Details
Stereochemistry | ABSOLUTE |
Molecular Formula | C8H18N4O2 |
Molecular Weight | 202.2541 |
Optical Activity | UNSPECIFIED |
Defined Stereocenters | 1 / 1 |
E/Z Centers | 0 |
Charge | 0 |
SHOW SMILES / InChI
SMILES
CN(C)C(=N)NCCC[C@H](N)C(O)=O
InChI
InChIKey=YDGMGEXADBMOMJ-LURJTMIESA-N
InChI=1S/C8H18N4O2/c1-12(2)8(10)11-5-3-4-6(9)7(13)14/h6H,3-5,9H2,1-2H3,(H2,10,11)(H,13,14)/t6-/m0/s1
N, N – Dimethylarginine, more known as asymmetric dimethylarginine (ADMA), a naturally occurring chemical found in blood plasma. It is formed by methylation of arginine residues in proteins and released after proteolysis. ADMA is an endogenous inhibitor of all isoforms of nitric oxide synthase, the enzyme that synthesizes nitric oxide from arginine. Elevated plasma concentrations of ADMA are associated with hypertension and other risk factors for cardiovascular disease. It is known, that chronic kidney disease (CDK) is associated with increased risk of renal and cardiovascular events and it has been claimed that asymmetric dimethylarginine (ADMA) and symmetric dimethylarginine (SDMA), are contributing factors. Nevertheless, the recent comprehensive analysis of methylarginines in a cohort of patients with non-dialysis CKD have revealed, the potential pathophysiological role of SDMA in CKD progression and atherosclerotic cardiovascular disease among non-dialysis CKD patients. Thus SDMA predicts CKD progression and future atherosclerotic cardiovascular events more consistently than other methylarginines. In addition, was also shown, that the maternal plasma ADMA concentration is an important indicator of fetal growth restriction in women with impaired placental perfusion independent of NO.
CNS Activity
Approval Year
Targets
Primary Target | Pharmacology | Condition | Potency |
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Target ID: CHEMBL2096621 Sources: https://www.ncbi.nlm.nih.gov/pubmed/16028689 |
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Target ID: CHEMBL2111405 Sources: https://www.ncbi.nlm.nih.gov/pubmed/16028689 |
Conditions
Condition | Modality | Targets | Highest Phase | Product |
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Diagnostic | Unknown Approved UseUnknown |
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Diagnostic | Unknown Approved UseUnknown |
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Diagnostic | Unknown Approved UseUnknown |
PubMed
Title | Date | PubMed |
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Dialysis improves endothelial function in humans. | 2001 Sep |
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Capillary electrophoretic and micellar electrokinetic separations of asymmetric dimethyl-L-arginine and structurally related amino acids: quantitation in human plasma. | 2004 Dec |
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A calcium channel blocker, benidipine, improves cell membrane fluidity in human subjects via a nitric oxide-dependent mechanism. An electron paramagnetic resonance investigation. | 2004 Dec |
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Weight loss reduces circulating asymmetrical dimethylarginine concentrations in morbidly obese women. | 2004 Dec |
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The transplanted liver graft is capable of clearing asymmetric dimethylarginine. | 2004 Dec |
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Elevation of asymmetric dimethylarginine (ADMA) in patients developing hepatic failure after major hepatectomy. | 2004 Nov-Dec |
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Asymmetric dimethyl-L-arginine (ADMA): a possible link between homocyst(e)ine and endothelial dysfunction. | 2005 Feb |
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Relations between plasma asymmetric dimethylarginine (ADMA) and risk factors for coronary disease. | 2006 Feb |
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Homocysteine and asymmetric dimethylarginine (ADMA): biochemically linked but differently related to vascular disease in chronic kidney disease. | 2007 |
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Elevated plasma asymmetric dimethyl-L-arginine in a patient with Gordon syndrome. | 2007 Jan |
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The relationship between plasma asymmetrical dimethyl-L-arginine and inflammation and adhesion molecule levels in subjects with normal, impaired, and diabetic glucose tolerance. | 2008 Jan |
Sample Use Guides
In Vitro Use Guide
Sources: https://www.ncbi.nlm.nih.gov/pubmed/26959555
Asymmetric dimethylarginine (N,N-DIMETHYLARGININE; ADMA) induces the mitochondrial translocation of endothelial nitric oxide synthase (eNOS) through the nitration-mediated activation of Akt1. The study was performed to elucidate the potential effect of ADMA on Akt1 phosphorylation and the mechanisms that are involved. Western blot analysis demonstrated that, although ADMA (10 μM, 2 h) does not change total Akt1 levels. Akt1 phosphorylation at T308 and S473 were significantly increased. It was also found that ADMA treatment significantly increased Akt1 translocation from cytosol to the plasma membrane, suggesting that upon ADMA stimulation, Akt1 was activated, at least in part, through recruitment to that plasma membrane.
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Classification Tree | Code System | Code | ||
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LOINC |
79635-9
Created by
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NCI_THESAURUS |
C73539
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LOINC |
74363-3
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LOINC |
80981-4
Created by
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C018524
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DTXSID401017725
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30315-93-6
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17929
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C124264
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63CV1GEK3Y
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DB01686
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123831
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ASYMMETRIC DIMETHYLARGININE
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PARENT (METABOLITE)
SUBSTANCE RECORD