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Journal articles on the topic 'Arginase'

Author: Grafiati

Published: 4 June 2021

Last updated: 25 July 2025

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1

Ren, Yuanyuan, Zhuozhuo Li, Wenqing Li, et al. "Arginase: Biological and Therapeutic Implications in Diabetes Mellitus and Its Complications." Oxidative Medicine and Cellular Longevity 2022 (October 26, 2022): 1–20. http://dx.doi.org/10.1155/2022/2419412.

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Arginase is a ubiquitous enzyme in the urea cycle (UC) that hydrolyzes L-arginine to urea and L-ornithine. Two mammalian arginase isoforms, arginase1 (ARG1) and arginase2 (ARG2), play a vital role in the regulation of β-cell functions, insulin resistance (IR), and vascular complications via modulating L-arginine metabolism, nitric oxide (NO) production, and inflammatory responses as well as oxidative stress. Basic and clinical studies reveal that abnormal alterations of arginase expression and activity are strongly associated with the onset and development of diabetes mellitus (DM) and its com

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Chen, Hui, Bonnie C. McCaig, Maeli Melotto, Sheng Yang He, and Gregg A. Howe. "Regulation of Plant Arginase by Wounding, Jasmonate, and the Phytotoxin Coronatine." Journal of Biological Chemistry 279, no. 44 (2004): 45998–6007. http://dx.doi.org/10.1074/jbc.m407151200.

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In mammalian cells, induced expression of arginase in response to wound trauma and pathogen infection plays an important role in regulating the metabolism ofl-arginine to either polyamines or nitric oxide (NO). In higher plants, which also utilize arginine for the production of polyamines and NO, the potential role of arginase as a control point for arginine homeostasis has not been investigated. Here, we report the characterization of two genes (LeARG1andLeARG2) fromLycopersicon esculentum(tomato) that encode arginase. Phylogenic analysis showed that LeARG1 and -2, like all other plant argina

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3

Elms, Shawn, Feng Chen, Yusi Wang, et al. "Insights into the arginine paradox: evidence against the importance of subcellular location of arginase and eNOS." American Journal of Physiology-Heart and Circulatory Physiology 305, no. 5 (2013): H651—H666. http://dx.doi.org/10.1152/ajpheart.00755.2012.

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Reduced production of nitric oxide (NO) is one of the first indications of endothelial dysfunction and precedes overt cardiovascular disease. Increased expression of Arginase has been proposed as a mechanism to account for diminished NO production. Arginases consume l-arginine, the substrate for endothelial nitric oxide synthase (eNOS), and l-arginine depletion is thought to competitively reduce eNOS-derived NO. However, this simple relationship is complicated by the paradox that l-arginine concentrations in endothelial cells remain sufficiently high to support NO synthesis. One mechanism prop

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4

Kitowska, Kamila, Dariusz Zakrzewicz, Melanie Königshoff, et al. "Functional role and species-specific contribution of arginases in pulmonary fibrosis." American Journal of Physiology-Lung Cellular and Molecular Physiology 294, no. 1 (2008): L34—L45. http://dx.doi.org/10.1152/ajplung.00007.2007.

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Lung fibrosis is characterized by increased deposition of ECM, especially collagens, and enhanced proliferation of fibroblasts. l-arginine is a key precursor of nitric oxide, asymmetric dimethylarginine, and proline, an amino acid enriched in collagen. We hypothesized that l-arginine metabolism is altered in pulmonary fibrosis, ultimately affecting collagen synthesis. Expression analysis of key enzymes in the arginine pathway, protein arginine methyltransferases (Prmt), arginine transporters, and arginases by quantitative (q) RT-PCR and Western blot revealed significant upregulation of arginas

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5

Marzęta-Assas, Patrycja, Damian Jacenik, and Zbigniew Zasłona. "Pathophysiology of Arginases in Cancer and Efforts in Their Pharmacological Inhibition." International Journal of Molecular Sciences 25, no. 18 (2024): 9782. http://dx.doi.org/10.3390/ijms25189782.

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Arginases are key enzymes that hydrolyze L-arginine to urea and L-ornithine in the urea cycle. The two arginase isoforms, arginase 1 (ARG1) and arginase 2 (ARG2), regulate the proliferation of cancer cells, migration, and apoptosis; affect immunosuppression; and promote the synthesis of polyamines, leading to the development of cancer. Arginases also compete with nitric oxide synthase (NOS) for L-arginine, and their participation has also been confirmed in cardiovascular diseases, stroke, and inflammation. Due to the fact that arginases play a crucial role in the development of various types o

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6

Dzikowska, A., J. P. Le Caer, P. Jonczyk, and P. Wëgleński. "Purification of arginase from Aspergillus nidulans." Acta Biochimica Polonica 41, no. 4 (1994): 467–71. http://dx.doi.org/10.18388/abp.1994_4700.

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Arginase (EC 3.5.3.1) of Aspergillus nidulans, the enzyme which enables the fungus to use arginine as the sole nitrogen source was purified to homogeneity. Molecular mass of the purified arginase subunit is 40 kDa and is similar to that reported for the Neurospora crassa (38.3 kDa) and Saccharomyces cerevisiae (39 kDa) enzymes. The native molecular mass of arginase is 125 kDa. The subunit/native molecular mass ratio suggests a trimeric form of the protein. The arginase protein was cleaved and partially sequenced. Two out of the six polypeptides sequenced show a high degree of homology to conse

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7

Belik, Jaques, Darakhshanda Shehnaz, Jingyi Pan, and Hartmut Grasemann. "Developmental changes in arginase expression and activity in the lung." American Journal of Physiology-Lung Cellular and Molecular Physiology 294, no. 3 (2008): L498—L504. http://dx.doi.org/10.1152/ajplung.00242.2007.

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Arginases compete with nitric oxide (NO) synthases for l-arginine as common substrate. Pulmonary vascular and airway diseases in which arginase activity is increased are associated with decreased NO production and reduced smooth muscle relaxation. The developmental patterns of arginase activity and type I and II isoforms expression in the lung have not been previously evaluated. Hypothesizing that lung arginase activity is developmentally regulated and highest in the fetus, we measured the expression of both arginase isoforms and total arginase activity in fetal, newborn, and adult rat lung, p

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8

Gao, Kai, Sergey Lunev, Mariska P. M. van den Berg, et al. "A synthetic peptide as an allosteric inhibitor of human arginase I and II." Molecular Biology Reports 48, no. 2 (2021): 1959–66. http://dx.doi.org/10.1007/s11033-021-06176-5.

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AbstractArginine metabolism mediated by arginases plays a critical role in cell and tissue function. The arginine hydrolysis is deeply involved in the urea cycle, which helps the kidney excrete ammonia from blood. Upregulation of arginases affects microenvironment stability due to the presence of excess urea in blood. To regulate the arginase activities properly, a synthetic peptide based on the structure of human arginase I was designed and assessed. Preliminary data shows it inhibits human arginase I and II with an IC50 of 2.4 ± 0.3 and 1.8 ± 0.1 mmol, respectively. Our kinetic analysis indi

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9

Ide, Alejandra Arteaga, Victor M. Hernández, Liliana Medina-Aparicio, et al. "Genetic regulation, biochemical properties and physiological importance of arginase from Sinorhizobium meliloti." Microbiology 166, no. 5 (2020): 484–97. http://dx.doi.org/10.1099/mic.0.000909.

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In bacteria, l-arginine is a precursor of various metabolites and can serve as a source of carbon and/or nitrogen. Arginine catabolism by arginase, which hydrolyzes arginine to l-ornithine and urea, is common in nature but has not been studied in symbiotic nitrogen-fixing rhizobia. The genome of the alfalfa microsymbiont Sinorhizobium meliloti 1021 has two genes annotated as arginases, argI1 (smc03091) and argI2 (sma1711). Biochemical assays with purified ArgI1 and ArgI2 (as 6His-Sumo-tagged proteins) showed that only ArgI1 had detectable arginase activity. A 1021 argI1 null mutant lacked argi

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10

Orellana, María-Soledad, Gonzalo A. Jaña, Maximiliano Figueroa, et al. "New Insights into the Determinants of Specificity in Human Type I Arginase: Generation of a Mutant That Is Only Active with Agmatine as Substrate." International Journal of Molecular Sciences 23, no. 12 (2022): 6438. http://dx.doi.org/10.3390/ijms23126438.

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Arginase catalyzes the hydrolysis of L-arginine into L-ornithine and urea. This enzyme has several analogies with agmatinase, which catalyzes the hydrolysis of agmatine into putrescine and urea. However, this contrasts with the highlighted specificity that each one presents for their respective substrate. A comparison of available crystal structures for arginases reveals an important difference in the extension of two loops located in the entrance of the active site. The first, denominated loop A (I129-L140) contains the residues that interact with the alpha carboxyl group or arginine of argin

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11

Erisir, M., E. Ercel, S. Yilmaz, and S. Ozan. "Evaluation of optimal conditions for arginase activity in streptozotocin induced diabetic rats." Veterinární Medicína 50, No. 2 (2012): 69–76. http://dx.doi.org/10.17221/5598-vetmed.

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The assay conditions needed to achieve maximal activity of liver and kidney arginase in diabetic and non-diabetic rats were investigated and compared. The physicochemical and kinetic properties of liver arginase in diabetic and control rats were very similar, those of kidney arginase were significantly different. It was found that preincubation temperature (68&deg;C), preincubation period (20 min), optimum pH (10.1) of liver arginase and K<sub>m</sub> (3.2) for its substrate, L-arginine, did not change in diabetic and non-diabetic rats. As a consequence of diabetes, the optimum

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12

Ikemoto, M., M. Tabata, T. Miyake, et al. "Expression of human liver arginase in Escherichia coli. Purification and properties of the product." Biochemical Journal 270, no. 3 (1990): 697–703. http://dx.doi.org/10.1042/bj2700697.

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Arginase is an enzyme that catalyses the hydrolysis of arginine to urea and ornithine. It is abundantly present in the liver of ureotelic animals (i.e. those whose excretion is characterized by the excretion of uric acid as the chief end-product of nitrogen metabolism), but its purification has hitherto not been simple, and the yield not high. Starting with a partially truncated cDNA for human liver arginase recently made available, we constructed an expression plasmid that had tandemly linked tac promotors placed upstream of a full-length cDNA. By selecting Escherichia coli strain KY1436 as t

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13

Munder, Markus, Klaus Eichmann, José M. Morán, Francisco Centeno, Germán Soler, and Manuel Modolell. "Th1/Th2-Regulated Expression of Arginase Isoforms in Murine Macrophages and Dendritic Cells." Journal of Immunology 163, no. 7 (1999): 3771–77. http://dx.doi.org/10.4049/jimmunol.163.7.3771.

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Abstract Activated murine macrophages metabolize arginine by two alternative pathways involving the enzymes inducible NO synthase (iNOS) or arginase. The balance between the two enzymes is competitively regulated by Th1 and Th2 T helper cells via their secreted cytokines: Th1 cells induce iNOS, whereas Th2 cells induce arginase. Whereas the role of macrophages expressing iNOS as inflammatory cells is well established, the functional competence of macrophages expressing arginase remains a matter of speculation. Two isoforms of mammalian arginases exist, hepatic arginase I and extrahepatic argin

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14

Tawfeeq Ali, Layth, Hanaa H. Hussein, and Salma Abdul Rudha Abbas. "Synthesis of Mn2O3 Nanoparticles and Determination of Its Inhibition Effect On Sera of Iraqi Patients with Diabetes Mellitus Type-2 and Diabetes Nephropathy." Al-Nahrain Journal of Science 27, no. 1 (2024): 14–22. http://dx.doi.org/10.22401/anjs.27.1.02.

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Manganese is essential for the synthesis of antioxidant enzymes and metabolic issues in Diabetes type 2 (DMT2), which is a worldwide disease, Chronic metabolic disorders cause insulin resistance, hyperglycemia, and complications like diabetic nephropathy. Arginase converts arginine to ornithine and urea. Increased arginase activity in DMT2 and diabetes nephropathy (DN)which has been linked to kidney damage, and arginase inhibitors can increase NO which is essential to vascular function. However, the molecular mechanisms of arginased is regulationare in DMT2 and DN are still unclear. This study

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15

van de Poll, Marcel C. G., Sebastiaan J. P. Hanssen, Maaike Berbée, et al. "Elevated plasma arginase-1 does not affect plasma arginine in patients undergoing liver resection." Clinical Science 114, no. 3 (2008): 231–41. http://dx.doi.org/10.1042/cs20070143.

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Arginine is an important substrate in health and disease. It is a commonly held view that arginase-1 release from injured erythrocytes and hepatocytes leads to arginine breakdown; however, the true relationship between plasma arginase-1 concentration and activity has remained unaddressed. In the present study, blood was sampled from patients undergoing liver resection, a known cause of hepatocyte injury and arginase-1 release, to determine arginase-1, arginine and ornithine plasma levels. Arginase activity was assessed in vitro by measuring changes in arginine and ornithine plasma levels durin

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16

Wong, Emily S. W., Ricky Y. K. Man, Kwok F. J. Ng, Susan W. S. Leung, and Paul M. Vanhoutte. "L-arginine and Arginase Products Potentiate Dexmedetomidine-induced Contractions in the Rat Aorta." Anesthesiology 128, no. 3 (2018): 564–73. http://dx.doi.org/10.1097/aln.0000000000002032.

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Abstract Background The α2-adrenergic sedative/anesthetic agent dexmedetomidine exerts biphasic effects on isolated arteries, causing endothelium-dependent relaxations at concentrations at or below 30 nM, followed by contractions at higher concentrations. l-arginine is a common substrate of endothelial nitric oxide synthase and arginases. This study was designed to investigate the role of l-arginine in modulating the overall vascular response to dexmedetomidine. Methods Isometric tension was measured in isolated aortic rings of Sprague Dawley rats. Cumulative concentrations of dexmedetomidine

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17

Vanhoutte, Paul M. "Arginine and Arginase." Circulation Research 102, no. 8 (2008): 866–68. http://dx.doi.org/10.1161/circresaha.108.175570.

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18

Grasemann, Hartmut, Thomas Jaecklin, Anne Mehl, et al. "Multitracer Stable Isotope Quantification of Arginase and Nitric Oxide Synthase Activity in a Mouse Model of Pseudomonas Lung Infection." Mediators of Inflammation 2014 (2014): 1–7. http://dx.doi.org/10.1155/2014/323526.

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Cystic fibrosis airways are deficient for L-arginine, a substrate for nitric oxide synthases (NOSs) and arginases. The rationale for this study was to quantify NOS and arginase activity in the mouse lung. Anesthetized unventilated mice received a primed constant stable isotope intravenous infusion containing labeled L-arginine, ornithine, and citrulline. The isotopic enrichment of each of the infused isotopomers and its product amino acids were measured in plasma and organ homogenates using liquid chromatography-tandem mass spectrometry. The effect of infection was studied three days after dir

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Albina, J. E., C. D. Mills, A. Barbul, et al. "Arginine metabolism in wounds." American Journal of Physiology-Endocrinology and Metabolism 254, no. 4 (1988): E459—E467. http://dx.doi.org/10.1152/ajpendo.1988.254.4.e459.

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Arginine metabolism in wounds was investigated in the rat in 1) lambda-carrageenan-wounded skeletal muscle, 2) Schilling chambers, and 3) subcutaneous polyvinyl alcohol sponges. All showed decreased arginine and elevated ornithine contents and high arginase activity. Arginase could be brought to the wound by macrophages, which were found to contain arginase activity. However, arginase was expressed by macrophages only after cell lysis and no arginase was released by viable macrophages in vitro. Thus the extracellular arginase of wounds may derive from dead macrophages within the injured tissue

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20

Shi, Ou, Sidney M. Morris, Huda Zoghbi, Carl W. Porter, and William E. O'Brien. "Generation of a Mouse Model for Arginase II Deficiency by Targeted Disruption of the Arginase II Gene." Molecular and Cellular Biology 21, no. 3 (2001): 811–13. http://dx.doi.org/10.1128/mcb.21.3.811-813.2001.

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ABSTRACT Mammals express two isoforms of arginase, designated types I and II. Arginase I is a component of the urea cycle, and inherited defects in arginase I have deleterious consequences in humans. In contrast, the physiologic role of arginase II has not been defined, and no deficiencies in arginase II have been identified in humans. Mice with a disruption in the arginase II gene were created to investigate the role of this enzyme. Homozygous arginase II-deficient mice were viable and apparently indistinguishable from wild-type mice, except for an elevated plasma arginine level which indicat

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Louis, Claudine A., Jonathan S. Reichner, William L. Henry, et al. "Distinct arginase isoforms expressed in primary and transformed macrophages: regulation by oxygen tension." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 274, no. 3 (1998): R775—R782. http://dx.doi.org/10.1152/ajpregu.1998.274.3.r775.

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Experiments were performed to identify arginase isoforms expressed in primary and transformed rodent macrophages and to determine the molecular mechanisms for the previously observed increase in arginase activity in macrophages cultured in hypoxia or anoxia. Results demonstrate the following: 1) mRNA and protein for hepatic-type AI arginase are expressed in primary cultures of rat and mouse peritoneal macrophages and are enhanced seven- and ninefold, respectively, by lipopolysaccharide (LPS). 2) mRNA for extrahepatic-type AII arginase is constitutively expressed in mouse, but not rat, peritone

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Morris, Sidney M., Diane Kepka-Lenhart, and Li-Chun Chen. "Differential regulation of arginases and inducible nitric oxide synthase in murine macrophage cells." American Journal of Physiology-Endocrinology and Metabolism 275, no. 5 (1998): E740—E747. http://dx.doi.org/10.1152/ajpendo.1998.275.5.e740.

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Activated macrophages avidly consume arginine via the action of inducible nitric oxide synthase (iNOS) and/or arginase. In contrast to our knowledge regarding macrophage iNOS expression, the stimuli and mechanisms that regulate expression of the cytosolic type I (arginase I) or mitochondrial type II (arginase II) isoforms of arginase in macrophages are poorly defined. We show that one or both arginase isoforms may be induced in the RAW 264.7 murine macrophage cell line and that arginase expression is regulated independently of iNOS expression. For example, 8-bromo-cAMP strongly induced both ar

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You, Hanning, Ting Gao, Timothy K. Cooper, Sidney M. Morris, and Alaa S. Awad. "Diabetic nephropathy is resistant to oral l-arginine or l-citrulline supplementation." American Journal of Physiology-Renal Physiology 307, no. 11 (2014): F1292—F1301. http://dx.doi.org/10.1152/ajprenal.00176.2014.

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Our recent publication showed that pharmacological blockade of arginases confers kidney protection in diabetic nephropathy via a nitric oxide (NO) synthase (NOS)3-dependent mechanism. Arginase competes with endothelial NOS (eNOS) for the common substrate l-arginine. Lack of l-arginine results in reduced NO production and eNOS uncoupling, which lead to endothelial dysfunction. Therefore, we hypothesized that l-arginine or l-citrulline supplementation would ameliorate diabetic nephropathy. DBA mice injected with multiple low doses of vehicle or streptozotocin (50 mg/kg ip for 5 days) were provid

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Yahiya, Islam, Asmaa Ali, Omnia Ali, and Ahmed Sultan. "Abstract P5-10-06: Arginine- depleting enzyme, pegylated arginase, isolated from beef-liver tissue induces growth inhibition, apoptosis, cell cycle arrest and inhibits induced mammary tumors: A promising strategy for human breast cancer treatment in vitro and in vivo." Cancer Research 82, no. 4_Supplement (2022): P5–10–06—P5–10–06. http://dx.doi.org/10.1158/1538-7445.sabcs21-p5-10-06.

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Abstract Arginine auxotrophy occurs in certain tumor types, renders tumors vulnerable to treatment with arginine-degrading enzymes, and leads to their rapid demise. Arginine is a semi-essential amino acid but is essential for rapidly proliferating cells. Thus, Arginine deprivation can be exploited as a potential targeted therapy for the treatment of various cancers. Arginase, an enzyme of the urea cycle, converts L-arginine to L-ornithine, which is the precursor of polyamines that are essential components of cell proliferation. However, Arginine deprivation and Arginase clinical implications i

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Scott, Jeremy A., Michelle L. North, Mahrouk Rafii, Hailu Huang, Paul Pencharz, and Hartmut Grasemann. "Plasma arginine metabolites reflect airway dysfunction in a murine model of allergic airway inflammation." Journal of Applied Physiology 118, no. 10 (2015): 1229–33. http://dx.doi.org/10.1152/japplphysiol.00865.2014.

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l-Arginine metabolism is important in the maintenance of airway tone. Shift of metabolism from the nitric oxide synthase to arginase pathways contributes to the increased airway responsiveness in asthma. We tested the hypothesis that systemic levels of l-arginine metabolites are biomarkers reflective of airway dysfunction. We used a mouse model of acute allergic airway inflammation to OVA that manifests with significant airway hyperresponsiveness to methacholine. To determine tissue arginase activity in vivo, the isotopic enrichment of an infused l-arginine stable isotope and its product amino

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Li, Hui, Cynthia J. Meininger, James R. Hawker, et al. "Regulatory role of arginase I and II in nitric oxide, polyamine, and proline syntheses in endothelial cells." American Journal of Physiology-Endocrinology and Metabolism 280, no. 1 (2001): E75—E82. http://dx.doi.org/10.1152/ajpendo.2001.280.1.e75.

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Endothelial cells (EC) metabolize l-arginine mainly by arginase, which exists as two distinct isoforms, arginase I and II. To understand the roles of arginase isoforms in EC arginine metabolism, bovine coronary venular EC were stably transfected with the Escherichia coli lacZ gene (lacZ-EC, control), rat arginase I cDNA (AI-EC), or mouse arginase II cDNA (AII-EC). Western blots and enzymatic assays confirmed high-level expression of arginase I in the cytosol of AI-EC and of arginase II in mitochondria of AII-EC. For determining arginine catabolism, EC were cultured for 24 h in DMEM containing

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Tratsiakovich, Yahor, Attila Kiss, Adrian T. Gonon, Jiangning Yang, Per-Ove Sjöquist, and John Pernow. "Inhibition of Rho kinase protects from ischaemia–reperfusion injury via regulation of arginase activity and nitric oxide synthase in type 1 diabetes." Diabetes and Vascular Disease Research 14, no. 3 (2017): 236–45. http://dx.doi.org/10.1177/1479164116687935.

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Aim: RhoA/Rho-associated kinase and arginase are implicated in vascular complications in diabetes. This study investigated whether RhoA/Rho-associated kinase and arginase inhibition protect from myocardial ischaemia–reperfusion injury in type 1 diabetes and the mechanisms behind these effects. Methods: Rats with streptozotocin-induced type 1 diabetes and non-diabetic rats were subjected to 30 min myocardial ischaemia and 2 h reperfusion after being randomized to treatment with (1) saline, (2) RhoA/Rho-associated kinase inhibitor hydroxyfasudil, (3) nitric oxide synthase inhibitor NG-monomethyl

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Buga, G. M., R. Singh, S. Pervin, et al. "Arginase activity in endothelial cells: inhibition by NG-hydroxy-L-arginine during high-output NO production." American Journal of Physiology-Heart and Circulatory Physiology 271, no. 5 (1996): H1988—H1998. http://dx.doi.org/10.1152/ajpheart.1996.271.5.h1988.

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Rat aortic endothelial cells were found to contain both constitutive and lipopolysaccharide (LPS)-inducible arginase activity. Studies were performed to determine whether induction of nitric oxide synthase (NOS) by LPS and cytokines is accompanied by sufficient arginase induction to render arginine concentrations rate limiting for high-output NO production. Unactivated cells contained abundant arginase activity accompanied by continuous urea formation. LPS induced the formation of both inducible NOS (iNOS) and arginase, and this was accompanied by increased production of NO, citrulline, and ur

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Mohammad, Mahmoud A., Inka C. Didelija, and Juan C. Marini. "Arginase II Plays a Central Role in the Sexual Dimorphism of Arginine Metabolism in C57BL/6 Mice." Journal of Nutrition 150, no. 12 (2020): 3133–40. http://dx.doi.org/10.1093/jn/nxaa318.

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ABSTRACT Background Sex differences in plasma concentration of arginine and arginase activity of different tissues have been reported in mice. In addition, male but not female C57BL/6 mice have a dietary arginine requirement for growth. Objective The goal of this research was to test the hypothesis that arginase II is a key factor in the sexual dimorphism of arginine metabolism. Methods Young adult male and female wild type (WT), and heterozygous and arginase II knockout mice on a C57BL/6 background mice were infused with labeled citrulline, arginine, ornithine, phenylalanine, and tyrosine to

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S. Clemente, Gonçalo, Aren van Waarde, Inês F. Antunes, Alexander Dömling, and Philip H. Elsinga. "Arginase as a Potential Biomarker of Disease Progression: A Molecular Imaging Perspective." International Journal of Molecular Sciences 21, no. 15 (2020): 5291. http://dx.doi.org/10.3390/ijms21155291.

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Arginase is a widely known enzyme of the urea cycle that catalyzes the hydrolysis of L-arginine to L-ornithine and urea. The action of arginase goes beyond the boundaries of hepatic ureogenic function, being widespread through most tissues. Two arginase isoforms coexist, the type I (Arg1) predominantly expressed in the liver and the type II (Arg2) expressed throughout extrahepatic tissues. By producing L-ornithine while competing with nitric oxide synthase (NOS) for the same substrate (L-arginine), arginase can influence the endogenous levels of polyamines, proline, and NO•. Several pathophysi

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Gotoh, Tomomi, and Masataka Mori. "Arginase II Downregulates Nitric Oxide (NO) Production and Prevents NO-mediated Apoptosis in Murine Macrophage-derived RAW 264.7 Cells." Journal of Cell Biology 144, no. 3 (1999): 427–34. http://dx.doi.org/10.1083/jcb.144.3.427.

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Excess nitric oxide (NO) induces apoptosis of some cell types, including macrophages. As NO is synthesized by NO synthase (NOS) from arginine, a common substrate of arginase, these two enzymes compete for arginine. There are two known isoforms of arginase, types I and II. Using murine macrophage-like RAW 264.7 cells, we asked if the induction of arginase II would downregulate NO production and hence prevent apoptosis. When cells were exposed to lipopolysaccharide (LPS) and interferon-γ (IFN-γ), the inducible form of NOS (iNOS) was induced, production of NO was elevated, and apoptosis followed.

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Fafula, R. V., U. P. Iefremova, O. K. Onufrovych, H. V. Maksymyuk, D. Z. Vorobets, and Z. D. Vorobets. "The kinetic properties of arginase in sperm cells of inferile men." Regulatory Mechanisms in Biosystems 9, no. 1 (2018): 80–84. http://dx.doi.org/10.15421/021811.

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Nowadays the role of NO in the development of male infertility is actively studied. Arginase (EC 3.5.3.1) is a manganese metalloenzyme which converts L-arginine to L-ornithine and urea and reciprocally regulates NO production. Although arginase activity has usually been detected in the reproductive tract, including spermatozoa, no data relating to the kinetic properties of the enzyme in ejaculated spermatozoa has been reported. This study was designed to study the kinetic parameters of arginase of spermatozoa of infertile men. Spermatozoa arginase activity was measured by determining levels of

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Alzayadneh, Ebaa M., Alia Shatanawi, R. William Caldwell, and Ruth B. Caldwell. "Methylglyoxal-Modified Albumin Effects on Endothelial Arginase Enzyme and Vascular Function." Cells 12, no. 5 (2023): 795. http://dx.doi.org/10.3390/cells12050795.

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Advanced glycation end products (AGEs) contribute significantly to vascular dysfunction (VD) in diabetes. Decreased nitric oxide (NO) is a hallmark in VD. In endothelial cells, NO is produced by endothelial NO synthase (eNOS) from L-arginine. Arginase competes with NOS for L-arginine to produce urea and ornithine, limiting NO production. Arginase upregulation was reported in hyperglycemia; however, AGEs’ role in arginase regulation is unknown. Here, we investigated the effects of methylglyoxal-modified albumin (MGA) on arginase activity and protein expression in mouse aortic endothelial cells

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Grasemann, Hartmut, Rupinder Dhaliwal, Julijana Ivanovska, et al. "Arginase inhibition prevents bleomycin-induced pulmonary hypertension, vascular remodeling, and collagen deposition in neonatal rat lungs." American Journal of Physiology-Lung Cellular and Molecular Physiology 308, no. 6 (2015): L503—L510. http://dx.doi.org/10.1152/ajplung.00328.2014.

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Arginase is an enzyme that limits substrate l-arginine bioavailability for the production of nitric oxide by the nitric oxide synthases and produces l-ornithine, which is a precursor for collagen formation and tissue remodeling. We studied the pulmonary vascular effects of arginase inhibition in an established model of repeated systemic bleomycin sulfate administration in neonatal rats that results in pulmonary hypertension and lung injury mimicking the characteristics typical of bronchopulmonary dysplasia. We report that arginase expression is increased in the lungs of bleomycin-exposed neona

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Benson, Renée C., Karen A. Hardy, and Claudia R. Morris. "Arginase and Arginine Dysregulation in Asthma." Journal of Allergy 2011 (April 26, 2011): 1–12. http://dx.doi.org/10.1155/2011/736319.

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In recent years, evidence has accumulated indicating that the enzyme arginase, which converts L-arginine into L-ornithine and urea, plays a key role in the pathogenesis of pulmonary disorders such as asthma through dysregulation of L-arginine metabolism and modulation of nitric oxide (NO) homeostasis. Allergic asthma is characterized by airway hyperresponsiveness, inflammation, and remodeling. Through substrate competition, arginase decreases bioavailability of L-arginine for nitric oxide synthase (NOS), thereby limiting NO production with subsequent effects on airway tone and inflammation. By

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Horodova-Andrieieva, T. V., O. Ye Akimov, V. O. Kostenko, O. H. Krasnov, V. I. Lyakhovskyi, and M. I. Kravtsiv. "The effect of the use of vacuum therapy and instillation of L-arginine in the treatment of purulent wounds on the activity of nitric oxide cycle enzymes." EMERGENCY MEDICINE 21, no. 1 (2025): 71–76. https://doi.org/10.22141/2224-0586.21.1.2025.1834.

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Background. The problem of treating purulent wounds remains one of the most urgent throughout the history of surgery. Nowadays, despite many years of experience and constant scientific research, the problem of diagnosis and treatment of purulent wounds does not lose its relevance. The purpose is to evaluate the effect of vacuum therapy and instillation of L-arginine in the treatment of a purulent wound on the production of nitric oxide by different isoforms of NO-synthase and the activity of the arginase pathway of L-arginine metabolism. Materials and methods. The experiment was conducted in

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Kitiyakara, Chagriya, Tina Chabrashvili, Pedro Jose, William J. Welch, and Christopher S. Wilcox. "Effects of dietary salt intake on plasma arginine." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 280, no. 4 (2001): R1069—R1075. http://dx.doi.org/10.1152/ajpregu.2001.280.4.r1069.

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Because l-arginine is degraded by hepatic arginase to ornithine and urea and is transported by the regulated 2A cationic amino acid y+ transporter (CAT2A), hepatic transport may regulate plasma arginine concentration. Groups of rats ( n = 6) were fed a diet of either low salt (LS) or high salt (HS) for 7 days to test the hypothesis that dietary salt intake regulates plasma arginine concentration and renal nitric oxide (NO) generation by measuring plasma arginine and ornithine concentrations, renal NO excretion, and expression of hepatic CAT2A, and arginase. LS rats had lower excretion of NO me

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Louis, Claudine A., Vino Mody, William L. Henry, Jonathan S. Reichner, and Jorge E. Albina. "Regulation of arginase isoforms I and II by IL-4 in cultured murine peritoneal macrophages." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 276, no. 1 (1999): R237—R242. http://dx.doi.org/10.1152/ajpregu.1999.276.1.r237.

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Macrophages can express two arginase isoforms with distinct subcellular localization (cytosolic AI and mitochondrial AII). These isoforms are products of different genes and are capable of differential induction. Experiments were performed to identify the specific arginase isoforms induced by interleukin (IL)-4, a Th2 cytokine shown by others to increase arginase activity in macrophages, and serum. Results indicate IL-4, in concert with serum, increases AI, but not AII, mRNA in cultured murine macrophages. Moreover, they show serum to induce both arginase isoforms and to be required for maxima

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Cook, H. T., A. Jansen, S. Lewis, et al. "Arginine metabolism in experimental glomerulonephritis: interaction between nitric oxide synthase and arginase." American Journal of Physiology-Renal Physiology 267, no. 4 (1994): F646—F653. http://dx.doi.org/10.1152/ajprenal.1994.267.4.f646.

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L-Arginine is metabolized by two pathways: 1) by nitric oxide synthase (NOS) to nitric oxide (NO) and 2) by arginase forming urea and L-ornithine. Inflammatory responses may involve a balance between the pathways, as NO is cytotoxic and vasodilatory and L-ornithine is a promoter of cell proliferation and matrix synthesis. In experimental glomerulonephritis we have previously shown that NOS is activated in nephritic glomeruli. We have now examined both pathways of L-arginine metabolism to study competition for L-arginine, temporal variation, and the sources of NOS and arginase. Acute in situ gl

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Puspitasari, Endah, Silvia Imana Nafiah, and Melinda Ayu Trinita. "Arginase as a potential cancer treatment: a review." Jurnal Ilmiah Farmasi 19, no. 2 (2023): 209–19. http://dx.doi.org/10.20885/jif.vol19.iss2.art18.

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Background: The high prevalence of cancer leads to the development of new strategies for cancer therapy. The FDA has already approved the amino-acid degrading enzyme as a treatment for lymphoma and leukemia. Furthermore, research related to other amino acid-degrading enzymes was carried out to open up the potential for the development of new cancer therapy strategies. As an amino acid-degrading enzyme, arginase breaks down arginine into urea and ornithine. It is an important part of the urea cycle and may be able to fight tumors.Objective: This article review aims to provide information relate

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Bivalacqua, Trinity J., Arthur L. Burnett, Wayne J. G. Hellstrom, and Hunter C. Champion. "Overexpression of arginase in the aged mouse penis impairs erectile function and decreases eNOS activity: influence of in vivo gene therapy of anti-arginase." American Journal of Physiology-Heart and Circulatory Physiology 292, no. 3 (2007): H1340—H1351. http://dx.doi.org/10.1152/ajpheart.00121.2005.

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Since both increased nitric oxide (NO) synthase (NOS) abundance and diminished NO signaling have been reported in the aging penis, the role of NO in the adaptations of aging remains controversial. Here we tested the hypothesis that arginase, an enzyme that competes with NOS for the substrate l-arginine, contributes to erectile dysfunction with advanced age in the B6/129 mouse strain. Arginase protein abundance, mRNA expression, and enzyme activity were elevated in aged compared with young penile endothelial cells. In addition, endothelial NOS (NOS3) protein abundance was greater in aged versus

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Suman, Mishra, and Mishra Rajnikant. "KCl-Dependent Release of Mitochondrial Membrane-Bound Arginase Appears to Be a Novel Variant of Arginase-II." Scientifica 2016 (2016): 1–10. http://dx.doi.org/10.1155/2016/3675283.

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Arginase regulates arginine metabolism, ornithine-urea cycle, and immunological surveillance. Arginase-I is predominant in cytosol, and arginase-II is localised in the mitochondria. A mitochondrial membrane-bound arginase has also been proposed to be adsorbed with outer membrane of mitochondria which gets released by 150 mM potassium chloride (KCl). It is presumed that inclusion of 150 mM KCl in the homogenization medium would not only facilitate release of arginase bound with outer membrane of mitochondria but also affect functional anatomy of mitochondria, mitochondrial enzymes, and proteins

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Waddington, Simon N., Frederick W. K. Tam, H. Terence Cook, and Victoria Cattell. "Arginase activity is modulated by IL-4 and HOArg in nephritic glomeruli and mesangial cells." American Journal of Physiology-Renal Physiology 274, no. 3 (1998): F473—F480. http://dx.doi.org/10.1152/ajprenal.1998.274.3.f473.

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Arginase shares a common substrate, l-arginine, with nitric oxide synthase (NOS). Both enzymes are active at inflammatory sites. To understand regulation of arginase and its relationship to nitric oxide (NO) production, we studied effects of N G-hydroxy-l-arginine (HOArg) and interleukin-4 (IL-4) on urea and[Formula: see text] synthesis by glomeruli during rat immune glomerulonephritis and compared these with macrophages and glomerular mesangial cells (MC). In nephritic glomeruli, elicited macrophages, and MC stimulated with IL-1 and adenosine 3′,5′-cyclic monophosphate agonists, increased arg

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Tadié, Jean-Marc, Priscilla Henno, Ingrid Leroy, et al. "Role of nitric oxide synthase/arginase balance in bronchial reactivity in patients with chronic obstructive pulmonary disease." American Journal of Physiology-Lung Cellular and Molecular Physiology 294, no. 3 (2008): L489—L497. http://dx.doi.org/10.1152/ajplung.00109.2007.

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Competition between nitric oxide synthases (NOSs) and arginases for their common substrate l-arginine could be involved in the regulation of cholinergic airway reactivity and subsequent airway remodeling. The aims of this study were to evaluate the relationships between the expression of this enzymatic balance and the effects of NOS and arginase inhibition on bronchoconstrictive response to acetylcholine of patients without and with early chronic obstructive pulmonary disease (COPD). Twenty-two human bronchi [15 COPD (9 GOLD-0, 6 GOLD-1, -2-A), 7 nonsmokers] were investigated for immunohistoch

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Ali, Asmaa, Omnia Ali, Doaa Othman, and Ahmed Sultan. "Abstract 6332: Pegylated arginase isolated from beef liver tissue inhibited cell proliferation, induced apoptosis & inhibits induced mammary tumors in human breast cancer in vitro & in vivo." Cancer Research 82, no. 12_Supplement (2022): 6332. http://dx.doi.org/10.1158/1538-7445.am2022-6332.

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Abstract Arginase, an enzyme of the urea cycle, converts L-arginine to L-ornithine, which is the precursor of polyamines that are essential components of cell proliferation. However, Arginine deprivation and Arginase clinical implications in human breast and liver cancers have not been fully elucidated. The objective of the current study was to investigate the potential role of the Arginine degrading enzyme, Arginase, on three cell lines; Luminal A breast cancer (T-47D), TNBC (MDA-MB-231), and HCC cell line, HepG2, respectively. Herein, Arginase was extracted and purified from the beef liver a

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Jung, Albert S., Hajime Kubo, Rachel Wilson, Steven R. Houser, and Kenneth B. Margulies. "Modulation of contractility by myocyte-derived arginase in normal and hypertrophied feline myocardium." American Journal of Physiology-Heart and Circulatory Physiology 290, no. 5 (2006): H1756—H1762. http://dx.doi.org/10.1152/ajpheart.01104.2005.

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l-Arginine, the sole substrate for the nitric oxide (NO) synthase (NOS) enzyme in producing NO, is also a substrate for arginase. We examined normal feline hearts and hearts with compensated left ventricular (LV) hypertrophy (LVH) produced by ascending aorta banding. Using Western blot analysis, we examined the abundance of arginase isozymes in crude homogenates and isolated cardiac myocytes obtained from the LVs of normal and LVH hearts. We examined the functional significance of myocyte arginase via measurement of shortening and intracellular calcium in isolated myocytes in the presence and

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Caldwell, R. William, Paulo C. Rodriguez, Haroldo A. Toque, S. Priya Narayanan, and Ruth B. Caldwell. "Arginase: A Multifaceted Enzyme Important in Health and Disease." Physiological Reviews 98, no. 2 (2018): 641–65. http://dx.doi.org/10.1152/physrev.00037.2016.

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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 a

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Reyes, Loretta Z., Pamela D. Winterberg, Roshan Punnoose George, et al. "Arginine Dysregulation and Myocardial Dysfunction in a Mouse Model and Children with Chronic Kidney Disease." Nutrients 15, no. 9 (2023): 2162. http://dx.doi.org/10.3390/nu15092162.

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Cardiovascular disease is the leading cause of death in chronic kidney disease (CKD). Arginine, the endogenous precursor for nitric oxide synthesis, is produced in the kidneys. Arginine bioavailability contributes to endothelial and myocardial dysfunction in CKD. Plasma from 129X1/SvJ mice with and without CKD (5/6th nephrectomy), and banked plasma from children with and without CKD were analyzed for amino acids involved in arginine metabolism, ADMA, and arginase activity. Echocardiographic measures of myocardial function were compared with plasma analytes. In a separate experiment, a non-spec

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Morris, Claudia R., Gregory Kato, Mirjana Poljakovic, et al. "The Arginine-to-Ornithine Ratio: Biomarker of Arginase Activity and Predictor of Mortality in Sickle Cell Disease." Blood 104, no. 11 (2004): 237. http://dx.doi.org/10.1182/blood.v104.11.237.237.

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Abstract Sickle cell disease (SCD) is characterized by a state of nitric oxide resistance and limited bioavailability of L-arginine, the substrate for nitric oxide synthesis. While nitric oxide resistance occurs secondary to inactivation of nitric oxide by plasma hemoglobin released during intravascular hemolysis and by reactive oxygen species, mechanisms that limit L-arginine are not known. We hypothesized that increased arginase activity in patients with SCD would shift arginine metabolism away from nitric oxide production and towards ornithine metabolism, contributing to endothelial dysfunc

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Chen, Bernadette, Andrea E. Calvert, Hongmei Cui, and Leif D. Nelin. "Hypoxia promotes human pulmonary artery smooth muscle cell proliferation through induction of arginase." American Journal of Physiology-Lung Cellular and Molecular Physiology 297, no. 6 (2009): L1151—L1159. http://dx.doi.org/10.1152/ajplung.00183.2009.

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Vascular remodeling and smooth muscle cell proliferation are hallmark pathogenic features of pulmonary artery hypertension (PAH). Alterations in the metabolism of l-arginine via arginase and nitric oxide synthase play a critical role in the endothelial dysfunction seen in PAH. l-arginine metabolism by arginase produces l-ornithine and urea. l-ornithine is a precursor for polyamine and proline synthesis, ultimately leading to an increase in cellular proliferation. Given the integral role of the smooth muscle layer in the pathogenesis of hypoxia-induced PAH, we hypothesized that hypoxia would in

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