The DOI matches its Crossref record; 121 of the 122 references it cites were found in a registry or an index.
Arginine Metabolism Revisited
Open accessAbstract
Mammalian arginine metabolism is complex due to the expression of multiple enzymes that utilize arginine as substrate and to interactions or competition between specific enzymes involved in arginine metabolism. Moreover, cells may contain multiple intracellular arginine pools that are not equally accessible to all arginine metabolic enzymes, thus presenting additional challenges to more fully understanding arginine metabolism. At the whole-body level, arginine metabolism ultimately results in the production of a biochemically diverse range of products, including nitric oxide, urea, creatine, polyamines, proline, glutamate, agmatine, and homoarginine. Included in this group of compounds are the methylated arginines (e.g., asymmetric dimethylarginine), which are released upon degradation of proteins containing methylated arginine residues. Changes in arginine concentration also can regulate cellular metabolism and function via a variety of arginine sensors. Although much is known about arginine metabolism, elucidation of the physiologic or pathophysiologic roles for all of the pathways and their metabolites remains an active area of investigation, as exemplified by current findings highlighted in this review.
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“Exacerbated arginase activity can decrease l-arginine levels and cause eNOS uncoupling (91, 144, 667, 804, 1039).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [667]
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Lysosomal amino acid transporter SLC38A9 signals arginine sufficiency to mTORC1
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The CASTOR Proteins Are Arginine Sensors for the mTORC1 Pathway
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Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation
Tejero, J., Shiva, S., & Gladwin, M. T. (2019) · Physiological Reviews · doi:10.1152/physrev.00036.2017 · Cited by 541
Myeloid Cell-Derived Arginase in Cancer Immune Response
Grzywa, T. M., Sosnowska, A., Matryba, P., Rydzyńska, Z., Jasiński, M., Nowis, D., & Gołąb, J. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.00938 · Cited by 446
Kurtz, C. B., Millet, Y. A., Puurunen, M. K., Perreault, M., Charbonneau, M. R., Isabella, V. M., Kotula, J. W., Antipov, E., Dagon, Y., Denney, W. S., et al. (2019) · Science Translational Medicine · doi:10.1126/scitranslmed.aau7975 · Cited by 399
Metabolic orchestration of the wound healing response
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Metadata
- Authors
- Morris, S. M.
- Affiliations
- University of Pittsburgh (US)
- Corresponding author
- Morris, Sidney M
- ORCID
- Morris, Sidney M
- Venue
- The Journal of Nutrition
- Publisher
- Elsevier BV
- Published
- 2016-12
- Volume
- 146
- Issue
- 12
- Pages
- 2579S-2586S
- ISSN
- 0022-3166 (ISSN-L)
- OpenAlex
- W2555868191
- Cited by
- 435
- References
- 122
- Citations by year
- 2026: 61 · 2025: 69 · 2024: 48 · 2023: 64 · 2022: 52 · 2021: 58 · 2020: 35 · 2019: 24 · 2018: 16 · 2017: 7
- FWCI
- 1.97
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Journal of Nutrition (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Amino Acid Enzymes and Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Polyamine Metabolism and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cancer-related gene regulation
- Keywords
- arginine metabolism, nitric oxide, urea, creatine, polyamines, proline, glutamate, agmatine, homoarginine, asymmetric dimethylarginine, enzyme competition, protein degradation
- MeSH terms
- Animals, Arginine, Mammals
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