ARGINASE: A CRITICAL REGULATOR OF NITRIC OXIDE SYNTHESIS AND VASCULAR FUNCTION
Open accessAbstract
SUMMARY: Arginase is the focal enzyme of the urea cycle hydrolysing l‐arginine to urea and l‐ornithine. Emerging studies have identified arginase in the vasculature and have implicated this enzyme in the regulation of nitric oxide (NO) synthesis and the development of vascular disease. Arginase inhibits the production of NO via several potential mechanisms, including competition with NO synthase (NOS) for the substrate l‐arginine, uncoupling of NOS resulting in the generation of the NO scavenger, superoxide and peroxynitrite, repression of the translation and stability of inducible NOS protein, inhibition of inducible NOS activity via the generation of urea and by sensitization of NOS to its endogenous inhibitor asymmetric dimethyl‐l‐arginine. Upregulation of arginase inhibits endothelial NOS‐mediated NO synthesis and may contribute to endothelial dysfunction in hypertension, ageing, ischaemia–reperfusion and diabetes. Arginase also redirects the metabolism of l‐arginine to l‐ornithine and the formation of polyamines and l‐proline, which are essential for smooth muscle cell growth and collagen synthesis. Therefore, the induction of arginase may also promote aberrant vessel wall remodelling and neointima formation. Arginase represents a promising novel therapeutic target that may reverse endothelial and smooth muscle cell dysfunction and prevent vascular disease.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
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 [259]
Cites
Vascular endothelial cells synthesize nitric oxide from L-arginine
Palmer, R. M. J., Ashton, D., & Moncada, S. (1988) · Nature · doi:10.1038/333664a0 · Cited by 4,745 · see citing works
Tabor, C. W., & Tabor, H. (1984) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.53.070184.003533 · Cited by 3,064 · see citing works
Arginine metabolism: nitric oxide and beyond
WU, G., & MORRIS, S. M. (1998) · Biochemical Journal · doi:10.1042/bj3360001 · Cited by 2,811 · see citing works
Drexler, H., Zeiher, A. M., Meinzer, K., & Just, H. (1991) · The Lancet · doi:10.1016/0140-6736(91)92372-9 · Cited by 801 · see citing works
Morris, C. R. (2005) · JAMA · doi:10.1001/jama.294.1.81 · Cited by 762 · see citing works
Antiatherogenic effects of L-arginine in the hypercholesterolemic rabbit.
Cooke, J. P., Singer, A. H., Tsao, P. S., Zera, P. H., Rowan, R. A., & Billingham, M. E. (1992) · Journal of Clinical Investigation · doi:10.1172/jci115937 · Cited by 687 · see citing works
Comparative properties of arginases
Jenkinson, C. P., Grody, W. W., & Cederbaum, S. D. (1996) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/0305-0491(95)02138-8 · Cited by 610 · see citing works
Nitric oxide and its role in the cardiovascular system
Loscalzo, J., & Welch, G. N. (1995) · Progress in Cardiovascular Diseases · doi:10.1016/s0033-0620(05)80001-5 · Cited by 599 · see citing works
Nitrogen metabolism and ornithine cycle function
Meijer, A. J., Lamers, W. H., & Chamuleau, R. A. F. M. (1990) · Physiological Reviews · doi:10.1152/physrev.1990.70.3.701 · Cited by 570 · see citing works
Arginine: Biochemistry, Physiology, and Therapeutic Implications
Barbul, A. (1986) · Journal of Parenteral and Enteral Nutrition · doi:10.1177/0148607186010002227 · Cited by 532 · see citing works
Berkowitz, D. E., White, R., Li, D., Minhas, K. M., Cernetich, A., Kim, S., Burke, S., Shoukas, A. A., Nyhan, D., Champion, H. C., et al. (2003) · Circulation · doi:10.1161/01.cir.0000092948.04444.c7 · Cited by 486 · see citing works
Lefer, A. M., & Lefer, D. J. (1996) · Cardiovascular Research · doi:10.1016/s0008-6363(96)00073-9 · Cited by 401 · see citing works
Li, H. Z., Meininger, C. J., Hawker, J. R., Haynes, T. E., Kepka‐Lenhart, D., Mistry, S. K., Morris, S. M., & Wu, G. (2001) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.2001.280.1.e75 · Cited by 389 · see citing works
Xu, W., Kaneko, F. T., Zheng, S., Comhair, S. A. A., Janocha, A. J., Goggans, T., Thunnissen, F. B. J. M., Farver, C., Hazen, S. L., Jennings, C., et al. (2004) · The FASEB Journal · doi:10.1096/fj.04-2317fje · Cited by 369 · see citing works
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 358 · see citing works
Ignarro, L. J., Buga, G. M., Liu, W., Bauer, P. M., Wu, G., & Soldato, P. D. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.071054698 · Cited by 331 · see citing works
Arginase modulates nitric oxide production in activated macrophages
Chang, C., Liao, J. C., & Kuo, L. (1998) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.1998.274.1.h342 · Cited by 300 · see citing works
Zhang, W., & Frei, B. B. (2001) · The FASEB Journal · doi:10.1096/fj.01-0260com · Cited by 300 · see citing works
Arginine Nutrition and Cardiovascular Function
Wu, G., & Meininger, C. J. (2000) · Journal of Nutrition · doi:10.1093/jn/130.11.2626 · Cited by 288 · see citing works
Buga, G. M., Singh, R., Pervin, S., Rogers, N. E., Schmitz, D. A., Jenkinson, C. P., Cederbaum, S. D., & Ignarro, L. J. (1996) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.1996.271.5.h1988 · Cited by 257 · see citing works
Thrombin Stimulates Human Endothelial Arginase Enzymatic Activity via RhoA/ROCK Pathway
Ming, X., Barandiér, C., Viswambharan, H., Kwak, B. R., Mach, F., Mazzolai, L., Hayoz, D., Ruffieux, J., Rusconi, S., Montani, J., et al. (2004) · Circulation · doi:10.1161/01.cir.0000142867.26182.32 · Cited by 237 · see citing works
Zhang, C., Hein, T. W., Wang, W., Chang, C., & Kuo, L. (2001) · The FASEB Journal · doi:10.1096/fj.00-0681fje · Cited by 230 · see citing works
Human type II arginase: sequence analysis and tissue-specific expression
Morris, S. M., Bhamidipati, D., & Kepka‐Lenhart, D. (1997) · Gene · doi:10.1016/s0378-1119(97)00099-1 · Cited by 216 · see citing works
Bivalacqua, T. J., Hellstrom, W. J. G., Kadowitz, P. J., & Champion, H. C. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.4874 · Cited by 212 · see citing works
Zhang, C., Hein, T. W., Wang, W., Miller, M. W., Fossum, T. W., McDonald, M. M., Humphrey, J. D., & Kuo, L. (2004) · Hypertension · doi:10.1161/01.hyp.0000146907.82869.f2 · Cited by 194 · see citing works
Cloning and Characterization of the Human Type II Arginase Gene
Vockley, J. G., Jenkinson, C. P., Shukla, H., Kern, R. M., Grody, W. W., & Cederbaum, S. D. (1996) · Genomics · doi:10.1006/geno.1996.0606 · Cited by 191 · see citing works
Carbon monoxide inhibits apoptosis in vascular smooth muscle cells
Liu, X. (2002) · Cardiovascular Research · doi:10.1016/s0008-6363(02)00410-8 · Cited by 182 · see citing works
Hein, T. W., Zhang, C., Wang, W., Chang, C., Thengchaisri, N., & Kuo, L. (2003) · The FASEB Journal · doi:10.1096/fj.03-0115fje · Cited by 182 · see citing works
El-Gayar, S., Thüring, H., Pfeilschifter, J. M., Röllinghoff, M., & Bogdan, C. (2003) · The Journal of Immunology · doi:10.4049/jimmunol.171.9.4561 · Cited by 180 · see citing works
Knockdown of Arginase I Restores NO Signaling in the Vasculature of Old Rats
White, A. R., Ryoo, S., Li, D., Champion, H. C., Steppan, J., Wang, D., Nyhan, D. P., Shoukas, A. A., Hare, J. M., & Berkowitz, D. E. (2005) · Hypertension · doi:10.1161/01.hyp.0000198543.34502.d7 · Cited by 179 · see citing works
Arginase and asthma: novel insights into nitric oxide homeostasis and airway hyperresponsiveness
Meurs, H., Maarsingh, H., & Zaagsma, J. (2003) · Trends in Pharmacological Sciences · doi:10.1016/s0165-6147(03)00227-x · Cited by 177 · see citing works
Boucher, J., Custot, J., Goff, S. V., Delaforge, M., Lepoivre, M., Tenu, J., Yapo, A., & Mansuy, D. (1994) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1994.2371 · Cited by 172 · see citing works
Mouse Model for Human Arginase Deficiency
Iyer, R. K., Yoo, P. K., Kern, R. M., Rozengurt, N., Tsoa, R. W., O’Brien, W. E., Yu, H., Grody, W. W., & Cederbaum, S. D. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.13.4491-4498.2002 · Cited by 171 · see citing works
Arginase: Structure, Mechanism, and Physiological Role in Male and Female Sexual Arousal
Christianson, D. W. (2005) · Accounts of Chemical Research · doi:10.1021/ar040183k · Cited by 168 · see citing works
Arginase 1 Overexpression in Psoriasis
Bruch‐Gerharz, D., Schnorr, O., Suschek, C. V., Beck, K., Pfeilschifter, J. M., Ruzicka, T., & Kolb-Bachofen, V. (2003) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)63811-4 · Cited by 163 · see citing works
Liu, W., Jacobs, A. T., Morris, S. M., & Ignarro, L. J. (2000) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.2000.279.1.c248 · Cited by 157 · see citing works
Soriano, F. G., Virág, L., & Szabó, C. (2001) · Journal of Molecular Medicine · doi:10.1007/s001090100236 · Cited by 157 · see citing works
Arginase inhibition increases nitric oxide production in bovine pulmonary arterial endothelial cells
Chicoine, L. G., Paffett, M. L., Young, T. L., & Nelin, L. D. (2004) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00194.2003 · Cited by 152 · see citing works
Demougeot, C., Prigent‐Tessier, A., Marie, C., & Berthelot, A. (2005) · Journal of Hypertension · doi:10.1097/01.hjh.0000166837.78559.93 · Cited by 149 · see citing works
Durante, W., Liao, L., Reyna, S. V., Peyton, K. J., & Schafer, A. I. (2001) · Circulation · doi:10.1161/01.cir.103.8.1121 · Cited by 145 · see citing works
Self-citationElevated arginase I expression in rat aortic smooth muscle cells increases cell proliferation
Liu, W., Wu, G., Morris, S. M., & Ignarro, L. J. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.161294898 · Cited by 144 · see citing works
Johnson, F. K., Johnson, R. A., Peyton, K. J., & Durante, W. (2004) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00758.2004 · Cited by 143 · see citing works
Self-citationShi, O., Morris, S. M., Zoghbi, H. Y., Porter, C. W., & O’Brien, W. E. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.3.811-813.2001 · Cited by 142 · see citing works
Tenu, J., Lepoivre, M., Moali, C., Brollo, M., Mansuy, D., & Boucher, J. (1999) · Nitric Oxide · doi:10.1006/niox.1999.0255 · Cited by 141 · see citing works
Hyperargininemia due to liver arginase deficiency
Crombez, E. A., & Cederbaum, S. D. (2004) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2004.11.004 · Cited by 135 · see citing works
Increased Arginase Activity in Cystic Fibrosis Airways
Grasemann, H., Schwiertz, R., Matthiesen, S., Racké, K., & Ratjen, F. A. (2005) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.200502-253oc · Cited by 123 · see citing works
Hey, C., Boucher, J., Goff, S. V., Ketterer, G., Wessler, I. K., & Racké, K. (1997) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0701143 · Cited by 103 · see citing works
Arginase pathway in human endothelial cells in pathophysiological conditions
Bachetti, T. (2004) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2004.05.004 · Cited by 103 · see citing works
Tarry, W. C., & Makhoul, R. G. (1994) · Arteriosclerosis and Thrombosis A Journal of Vascular Biology · doi:10.1161/01.atv.14.6.938 · Cited by 101 · see citing works
Complete nucleotide sequence of cDNA and deduced amino acid sequence of rat liver arginase.
Kawamoto, S., Amaya, Y., Murakami, K., et al. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)45565-2 · Cited by 93 · see citing works
Durante, W., Liao, L., Reyna, S. V., Peyton, K. J., & Schafer, A. I. (2000) · The FASEB Journal · doi:10.1096/fj.99-0960com · Cited by 93 · see citing works
Self-citationJohn, S., & Schmieder, R. E. (2003) · Current Hypertension Reports · doi:10.1007/s11906-003-0021-1 · Cited by 91 · see citing works
L-Arginine in cardiovascular disease: dream or reality?
Tousoulis, D., Antoniades, C. A., Tentolouris, C. A., Goumas, G., Stefanadis, C., & Toutouzas, P. C. (2002) · Vascular Medicine · doi:10.1191/1358863x02vm434ra · Cited by 86 · see citing works
Dizikes, G. J., Grody, W. W., Kern, R. M., & Cederbaum, S. D. (1986) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(86)80333-3 · Cited by 83 · see citing works
Bohlooly‐Y, M., Olsson, B., Bruder, C. E. G., Lindén, D., Sjögren, K., Bjursell, M., Egecioglu, E., Svensson, L., Brodin, P., Waterton, J. C., et al. (2005) · Diabetes · doi:10.2337/diabetes.54.1.51 · Cited by 83 · see citing works
Böger, R. H., & Bode‐Böger, S. M. (2000) · Seminars in Thrombosis and Hemostasis · doi:10.1055/s-2000-13210 · Cited by 81 · see citing works
Durante, W., Liao, L., Iftikhar, I., et al. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.20.11838 · Cited by 76 · see citing works
Self-citationExpression and Activity of Arginase Isoenzymes During Normal and Diabetes-Impaired Skin Repair
Kämpfer, H., Pfeilschifter, J. M., & Frank, S. (2003) · Journal of Investigative Dermatology · doi:10.1046/j.1523-1747.2003.12610.x · Cited by 75 · see citing works
Berka, V., Wu, G., Yeh, H.-C., Palmer, G., & Tsai, A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m404044200 · Cited by 69 · see citing works
Urea inhibits inducible nitric oxide synthase in macrophage cell line
Prabhakar, S. S., Zeballos, G. A., Montoya‐Zavala, M., et al. (1997) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1997.273.6.c1882 · Cited by 62 · see citing works
Identification of Macrophage Arginase I as a New Candidate Gene of Atherosclerosis Resistance
Teupser, D., Burkhardt, R., Wilfert, W., Haffner, I., Nebendahl, K., & Thiery, J. (2005) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000195791.83380.4c · Cited by 61 · see citing works
Cytokine-Induced Endothelial Arginase Expression Is Dependent on Epidermal Growth Factor Receptor
Nelin, L. D., Chicoine, L. G., Reber, K. M., English, B. K., Young, T. L., & Liu, Y. (2005) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2005-0039oc · Cited by 53 · see citing works
Nishimura, H., Rosenblum, W. I., Nelson, G. H., et al. (1991) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.1991.261.1.h15 · Cited by 52 · see citing works
INCREASED ARGINASE ACTIVITY IN AORTA OF MINERALOCORTICOID-SALT HYPERTENSIVE RATS
Rodriguez, S., Richert, L., & Berthelot, A. (2000) · Clinical and Experimental Hypertension · doi:10.1081/ceh-100100063 · Cited by 48 · see citing works
Durante, W., Liao, L., Peyton, K. J., & Schafer, A. I. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.48.30154 · Cited by 47 · see citing works
Self-citationNelin, L. D., Nash, H. E., & Chicoine, L. G. (2001) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.2001.281.5.l1232 · Cited by 46 · see citing works
Corraliza, I., & Moncada, S. (2002) · PubMed · Cited by 43 · see citing works
Regulation of L-Arginine Transport and Metabolism in Vascular Smooth Muscle Cells
Durante, W. (2001) · Cell Biochemistry and Biophysics · doi:10.1385/cbb:35:1:19 · Cited by 39 · see citing works
Self-citationDurante, W., Liao, L., Peyton, K. J., et al. (1998) · Circulation Research · doi:10.1161/01.res.83.2.217 · Cited by 39 · see citing works
Self-citationJung, A. S., Kubo, H., Wilson, R., et al. (2005) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.01104.2005 · Cited by 30 · see citing works
Loyaga‐Rendon, R. Y., Sakamoto, S., Beppu, M., Asô, T., Ishizaka, M., Takahashi, R., & Azuma, H. (2004) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2004.09.006 · Cited by 27 · see citing works
An experiment of nature: genetic l-arginine deficiency and NO insufficiency
Loscalzo, J. (2001) · Journal of Clinical Investigation · doi:10.1172/jci13848 · Cited by 23 · see citing works
Intimal hyperplasia is reduced by ornithine decarboxylase inhibition
Endean, E. D., Kispert, J. F., Martin, K. W., et al. (1991) · Journal of Surgical Research · doi:10.1016/0022-4804(91)90054-p · Cited by 18 · see citing works
Arginase in Glomerulonephritis
Waddington, S. N., & Cattell, V. (2000) · Nephron Experimental Nephrology · doi:10.1159/000020660 · Cited by 11 · see citing works
ARGINASE PROMOTES VASCULAR SMOOTH MUSCLE CELL PROLIFERATION AND NEOINTIMA FORMATION
Durante, W., Tulis, D. A., KeswaniI, A. N., et al. (2004) · Cardiovascular Pathology · doi:10.1016/j.carpath.2004.03.131 · Cited by 1 · see citing works
Self-citation
Flagged first, then by citations
Research works printed but not linked: 1
- Durante W, 2005, Arginase induces endothelial dysfunction and hypertension in obese Zucker rats, Diabetes, 54, A51
Cited by
Sorted by citations
Understanding the Mysterious M2 Macrophage through Activation Markers and Effector Mechanisms
Rőszer, T. (2015) · Mediators of Inflammation · doi:10.1155/2015/816460 · Cited by 1,762 · see citing works
“Similarly, CD206 expressing human decidual macrophages produce IL-10 and CCL18 with a possible role in the maternal immunological tolerance of the fetus [79].”
BackgroundArginine 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 · see citing works
“Therefore, relative changes in their enzymatic activities serve as major determinants of NO and polyamine production in many cell types (Durante et al. 2007; Li et al. 2001; Wei et al. 2001).”
BackgroundKolluru, G. K., Bir, S. C., & Kevil, C. G. (2012) · International Journal of Vascular Medicine · doi:10.1155/2012/918267 · Cited by 728 · see citing works
“many of the vascular complications observed during diabetes [183].”
BackgroundTakeda, N., O'Dea, E. L., Doedens, A. L., Kim, J., Weidemann, A., Stockmann, C., Asagiri, M., Simon, M. C., Hoffmann, A., & Johnson, R. S. (2010) · Genes & Development · doi:10.1101/gad.1881410 · Cited by 621 · see citing works
Self-citationAmino acid metabolism in health and disease
Ling, Z., Jiang, Y.-F., Ru, J.-N., Lu, J.-H., Ding, B., & Wu, J. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01569-3 · Cited by 574 · see citing works
“171,205,206 Fig.”
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
Arginase: A Multifaceted Enzyme Important in Health and Disease
Caldwell, R. W., Rodriguez, P. C., Toque, H. A., Narayanan, S. P., & Caldwell, R. B. (2018) · Physiological Reviews · doi:10.1152/physrev.00037.2016 · Cited by 495 · see citing works
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 · see citing works
“Various aspects of functional roles of the arginases in vascular biology, including atherosclerosis, have been reviewed recently and thus will not be considered here (Morris, 2005; Huynh and Chin-Dusting, 2006; Yang and Ming, 2006; Durante et al., 2007; Santhanam et al., 2008).”
BackgroundCellular backpacks for macrophage immunotherapy
Shields, C. W., Evans, M. A., Wang, L. L.-W., Baugh, N., Iyer, S., Wu, D., Zhao, Z.-M., Pusuluri, A., Ukidve, A., Pan, D. C., et al. (2020) · Science Advances · doi:10.1126/sciadv.aaz6579 · Cited by 360 · see citing works
“Arg-1 affects NO synthase and downregulates NO production (32).”
BackgroundCutaneous Vasodilator and Vasoconstrictor Mechanisms in Temperature Regulation
Johnson, J. M., Minson, C. T., & Kellogg, D. L. (2014) · Comprehensive physiology · doi:10.1002/cphy.c130015 · Cited by 459 · see citing works
Vanhoutte, P. M., Zhao, Y., Xu, A., & Leung, S. W. S. (2016) · Circulation Research · doi:10.1161/circresaha.116.306531 · Cited by 391 · see citing works
Regulation of nitric oxide production in health and disease
Luiking, Y. C., ENGELEN, M. P. K. J., & Deutz, N. E. P. (2009) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/mco.0b013e328332f99d · Cited by 332 · see citing works
Pernow, J., & Jung, C. (2013) · Cardiovascular Research · doi:10.1093/cvr/cvt036 · Cited by 311 · see citing works
“Interestingly, L-arginine is also a substrate for arginase, which converts L-arginine to L-ornithine and urea.(3) This means that the production of NO is dependent on the relative expression and activities of arginase and eNOS.”
BackgroundBissonnette, É. Y., Lauzon‐Joset, J., Debley, J. S., & Ziegler, S. F. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.583042 · Cited by 252 · see citing works
Kim, J. H., Bugaj, L. J., Oh, Y. J., Bivalacqua, T. J., Ryoo, S., Soucy, K. G., Santhanam, L., Webb, A. K., Camara, A., Sikka, G., et al. (2009) · Journal of Applied Physiology · doi:10.1152/japplphysiol.91393.2008 · Cited by 244 · see citing works
“Arginase activation contributes to increased production of proline and polyamine, which are associated with collagen and smooth muscle proliferation, respectively (22).”
BackgroundFeig, J. E., Parathath, S., Rong, J. X., Mick, S. L., Vengrenyuk, Y., Grauer, L., Young, S. G., & Fisher, E. A. A. (2011) · Circulation · doi:10.1161/circulationaha.110.984146 · Cited by 236 · see citing works
Tang, W. H. W., Wang, Z., Cho, L., Brennan, D. M., & Hazen, S. L. (2009) · Journal of the American College of Cardiology · doi:10.1016/j.jacc.2009.02.036 · Cited by 221 · see citing works
George, A., Pushkaran, S., Konstantinidis, D. G., Koochaki, S., Malik, P., Mohandas, N., Zheng, Y., Joiner, C. H., & Kalfa, T. A. (2013) · Blood · doi:10.1182/blood-2012-07-441188 · Cited by 218 · see citing works
Arginine and Citrulline and the Immune Response in Sepsis
Wijnands, K. A. P., Castermans, T. M. R., Hommen, M., Meesters, D. M., & Poeze, M. (2015) · Nutrients · doi:10.3390/nu7031426 · Cited by 208 · see citing works
“Arginine utilization is enhanced by the catabolic activity of arginase [2,139,140] and NOS2 or by an”
BackgroundFélétou, M. (2011) · Colloquium Series on Integrated Systems Physiology From Molecule to Function · doi:10.4199/c00031ed1v01y201105isp019 · Cited by 202 · see citing works
Mechanisms of Vasculopathy in Sickle Cell Disease and Thalassemia
Morris, C. R. (2008) · Hematology · doi:10.1182/asheducation-2008.1.177 · Cited by 196 · see citing works
“Therefore, the induction of arginase may also promote aberrant vessel wall remodelling and neointima formation.(13) Proline is an amino acid that is also involved in lung”
BackgroundBrocq, M. L. L., Leslie, S. J., Milliken, P. H., & Megson, I. L. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.2013 · Cited by 190 · see citing works
“What is clear is that the interaction of L-arginine with NOS is dependent as much on the activity of the enzyme responsible for its conversion to ornithine, arginase (102), and on the synthesis and metabolic pathways (e.”
Shemyakin, A. S., Kövamees, O., Rafnsson, A. T., Böhm, F., Svenarud, P. K., Settergren, M., Jung, C., & Pernow, J. (2012) · Circulation · doi:10.1161/circulationaha.112.140335 · Cited by 185 · see citing works
Automated GC–MS analysis of free amino acids in biological fluids
Kaspar, H., Dettmer, K., Gronwald, W., & Oefner, P. J. (2008) · Journal of Chromatography B · doi:10.1016/j.jchromb.2008.06.018 · Cited by 180 · see citing works
Yi, H., Guo, C., Yu, X., Zuo, D., & Wang, X. (2012) · The Journal of Immunology · doi:10.4049/jimmunol.1200086 · Cited by 173 · see citing works
“ginase activity and potential different outcomes (42), further studies are necessary to understand the precise role of arginase 1 in MDSC-driven Th17 polarization.”
Arginine—Dual roles as an onconutrient and immunonutrient
Albaugh, V. L., Pinzon‐Guzman, C., & Barbul, A. (2016) · Journal of Surgical Oncology · doi:10.1002/jso.24490 · Cited by 173 · see citing works
“Biochemically the Km of arginase-1 is 5mM [82], much higher than the typical arginine concentration in the plasma that is”
BackgroundSanthanam, L., Christianson, D. W., Nyhan, D. P., & Berkowitz, D. E. (2008) · Journal of Applied Physiology · doi:10.1152/japplphysiol.90627.2008 · Cited by 166 · see citing works
“Ornithine, the product of the conversion of L-arginine to urea is the precursor for the synthesis of primary amino acid, proline and the polyamine-derived amino acids, spermidine and spermine, that could be important in altering vascular properties(30).”
Nitric oxide: Orchestrator of endothelium-dependent responses
Félétou, M., Köhler, R., & Vanhoutte, P. M. (2011) · Annals of Medicine · doi:10.3109/07853890.2011.585658 · Cited by 163 · see citing works
Arginine metabolism and deprivation in cancer therapy
Zou, S., Wang, X., Liu, P., Ke, C., & Xu, S. (2019) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2019.109210 · Cited by 159 · see citing works
Jones, C. V., & Ricardo, S. D. (2013) · Organogenesis · doi:10.4161/org.25676 · Cited by 147 · see citing works
Yang, J., Gonon, A. T., Sjöquist, P.-O., Lundberg, J. O., & Pernow, J. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1307058110 · Cited by 147 · see citing works
“After the washing step, the same volume of L-arginine-containing KH buffer was added to the RBCs and gently mixed and incubated with nor-NOHA (0.1–1 mM) at 37 °C for 30 min.”
BackgroundInfluentialArginase inhibition mediates cardioprotection during ischaemia–reperfusion
Jung, C., Gonon, A. T., Sjoquist, P.-O., Lundberg, J. O., & Pernow, J. (2010) · Cardiovascular Research · doi:10.1093/cvr/cvp303 · Cited by 139 · see citing works
Wijnands, K. A. P., Vink, H., Briedé, J. J., van Faassen, E. E., Lamers, W. H., Buurman, W. A., & Poeze, M. (2012) · PLoS ONE · doi:10.1371/journal.pone.0037439 · Cited by 136 · see citing works
“Especially, enhanced activity of Arginase-1 [20,21] and iNOS (NOS2), but also diminished de novo arginine synthesis from citrulline and a diminished de novo citrulline synthesis are relevant mechanism which contribute to arginine deficiency [17,19,22].”
BackgroundBailey, S. J., Winyard, P. G., Vanhatalo, A., Blackwell, J. R., DiMenna, F. J., Wilkerson, D. P., & Jones, A. M. (2010) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00503.2010 · Cited by 132 · see citing works
Scioli, M. G., Bielli, A., Arcuri, G., Ferlosio, A., & Orlandi, A. (2014) · Vascular Cell · doi:10.1186/2045-824x-6-19 · Cited by 132 · see citing works
“In mammals, nitric oxide (NO) is produced by a family of enzymes, named nitric oxide synthases (NOSs), that catalyse the production NO from L-arginine.”
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 126 · see citing works
“Therefore, relative changes in their enzymatic activities serve as major determinants of NO and polyamine production in many cell types (Durante et al. 2007; Li et al. 2001).”
BackgroundBok, E., Chung, Y. C., Kim, K., Baik, H. H., Shin, W.-H., & Jin, B. K. (2018) · Experimental & Molecular Medicine · doi:10.1038/s12276-018-0111-4 · Cited by 125 · see citing works
Cardiovascular Effects of Caffeic Acid and Its Derivatives: A Comprehensive Review
Silva, H., & Lopes, N. M. F. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.595516 · Cited by 129 · see citing works
Berryman, C. E., Preston, A. G., Karmally, W., Deckelbaum, R. J., & Kris‐Etherton, P. M. (2011) · Nutrition Reviews · doi:10.1111/j.1753-4887.2011.00383.x · Cited by 125 · see citing works
Nitrosative Stress and Its Association with Cardiometabolic Disorders
Pérez-Torres, I., Manzano-Pech, L., Rubio-Ruiz, M. E., Soto, M. E., & Guarner‐Lans, V. (2020) · Molecules · doi:10.3390/molecules25112555 · Cited by 124 · see citing works
“This alters the electron transfer in NOS that leads to its decoupling, with subsequently less generation of NO and more production of O2− [28].”
BackgroundRole of arginine in superficial wound healing in man
Debats, I. B. J. G., Wolfs, T. G. A. M., Gotoh, T., Cleutjens, J. P. M., Peutz‐Kootstra, C. J., & van der Hulst, R. R. W. J. (2009) · Nitric Oxide · doi:10.1016/j.niox.2009.07.006 · Cited by 121 · see citing works
M2 macrophage polarisation is associated with alveolar formation during postnatal lung development
Jones, C. V., Williams, T. M., Walker, K. A., Dickinson, H., Sakkal, S., Rumballe, B. A., Little, M. H., Jenkin, G., & Ricardo, S. D. (2013) · Respiratory Research · doi:10.1186/1465-9921-14-41 · Cited by 111 · see citing works
“Arg1 is associated with collagen formation and ECM production [47].”
BackgroundCharacterization of a preclinical model of chronic ischemic wound
Roy, S., Biswas, S., Khanna, S., Gordillo, G. M., Bergdall, V. K., Green, J., Marsh, C. B., Gould, L. J., & Sen, C. K. (2009) · Physiological Genomics · doi:10.1152/physiolgenomics.90362.2008 · Cited by 107 · 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
“In view of the importance of NO and L-arginine in endothelial function, the imbalance between arginase and NOS due to arginase upregulation can induce the overconsumption of Larginine, provoking a lack of substrate for NOS to produce NO [19, 29], leading to endothelial dysfunction.”
BackgroundBagnost, T., Ma, L., da Silva, R., Rezakhaniha, R., Houdayer, C., Stergiopulos, N., André, C., Guillaume, Y. C., Berthelot, A., & Demougeot, C. (2010) · Cardiovascular Research · doi:10.1093/cvr/cvq081 · Cited by 107 · see citing works
Arginine and Arginases Modulate Metabolism, Tumor Microenvironment and Prostate Cancer Progression
Matos, A., Carvalho, M., Bicho, M., & Ribeiro, R. J. T. (2021) · Nutrients · doi:10.3390/nu13124503 · Cited by 106 · see citing works
“Nitric oxide is a simple gas molecule with many roles in cancer-related mechanisms [40,44,45].”
BackgroundAkimov, O. Y., & Kostenko, V. О. (2016) · The Ukrainian Biochemical Journal · doi:10.15407/ubj88.06.070 · Cited by 95 · see citing works
“This situation changes drastically during pathogenic states [4].”
BackgroundRevisiting the Mechanisms of Immune Evasion Employed by Human Parasites
Chulanetra, M., & Chaicumpa, W. (2021) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2021.702125 · Cited by 95 · see citing works
“L-arginase inhibits the production of nitric oxide (NO) via several potential mechanisms, including competition with iNOS for L-arginine and the generation of scavengers for nitric oxide (NO), superoxide, and peroxynitrite (Durante et al., 2007).”
BackgroundNarayanan, S. P., Rojas, M., Suwanpradid, J., Toque, H. A., Caldwell, R. W., & Caldwell, R. B. (2013) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2013.06.002 · Cited by 94 · see citing works
Kotthaus, J., Wahl, B., Havemeyer, A., Kotthaus, J., Schade, D., Garbe-Schönberg, D., Mendel, R., Bittner, F., & Clement, B. (2011) · Biochemical Journal · doi:10.1042/bj20100960 · Cited by 88 · see citing works
Role of Arginase in Vessel Wall Remodeling
Durante, W. (2013) · Frontiers in Immunology · doi:10.3389/fimmu.2013.00111 · Cited by 90 · see citing works
Self-citationArginase 1 contributes to diminished coronary arteriolar dilation in patients with diabetes
Beleznai, T., Fehér, A., Spielvogel, D., Lansman, S. L., & Bagi, Z. A. (2011) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00831.2010 · Cited by 90 · see citing works
A long-term study on female mice fed on a genetically modified soybean: effects on liver ageing
Malatesta, M., Boraldi, F., Annovi, G., Baldelli, B., Battistelli, S., Biggiogera, M., & Quaglino, D. (2008) · Histochemistry and Cell Biology · doi:10.1007/s00418-008-0476-x · Cited by 88 · see citing works
“Arginine cleavage generates urea and ornithine, the latter being necessary for tissue repair processes (Witte and Barbul 2003; Durante et al. 2007) as well as for citrullin production in the mito-”
BackgroundRoyo, F., Moreno, L., Mleczko, J., Palomo, L., González, E., Cabrera, D., Cogolludo, A. L., Pérez‐Vizcaíno, F., Liempd, S. M. V., & Falcón‐Pérez, J. M. (2017) · Scientific Reports · doi:10.1038/srep42798 · Cited by 88 · see citing works
L-Norvaline Reverses Cognitive Decline and Synaptic Loss in a Murine Model of Alzheimer's Disease
Polis, B., Srikanth, K. D., Elliott, E., Gil-Henn, H., & Samson, A. O. (2018) · Neurotherapeutics · doi:10.1007/s13311-018-0669-5 · Cited by 85 · see citing works
“A growing body of evidence indicates that NO induces neuroprotection by triggering vasodilation and increasing the blood supply to neurons, thereby reducing their susceptibility to oxidative stress [29].”
BackgroundAmino acids: key sources for immunometabolites and immunotransmitters
Miyajima, M. (2020) · International Immunology · doi:10.1093/intimm/dxaa019 · Cited by 88 · see citing works
Bioinformatics methods in drug repurposing for Alzheimer’s disease
Siavelis, J. C., Bourdakou, M. M., Athanasiadis, E. I., Spyrou, G. M., & Nikita, K. S. (2015) · Briefings in Bioinformatics · doi:10.1093/bib/bbv048 · Cited by 84 · see citing works
Chen, B., Calvert, A. E., Cui, H., & Nelin, L. D. (2009) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00183.2009 · Cited by 88 · see citing works
L-Citrulline: A Non-Essential Amino Acid with Important Roles in Human Health
Aguayo, E., Martínez‐Sánchez, A., Fernández-Lobato, B., & Alacid, F. (2021) · Applied Sciences · doi:10.3390/app11073293 · Cited by 92 · see citing works
“However, to a much lesser extent, arginase I has been detected in extra-hepatic tissues such as endothelial cells as well as vascular smooth muscle cells [23].”
Backgroundl-Arginine and COVID-19: An Update
Adebayo, A., Varzideh, F., Wilson, S. M., Gambardella, J., Eacobacci, M., Jankauskas, S. S., Donkor, K., Kansakar, U., Trimarco, V., Mone, P., et al. (2021) · Nutrients · doi:10.3390/nu13113951 · Cited by 87 · see citing works
“A substrate competition occurs between NOS and arginase [25,26].”
BackgroundArginase-2 Mediates Diabetic Renal Injury
Morris, S. M., Gao, T., Cooper, T. K., Kepka‐Lenhart, D., & Awad, A. S. (2011) · Diabetes · doi:10.2337/db11-0901 · Cited by 85 · see citing works
Senescent Microglia: The Key to the Ageing Brain?
Greenwood, E. K., & Brown, D. R. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22094402 · Cited by 84 · see citing works
“Arginase 1, an enzyme with the capacity to diminish NO production [38], has been suggested as a specific M2 marker [39,40], as has Found in Inflammatory Zone 1 (FIZZ1), a secreted protein encouraging the deposition of an extracellular matrix [41,42].”
BackgroundKetonen, J., Pilvi, T. K., & Mervaala, E. M. A. (2010) · Heart and Vessels · doi:10.1007/s00380-009-1182-x · Cited by 81 · see citing works
“35 Oxidative stress may also increase the level of asymmetric dimethylarginine (ADMA) and induce endothelial arginase expression, both of which compete with L-arginine from eNOS.(26,30,31) We found that preincubation of vascular rings with Tiron, a cellpermeable, nonenzymatic scavenger of superoxide anion,(17)”
BackgroundŁuczak, A., Madej, M., Kasprzyk, A., & Doroszko, A. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/1417981 · Cited by 90 · see citing works
“Similarly, promoting abnormal remodeling and neointimal hyperplasia reduced NO bioavailability [134, 135].”
BackgroundElms, S. C., Chen, F., Wang, Y., Qian, J., Askari, B., Yu, Y., Pandey, D., Iddings, J. A., Caldwell, R. B., & Fulton, D. J. (2013) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00755.2012 · Cited by 83 · see citing works
“The importance of arginase to this relationship is underscored by a large number of studies showing that arginase expression and activity are increased in many cardiovascular disease states, such as atherosclerosis and diabetes, and that this occurs contemporaneously with reduced NO levels (2, 11, 32, 46, 53, 56, 57).”
BackgroundInfluentialHypoxic upregulation of arginase II in human lung endothelial cells
Krotova, K. Y., Patel, J. M., Block, E. R., & Zharikov, S. I. (2010) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00068.2010 · Cited by 80 · see citing works
“It has been shown that arginase is responsible for reduced NO levels in many pathological conditions (10, 16, 28, 29, 52, 53).”
BackgroundEndothelial dysfunction and vascular disease in later life
Virdis, A., Ghiadoni, L., Giannarelli, C., & Taddei, S. (2010) · Maturitas · doi:10.1016/j.maturitas.2010.04.006 · Cited by 79 · see citing works
Bench to bedside review: therapeutic modulation of nitric oxide in sepsis—an update
Lambden, S. (2019) · Intensive Care Medicine Experimental · doi:10.1186/s40635-019-0274-x · Cited by 79 · see citing works
Arginase inhibition restores in vivo coronary microvascular function in type 2 diabetic rats
Grönros, J., Jung, C., Lundberg, J. O., Cerrato, R., Östenson, C., & Pernow, J. (2011) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00560.2010 · Cited by 76 · see citing works
Gr1intCD11b+ Myeloid-Derived Suppressor Cells in Mycobacterium tuberculosis Infection
Obregón-Henao, A., Henao-Tamayo, M., Orme, I. M., & Ordway, D. J. (2013) · PLoS ONE · doi:10.1371/journal.pone.0080669 · Cited by 74 · see citing works
“It would be interesting to evaluate if arginase has a causal role in lung necrosis, by indirectly affecting endothelial function in blood vessels in close proximity to granulomas [52].”
BackgroundHolowatz, L. A., Santhanam, L., Webb, A. K., Berkowitz, D. E., & Kenney, W. L. (2011) · The Journal of Physiology · doi:10.1113/jphysiol.2010.203935 · Cited by 77 · see citing works
“Functionally, we could not determine the specific arginase isoform mediating the reduction in NO bioavailability due to the lack of isoform specific inhibitors (Cederbaum et al. 2004; Durante et al. 2007).”
BackgroundNitric oxide in the regulation of the sleep-wake states
Cespuglio, R., Amrouni, D., Meiller, A., Buguet, A., & Gautier-Sauvigné, S. (2012) · Sleep Medicine Reviews · doi:10.1016/j.smrv.2012.01.006 · Cited by 73 · see citing works
Álvares, T. S., Conte, C. A., Paschoalin, V. M. F., Silva, J. T., Meirelles, C. D. M., Bhambhani, Y. N., & Gomes, P. S. C. (2012) · Applied Physiology, Nutrition, and Metabolism · doi:10.1139/h11-144 · Cited by 71 · see citing works
NOX2-Induced Activation of Arginase and Diabetes-Induced Retinal Endothelial Cell Senescence
Rojas, M., Lemtalsi, T., Toque, H. A., Xu, Z., Fulton, D. J., Caldwell, R. W., & Caldwell, R. B. (2017) · Antioxidants · doi:10.3390/antiox6020043 · Cited by 73 · see citing works
“Arginase activity was assayed by measuring urea production from L-arginine as previously described [31].”
BackgroundDschietzig, T. B., Brecht, A., Bartsch, C., Baumann, G., Stangl, K., & Alexiou, K. (2012) · Cardiovascular Research · doi:10.1093/cvr/cvs149 · Cited by 71 · see citing works
“The prevailing scientific opinion is that the enzyme starves eNOS from L-arginine, which then results in uncoupling, superoxide production, peroxynitrite rise, and oxidative damage to the catalytic centre of eNOS.(41)”
BackgroundImmunohistochemical study of arginase 1 and 2 in various tissues of rats
Choi, S., Park, C., Ahn, M., Lee, J. H., & Shin, T. (2011) · Acta Histochemica · doi:10.1016/j.acthis.2011.09.002 · Cited by 70 · see citing works
Arginase 2 promotes neurovascular degeneration during ischemia/reperfusion injury
Shosha, E., Xu, Z., Yokota, H., SAUL, A. B., Rojas, M., Caldwell, R. W., Caldwell, R. B., & Narayanan, S. P. (2016) · Cell Death and Disease · doi:10.1038/cddis.2016.295 · Cited by 68 · see citing works
Assar, M. E., Angulo, J., Santos‐Ruiz, M., de Adana, J. C. R., Martínez, M. L. P., Sánchez‐Ferrer, A., Hernández, A., & Rodríguez‐Mañas, L. (2016) · The Journal of Physiology · doi:10.1113/jp271836 · Cited by 69 · see citing works
Pulmonary hypertension in thalassemia
Morris, C. R., & Vichinsky, E. P. (2010) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2010.05580.x · Cited by 67 · see citing works
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 I is a cytosolic enzyme expressed primarily in the liver but also in vascular smooth muscle, endothelial cells and the myocardium [12,13].”
BackgroundKövamees, O., Shemyakin, A. S., Checa, A., Wheelock, C. E., Lundberg, J. O., Östenson, C., & Pernow, J. (2016) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2016-2007 · Cited by 70 · see citing works
Cziráki, A., Lenkey, Z., Sulyok, E., Szokodi, I., & Koller, Á. (2020) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.569914 · Cited by 68 · see citing works
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
“Both isoforms of arginase are expressed in the cardiovascular system [15].”
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
“The American Journal of Pathology, Vol. 175, No. 2, August 2009 Copyright © American Society for Investigative Pathology DOI: 10.2353/ajpath.2009.081115 891 vascular endothelial cells, smooth muscle cells, and macrophages.21–23 Given that L-arginine is also an indispensible substrate for nitric oxide synthase (NOS) in…”
BackgroundInfluentialQuarta, A., Berneman, Z. N., & Ponsaerts, P. (2020) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2020.03.023 · Cited by 67 · see citing works
Sabe, S. A., Feng, J., Sellke, F. W., & Abid, M. R. (2022) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00603.2021 · Cited by 68 · see citing works
Bizjak, D. A., Brinkmann, C. K., Bloch, W., & Grau, M. (2015) · PLoS ONE · doi:10.1371/journal.pone.0125206 · Cited by 67 · see citing works
“Different cardiovascular disease states are described which exhibit decreased NO availability and increased arginase activity such as hypertension and diabetes [47,79–81].”
BackgroundGinnan, R. G., Guikema, B. J., Halligan, K. E., Singer, H. A., & Jourd’heuil, D. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.12.025 · Cited by 65 · see citing works
Ascorbic acid or l -arginine improves cutaneous microvascular function in chronic kidney disease
DuPont, J. J., Farquhar, W. B., Townsend, R. R., & Edwards, D. G. (2011) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00419.2011 · Cited by 65 · see citing works
“The two known isoforms of arginase (arginase I and arginase II) exist in the vasculature and have been implicated in endothelial dysfunction (9).”
BackgroundArginase 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
“Previous studies in our lab and others indicate that diabetes elevates vascular Arg activity, which contributes to endothelial dysfunction [11,12,13].”
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
Heung, L. J., & Hohl, T. M. (2019) · PLoS Pathogens · doi:10.1371/journal.ppat.1007627 · Cited by 62 · see citing works
Hanff, E., Ruben, S., Kreuzer, M., Bollenbach, A., Kayacelebi, A. A., Das, A. M., von Versen‐Höynck, F., von Kaisenberg, C., Haffner, D., Ückert, S., et al. (2019) · Amino Acids · doi:10.1007/s00726-018-02688-w · Cited by 63 · see citing works
The ageing endothelium, cardiovascular risk and disease in man
Versari, D., Daghini, E., Virdis, A., Ghiadoni, L., & Taddei, S. (2008) · Experimental Physiology · doi:10.1113/expphysiol.2008.043356 · Cited by 62 · 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
“…to be involved in the decreased production of NO observed in different pathologies associated with low- or high-grade inflammation (Lee et al., 2003; Demougeot et al., 2005; Topal et al., 2006; Durante et al., 2007; Khallou-Laschet et al., 2010; Lewis et al., 2010; Benson et al., 2011).”
BackgroundElnaggar, M. A., Seo, S. H., Gobaa, S., Lim, K. S., Bae, I., Jeong, M. H., Han, D. K., & Joung, Y. K. (2016) · Small · doi:10.1002/smll.201600337 · Cited by 64 · see citing works
Mechanisms of sepsis-induced acute liver injury: a comprehensive review
Guo, Y., Guo, W., Chen, H., Sun, J., & Yin, Y. (2025) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2025.1504223 · Cited by 73 · see citing works
“In studies related to liver diseases, ARG1 can regulate nitric oxide levels and vascular function (Durante et al., 2007), modulate immune responses, and promote tissue repair (Wynn and Ramalingam, 2012).”
Prieto, C. P., Krause, B. J., Quezada, C., Martín, R. S., Sobrevía, L., & Casanello, P. C. (2011) · Placenta · doi:10.1016/j.placenta.2011.09.003 · Cited by 60 · see citing works
“Despite that arginase-2 has been classically described as a mitochondrial enzyme [9,11], several studies have shown the presence of a functional arginase-2 outside themitochondria [16,20,33,34].”
BackgroundMacrophage heterogeneity and energy metabolism
Verdeguer, F., & Aouadi, M. (2017) · Experimental Cell Research · doi:10.1016/j.yexcr.2017.03.043 · Cited by 59 · see citing works
Kövamees, O., Shemyakin, A., & Pernow, J. (2014) · PLoS ONE · doi:10.1371/journal.pone.0103260 · Cited by 57 · see citing works
“Endothelium-dependent vasodilatation was assessed by flow-mediated dilatation (FMD) of the radial artery before and after 20 min ischemia-reperfusion during intra-arterial infusion of the arginase inhibitor (Nv-hydroxy-norL-arginine, 0.1 mg/min) or saline.”
BackgroundInfluential
- Authors
- Durante, W., Johnson, F. K., & Johnson, R. A.
- Affiliations
- University of Missouri (US)
- Tulane University (US)
- Corresponding author
- Durante, William
- Venue
- Clinical and Experimental Pharmacology and Physiology
- Publisher
- Wiley
- Published
- 2007-04-26
- Volume
- 34
- Issue
- 9
- Pages
- 906-911
- ISSN
- 0305-1870 (ISSN-L)
- 1440-1681
- PMC
- PMC1955221
- OpenAlex
- W2125031388
- Cited by
- 577
- References
- 75
- Citations by year
- 2026: 25 · 2025: 29 · 2024: 21 · 2023: 27 · 2022: 32 · 2021: 45 · 2020: 33 · 2019: 21 · 2018: 25 · 2017: 23 · 2016: 33 · 2015: 25 · 2014: 45 · 2013: 40 · 2012: 29
- FWCI
- 2.88
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Clinical and Experimental Pharmacology and Physiology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Heart, Lung, and Blood Institute (R01HL074966, R01HL076187, R01HL059976)
- National Center for Research Resources (P20RR017659)
- Topics
- Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
- 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
- Keywords
- arginase, nitric oxide production, nitric oxide synthase, arginine metabolism, urea cycle, endothelial dysfunction, vascular disease, asymmetric dimethylarginine, inducible nitric oxide synthase, superoxide, peroxynitrite, polyamines, proline, smooth muscle cell proliferation, neointima formation, hypertension, ischaemia-reperfusion, diabetes mellitus, aging
- MeSH terms
- Animals, Arginase, Arginine, Cardiovascular Diseases, Collagen, Endothelium, Vascular, Homeostasis, Humans, Muscle, Smooth, Vascular, Nitric Oxide, Urea, Reactive Oxygen Species, Cell Proliferation, Nitric Oxide Synthase Type III
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review