Isolation and identification of NG-Monomethyl NG, NG-Dimethyl- and NG,NG-Dimethylarginine from the hydrolysate of proteins of bovine brain

Nakajima, Teruo; Matsuoka, Yukio; Kawaguchi, Yasuo

doi:10.1016/0304-4165(71)90206-6

Cited by 70 publications

(21 citation statements)

References 20 publications

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“…In fact, Paik and Kim (18) specifically ruled out the existence of ␦-N-methylarginine in hydrolysates of rat liver nuclei when they found that alkaline treatment of guanidino-[methyl-14 C]arginine derivatives yielded radiolabeled methylurea and methylamine; no radioactive product co-chromatographed with a synthetic ␦-N-methylornithine standard. Nakajima et al (19) concurred with this result in similar experiments using hydrolysates of proteins from bovine brain and various rat organs. There appear to be no further studies of the possible existence of ␦-N-methylarginine residues in proteins since these reports were published.…”

Section: ␦-N-methylarginine In Yeast Proteinssupporting

confidence: 77%

δ-N-Methylarginine Is a Novel Posttranslational Modification of Arginine Residues in Yeast Proteins

Zobel-Thropp¹,

Gary²,

Clarke³

1998

Journal of Biological Chemistry

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We have found a novel modification of protein arginine residues in the yeast Saccharomyces cerevisiae. Intact yeast cells lacking RMT1, the gene encoding the protein -N G -arginine methyltransferase, were labeled with the methyl donor S-adenosyl-L-[methyl-3 H]methionine. The protein fraction was acid-hydrolyzed to free amino acids, which were then fractionated on a high resolution sulfonated polystyrene cation exchange column at pH 5.27 and 55°C. In the absence of the -N G ,N G -[ 3 H]dimethylarginine product of the RMT1 methyltransferase, we were able to detect a previously obscured 3 H-methylated species that migrated in the region of methylated arginine derivatives. The [ 3 H]methyl group(s) of this unknown species were not volatilized by treatment with 2 M NaOH at 55°C for up to 48 h, suggesting that they were not modifications of the terminal -guanidino nitrogen atoms. However, this base treatment did result in the formation of a new 3 H-methylated derivative that co-chromatographed with ␦-N-methylornithine on high resolution cation exchange chromatography, on reverse phase high pressure liquid chromatography, and on thin layer chromatography. From these data, we suggest that the identity of the original unknown methylated residue is ␦-N-monomethylarginine. The presence of this methylated residue in yeast cells defines a novel type of protein modification reaction in eukaryotes.

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Section: ␦-N-methylarginine In Yeast Proteinssupporting

confidence: 77%

δ-N-Methylarginine Is a Novel Posttranslational Modification of Arginine Residues in Yeast Proteins

Zobel-Thropp¹,

Gary²,

Clarke³

1998

Journal of Biological Chemistry

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“…Prior to the administration of L-NMMA, the female subjects had negative pregnancy test results. It should be noted that methylated arginine compounds such as L-NMMA are normally present in mammalian tissues (including human) and have well-defined clearance pathways (Nakajima, Matsuoka & Kakimoto, 1971;Carnegie, Fellows & Symington, 1977). Additionally, the experience to date with L-NMMA in humans and other species indicates that low doses are nontoxic (Vallance et al 1989;Kilbourn et al 1992).…”

Section: Subjectsmentioning

confidence: 99%

Nitric oxide contributes to the rise in forearm blood flow during mental stress in humans.

Dietz

Rivera

Eggener

et al. 1994

The Journal of Physiology

206

218

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1. Our aim was to determine whether the vasodilating substance nitric oxide (NO) contributes to the rise in forearm blood flow observed during mental stress in humans. We also determined whether the NO might be released as a result of cholinergic stimulation of the vascular endothelium. 2. Blood flow was measured in both forearms using plethysmography during several 3‐5 min bouts of a colour word test. In one forearm the nitric oxide synthase blocker NG‐monomethyl‐L‐arginine (L‐NMMA) and other drugs were infused via a brachial artery catheter. The contralateral forearm served as a control. 3. When L‐NMMA was given prior to mental stress it blunted the rise in blood flow in the treated forearm almost completely. The normal blood flow response returned during a second bout of stress conducted after a wash‐out period. During a third bout of mental stress, administration of more L‐NMMA again blunted the blood flow responses to mental stress. 4. When atropine was given prior to mental stress, the increases in blood flow were reduced in the treated forearm. Subsequent administration of both atropine and L‐NMMA caused a somewhat greater reduction in the blood flow responses than those observed with atropine alone. 5. These data demonstrate that NO plays a role in forearm vasodilatation during mental stress in humans. It is likely that most of the NO is released by cholinergic stimulation of the vascular endothelium.

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“…The methylated species were later determined to be arginine derivatives that had been mono-and dimethylated on their guanidino group (Paik and Kim, 1968;Nakajima et al, 1971). S-Adenosyl-L-methionine-dependent methyltransferase activities that catalyze these reactions have now been characterized in a number of eukaryotic tissues and organisms.…”

mentioning

confidence: 99%

The Predominant Protein-arginine Methyltransferase from Saccharomyces cerevisiae

Gary¹,

Lin

Yang³

et al. 1996

Journal of Biological Chemistry

186

237

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We have identified the major enzymatic activity responsible for the S-adenosyl-L-methionine-dependent methylation of arginine residues (EC 2.1. Evidence for the posttranslational methylation of arginine residues in proteins was first provided by the presence of radioactive species chromatographing at positions near that of arginine in acid hydrolysates of isolated calf thymus nuclei incubated with S-adenosyl-L- [methyl-14

show abstract

Isolation and identification of NG-Monomethyl NG, NG-Dimethyl- and NG,NG-Dimethylarginine from the hydrolysate of proteins of bovine brain

Cited by 70 publications

References 20 publications

δ-N-Methylarginine Is a Novel Posttranslational Modification of Arginine Residues in Yeast Proteins

δ-N-Methylarginine Is a Novel Posttranslational Modification of Arginine Residues in Yeast Proteins

Nitric oxide contributes to the rise in forearm blood flow during mental stress in humans.

The Predominant Protein-arginine Methyltransferase from Saccharomyces cerevisiae

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