Abstract
Asymmetric and symmetric dimethylarginine (ADMA and SDMA, respectively) are risk factors for the cardiovascular and renal systems. There is a paucity of data in humans regarding variations of protein L-arginine (Arg) methylation leading to ADMA and SDMA. In this study, we introduced and used Arg dimethylation indices based on the creatinine-corrected urinary excretion of SDMA and ADMA, and its major metabolite dimethylamine (DMA). The main objective of the present study was to assess whether, and to which extent, a high-fat protein meal (HFM), a classical allostatic load eliciting various adverse effects, may contribute to Arg dimethylation in proteins in humans. Reliable gas chromatography–mass spectrometry methods were used to measure the concentration of ADMA, DMA, SDMA, and creatinine in spot urine samples collected before (0 h), and after (2, 4, 6 h) three HFM sessions in 10 healthy overweight individuals. At baseline, urinary ADMA, DMA, and SDMA excretion correlated positively with circulating TNF-α and IL-6. Arg dimethylation indices did not change postprandially. Our study shows that three HFMs do not contribute to Arg dimethylation in proteins. The proposed indices should be useful to determine extent and status of the whole-body Arg dimethylation in proteins in humans under various conditions.
Highlights
L-Arginine (Arg) is a nutritionally semi-essential proteinogenic amino acid
Our study shows that three high-fat protein meal (HFM) do not contribute to Arg dimethylation in proteins
Arg is the substrate of all known nitric oxide synthase (NOS; EC 1.14.13.39) isoforms, which are present in virtually all cell types and oxidize the guanidine (NG ) imine group of free Arg to nitric oxide (NO) via an NG -hydroxy-L-arginine intermediate
Summary
L-Arginine (Arg) is a nutritionally semi-essential proteinogenic amino acid. It is involved in many pathways and numerous physiological processes [1,2]. MMA, ADMA, and SDMA inhibit the activity of the three NOS isoforms by distinctly different mechanisms and inhibitory potency [6,7]. Like their parent molecule Arg, MMA, ADMA, and SDMA exist in two forms: as residues of certain proteins, and as free acids produced by regular proteolysis of those NG -methylated proteins. The free guanidine group of Arg moieties in proteins undergo posttranslational methylation, which is catalyzed by the family of the protein arginine methyltransferases (PRMT; EC 2.1.1.125) [8,9,10]; the methyl group for this reaction is provided by the universal cofactor S-adenosylmethionine (SAM) (Figure 1)
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