which generates NO in other kingdoms.
Function
In mammals, the endothelial isoform is the primary signal generator in the control of vascular tone, insulin secretion, and airway tone, is involved in regulation of cardiac function and angiogenesis (growth of new blood vessels). NO produced by eNOS has been shown to be a vasodilator identical to the endothelium-derived relaxing factor produced in response to shear from increased blood flow in arteries. This dilates blood vessels by relaxing smooth muscle in their linings. eNOS is the primary controller of smooth muscle tone. NO activates guanylate cyclase, which induces smooth muscle relaxation by:
- Increased intracellular cGMP, which inhibits calcium entry into the cell, and decreases intracellular calcium concentrations
- Activation of K+ channels, which leads to hyperpolarization and relaxation
- Stimulates a cGMP-dependent protein kinase that activates myosin light chain phosphatase, the enzyme that dephosphorylates myosin light chains, which leads to smooth muscle relaxation.
eNOS plays a critical role in embryonic heart development and morphogenesis of coronary arteries and cardiac valves.[4]
The neuronal isoform is involved in the development of nervous system. It functions as a retrograde neurotransmitter important in long term potentiation and hence is likely to be important in memory and learning. nNOS has many other physiological functions, including regulation of cardiac function and peristalsis and sexual arousal in males and females. An alternatively spliced form of nNOS is a major muscle protein that produces signals in response to calcium release from the SR. nNOS in the heart protects against cardiac arrhythmia induced by myocardial infarction.[5]
The primary receiver for NO produced by eNOS and nNOS is soluble guanylate cyclase, but many secondary targets have been identified. S-nitrosylation appears to be an important mode of action.
The inducible isoform iNOS produces large amounts of NO as a defense mechanism. It is synthesized by many cell types in response to cytokines and is an important factor in the response of the body to attack by parasites, bacterial infection, and tumor growth. It is also the cause of septic shock and may play a role in many diseases with an autoimmune etiology.
NOS signaling is involved in development and in fertilization in vertebrates. It has been implicated in transitions between vegetative and reproductive states in invertebrates, and in differentiation leading to spore formation in slime molds. NO produced by bacterial NOS is protective against oxidative damage.
Classification
Different members of the NOS family are encoded by separate genes.[6] There are three known isoforms in mammals, two are constitutive (cNOS) and the third is inducible (iNOS).[7] Cloning of NOS enzymes indicates that cNOS include both brain constitutive (NOS1) and endothelial constitutive (NOS3); the third is the inducible (NOS2) gene.[7] Recently, NOS activity has been demonstrated in several bacterial species, including notorious pathogens Bacillus anthracis and Staphylococcus aureus.[8]
The different forms of NO synthase have been classified as follows:
| Name | Gene(s) | Location | Function |
| Neuronal NOS (nNOS or NOS1) | NOS1 (Chromosome 12) |
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| Inducible NOS (iNOS or NOS2)
Calcium insensitive |
NOS2 (Chromosome 17) |
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| Endothelial NOS (eNOS or NOS3 or cNOS) | NOS3 (Chromosome 7) |
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| Bacterial NOS (bNOS) | multiple |
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nNOS
Neuronal NOS (nNOS) produces NO in nervous tissue in both the central and peripheral nervous systems. Its functions include:[9]
• Synaptic plasticity in the central nervous system (CNS) • Smooth muscle relaxation • Central regulation of blood pressure • Vasodilatation via peripheral nitrergic nerves
Neuronal NOS also performs a role in cell communication and is associated with plasma membranes. nNOS action can be inhibited by NPA (N-propyl-L-arginine). This form of the enzyme is specifically inhibited by 7-nitroindazole.[10]
The subcellular localisation of nNOS in skeletal muscle is mediated by anchoring of nNOS to dystrophin. nNOS contains an additional N-terminal domain, the PDZ domain.[11]
The gene coding for nNOS is located on Chromosome 12.[12]
iNOS
As opposed to the critical calcium-dependent regulation of constitutive NOS enzymes (nNOS and eNOS), iNOS has been described as calcium-insensitive, likely due to its tight non-covalent interaction with calmodulin (CaM) and Ca2+. The gene coding for iNOS is located on Chromosome 17.[12] While evidence for ‘baseline’ iNOS expression has been elusive, IRF1 and NF-κB-dependent activation of the inducible NOS promoter supports an inflammation mediated stimulation of this transcript. iNOS produces large quantities of NO upon stimulation, such as by proinflammatory cytokines (e.g. Interleukin-1, Tumor necrosis factor alpha and Interferon gamma).[13]
Induction of the high-output iNOS usually occurs in an oxidative environment, and thus high levels of NO have the opportunity to react with superoxide leading to peroxynitrite formation and cell toxicity. These properties may define the roles of iNOS in host immunity, enabling its participation in anti-microbial and anti-tumor activities as part of the oxidative burst of macrophages.[14]
It has been suggested that pathologic generation of nitric oxide through increased iNOS production may decrease tubal ciliary beats and smooth muscle contractions and thus affect embryo transport, which may consequently result in ectopic pregnancy.[15]
eNOS
Main article: Endothelial NOS
Endothelial NOS (eNOS), also known as nitric oxide synthase 3 (NOS3), generates NO in blood vessels and is involved with regulating vascular function. The gene coding for eNOS is located on Chromosome 7.[12] A constitutive Ca2+ dependent NOS provides a basal release of NO. eNOS is associated with "caveolae" a component of plasma membranes surrounding cells, and the membranes of Golgi bodies within cells. eNOS localisation to endothelial membranes is mediated by cotranslational N-terminal myristoylation and post-translational palmitoylation.[16]
bNOS
Bacterial NOS (bNOS) has been shown to protect bacteria against oxidative stress, diverse antibiotics, and host immune response. bNOS plays a key role in the transcription of superoxide dismutase (SodA). Bacteria late in the log phase who do not possess bNOS fail to upregulate SodA, which disables the defenses against harmful oxidative stress. Initially, bNOS may have been present to prepare the cell for stressful conditions but now seems to help shield the bacteria against conventional antimicrobials. As a clinical application, a bNOS inhibitor could be produced to decrease the load of Gram positive bacteria.[17][18]
Chemical reaction
Nitric oxide synthases produce NO by catalysing a five-electron oxidation of a guanidino nitrogen of L-arginine (L-Arg). Oxidation of L-Arg to L-citrulline occurs via two successive monooxygenation reactions producing Nω-hydroxy-L-arginine (NOHLA) as an intermediate. 2 mol of O2 and 1.5 mol of NADPH are consumed per mole of NO formed.[2]
Structure
The enzymes exist as homodimers. In eukaryotes, each monomer consisting of two major regions: an N-terminal oxygenase domain, which belongs to the class of heme-thiolate proteins, and a multi-domain C-terminal reductase, which is homologous to NADPH:cytochrome P450 reductase (EC 1.6.2.4) and other flavoproteins. The FMN binding domain is homologous to flavodoxins, and the two domain fragment containing the FAD and NADPH binding sites is homologous to flavodoxin-NADPH reductases. The interdomain linker between the oxygenase and reductase domains contains a calmodulin-binding sequence. The oxygenase domain is a unique extended beta sheet cage with binding sites for heme and pterin.
NOSs can be dimeric, calmodulin-dependent or calmodulin-containing cytochrome p450-like hemoprotein that combines reductase and oxygenase catalytic domains in one dimer, bear both flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN), and carry out a 5`-electron oxidation of non-aromatic amino acid arginine with the aid of tetrahydrobiopterin.[19]
All three isoforms (each of which is presumed to function as a homodimer during activation) share a carboxyl-terminal reductase domain homologous to the cytochrome P450 reductase. They also share an amino-terminal oxygenase domain containing a heme prosthetic group, which is linked in the middle of the protein to a calmodulin-binding domain. Binding of calmodulin appears to act as a "molecular switch" to enable electron flow from flavin prosthetic groups in the reductase domain to heme. This facilitates the conversion of O2 and L-arginine to NO and L-citrulline. The oxygenase domain of each NOS isoform also contains an BH4 prosthetic group, which is required for the efficient generation of NO. Unlike other enzymes where BH4 is used as a source of reducing equivalents and is recycled by dihydrobiopterin reductase (EC 1.5.1.33), BH4 activates heme-bound O2 by donating a single electron, which is then recaptured to enable nitric oxide release.
The first nitric oxide synthase to be identified was found in neuronal tissue (NOS1 or nNOS); the endothelial NOS (eNOS or NOS3) was the third to be identified. They were originally classified as "constitutively expressed" and "Ca2+ sensitive" but it is now known that they are present in many different cell types and that expression is regulated under specific physiological conditions.
In NOS1 and NOS3, physiological concentrations of Ca2+ in cells regulate the binding of calmodulin to the "latch domains", thereby initiating electron transfer from the flavins to the heme moieties. In contrast, calmodulin remains tightly bound to the inducible and Ca2+-insensitive isoform (iNOS or NOS2) even at a low intracellular Ca2+ activity, acting essentially as a subunit of this isoform.
Nitric oxide may itself regulate NOS expression and activity. Specifically, NO has been shown to play an important negative feedback regulatory role on NOS3, and therefore vascular endothelial cell function.[20] This process, known formally as S-nitrosation (and referred to by many in the field as S-nitrosylation), has been shown to reversibly inhibit NOS3 activity in vascular endothelial cells. This process may be important because it is regulated by cellular redox conditions and may thereby provide a mechanism for the association between "oxidative stress" and endothelial dysfunction. In addition to NOS3, both NOS1 and NOS2 have been found to be S-nitrosated, but the evidence for dynamic regulation of those NOS isoforms by this process is less complete[citation needed]. In addition, both NOS1 and NOS2 have been shown to form ferrous-nitrosyl complexes in their heme prosthetic groups that may act partially to self-inactivate these enzymes under certain conditions[citation needed]. The rate-limiting step for the production of nitric oxide may well be the availability of L-arginine in some cell types. This may be particularly important after the induction of NOS2.
Inhibitors
Ronopterin (VAS-203), also known as 4-amino-tetrahydrobiopterin (4-ABH4), an analogue of BH4 (a cofactor of NOS), is an NOS inhibitor that is under development as a neuroprotective agent for the treatment of traumatic brain injury.[1] Other NOS inhibitors that have been or are being researched for possible clinical use include cindunistat, A-84643, ONO-1714, L-NOARG, NCX-456, VAS-2381, GW-273629, NXN-462, CKD-712, KD-7040, and guanidinoethyldisulfide, among others.
See also
- Biological functions of nitric oxide
- Nitric-oxide synthase (NAD(P)H-dependent)
- Nitric oxide synthase 2 (inducible)
References
- ^ PDB: 3N5P; Delker SL, Xue F, Li H, Jamal J, Silverman RB, Poulos TL (December 2010). "Role of zinc in isoform-selective inhibitor binding to neuronal nitric oxide synthase". Biochemistry. 49 (51): 10803–10. doi:10.1021/bi1013479. PMC 3193998 . PMID 21138269.
- ^ a b c Knowles RG, Moncada S (March 1994). "Nitric oxide synthases in mammals". Biochem. J. 298 (2): 249–58. PMC 1137932 . PMID 7510950.
- ^ Liu Q, Gross SS (1996). "Binding sites of nitric oxide synthases". Meth. Enzymol. 268: 311–24. doi:10.1016/S0076-6879(96)68033-1. PMID 8782597.
- ^ Liu Y, Feng Q (July 2012). "NOing the heart: role of nitric oxide synthase-3 in heart development". Differentiation. 84 (1): 54–61. doi:10.1016/j.diff.2012.04.004. PMID 22579300.
- ^ Burger DE, Lu X, Lei M, Xiang FL, Hammoud L, Jiang M, Wang H, Jones DL, Sims SM, Feng Q (October 2009). "Neuronal nitric oxide synthase protects against myocardial infarction-induced ventricular arrhythmia and mortality in mice". Circulation. 120 (14): 1345–54. doi:10.1161/CIRCULATIONAHA.108.846402. PMID 19770398.
- ^ Taylor BS, Kim YM, Wang Q, Shapiro RA, Billiar TR, Geller DA (November 1997). "Nitric oxide down-regulates hepatocyte-inducible nitric oxide synthase gene expression". Arch Surg. 132 (11): 1177–83. doi:10.1001/archsurg.1997.01430350027005. PMID 9366709.
- ^ a b Stuehr DJ (May 1999). "Mammalian nitric oxide synthases". Biochim. Biophys. Acta. 1411 (2–3): 217–30. doi:10.1016/S0005-2728(99)00016-X. PMID 10320659.
- ^ Gusarov I, Starodubtseva M, Wang ZQ, McQuade L, Lippard SJ, Stuehr DJ, Nudler E (May 2008). "Bacterial Nitric-oxide Synthases Operate without a Dedicated Redox Partner". J. Biol. Chem. 283 (19): 13140–7. doi:10.1074/jbc.M710178200. PMC 2442334 . PMID 18316370.
- ^ Förstermann, Ulrich; Sessa, William (Apr 2012). "Nitric oxide synthases: regulation and function". European Heart Journal. 33 (7): 829–837. PMC 3345541 .
- ^ Southan GJ, Szabó C (February 1996). "Selective pharmacological inhibition of distinct nitric oxide synthase isoforms". Biochem. Pharmacol. 51 (4): 383–94. doi:10.1016/0006-2952(95)02099-3. PMID 8619882.
- ^ Ponting CP, Phillips C (March 1995). "DHR domains in syntrophins, neuronal NO synthases and other intracellular proteins". Trends Biochem. Sci. 20 (3): 102–3. doi:10.1016/S0968-0004(00)88973-2. PMID 7535955.
- ^ a b c Knowles RG, Moncada S (March 1994). "Nitric oxide synthases in mammals". Biochem. J. 298 (2): 249–58. PMC 1137932 . PMID 7510950.
- ^ Green SJ, Scheller LF, Marletta MA, Seguin MC, Klotz FW, Slayter M, Nelson BJ, Nacy CA (December 1994). "Nitric oxide: cytokine-regulation of nitric oxide in host resistance to intracellular pathogens". Immunol. Lett. 43 (1-2): 87–94. doi:10.1016/0165-2478(94)00158-8. PMID 7537721.
- ^ Mungrue IN, Husain M, Stewart DJ (October 2002). "The role of NOS in heart failure: lessons from murine genetic models". Heart Fail Rev. 7 (4): 407–22. PMID 12379825.
- ^ Al-Azemi M, Refaat B, Amer S, Ola B, Chapman N, Ledger W (August 2010). "The expression of inducible nitric oxide synthase in the human fallopian tube during the menstrual cycle and in ectopic pregnancy". Fertil. Steril. 94 (3): 833–40. doi:10.1016/j.fertnstert.2009.04.020. PMID 19482272.
- ^ Liu J, Hughes TE, Sessa WC (June 1997). "The First 35 Amino Acids and Fatty Acylation Sites Determine the Molecular Targeting of Endothelial Nitric Oxide Synthase into the Golgi Region of Cells: A Green Fluorescent Protein Study". J. Cell Biol. 137 (7): 1525–35. doi:10.1083/jcb.137.7.1525. PMC 2137822 . PMID 9199168.
- ^ Gusarov I, Nudler E (September 2005). "NO-mediated cytoprotection: Instant adaptation to oxidative stress in bacteria". Proc. Natl. Acad. Sci. U.S.A. 102 (39): 13855–60. doi:10.1073/pnas.0504307102. PMC 1236549 . PMID 16172391.
- ^ Gusarov I, Shatalin K, Starodubtseva M, Nudler E (September 2009). "Endogenous Nitric Oxide Protects Bacteria Against a Wide Spectrum of Antibiotics". Science. 325 (5946): 1380–4. doi:10.1126/science.1175439. PMC 2929644 . PMID 19745150.
- ^ Chinje EC, Stratford IJ (1997). "Role of nitric oxide in growth of solid tumours: a balancing act". Essays Biochem. 32: 61–72. PMID 9493011.
- ^ Kopincová, Jana; Púzserová, Angelika; Bernátová, Iveta (2011-06-01). "Biochemical aspects of nitric oxide synthase feedback regulation by nitric oxide". Interdisciplinary Toxicology. 4 (2). doi:10.2478/v10102-011-0012-z. ISSN 1337-9569.
External links
- Nitric oxide synthase at the US National Library of Medicine Medical Subject Headings (MeSH)
- The Nobel Prize in Physiology or Medicine 1998
- University of Edinburgh, School of Chemistry - NO Synthase
- Nitric Oxide Synthase in Proteopedia
Enzymes involved in neurotransmission
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| arginine→NO |
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| choline→Acetylcholine |
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Oxidoreductases: dioxygenases, including steroid hydroxylases (EC 1.14)
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| 1.14.11: 2-oxoglutarate |
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| 1.14.13: NADH or NADPH |
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| 1.14.14: reduced flavin or flavoprotein |
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| 1.14.15: reduced iron-sulfur protein |
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| 1.14.16: reduced pteridine (BH4 dependent) |
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| 1.14.17: reduced ascorbate |
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| 1.14.18-19: other |
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| 1.14.99 - miscellaneous |
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Enzymes
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Nitric oxide signaling modulators
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- Molecular and Cellular Biology portal
UpToDate Contents
全文を閲覧するには購読必要です。 To read the full text you will need to subscribe.
- 1. 一酸化窒素と腎臓 nitric oxide and the kidney
- 2. 心不全における一酸化窒素、その他のホルモン、サイトカイン、およびケモカイン nitric oxide other hormones cytokines and chemokines in heart failure
- 3. 呼気中一酸化窒素の分析および適用 exhaled nitric oxide analysis and applications
- 4. 核間性眼筋麻痺 internuclear ophthalmoplegia
- 5. 非ステロイド性抗炎症剤（NSAIDs）：作用機序 nsaids mechanism of action
English Journal
- Abnormally decreased NO and augmented CO production in islets of the leptin-deficient ob/ob mouse might contribute to explain hyperinsulinemia and islet survival in leptin-resistant type 2 obese diabetes.
- Jimenez-Feltstrom J, Salehi A, Meidute Abaraviciene S, Henningsson R, Lundquist I.SourceDepartment of Clinical Sciences, Islet Cell Physiology, SUS, University of Lund, SE-20502 Malmo, Sweden.
- Regulatory peptides.Regul Pept.2011 Oct 10;170(1-3):43-51. Epub 2011 May 26.
- The role of the gaseous messengers NO and CO for β-cell function and survival is controversial. We examined this issue in the hyperglycemic-hyperinsulinemic ob/ob mouse, an animal model of type 2 obese diabetes, by studying islets from obese vs lean mice regarding glucose-stimulated insulin release
- PMID 21620903
- Altered regulation of renal nitric oxide and atrial natriuretic peptide systems in angiotensin II-induced hypertension.
- Bae EH, Ma SK, Lee J, Kim SW.SourceDepartment of Internal Medicine, Chonnam National University Medical School, Gwangju, Republic of Korea.
- Regulatory peptides.Regul Pept.2011 Oct 10;170(1-3):31-7. Epub 2011 May 25.
- The present study was aimed to determine whether there is an altered role of local nitric oxide (NO) and atrial natriuretic peptide (ANP) systems in the kidney in association with the angiotensin (Ang) II-induced hypertension. Male Sprague-Dawley rats were used. Ang II (100 ng・min?1・kg?1) wa
- PMID 21616096
Japanese Journal
- Protective Effects of Ginger against Aspirin-Induced Gastric Ulcers in Rats
- Wang Zhongzhi,Hasegawa Junichi,Wang Xinhui,Matsuda Akiko,Tokuda Takahiro,Miura Norimasa,Watanabe Tatsuo
- Yonago Acta medica 54(1), 11-19, 2011-03
- … however, it did ameliorate the aspirin-induced increases in mucosal activity of the inducible form of NO synthase (iNOS) and plasma tumor necrosis factor (TNF)-α and interleukin (IL)-1β levels. … Both 6-gingerol and 6-shogaol reduced aspirin induced ulcer formation, mucosal iNOS and plasma TNF-α and IL-1β levels. …
- NAID 120002890329
- Sasa quelpaertensis phenylpropanoid derivative suppresses lipopolysaccharide-induced nitric oxide synthase and cyclo-oxygenase-2 expressions in RAW 264.7 cells
- Moon Ji-Young,Yang Eun-Jin,Kim Sang Suk [他]
- 薬学雑誌 131(6), 961-967, 2011
- NAID 40018874087
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Related Pictures
★リンクテーブル★
| リンク元 | 「一酸化窒素」「誘導型NO合成酵素」「構成型NOS」「inducible NO-synthase」 |
| 関連記事 | 「iNO」 |
「一酸化窒素」
平滑筋弛緩作用
- NOは血管内皮細胞で産生される
- NO放出のトリガーはアセチルコリン、ブラジキニン、ヒスタミン、サブスタンスPである (SPC.52)。
- NOは平滑筋でcGMPの産生を増加させることで平滑筋を弛緩させている
- NOは下部食道括約筋も弛緩させる
- →NOの分泌が失われると下部食道括約筋が緊張しアカラジアを生じる
炎症との関連(BPT.50)
- iNOSにより産生される
- 1. vasodilation：血管平滑筋の弛緩
- 2. 血小板活性化の全ての段階の拮抗作用(adhesion, aggregation, and degranulation
- 3. 炎症部位への白血球のリクルートメントの減少
- 4. 活性化マクロファージの中でのバクテリア障害物質としての作用
メモ
- 笑気、酸化二窒素、N2Oはnitrous oxideなので間違えないように
「誘導型NO合成酵素」
- 英
- inducible NO synthase inducible NO-synthase inducible nitric oxide synthase, inducible NOS iNOS
- 同
- 誘導型一酸化窒素合成酵素、誘導型NOS
- 関
- NO
分類 (BPT.50)
- Type I：nNOS：constitutively expressed
- Type II：iNOS：present in macrophages and endothelial cells. also present in many other cells types, including hepatocytes, cardiac myocytes, and respiratory epithelium.
- Type III：eNOS：constitutively expressed. endothelium
産生
- 炎症性サイトカインにより発現が誘導される：IL-1, INF, INF-γ, bacterial endotoxin。(BPT.50)
「構成型NOS」
- 英
- cNOS
- 同
- 構成一酸化窒素合成酸素
- 関
- iNOS
「inducible NO-synthase」
- 同
- iNOS
「iNO」
- 同
- iNO
- 関
- Inhaled nitric oxide