Biological significance of endogenous methylarginines that inhibit nitric oxide synthases

Leiper, J

doi:10.1016/s0008-6363(99)00162-5

Cited by 458Nitric Oxide and Endothelin EffectsCancer-related gene regulationPolyamine Metabolism and Applications

Biological significance of endogenous methylarginines that inhibit nitric oxide synthases

Leiper, J·1999·Cardiovascular Research

DOI 10.1016/s0008-6363(99)00162-5

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Abstract

The guanidino-methylated arginine analogue NG monomethyl-L-arginine (L-NMMA) has been the standard nitric oxide synthase inhibitor used to evaluate the role of the L-arginine:nitric oxide pathway. However, L-NMMA and other methylated arginine residues are also synthesised in vivo by the action of a family of enzymes known as protein arginine methyltransferases. Proteolysis of proteins containing methylated arginine residues releases free methylarginine residues into the cytosol from where they may pass out of the cell into plasma. Of the three known methylarginine residues produced in mammals only asymmetrically methylated forms (L-NMMA and asymmetric dimethylarginine (ADMA)) but not symmetrically methylated arginine (symmetric dimethylarginine (SDMA)) inhibit nitric oxide synthase (NOS). We and others have proposed that endogenously produced asymmetrically methylated arginines may modulate NO production and that the accumulation of these residues in disease states may contribute to pathology. The activity of the enzyme dimethylarginine dimethylaminohydrolase that metabolises asymmetric methylarginines may be of critical importance in affecting NO pathways in health or disease.

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Production of adequate NO in the vascular endothelium is critical for regulation of blood flow and vasodilation.
“The production of adequate levels of NO in the vascular endothelium is critical for the regulation of blood flow and vasodilation”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [565]

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Authors: Leiper, J.
Affiliations: University College London (GB)
Corresponding author: Leiper, J
ORCID: Leiper, J
Venue: Cardiovascular Research
Publisher: Oxford University Press (OUP)
Published: 1999-08-15
Volume: 43
Issue: 3
Pages: 542-548
ISSN: 0008-6363 (ISSN-L)
DOI: 10.1016/s0008-6363(99)00162-5
OpenAlex: W2153125904
Cited by: 458
References: 54
Citations by year: 2026: 3 · 2025: 7 · 2024: 5 · 2023: 10 · 2022: 5 · 2021: 12 · 2020: 13 · 2019: 13 · 2018: 10 · 2017: 16 · 2016: 12 · 2015: 23 · 2014: 18 · 2013: 23 · 2012: 20
FWCI: 1.94
Type: journal article
Language: en
Open access: closed
Locations: Cardiovascular Research (publishedVersion)
PubMed (publishedVersion)
UCL Discovery (University College London) (submittedVersion)
Topics: Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cancer-related gene regulation
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Polyamine Metabolism and Applications
Keywords: nitric oxide synthase inhibition, L-NMMA, asymmetric dimethylarginine, symmetric dimethylarginine, protein arginine methyltransferase, dimethylarginine dimethylaminohydrolase, L-arginine-nitric oxide pathway, nitric oxide production, asymmetric methylation
MeSH terms: Amidohydrolases, Animals, Arginine, Cytosol, Enzyme Inhibitors, Humans, Hydrolases, Isoenzymes, Nitric Oxide, Protein-Arginine N-Methyltransferases, Nitric Oxide Synthase, omega-N-Methylarginine

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Biological significance of endogenous methylarginines that inhibit nitric oxide synthases

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