Arginase: A Multifaceted Enzyme Important in Health and Disease

Caldwell, R. William; Rodriguez, Paulo C.; Toque, Haroldo A.; Narayanan, S. Priya; Caldwell, Ruth B.

doi:10.1152/physrev.00037.2016

Cited by 502Amino Acid Enzymes and MetabolismNitric Oxide and Endothelin EffectsPolyamine Metabolism and Applications

Arginase: A Multifaceted Enzyme Important in Health and Disease

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Caldwell, R. William, Rodriguez, Paulo C., Toque, Haroldo A., Narayanan, S. Priya, Caldwell, Ruth B.·2018·Physiological Reviews

DOI 10.1152/physrev.00037.2016PMC PMC5966718

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Abstract

The arginase enzyme developed in early life forms and was maintained during evolution. As the last step in the urea cycle, arginase cleaves l-arginine to form urea and l-ornithine. The urea cycle provides protection against excess ammonia, while l-ornithine is needed for cell proliferation, collagen formation, and other physiological functions. In mammals, increases in arginase activity have been linked to dysfunction and pathologies of the cardiovascular system, kidney, and central nervous system and also to dysfunction of the immune system and cancer. Two important aspects of the excessive activity of arginase may be involved in diseases. First, overly active arginase can reduce the supply of l-arginine needed for the production of nitric oxide (NO) by NO synthase. Second, too much l-ornithine can lead to structural problems in the vasculature, neuronal toxicity, and abnormal growth of tumor cells. Seminal studies have demonstrated that increased formation of reactive oxygen species and key inflammatory mediators promote this pathological elevation of arginase activity. Here, we review the involvement of arginase in diseases affecting the cardiovascular, renal, and central nervous system and cancer and discuss the value of therapies targeting the elevated activity of arginase.

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Exacerbated arginase activity can decrease l-arginine levels and cause eNOS uncoupling.
“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 [144]
Arginases play an important role in the regulation of l-arginine levels.
“Finally, it must be noted that arginases play an important role in the regulation of l-arginine levels (144, 259, 734, 804).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [144]

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Gu, X., Samuel, S., El-Shabrawey, M., Caldwell, R. B., Bartoli, M., Marcus, D. M., & Brooks, S. E. (2002) · PubMed · Cited by 79 · see citing works
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A Large-Scale Chemical Screen for Regulators of the Arginase 1 Promoter Identifies the Soy Isoflavone Daidzeinas a Clinically Approved Small Molecule That Can Promote Neuronal Protection or Regeneration via a cAMP-Independent Pathway
Ma, T. C., Campana, A., Lange, P. S., Lee, H., Banerjee, K., Bryson, J. B., Mahishi, L., Alam, S., Giger, R. J., Barnes, S., et al. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.5266-09.2010 · Cited by 79 · see citing works
Is the Urea Cycle Involved in Alzheimer's Disease?
Hansmannel, F., Sillaire, A. R., Kamboh, M. I., Lendon, C. L., Pasquier, F., Hannequin, D., Laumet, G. O., Mounier, A., Ayral, A., DeKosky, S. T., et al. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-100630 · Cited by 78 · see citing works
Development of Novel Arginase Inhibitors for Therapy of Endothelial Dysfunction
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Arginase inhibition restores in vivo coronary microvascular function in type 2 diabetic rats
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Expression and Activity of Arginase Isoenzymes During Normal and Diabetes-Impaired Skin Repair
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Transport of extracellular l -arginine via cationic amino acid transporter is required during in vivo endothelial nitric oxide production
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Increased Synthesis of Spermidine as a Result of Upregulation of Arginase I Promotes Axonal Regeneration in Culture andIn Vivo
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NOX2-Induced Activation of Arginase and Diabetes-Induced Retinal Endothelial Cell Senescence
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Alterations in NF kappa B/Rel family proteins in splenic T-cells from tumor-bearing mice and reversal following therapy.
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Arginase-1 is expressed exclusively by infiltrating myeloid cells in CNS injury and disease
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Simvastatin Improves Diabetes-Induced Coronary Endothelial Dysfunction
Tawfik, H. E., El‐Remessy, A. B., Matragoon, S., Ma, G., Caldwell, R. B., & Caldwell, R. W. (2006) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.106.106823 · Cited by 70 · see citing works
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Increased arginase levels in heart failure represent a therapeutic target to rescue microvascular perfusion
Quitter, F., Figulla, H. R., Ferrari, M. W., Pernow, J., & Jung, C. (2013) · Clinical Hemorheology and Microcirculation · doi:10.3233/ch-2012-1617 · Cited by 70 · see citing works
Targeting Ornithine Decarboxylase by α-Difluoromethylornithine Inhibits Tumor Growth by Impairing Myeloid-Derived Suppressor Cells
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Neurotoxicity of reactive aldehydes: The concept of “aldehyde load” as demonstrated by neuroprotection with hydroxylamines
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Arginase 2 deficiency reduces hyperoxia-mediated retinal neurodegeneration through the regulation of polyamine metabolism
Narayanan, S. P., Xu, Z., Putluri, N., Sreekumar, A., Lemtalsi, T., Caldwell, R. W., & Caldwell, R. B. (2014) · Cell Death and Disease · doi:10.1038/cddis.2014.23 · Cited by 68 · see citing works
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Local Arginase Inhibition during Early Reperfusion Mediates Cardioprotection via Increased Nitric Oxide Production
Gonon, A. T., Jung, C., Katz, A., Westerblad, H., Shemyakin, A. S., Sjöquist, P.-O. B., Lundberg, J. O., & Pernow, J. (2012) · PLoS ONE · doi:10.1371/journal.pone.0042038 · Cited by 68 · see citing works
Arginase 2 promotes neurovascular degeneration during ischemia/reperfusion injury
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Expression of arginine decarboxylase in brain regions and neuronal cells
Iyo, A. H., Zhu, M., Ordway, G. A., & Regunathan, S. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03544.x · Cited by 67 · see citing works
Arginase Activity Mediates Retinal Inflammation in Endotoxin-Induced Uveitis
Zhang, W., Baban, B., Rojas, M., Tofigh, S., Virmani, S. K., Patel, C., Behzadian, M. A., Romero, M. J., Caldwell, R. W., & Caldwell, R. B. (2009) · American Journal Of Pathology · doi:10.2353/ajpath.2009.081115 · Cited by 67 · see citing works
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Ornithine deficiency in the arginase double knockout mouse
Deignan, J. L., Livesay, J. C., Yoo, P. K., GOODMAN, S., O’Brien, W. E., IYER, R., Cederbaum, S. D., & Grody, W. W. (2006) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2006.04.007 · Cited by 66 · see citing works
The role of arginase I in diabetes-induced retinal vascular dysfunction in mouse and rat models of diabetes
Elms, S. C., Toque, H. A., Rojas, M., Xu, Z., Caldwell, R. W., & Caldwell, R. B. (2012) · Diabetologia · doi:10.1007/s00125-012-2789-5 · Cited by 66 · see citing works
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Intracellular l-arginine concentration does not determine NO production in endothelial cells: Implications on the “l-arginine paradox”
Shin, S., Mohan, S., & Fung, H. (2011) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2011.09.112 · Cited by 65 · see citing works
Arginase II Deletion Increases Corpora Cavernosa Relaxation in Diabetic Mice
Toque, H. A., Tostes, R. C., Yao, L., Xu, Z., Webb, R. C., Caldwell, R. B., & Caldwell, R. W. (2010) · The Journal of Sexual Medicine · doi:10.1111/j.1743-6109.2010.02098.x · Cited by 65 · see citing works
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Shaping the Murine Macrophage Phenotype: IL-4 and Cyclic AMP Synergistically Activate the Arginase I Promoter
Sheldon, K. E., Shandilya, H. K., Kepka‐Lenhart, D., Poljakovic, M., Ghosh, A., & Morris, S. M. (2013) · The Journal of Immunology · doi:10.4049/jimmunol.1202102 · Cited by 65 · see citing works
Biochemical and Functional Profile of a Newly Developed Potent and Isozyme-Selective Arginase Inhibitor
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Blocking a vicious cycle nNOS/peroxynitrite/AMPK by S-nitrosoglutathione: implication for stroke therapy
Khan, M., Dhammu, T. S., Matsuda, F., Singh, A. K., & Singh, I. (2015) · BMC Neuroscience · doi:10.1186/s12868-015-0179-x · Cited by 64 · see citing works
Contrasting features of urea cycle disorders in human patients and knockout mouse models
Deignan, J. L., Cederbaum, S. D., & Grody, W. W. (2008) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2007.08.123 · Cited by 64 · see citing works
Arginase as a mediator of diabetic retinopathy
Patel, C. (2013) · Frontiers in Immunology · doi:10.3389/fimmu.2013.00173 · Cited by 64 · see citing works
Eflornithine (DFMO) Prevents Progression of Pancreatic Cancer by Modulating Ornithine Decarboxylase Signaling
Mohammed, A., Janakiram, N. B., Madka, V., Ritchie, R. L., Brewer, M. F., Biddick, L., Patlolla, J. M. R., Sadeghi, M., Lightfoot, S. A., Steele, V. E., et al. (2014) · Cancer Prevention Research · doi:10.1158/1940-6207.capr-14-0176 · Cited by 64 · see citing works
Transcriptional Regulation of Endothelial Arginase 2 by Histone Deacetylase 2
Pandey, D., Sikka, G., Bergman, Y., Kim, J. H., Ryoo, S., Romer, L. H., & Berkowitz, D. E. (2014) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.114.303685 · Cited by 63 · see citing works
Effect of stroke on arginase expression and localization in the rat brain
Quirié, A., Demougeot, C., Bertrand, N., Mossiat, C. M., Garnier, P. E., Marie, C., & Prigent‐Tessier, A. (2013) · European Journal of Neuroscience · doi:10.1111/ejn.12111 · Cited by 62 · see citing works
Novel Roles for Arginase in Cell Survival, Regeneration, and Translation in the Central Nervous System
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Macrophage: SHIP of Immunity
Mills, C., Thomas, A. C., Lenz, L., & Munder, M. (2014) · Frontiers in Immunology · doi:10.3389/fimmu.2014.00620 · Cited by 59 · see citing works
Arginase inhibition mediates renal tissue protection in diabetic nephropathy by a nitric oxide synthase 3-dependent mechanism
You, H., Gao, T., Cooper, T. K., Morris, S. M., & Awad, A. S. (2013) · Kidney International · doi:10.1038/ki.2013.215 · Cited by 58 · see citing works
Effect of Arginase Inhibition on Ischemia-Reperfusion Injury in Patients with Coronary Artery Disease with and without Diabetes Mellitus
Kövamees, O., Shemyakin, A., & Pernow, J. (2014) · PLoS ONE · doi:10.1371/journal.pone.0103260 · Cited by 57 · see citing works
Arginase 2 Deletion Reduces Neuro-Glial Injury and Improves Retinal Function in a Model of Retinopathy of Prematurity
Narayanan, S. P., Suwanpradid, J., SAUL, A. B., Xu, Z., Still, A., Caldwell, R. W., & Caldwell, R. B. (2011) · PLoS ONE · doi:10.1371/journal.pone.0022460 · Cited by 57 · see citing works
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L-Arginine and Free Radical Scavengers Increase Cerebral Blood Flow and Brain Tissue Nitric Oxide Concentrations after Controlled Cortical Impact Injury in Rats
Cherian, L., & Robertson, C. S. (2003) · Journal of Neurotrauma · doi:10.1089/08977150360517209 · Cited by 55 · see citing works
Alterations of the Arginine Metabolome in Sickle Cell Disease
Morris, C. R. (2014) · Hematology/Oncology Clinics of North America · doi:10.1016/j.hoc.2013.11.008 · Cited by 54 · see citing works
Sustained Arginase 1 Expression Modulates Pathological Tau Deposits in a Mouse Model of Tauopathy
Hunt, J. B., Nash, K. R., Placides, D. S., Moran, P., Selenica, M. B., Abuqalbeen, F., Ratnasamy, K., Slouha, N., Ospina, S. R., Savlia, M., et al. (2015) · Journal of Neuroscience · doi:10.1523/jneurosci.3959-14.2015 · Cited by 53 · see citing works
Activated Rho Kinase Mediates Diabetes-Induced Elevation of Vascular Arginase Activation and Contributes to Impaired Corpora Cavernosa Relaxation: Possible Involvement of p38 MAPK Activation
Toque, H. A., Nunes, K. P., Yao, L., Liao, J. K., Webb, R. C., Caldwell, R. B., & Caldwell, R. W. (2013) · The Journal of Sexual Medicine · doi:10.1111/jsm.12134 · Cited by 52 · see citing works
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Macrophages and metabolism in the tumor microenvironment
Vitale, I., Manic, G., Coussens, L. M., Kroemer, G., & Galluzzi, L. (2019) · Cell Metabolism · doi:10.1016/j.cmet.2019.06.001 · Cited by 1,837 · see citing works
Methylglyoxal, a Highly Reactive Dicarbonyl Compound, in Diabetes, Its Vascular Complications, and Other Age-Related Diseases
Schalkwijk, C., & Stehouwer, C. D. A. (2019) · Physiological Reviews · doi:10.1152/physrev.00001.2019 · Cited by 630 · see citing works
Quantification of microenvironmental metabolites in murine cancers reveals determinants of tumor nutrient availability
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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 · see citing works
Coupled scRNA-Seq and Intracellular Protein Activity Reveal an Immunosuppressive Role of TREM2 in Cancer
Katzenelenbogen, Y., Sheban, F., Yalin, A., Yofe, I., Svetlichnyy, D., Jaitin, D. A., Bornstein, C., Moshe, A., Keren-Shaul, H., Cohen, M., et al. (2020) · Cell · doi:10.1016/j.cell.2020.06.032 · Cited by 498 · see citing works
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 434 · see citing works
Endothelial dysfunction due to eNOS uncoupling: molecular mechanisms as potential therapeutic targets
Janaszak-Jasiecka, A., Płoska, A., Wierońska, J. M., Dobrucki, L. W., & Kalinowski, L. (2023) · Cellular & Molecular Biology Letters · doi:10.1186/s11658-023-00423-2 · Cited by 358 · see citing works
The relationship between nutrition and the immune system
Munteanu, C., & Schwartz, B. (2022) · Frontiers in Nutrition · doi:10.3389/fnut.2022.1082500 · Cited by 315 · see citing works
Nitric oxide signalling in kidney regulation and cardiometabolic health
Carlström, M. (2021) · Nature Reviews Nephrology · doi:10.1038/s41581-021-00429-z · Cited by 264 · see citing works
Immune biology of glioma associated macrophages and microglia: Functional and therapeutic implications
Wei, J., Chen, P., Gupta, P., Ott, M., Zamler, D. B., Kassab, C., Bhat, K., Curran, M. A., de Groot, J., & Heimberger, A. B. (2019) · Neuro-Oncology · doi:10.1093/neuonc/noz212 · Cited by 192 · see citing works
Endothelial Dysfunction Driven by Hypoxia—The Influence of Oxygen Deficiency on NO Bioavailability
Janaszak‐Jasiecka, A., Siekierzycka, A., Płoska, A., Dobrucki, I. T., & Kalinowski, L. (2021) · Biomolecules · doi:10.3390/biom11070982 · Cited by 189 · see citing works
Arginase 1 is a key driver of immune suppression in pancreatic cancer
Menjivar, R. E., Nwosu, Z. C., Du, W., Donahue, K. L., Hong, H. S., Espinoza, C. E., Brown, K. L., Velez-Delgado, A., Yan, W., Lima, F., et al. (2023) · eLife · doi:10.7554/elife.80721 · Cited by 180 · see citing works
Tumor battlefield within inflamed, excluded or desert immune phenotypes: the mechanisms and strategies
Zheng, S., Wang, W., Shen, L., Yao, Y., Xia, W.-J., & Ni, C. (2024) · Experimental Hematology & Oncology · doi:10.1186/s40164-024-00543-1 · Cited by 180 · see citing works
The Roles of Functional Amino Acids in Plant Growth and Development
Kawade, K., Tabeta, H., Ferjani, A., & Hirai, M. Y. (2023) · Plant and Cell Physiology · doi:10.1093/pcp/pcad071 · Cited by 140 · see citing works
Arginase as a Potential Biomarker of Disease Progression: A Molecular Imaging Perspective
Clemente, G. S., van Waarde, A., Antunes, I. F., Dömling, A. S. S., & Elsinga, P. H. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21155291 · Cited by 138 · see citing works
The roles of arginases and arginine in immunity
Canè, S., Geiger, R., & Bronte, V. (2024) · Nature reviews. Immunology · doi:10.1038/s41577-024-01098-2 · Cited by 135 · see citing works
Neutrophil-to-Lymphocyte Ratio and Outcomes in Louisiana COVID-19 Patients
Tatum, D. M., Taghavi, S., Houghton, A., Stover, J. R., Toraih, E. A., & Duchesne, J. C. (2020) · Shock · doi:10.1097/shk.0000000000001585 · Cited by 133 · see citing works
Arginase: shedding light on the mechanisms and opportunities in cardiovascular diseases
Li, Z., Wang, L., Ren, Y., Huang, Y., Liu, W., Lv, Z., Lü, Q., Yu, Y., & Xiong, Y. (2022) · Cell Death Discovery · doi:10.1038/s41420-022-01200-4 · Cited by 114 · see citing works
Mechanisms of obesity-induced metabolic and vascular dysfunctions
Caldwell, R. W. (2019) · Frontiers in bioscience · doi:10.2741/4758 · Cited by 112 · see citing works
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Increased immunosuppression impairs tissue homeostasis with aging and age-related diseases
Salminen, A. (2020) · Journal of Molecular Medicine · doi:10.1007/s00109-020-01988-7 · Cited by 110 · see citing works
Breast cancer–derived GM-CSF regulates arginase 1 in myeloid cells to promote an immunosuppressive microenvironment
Su, X., Xu, Y., Fox, G. C., Xiang, J., Kwakwa, K. A., Davis, J. L., Belle, J. I., Lee, W., Wong, W., Fontana, F., et al. (2021) · Journal of Clinical Investigation · doi:10.1172/jci145296 · Cited by 109 · see citing works
Mitochondrial arginase-2 is a cell‑autonomous regulator of CD8+ T cell function and antitumor efficacy
Líndez, A.-A. M. I., Dunand-Sauthier, I., Conti, M., Gobet, F., Núñez, N. G., Hannich, J. T., Riezman, H., Geiger, R., Piersigilli, A., Hahn, K., et al. (2019) · JCI Insight · doi:10.1172/jci.insight.132975 · Cited by 104 · see citing works
Arterial Stiffness Assessed by Cardio-Ankle Vascular Index
Namba, T., Masaki, N., Takase, B., & Adachi, T. K. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20153664 · Cited by 103 · see citing works
Integrated metabolomics and network pharmacology to reveal the mechanisms of hydroxysafflor yellow A against acute traumatic brain injury
Li, T., Zhang, W., Hu, E., Sun, Z., Li, P., Yu, Z., Zhu, X., Zheng, F., Xing, Z., Xia, Z., et al. (2021) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2021.01.033 · Cited by 102 · see citing works
Fueling neurodegeneration: metabolic insights into microglia functions
Sadeghdoust, M., Das, A., & Kaushik, D. K. (2024) · Journal of Neuroinflammation · doi:10.1186/s12974-024-03296-0 · Cited by 101 · see citing works
Severe COVID-19 Is Characterized by an Impaired Type I Interferon Response and Elevated Levels of Arginase Producing Granulocytic Myeloid Derived Suppressor Cells
Dean, M. J., Ochoa, J. B., Sanchez‐Pino, M. D., Zabaleta, J., Garai, J., Valle, L. D., Wyczechowska, D. D., Baiamonte, L. B., Philbrook, P., Majumder, R., et al. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.695972 · Cited by 85 · see citing works
Tumor-Associated Extracellular Matrix: How to Be a Potential Aide to Anti-tumor Immunotherapy?
He, Y., Liu, T., Dai, S., Xu, Z., Wang, L., & Luo, F. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.739161 · Cited by 83 · see citing works
Hyperuricemia: A key contributor to endothelial dysfunction in cardiovascular diseases
Wei, X., Zhang, M., Huang, S., Lan, X., Zheng, J. J., Luo, H., He, Y. Z., & Lei, W. (2023) · The FASEB Journal · doi:10.1096/fj.202300393r · Cited by 81 · see citing works
Pancreatic tumors exhibit myeloid-driven amino acid stress and upregulate arginine biosynthesis
Saab, J. J. A., Dzierozynski, L. N., Jonker, P. B., AminiTabrizi, R., Shah, H., Menjivar, R. E., Scott, A. J., Nwosu, Z. C., Zhu, Z., Chen, R. N., et al. (2023) · eLife · doi:10.7554/elife.81289 · Cited by 80 · see citing works
A review of nitric oxide and oxidative stress in typical ovulatory women and in the pathogenesis of ovulatory dysfunction in PCOS
Awonuga, A. O., Camp, O. G., & Abu‐Soud, H. M. (2023) · Reproductive Biology and Endocrinology · doi:10.1186/s12958-023-01159-6 · Cited by 79 · see citing works
Arginase 1 promotes retinal neurovascular protection from ischemia through suppression of macrophage inflammatory responses
Fouda, A. Y., Xu, Z., Shosha, E., Lemtalsi, T., Chen, J., Toque, H. A., Tritz, R., Cui, X., Stansfield, B. K., Huo, Y., et al. (2018) · Cell Death and Disease · doi:10.1038/s41419-018-1051-6 · Cited by 77 · see citing works
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Polyamine Immunometabolism: Central Regulators of Inflammation, Cancer and Autoimmunity
Chia, T.-Y., Zolp, A. J., & Miska, J. M. (2022) · Cells · doi:10.3390/cells11050896 · Cited by 75 · see citing works
Gut Microbiota and its Metabolites: Bridge of Dietary Nutrients and Alzheimer’s Disease
Zhu, G., Zhao, J., Zhang, H., Wang, G., & Chen, W. (2023) · Advances in Nutrition · doi:10.1016/j.advnut.2023.04.005 · Cited by 75 · see citing works
Erythrocyte metabolism
Chatzinikolaou, P. N., Margaritelis, N. V., Paschalis, V., Theodorou, A. A., Vrabas, I. S., Kyparos, A., D’Alessandro, A., & Nikolaidis, M. G. (2024) · Acta Physiologica · doi:10.1111/apha.14081 · Cited by 74 · see citing works
A Novel Oral Arginase 1/2 Inhibitor Enhances the Antitumor Effect of PD-1 Inhibition in Murine Experimental Gliomas by Altering the Immunosuppressive Environment
Pilanc, P., Wojnicki, K., Roura, A.-J., Cyranowski, S., Ellert‐Miklaszewska, A., Ochocka, N., Gielniewski, B., Grzybowski, M. M., Błaszczyk, R., Stańczak, P. S., et al. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2021.703465 · Cited by 72 · see citing works
Small-molecule agents for cancer immunotherapy
Wang, F., Fu, K., Wang, Y., Pan, C., Wang, X., Liu, Z., Yang, C., Zheng, Y. Y., Li, X., Lu, Y., et al. (2023) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2023.12.010 · Cited by 71 · see citing works
Nanomotors-loaded microneedle patches for the treatment of bacterial biofilm-related infections of wound
Chen, L., Fang, D., Zhang, J., Xiao, X., Li, N., Li, Y., Wan, M., & Mao, C. (2023) · Journal of Colloid and Interface Science · doi:10.1016/j.jcis.2023.05.080 · Cited by 68 · see citing works
Melanoma-associated fibroblasts impair CD8+ T cell function and modify expression of immune checkpoint regulators via increased arginase activity
Érsek, B., Silló, P., Çakır, U., Molnár, V., Bencsik, A., Mayer, B., Mezey, É., Kárpáti, S., Pós, Z., & Németh, K. (2020) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03517-8 · Cited by 68 · see citing works
Ginseng-derived nanoparticles reprogram macrophages to regulate arginase-1 release for ameliorating T cell exhaustion in tumor microenvironment
Lv, Y., Li, M., Weng, L., Huang, H., Mao, Y., Yang, D. A., Wei, Q., Zhao, M., Qin, W. D., Rui, K., et al. (2023) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-023-02888-7 · Cited by 67 · see citing works
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Arginase: an old enzyme with new tricks
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Authors: Caldwell, R. W., Rodriguez, P. C., Toque, H. A., Narayanan, S. P., & Caldwell, R. B.
Affiliations: Augusta University (US)
Department of Pharmacology & Toxicology, Vision Discovery Institute, Department of Medicine–Hematology and Oncology, Department of Occupational Therapy, School of Allied Health Sciences, and Vascular Biology Center, Medical College of Georgia, Augusta University, Augusta, Georgia; and VA Medical Center, Augusta, Georgia
ORCID: Narayanan, S. Priya
Caldwell, Ruth B.
Venue: Physiological Reviews
Publisher: American Physiological Society
Published: 2018-04-01
Volume: 98
Issue: 2
Pages: 641-665
ISSN: 0031-9333 (ISSN-L)
1522-1210
DOI: 10.1152/physrev.00037.2016
PMC: PMC5966718
OpenAlex: W2785791389
Cited by: 495
References: 257
Citations by year: 2026: 67 · 2025: 62 · 2024: 92 · 2023: 80 · 2022: 64 · 2021: 56 · 2020: 43 · 2019: 23 · 2018: 8
FWCI: 3.19
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Physiological Reviews (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: HHS | NIH | National Heart, Lung, and Blood Institute (NHBLI) (RO1HL070215 rwc)
HHS | NIH | National Eye Institute (NEI) (RO1EY011766 MPI RBC & RWC)
American Heart Association (AHA) (13SDG174100007, 11SDG7440088)
HHS | NIH | National Cancer Institute (NCI) (RO1CA18485)
U.S. Department of Veterans Affairs (VA) (I01BX003221)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Amino Acid Enzymes and Metabolism
Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Polyamine Metabolism and Applications
Keywords: arginase, urea cycle, L-arginine, L-ornithine, nitric oxide, nitric oxide synthase, reactive oxygen species, inflammation, cardiovascular disease, kidney disease, central nervous system disorders, cancer, arginase inhibitors, ammonia detoxification
MeSH terms: Animals, Arginase, Arginine, Endothelium, Vascular, Humans, Nitric Oxide, Urea, Reactive Oxygen Species

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Arginase: A Multifaceted Enzyme Important in Health and Disease

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