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MetabolomicsMechanical force promotes dimethylarginine dimethylaminohydrolase 1-mediated hydrolysis of the metabolite asymmetric dimethylarginine to enhance bone formation

Mechanical force is critical for the development and remodeling of bone. Here we report that mechanical force regulates the production of the metabolite asymmetric dimethylarginine (ADMA) via regulating the hydrolytic enzyme dimethylarginine dimethylaminohydrolase 1 (Ddah1) expression in osteobla...

2021-11-23 | MTBLS3725 | MetaboLights
MetabolomicsCyclooxygenase-2, Asymmetric Dimethylarginine, and the Cardiovascular Hazard From Nonsteroidal Anti-Inflammatory Drugs (Murine kidney and plasma UPLC-MS/MS assay)

BACKGROUND: Large-scale, placebo-controlled trials established that nonsteroidal anti-inflammatory drugs confer a cardiovascular hazard: this has been attributed to depression of cardioprotective products of cyclooxygenase (COX)-2, especially prostacyclin. An alternative mechanis...

2019-08-22 | MTBLS680 | MetaboLights
TranscriptomicsTranscription profiling of human coronary artery endothelial cells treated with ADMA at 2uM (a pathophysiological dose) and 100uM (a pharmacological dose), for 24h
Asymmetric dimethylarginine (ADMA) is a naturally occurring inhibitor of nitric oxide synthesis that accumulates in wide range of diseases associated with endothelial dysfunction and enhanced atherosclerosis. Plasma ADMA has been implicated as a major novel cardiovascular risk factor, but the mechan...
ORGANISM(S): Homo sapiens 
2005-09-01 | E-MEXP-377 | biostudies-arrayexpress
MetabolomicsCyclooxygenase-2, Asymmetric Dimethylarginine, and the Cardiovascular Hazard From Nonsteroidal Anti-Inflammatory Drugs (Murine and human plasma quantitative L-arginine and methylarginines UPLC-MS/MS assay)

BACKGROUND: Large-scale, placebo-controlled trials established that nonsteroidal anti-inflammatory drugs confer a cardiovascular hazard: this has been attributed to depression of cardioprotective products of cyclooxygenase (COX)-2, especially prostacyclin. An alternative mechanis...

2019-08-22 | MTBLS685 | MetaboLights
UnknownTransient changes in L-arginine, asymmetric and symmetric dimethyl arginine in triathletes following Norseman Xtreme Triathlon.
Not available
S-EPMC11527713 | biostudies-literature
UnknownAn association between L-arginine/asymmetric dimethyl arginine balance, obesity, and the age of asthma onset phenotype.
Not available
S-EPMC3570651 | biostudies-literature
ProteomicsDeep protein methylation profiling by combined chemical and immunoaffinity approaches reveals novel PRMT1 targets
Protein methylation has been implicated in many important biological contexts including signaling, metabolism, and transcriptional control. Despite the importance of this post- translational modification, the global analysis of protein methylation by mass spectrometry-based proteomics has not been e...
ORGANISM(S): Homo sapiens (Human) 
2019-08-28 | PXD012357 | Pride
Prmt1 Prmt Ptm Liquid chromatography Methylation Lysine Sdma Mma Mass spectrometry Posttranslational modification Dimethyl Monomethyl Adma Proteomics Q exactive plus Arginine Lcms 
ProteomicsImproved discrimination of asymmetric and symmetric protein arginine dimethylation by optimizing the normalized collision energy in LC-MS proteomics
Here we optimize the HCD Normalized Collision Energy (NCE) in order to generate neutral losses of monomethylamine and dimethylamine which can be lost by symmetric dimethylarginine and asymmetric dimethylarginine, respectively. By testing a range of NCEs across two different methyl enrichment techniq...
ORGANISM(S): Homo sapiens (Human) 
2020-05-27 | PXD017193 | Pride
Arginine Prmt Mass spectrometry Methylation Adma Ptm Hcd Neutral loss Proteomics Sdma Lcms 
GenomicsAsymmetrical methyltransferase PRMT3 regulates human mesenchymal stem cell osteogenesis via miR-3648
Histone arginine methylation, which is catalyzed by protein arginine methyltransferases (PRMTs), plays a key regulatory role in various biological processes, including signal transduction, RNA splicing, transcription and chromatin remodeling, and DNA repair. Several PRMTs are involved in skeletal de...
ORGANISM(S): Homo sapiens 
2019-08-20 | GSE124674 | GEO
UnknownResolution and quantification of arginine, monomethylarginine, asymmetric dimethylarginine, and symmetric dimethylarginine in plasma using HPLC with internal calibration.
Not available
S-EPMC4755038 | biostudies-literature
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