Cited by 436Amino Acid Enzymes and MetabolismPolyamine Metabolism and ApplicationsCancer-related gene regulation

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Arginine Metabolism Revisited

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Morris, Sidney M·2016·The Journal of Nutrition

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Abstract

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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Arginine metabolism: nitric oxide and beyond
WU, G., & MORRIS, S. M. (1998) · Biochemical Journal · doi:10.1042/bj3360001 · Cited by 2,811
Self-citation
Protein Arginine Methylation in Mammals: Who, What, and Why
Bedford, M. T., & Clarke, S. G. (2009) · Molecular Cell · doi:10.1016/j.molcel.2008.12.013 · Cited by 1,810
An amino-acid taste receptor
Nelson, G., Chandrashekar, J. V., Hoon, M. A., Feng, L., Zhao, G., Ryba, N. J. P., & Zuker, C. S. (2002) · Nature · doi:10.1038/nature726 · Cited by 1,523
Arginine metabolism and nutrition in growth, health and disease
Wu, G., Bazer, F. W., Davis, T. A., Kim, S. W., Li, P., Marc Rhoads, J., Carey Satterfield, M., Smith, S. B., Spencer, T. E., & Yin, Y. (2009) · Amino Acids · doi:10.1007/s00726-008-0210-y · Cited by 1,362
Nutrient-sensing mechanisms and pathways
Efeyan, A., Comb, W. C., & Sabatini, D. M. (2015) · Nature · doi:10.1038/nature14190 · Cited by 1,110
PAD, a growing family of citrullinating enzymes: genes, features and involvement in disease
Vossenaar, E. R., Zendman, A. J. W., VENROOIJ, W. J. V., & Pruijn, G. J. M. (2003) · BioEssays · doi:10.1002/bies.10357 · Cited by 986
Lysosomal amino acid transporter SLC38A9 signals arginine sufficiency to mTORC1
Wang, S., Tsun, Z.-Y., Wolfson, R. L., Shen, K., Wyant, G. A., Plovanich, M., Yuan, E. D., Jones, T. D., Chantranupong, L., Comb, W. C., et al. (2015) · Science · doi:10.1126/science.1257132 · Cited by 865
The CASTOR Proteins Are Arginine Sensors for the mTORC1 Pathway
Chantranupong, L., Scaria, S. M., Saxton, R. A., Gygi, M. P., Shen, K., Wyant, G. A., Wang, T., Harper, J. W., Gygi, S. P., & Sabatini, D. M. (2016) · Cell · doi:10.1016/j.cell.2016.02.035 · Cited by 843
Arginase: an emerging key player in the mammalian immune system
Munder, M. (2009) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2009.00291.x · Cited by 725
CATs and HATs: the SLC7 family of amino acid transporters
Verrey, F., Closs, E. I., Wagner, C. A., Palacı́n, M., Endou, H., & Kanai, Y. (2004) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-003-1086-z · Cited by 709
SLC38A9 is a component of the lysosomal amino acid sensing machinery that controls mTORC1
Rebsamen, M., Pochini, L., Stasyk, T., de Araújo, M. E. G., Galluccio, M., Kandasamy, R. K., Snijder, B., Fauster, A., Rudashevskaya, E. L., Bruckner, M., et al. (2015) · Nature · doi:10.1038/nature14107 · Cited by 673
Arginine Metabolism: Boundaries of Our Knowledge
Morris, S. M. (2007) · Journal of Nutrition · doi:10.1093/jn/137.6.1602s · Cited by 649
Self-citation
Signaling Pathways and Molecular Mechanisms through which Branched-Chain Amino Acids Mediate Translational Control of Protein Synthesis
Kimball, S. R., & Jefferson, L. S. (2006) · Journal of Nutrition · doi:10.1093/jn/136.1.227s · Cited by 637
Recent advances in arginine metabolism: roles and regulation of the arginases
Morris Jr, S. M. (2009) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2009.00278.x · Cited by 485
Biological significance of endogenous methylarginines that inhibit nitric oxide synthases
Leiper, J. (1999) · Cardiovascular Research · doi:10.1016/s0008-6363(99)00162-5 · Cited by 458
Arginine: beyond protein
Morris, S. M. (2006) · American Journal of Clinical Nutrition · doi:10.1093/ajcn/83.2.508s · Cited by 430
Self-citation
Translational control of inducible nitric oxide synthase expression by arginine can explain the arginine paradox
Lee, J.-H., Ryu, H., Ferrante, R. J., Morris, S. M., & Ratan, R. R. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0735876100 · Cited by 365
Self-citation
Purification and properties of a new enzyme, N, N-dimethylarginine dimethylaminohydrolase, from rat kidney
Ogawa, T., Kimoto, M., & Sasaoka, K. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)81786-0 · Cited by 364
Plasma Membrane Transporters for Arginine
Closs, E. I., Simon, A., Vékony, N., & Rotmann, A. (2004) · Journal of Nutrition · doi:10.1093/jn/134.10.2752s · Cited by 297
The role of asymmetric and symmetric dimethylarginines in renal disease
Schwedhelm, E., & Böger, R. H. (2011) · Nature Reviews Nephrology · doi:10.1038/nrneph.2011.31 · Cited by 262
Arginine de novo and nitric oxide production in disease states
Luiking, Y. C., Have, G. A. M. T., Wolfe, R. R., & Deutz, N. E. P. (2012) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00284.2012 · Cited by 250
Evidence for the Pathophysiological Role of Endogenous Methylarginines in Regulation of Endothelial NO Production and Vascular Function
Cardounel, A. J., Cui, H., Samouilov, A., Johnson, W., Kearns, P. N., Tsai, A.-L., Berka, V., & Zweier, J. L. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m603606200 · Cited by 249
Structure and Function of Cationic Amino Acid Transporters (CATs)
Closs, E. I., Boissel, J., Habermeier, A., & Rotmann, A. (2006) · The Journal of Membrane Biology · doi:10.1007/s00232-006-0875-7 · Cited by 249
Amino acid sensing in dietary-restriction-mediated longevity: roles of signal-transducing kinases GCN2 and TOR
Gallinetti, J., Harputlugil, E., & Mitchell, J. R. (2012) · Biochemical Journal · doi:10.1042/bj20121098 · Cited by 234
Requirement of argininosuccinate lyase for systemic nitric oxide production
Erez, A., Nagamani, S. C. S., Shchelochkov, O. A., Premkumar, M. H., Campeau, P. M., Chen, Y., Garg, H. K., Li, L., Mian, A., Bertin, T. K., et al. (2011) · Nature Medicine · doi:10.1038/nm.2544 · Cited by 233
REGULATION OF CATIONIC AMINO ACID TRANSPORT: The Story of the CAT-1 Transporter
Hatzoglou, M., Fernandez, J., Yaman, İ., & Closs, E. I. (2004) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.23.011702.073120 · Cited by 218
Aldehyde dehydrogenase 1a1 mediates a GABA synthesis pathway in midbrain dopaminergic neurons
Kim, J.-I., Ganesan, S., Luo, S. X., Wu, Y.-W., Park, E., Huang, E. J., Chen, L., & Ding, J. B. (2015) · Science · doi:10.1126/science.aac4690 · Cited by 217
Deorphanization of GPRC6A: A Promiscuous l-α-Amino Acid Receptor with Preference for Basic Amino Acids
Wellendorph, P., Hansen, K. B., Balsgaard, A., Greenwood, J. R., Egebjerg, J., & Bräuner‐Osborne, H. (2004) · Molecular Pharmacology · doi:10.1124/mol.104.007559 · Cited by 207
Substrate Specificity of NO Synthases: Detailed Comparison of l -Arginine, Homo- l -arginine, Their Nω-Hydroxy Derivatives, and Nω-Hydroxynor- l -arginine
Moali, C., Boucher, J., Sari, M., Stuehr, D. J., & Mansuy, D. (1998) · Biochemistry · doi:10.1021/bi980742t · Cited by 203
Putrescine catabolism in mammalian brain
Seiler, N., & Al‐Therib, M. J. (1974) · Biochemical Journal · doi:10.1042/bj1440029 · Cited by 201
The G Protein-Coupled Taste Receptor T1R1/T1R3 Regulates mTORC1 and Autophagy
Wauson, E., Zaganjor, E., Lee, A.-Y., Guerra, M. L., Ghosh, A. B., Bookout, A. L., Chambers, C. P., Jivan, A., McGlynn, K., Hutchison, M. R., et al. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.08.001 · Cited by 199
Regulation of Internal Ribosomal Entry Site-mediated Translation by Phosphorylation of the Translation Initiation Factor eIF2α
Fernandez, J., Yaman, İ., Sarnow, P., Snider, M. D., & Hatzoglou, M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201052200 · Cited by 196
Protein arginine methylation of non-histone proteins and its role in diseases
Han, W., Mundade, R., Lange, K., & Lu, T. (2013) · Cell Cycle · doi:10.4161/cc.27353 · Cited by 193
Citrulline: From metabolism to therapeutic use
Bahri, S., Zerrouk, N., Aussel, C., Moinard, C., Crenn, P., Curis, E., Chaumeil, J., Cynober, L., & Sfar, S. (2012) · Nutrition · doi:10.1016/j.nut.2012.07.002 · Cited by 186
Homoarginine, Cardiovascular Risk, and Mortality
März, W., Meinitzer, A., Drechsler, C., Pilz, S., Krane, V., Kleber, M. E., Fischer, J. E., Winkelmann, B. R., Böhm, B. O., Ritz, E., et al. (2010) · Circulation · doi:10.1161/circulationaha.109.908988 · Cited by 186
Role of Dimethylarginine Dimethylaminohydrolases in the Regulation of Endothelial Nitric Oxide Production
Pope, A. J., Karuppiah, K. M., Kearns, P. N., Xia, Y., & Cardounel, A. J. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.037036 · Cited by 185
Sustained Generation of Nitric Oxide and Control of Mycobacterial Infection Requires Argininosuccinate Synthase 1
Qualls, J. E., Subramanian, C., Rafi, W., Smith, A. M., Balouzian, L., DeFreitas, A. A., Shirey, K. A., Reutterer, B., Kernbauer, E., Stockinger, S., et al. (2012) · Cell Host & Microbe · doi:10.1016/j.chom.2012.07.012 · Cited by 184
Role of arginine metabolism in immunity and immunopathology
Peranzoni, E., Marigo, I., Dolcetti, L., Ugel, S., Sonda, N., Taschin, E., Mantelli, B., Bronte, V., & Zanovello, P. (2007) · Immunobiology · doi:10.1016/j.imbio.2007.09.008 · Cited by 181
Argininosuccinate synthase: at the center of arginine metabolism.
(2011) · Europe PMC (PubMed Central) · Cited by 176
Rat Liver Arginase: Kinetic Mechanism, Alternate Substrates, and Inhibitors
Reczkowski, R. S., & Ash, D. E. (1994) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1994.1276 · Cited by 168
Two Distinct Determinants of Ligand Specificity in T1R1/T1R3 (the Umami Taste Receptor)
Toda, Y., Nakagita, T., Hayakawa, T., Okada, S., Narukawa, M., Imai, H., Ishimaru, Y., & Misaka, T. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.494443 · Cited by 159
Citrulline and nitrogen homeostasis: an overview
Breuillard, C., Cynober, L., & Moinard, C. (2015) · Amino Acids · doi:10.1007/s00726-015-1932-2 · Cited by 159
Targeting arginine metabolism pathway to treat arginine-dependent cancers
Qiu, F., Huang, J., & Sui, M. (2015) · Cancer Letters · doi:10.1016/j.canlet.2015.04.020 · Cited by 158
Channeling of Urea Cycle Intermediates in Situ in Permeabilized Hepatocytes
Cheung, C. W., Cohen, N. S., & Raijman, L. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)84958-x · Cited by 156
Analysis of Citrulline, Arginine, and Methylarginines Using High‐Performance Liquid Chromatography
Wu, G., & Meininger, C. J. (2008) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(07)00810-5 · Cited by 150
Homoarginine Levels Are Regulated by l -Arginine:Glycine Amidinotransferase and Affect Stroke Outcome
Choe, C., Atzler, D., Wild, P. S., Carter, A. M., Böger, R. H., Ojeda, F., Simova, O., Stockebrand, M. C., Lackner, K. J., Nabuurs, C. I. H. C., et al. (2013) · Circulation · doi:10.1161/circulationaha.112.000580 · Cited by 148
ARG2 impairs endothelial autophagy through regulation of MTOR and PRKAA/AMPK signaling in advanced atherosclerosis
Xiong, Y., Yepuri, G., Forbiteh, M., Yu, Y., Montani, J., Yang, Z., & Ming, X. (2014) · Autophagy · doi:10.4161/15548627.2014.981789 · Cited by 143
Arginine and Leucine regulate p70 S6 kinase and 4E-BP1 in intestinal epithelial cells
Ban, H., Shigemitsu, K., Yamatsuji, T., Haisa, M., Nakajo, T., Takaoka, M., Nobuhisa, T., Gündüz, M., Tanaka, N., & Naomoto, Y. (2004) · International Journal of Molecular Medicine · doi:10.3892/ijmm.13.4.537 · Cited by 142
Dimethylarginine Dimethylaminohydrolase-1 Is the Critical Enzyme for Degrading the Cardiovascular Risk Factor Asymmetrical Dimethylarginine
Hu, X., Atzler, D., Xu, X. Y., Zhang, P., Guo, H., Lu, Z., Fassett, J., Schwedhelm, E., Böger, R. H., Bache, R. J., et al. (2011) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.110.222638 · Cited by 138
Cloning and characterization of a Family C orphan G‐protein coupled receptor
Kuang, D., Yao, Y., Lam, J., Tsushima, R. G., & Hampson, D. R. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03025.x · Cited by 133
l-Arginine and its metabolites in kidney and cardiovascular disease
Popolo, A., Adesso, S., Pinto, A., Autore, G., & Marzocco, S. (2014) · Amino Acids · doi:10.1007/s00726-014-1825-9 · Cited by 129
Glutamine is an important precursor for de novo synthesis of arginine in humans
Ligthart‐Melis, G. C., van de Poll, M. C. G., Boelens, P. G., Dejong, C. H. C., Deutz, N. E. P., & van Leeuwen, P. A. M. (2008) · American Journal of Clinical Nutrition · doi:10.1093/ajcn/87.5.1282 · Cited by 120
The GPCR , class C , group 6, subtype A ( GPRC6A ) receptor: from cloning to physiological function
Clemmensen, C., Smajilovic, S., Wellendorph, P., & Bräuner‐Osborne, H. (2013) · British Journal of Pharmacology · doi:10.1111/bph.12365 · Cited by 103
Role of Neutral Amino Acid Transport and Protein Breakdown for Substrate Supply of Nitric Oxide Synthase in Human Endothelial Cells
Simon, A., Plies, L., Habermeier, A., Martiné, U., Reining, M., & Closs, E. I. (2003) · Circulation Research · doi:10.1161/01.res.0000097761.19223.0d · Cited by 102
Low homoarginine concentration is a novel risk factor for heart disease
Pilz, S., Meinitzer, A., Tomaschitz, A., Drechsler, C., Ritz, E., Krane, V., Wanner, C., Boehm, B. O., & Marz, W. (2011) · Heart · doi:10.1136/hrt.2010.220731 · Cited by 102
Broad-spectrum l-amino acid sensing by class 3 G-protein-coupled receptors
Conigrave, A. D., & Hampson, D. R. (2006) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2006.10.012 · Cited by 101
Argininosuccinate Synthase Expression Is Required to Maintain Nitric Oxide Production and Cell Viability in Aortic Endothelial Cells
Goodwin, B. L., Solomonson, L. P., & Eichler, D. C. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m308160200 · Cited by 100
Mitochondrial Arginase II Modulates Nitric-Oxide Synthesis through Nonfreely Exchangeable l-Arginine Pools in Human Endothelial Cells
Topal, G., Brunet, A., Walch, L., Boucher, J., & David‐Dufilho, M. (2006) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.106.103747 · Cited by 100
Multiligand Specificity and Wide Tissue Expression of GPRC6A Reveals New Endocrine Networks
Pi, M., & Quarles, L. D. (2012) · Endocrinology · doi:10.1210/en.2011-2117 · Cited by 95
Safety and Effectiveness of Arginine in Adults
McNeal, C. J., Meininger, C. J., Reddy, D., Wilborn, C., & Wu, G. (2016) · Journal of Nutrition · doi:10.3945/jn.116.234740 · Cited by 93
Arginase‐II Induces Vascular Smooth Muscle Cell Senescence and Apoptosis Through p66Shc and p53 Independently of Its l ‐Arginine Ureahydrolase Activity: Implications for Atherosclerotic Plaque Vulnerability
Xiong, Y., Yu, Y., Montani, J., Yang, Z., & Ming, X. (2013) · Journal of the American Heart Association · doi:10.1161/jaha.113.000096 · Cited by 91
Arginine-induced stimulation of protein synthesis and survival in IPEC-J2 cells is mediated by mTOR but not nitric oxide
Bauchart‐Thevret, C., Cui, L., Wu, G., & Burrin, D. G. (2010) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00068.2010 · Cited by 91
Homoarginine, arginine, and relatives: analysis, metabolism, transport, physiology, and pathology
Tsikas, D., & Wu, G. (2015) · Amino Acids · doi:10.1007/s00726-015-2055-5 · Cited by 90
Homoarginine and Cardiovascular Outcome in the Population-Based Dallas Heart Study
Atzler, D., Gore, M. O., Ayers, C. R., Choe, C., Böger, R. H., de Lemos, J. A., McGuire, D. K., & Schwedhelm, E. (2014) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.114.304398 · Cited by 89
Glutamine is a key regulator for amino acid-controlled cell growth through the mTOR signaling pathway in rat intestinal epithelial cells.
Nakajo, T., Yamatsuji, T., Ban, H., Shigemitsu, K., Haisa, M., Motoki, T., Noma, K., Nobuhisa, T., Matsuoka, J., Gunduz, M., et al. (2004) · Biochemical and Biophysical Research Communications - BBRC · doi:10.1016/j.bbrc.2004.11.015 · Cited by 88
Promiscuous activity of arginine:glycine amidinotransferase is responsible for the synthesis of the novel cardiovascular risk factor homoarginine
Davids, M., Ndika, J., Salomons, G. S., Blom, H. J., & Teerlink, T. (2012) · FEBS Letters · doi:10.1016/j.febslet.2012.08.020 · Cited by 87
Reference Intervals for Plasma L-Arginine and the L-Arginine:Asymmetric Dimethylarginine Ratio in the Framingham Offspring Cohort
Lüneburg, N., Xanthakis, V., Schwedhelm, E., SULLIVAN, L. M., Maas, R., Anderssohn, M., Riederer, U., Glazer, N. L., Vasan, R. S., & Böger, R. H. (2011) · Journal of Nutrition · doi:10.3945/jn.111.148197 · Cited by 86
Arginyltransferase ATE1 Catalyzes Midchain Arginylation of Proteins at Side Chain Carboxylates In Vivo
Wang, J., Han, X., Wong, C. C. L., Cheng, H., Aslanian, A., Xu, T., Leavis, P. C., Röder, H., Hedstrom, L., Yates, J. R., et al. (2014) · Chemistry & Biology · doi:10.1016/j.chembiol.2013.12.017 · Cited by 86
The biochemistry, measurement and current clinical significance of asymmetric dimethylarginine
Blackwell, S. (2009) · Annals of Clinical Biochemistry International Journal of Laboratory Medicine · doi:10.1258/acb.2009.009196 · Cited by 84
Arginine deprivation in cancer therapy
Feun, L. G., Kuo, M. T., & Savaraj, N. (2014) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/mco.0000000000000122 · Cited by 84
A direct screen for c-di-GMP modulators reveals a Salmonella Typhimurium periplasmic ʟ-arginine–sensing pathway
Mills, E., Petersen, E. M., Kulasekara, B. R., & Miller, S. I. (2015) · Science Signaling · doi:10.1126/scisignal.aaa1796 · Cited by 84
Catabolism and safety of supplemental l-arginine in animals
Wu, Z., Hou, Y., Hu, S., Bazer, F. W., Meininger, C. J., McNeal, C. J., & Wu, G. (2016) · Amino Acids · doi:10.1007/s00726-016-2245-9 · Cited by 84
L-Homoarginine and cardiovascular disease
Atzler, D., Schwedhelm, E., & Choe, C. (2014) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/mco.0000000000000123 · Cited by 81
Protein arginine methyltransferases (PRMTs): Role in chromatin organization
Jahan, S., & Davie, J. R. (2014) · Advances in Biological Regulation · doi:10.1016/j.jbior.2014.09.003 · Cited by 80
Minireview: Nutrient Sensing by G Protein-Coupled Receptors
Wauson, E., Lorente-Rodríguez, A., & Cobb, M. H. (2013) · Molecular Endocrinology · doi:10.1210/me.2013-1100 · Cited by 79
AGXT2: a promiscuous aminotransferase
Rodionov, R. N., Jarzebska, N., Weiss, N., & Lentz, S. R. (2014) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2014.09.005 · Cited by 79
Homoarginine in the renal and cardiovascular systems
Pilz, S., Meinitzer, A., Gaksch, M., Grübler, M. R., Verheyen, N., Drechsler, C., Hartaigh, B. Ó., Lang, F. J. W., Alesutan, I., Voelkl, J. G. J., et al. (2015) · Amino Acids · doi:10.1007/s00726-015-1993-2 · Cited by 77
Arginyltransferase, Its Specificity, Putative Substrates, Bidirectional Promoter, and Splicing-derived Isoforms
Hu, R., Brower, C. S., Wang, H., Davydov, I. V., Sheng, J., Zhou, J., Kwon, Y. T., & Varshavsky, A. J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m604355200 · Cited by 77
On the substrate specificity of nitric oxide synthase
Hecker, M., Walsh, D. T., & Vane, J. R. (1991) · FEBS Letters · doi:10.1016/0014-5793(91)81434-a · Cited by 75
Cloning of human agmatinase. An alternate path for polyamine synthesis induced in liver by hepatitis B virus
Mistry, S. K., Burwell, T., Chambers, R. M., Rudolph‐Owen, L. A., Spaltmann, F., Cook, W. J., & Morris, S. M. (2002) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00386.2001 · Cited by 73
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Rosenthal, M. D., Carrott, P. W., Patel, J. J., Kiraly, L. N., & Martindale, R. G. (2016) · Journal of Nutrition · doi:10.3945/jn.115.228544 · Cited by 73
Stable isotope dilution assay for liquid chromatography–tandem mass spectrometric determination of l-homoarginine in human plasma
Atzler, D., Mieth, M., Maas, R., Böger, R. H., & Schwedhelm, E. (2011) · Journal of Chromatography B · doi:10.1016/j.jchromb.2011.06.016 · Cited by 65
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Marini, J. C. (2012) · Journal of Nutrition · doi:10.3945/jn.111.153825 · Cited by 65
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Sell, D. R., & Monnier, V. M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m408946200 · Cited by 64
Accessibility of endothelial and inducible nitric oxide synthase to the intracellular citrulline–arginine regeneration pathway
Shen, L., Beloussow, K., & Shen, W. (2004) · Biochemical Pharmacology · doi:10.1016/j.bcp.2004.09.003 · Cited by 60
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Tomlinson, C., Rafii, M., Ball, R. O., & Pencharz, P. B. (2011) · Journal of Nutrition · doi:10.3945/jn.110.137224 · Cited by 59
Regulation of Endothelial Nitric Oxide Synthase Activity by Protein-Protein Interaction
Su, Y. (2014) · Current Pharmaceutical Design · doi:10.2174/13816128113196660752 · Cited by 57
Glutamine: precursor or nitrogen donor for citrulline synthesis?
Marini, J. C., Didelija, I. C., Castillo, L., & Lee, B. (2010) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00080.2010 · Cited by 54
Homoarginine and mortality in an older population: the H oorn study
Pilz, S., Teerlink, T., Scheffer, P. G., Meinitzer, A., Rutters, F., Tomaschitz, A., Drechsler, C., Kienreich, K., Nijpels, G., Stehouwer, C. D. A., et al. (2013) · European Journal of Clinical Investigation · doi:10.1111/eci.12208 · Cited by 52
GABAergic system in the developing mammalian retina: dual sources of GABA at early stages of postnatal development
Yamasaki, E. N., Barbosa, V. D., Mello, F. G. D., & Hokoç, J. N. (1999) · International Journal of Developmental Neuroscience · doi:10.1016/s0736-5748(99)00002-7 · Cited by 49
Biosynthesis of homoarginine (hArg) and asymmetric dimethylarginine (ADMA) from acutely and chronically administered free l-arginine in humans
Kayacelebi, A. A., Langen, J., Weigt-Usinger, K., Chobanyan-Jürgens, K., Mariotti, F., Schneider, J. Y., Rothmann, S., Frölich, J. C., Atzler, D., Choe, C., et al. (2015) · Amino Acids · doi:10.1007/s00726-015-2012-3 · Cited by 47
Differential Requirements for l -Citrulline and l -Arginine during Antimycobacterial Macrophage Activity
Rapovy, S. M., Zhao, J., Bricker, R. L., Schmidt, S., Setchell, K. D. R., & Qualls, J. E. (2015) · The Journal of Immunology · doi:10.4049/jimmunol.1500800 · Cited by 45
Mitochondrial transporters for ornithine and related amino acids: a review
Monné, M., Miniero, D. V., Daddabbo, L., Palmieri, L., Porcelli, V., & Palmieri, F. (2015) · Amino Acids · doi:10.1007/s00726-015-1990-5 · Cited by 44
Arginine synthesis from enteral glutamine in healthy adults in the fed state
Tomlinson, C., Rafii, M., Ball, R. O., & Pencharz, P. B. (2011) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00006.2011 · Cited by 44
Systemic hypertension in two patients with ASL deficiency: A result of nitric oxide deficiency?
Brunetti‐Pierri, N., Erez, A., Shchelochkov, O. A., Craigen, W. J., & Lee, B. (2009) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2009.06.006 · Cited by 43
Methods using stable isotopes to measure nitric oxide (NO) synthesis in the l-arginine/NO pathway in health and disease
van Eijk, H. M. H., Luiking, Y. C., & Deutz, N. E. P. (2006) · Journal of Chromatography B · doi:10.1016/j.jchromb.2006.08.054 · Cited by 42
Role of asymmetrical dimethylarginine in the progression of renal disease
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Marini, J. C. (2015) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/mco.0000000000000233 · Cited by 41
Systemic inflammation is linked to low arginine and high ADMA plasma levels resulting in an unfavourable NOS substrate-to-inhibitor ratio: the Hoorn Study
van der Zwan, L. P., Scheffer, P. G., Dekker, J. M., Stehouwer, C. D. A., Heine, R. J., & Teerlink, T. (2011) · Clinical Science · doi:10.1042/cs20100595 · Cited by 40
GC–MS and GC–MS/MS measurement of the cardiovascular risk factor homoarginine in biological samples
Kayacelebi, A. A., Beckmann, B., Gutzki, F., Jordan, J., & Tsikas, D. (2014) · Amino Acids · doi:10.1007/s00726-014-1774-3 · Cited by 40
Mass spectrometric quantification of L-arginine and its pathway related substances in biofluids: The road to maturity
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Two cases suggesting a role for the L–arginine nitric oxide pathway in neonatal blood pressure regulation
Fakler, C., Kaftan, H., & Nelin, L. (1995) · Acta Paediatrica · doi:10.1111/j.1651-2227.1995.tb13673.x · Cited by 38
Plasma concentrations of arginine and asymmetric dimethylarginine do not reflect their intracellular concentrations in peripheral blood mononuclear cells
Davids, M., & Teerlink, T. (2013) · Metabolism · doi:10.1016/j.metabol.2013.05.017 · Cited by 34
Asymmetric dimethylarginine and critical illness
Brinkmann, S. J. H., de Boer, M. C., Buijs, N., & van Leeuwen, P. A. M. (2013) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/mco.0000000000000020 · Cited by 33
Role of dimethylarginine dimethylaminohydrolase activity in regulation of tissue and plasma concentrations of asymmetric dimethylarginine in an animal model of prolonged critical illness
Davids, M., Richir, M. C., Visser, M., Ellger, B., den Berghe, G. V., van Leeuwen, P. A. M., & Teerlink, T. (2011) · Metabolism · doi:10.1016/j.metabol.2011.08.007 · Cited by 29
Extrarenal citrulline disposal in mice with impaired renal function
Marini, J. C., Didelija, I. C., & Fiorotto, M. L. (2014) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00289.2014 · Cited by 28
Plasma and tissue homoarginine concentrations in healthy and obese humans
May, M., Kayacelebi, A. A., Bátkai, S., Jordan, J., Tsikas, D., & Engeli, S. (2015) · Amino Acids · doi:10.1007/s00726-015-1922-4 · Cited by 27
Opposite Associations of Plasma Homoarginine and Ornithine with Arginine in Healthy Children and Adolescents
Jaźwińska-Kozuba, A., Martens‐Lobenhoffer, J., Kruszelnicka, O., Rycaj, J., Chyrchel, B., Surdacki, A., & Bode‐Böger, S. M. (2013) · International Journal of Molecular Sciences · doi:10.3390/ijms141121819 · Cited by 26
Bioanalytical profile of the l-arginine/nitric oxide pathway and its evaluation by capillary electrophoresis
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Sources of arginine for induced nitric oxide synthesis in the isolated perfused liver
Pastor, C. M., Morris, S. M., & Billiar, T. R. (1995) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.1995.269.6.g861 · Cited by 23
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Glutamine: precursor or nitrogen donor for citrulline synthesis?
Ligthart‐Melis, G. C., Vermeulen, M. A. R., van Leeuwen, P. A. M., & Deutz, N. E. P. (2010) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00425.2010 · Cited by 19
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Martens‐Lobenhoffer, J., & Bode‐Böger, S. M. (2014) · Journal of Chromatography B · doi:10.1016/j.jchromb.2014.11.009 · Cited by 18
Relative contribution of different l-arginine sources to the substrate supply of endothelial nitric oxide synthase
Karbach, S. H., Simon, A., Slenzka, A., Jaenecke, I., Habermeier, A., Martiné, U., Förstermann, U., & Closs, E. I. (2011) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2011.07.024 · Cited by 17
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Decoding the Substrate Supply to Human Neuronal Nitric Oxide Synthase
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Ligthart‐Melis, G. C., Marini, J. C., ENGELEN, M. P. K. J., & Deutz, N. E. P. (2015) · American Journal of Clinical Nutrition · doi:10.3945/ajcn.114.104679 · Cited by 7
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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)
DOI: 10.3945/jn.115.226621
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: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 2248 d)
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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