Arginase inhibition mediates cardioprotection during ischaemia–reperfusion

Arginine metabolism: nitric oxide and beyond

WU, G., & MORRIS, S. M. (1998) · Biochemical Journal · doi:10.1042/bj3360001 · Cited by 2,811

The nitrate-nitrite-nitric oxide pathway in physiology and therapeutics

Lundberg, J. O., Weitzberg, E., & Gladwin, M. T. (2008) · Nature Reviews Drug Discovery · doi:10.1038/nrd2466 · Cited by 2,739

High performance liquid chromatographic determination of subpicomole amounts of amino acids by precolumn fluorescence derivatization with o-phthaldialdehyde

Lindroth, P., & Mopper, K. (1979) · Analytical Chemistry · doi:10.1021/ac50047a019 · Cited by 1,838

Cytoprotective effects of nitrite during in vivo ischemia-reperfusion of the heart and liver

Duranski, M. R., Greer, J. J. M., Dejam, A., Jaganmohan, S., Hogg, N., Langston, W., Patel, R. P., Yet, S.-F., Wang, X., Kevil, C. G., et al. (2005) · Journal of Clinical Investigation · doi:10.1172/jci22493 · Cited by 674

The emerging biology of the nitrite anion

Gladwin, M. T., Schechter, A. N., Kim-Shapiro, D. B., Patel, R. P., Hogg, N., Shiva, S., Cannon, R. O., Kelm, M., Wink, D. A., Espey, M. G., et al. (2005) · Nature Chemical Biology · doi:10.1038/nchembio1105-308 · Cited by 609

The increase in plasma nitrite after a dietary nitrate load is markedly attenuated by an antibacterial mouthwash

Govoni, M., Jansson, E. Å., Weitzberg, E., & Lundberg, J. O. (2008) · Nitric Oxide · doi:10.1016/j.niox.2008.08.003 · Cited by 602

ARGINASE: A CRITICAL REGULATOR OF NITRIC OXIDE SYNTHESIS AND VASCULAR FUNCTION

Durante, W., Johnson, F. K., & Johnson, R. A. (2007) · Clinical and Experimental Pharmacology and Physiology · doi:10.1111/j.1440-1681.2007.04638.x · Cited by 577

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

Adiponectin Cardioprotection After Myocardial Ischemia/Reperfusion Involves the Reduction of Oxidative/Nitrative Stress

Tao, L., Gao, E., Jiao, X., Yuan, Y., Li, S., Christopher, T. A., Lopez, B. L., Koch, W. J., Chan, L., Goldstein, B. J., et al. (2007) · Circulation · doi:10.1161/circulationaha.106.666941 · Cited by 452

The ubiquitous role of nitric oxide in cardioprotection

Jones, S. P., & Bolli, R. (2006) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2005.09.011 · Cited by 434

Strategies to increase nitric oxide signalling in cardiovascular disease

Lundberg, J. O., Gladwin, M. T., & Weitzberg, E. (2015) · Nature Reviews Drug Discovery · doi:10.1038/nrd4623 · Cited by 576

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

Roles of dietary inorganic nitrate in cardiovascular health and disease

Lundberg, J. O., Carlström, M., Larsen, F. J., & Weitzberg, E. (2011) · Cardiovascular Research · doi:10.1093/cvr/cvq325 · Cited by 355

Arginase: an old enzyme with new tricks

Caldwell, R. B., Toque, H. A., Narayanan, S. P., & Caldwell, R. W. (2015) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2015.03.006 · Cited by 358

Arginase as a potential target in the treatment of cardiovascular disease: reversal of arginine steal?

Pernow, J., & Jung, C. (2013) · Cardiovascular Research · doi:10.1093/cvr/cvt036 · Cited by 318

Arginine de novo and nitric oxide production in disease states

Luiking, Y. C., Have, G. A. M. T., Wolfe, R. R., & Deutz, N. E. P. (2012) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00284.2012 · Cited by 250

Biology of nitrogen oxides in the gastrointestinal tract

Lundberg, J. O., & Weitzberg, E. (2013) · Gut · doi:10.1136/gutjnl-2011-301649 · Cited by 200

Nitric Oxide: A Guardian for Vascular Grafts?

de Mel, A., Murad, F., & Seifalian, A. M. (2011) · Chemical Reviews · doi:10.1021/cr200008n · Cited by 190

Arginase Inhibition Improves Endothelial Function in Patients With Coronary Artery Disease and Type 2 Diabetes Mellitus

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

Polyamine metabolism in Leishmania: from arginine to trypanothione

Colotti, G., & Ilari, A. (2010) · Amino Acids · doi:10.1007/s00726-010-0630-3 · Cited by 166

Nitric Oxide Synthases in Heart Failure

Carnicer, R., Crabtree, M. J., Sivakumaran, V., Casadei, B., & Kass, D. A. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4824 · Cited by 170

Arginase regulates red blood cell nitric oxide synthase and export of cardioprotective nitric oxide bioactivity

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

Arginase Inhibitors: A Rational Approach Over One Century

Pudlo, M., Demougeot, C., & Girard, C. (2016) · Medicinal Research Reviews · doi:10.1002/med.21419 · Cited by 151

Arginase as a Potential Biomarker of Disease Progression: A Molecular Imaging Perspective

Clemente, G. S., van Waarde, A., Antunes, I. F., Dömling, A. S. S., & Elsinga, P. H. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21155291 · Cited by 140

Cross-talk Between Nitrate-Nitrite-NO and NO Synthase Pathways in Control of Vascular NO Homeostasis

Carlström, M., Liu, M., Yang, T., Zollbrecht, C., Huang, L., Peleli, M., Borniquel, S., Kishikawa, H., Hezel, M., Persson, A. E. G., et al. (2015) · Antioxidants & Redox Signaling · doi:10.1089/ars.2013.5481 · Cited by 130

The metabolic advantage of tumor cells

Israël, M., & Schwartz, L. H. (2011) · Molecular Cancer · doi:10.1186/1476-4598-10-70 · Cited by 130

Circulating endothelial and platelet derived microparticles reflect the size of myocardium at risk in patients with ST-elevation myocardial infarction

Jung, C., Sörensson, P., Saleh, N., Arheden, H., Rydén, L., & Pernow, J. (2011) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2011.12.025 · Cited by 114

Inorganic nitrite therapy: historical perspective and future directions

Kevil, C. G., Kolluru, G. K., Pattillo, C. B., & Giordano, T. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.04.042 · Cited by 113

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 118

Neutrophil degranulation and myocardial infarction

Zhang, N., Aiyasiding, X., Li, W., Liao, H.-H., & Tang, Q. (2022) · Cell Communication and Signaling · doi:10.1186/s12964-022-00824-4 · Cited by 115

Obesity-induced vascular dysfunction and arterial stiffening requires endothelial cell arginase 1

Bhatta, A., Yao, L., Xu, Z., Toque, H. A., Chen, J., Atawia, R. T., Fouda, A. Y., Bagi, Z. A., Lucas, R., Caldwell, R. B., et al. (2017) · Cardiovascular Research · doi:10.1093/cvr/cvx164 · Cited by 108

Nitric Oxide Signaling and Regulation in the Cardiovascular System: Recent Advances

Carlström, M., Weitzberg, E., & Lundberg, J. O. (2024) · Pharmacological Reviews · doi:10.1124/pharmrev.124.001060 · Cited by 103

OxLDL Triggers Retrograde Translocation of Arginase2 in Aortic Endothelial Cells via ROCK and Mitochondrial Processing Peptidase

Pandey, D., Bhunia, A. K., Oh, Y. J., Chang, F., Bergman, Y., Kim, J. H., Serbo, J. V., Boronina, T. N., Cole, R. N., Eyk, J. E. V., et al. (2014) · Circulation Research · doi:10.1161/circresaha.115.304262 · Cited by 94

Arginase in retinopathy

Narayanan, 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 96

Mechanisms underlying blood pressure reduction by dietary inorganic nitrate

Carlström, M., Lundberg, J. O., & Weitzberg, E. (2018) · Acta Physiologica · doi:10.1111/apha.13080 · Cited by 87

FoxO4 Promotes Early Inflammatory Response Upon Myocardial Infarction via Endothelial Arg1

Zhu, M., Goetsch, S. C., Wang, Z., Luo, R., Hill, J. A., Schneider, J. W., Morris, S. M., & Liu, Z. (2015) · Circulation Research · doi:10.1161/circresaha.115.306919 · Cited by 80

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

Increased arginase levels in heart failure represent a therapeutic target to rescue microvascular perfusion

Quitter, F., Figulla, H. R., Ferrari, M. W., Pernow, J., & Jung, C. (2013) · Clinical Hemorheology and Microcirculation · doi:10.3233/ch-2012-1617 · Cited by 70

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

Local Arginase Inhibition during Early Reperfusion Mediates Cardioprotection via Increased Nitric Oxide Production

Gonon, A. T., Jung, C., Katz, A., Westerblad, H., Shemyakin, A. S., Sjöquist, P.-O. B., Lundberg, J. O., & Pernow, J. (2012) · PLoS ONE · doi:10.1371/journal.pone.0042038 · Cited by 68

Red Blood Cells in Type 2 Diabetes Impair Cardiac Post-Ischemic Recovery Through an Arginase-Dependent Modulation of Nitric Oxide Synthase and Reactive Oxygen Species

Yang, J., Zheng, X., Mahdi, A., Zhou, Z., Tratsiakovich, Y., Jiao, T., Kiss, A., Kövamees, O., Alvarsson, M., Catrina, S., et al. (2018) · JACC Basic to Translational Science · doi:10.1016/j.jacbts.2018.03.006 · Cited by 66

Effect of Arginase Inhibition on Ischemia-Reperfusion Injury in Patients with Coronary Artery Disease with and without Diabetes Mellitus

Kövamees, O., Shemyakin, A., & Pernow, J. (2014) · PLoS ONE · doi:10.1371/journal.pone.0103260 · Cited by 57

Improvement in endothelial function in cardiovascular disease - Is arginase the target?

Mahdi, A., Kövamees, O., & Pernow, J. (2019) · International Journal of Cardiology · doi:10.1016/j.ijcard.2019.11.004 · Cited by 59

Identification of biomarkers for essential hypertension based on metabolomics

Deng, Y., Huang, C., Su, J., Pan, C., & Ke, C. (2020) · Nutrition Metabolism and Cardiovascular Diseases · doi:10.1016/j.numecd.2020.11.023 · Cited by 57

Caffeic acid and chlorogenic acid: Evaluation of antioxidant effect and inhibition of key enzymes linked with hypertension

Agunloye, O. M., & Oboh, G. (2018) · Journal of Food Biochemistry · doi:10.1111/jfbc.12541 · Cited by 53

Nitric Oxide Synthetic Pathway in Red Blood Cells Is Impaired in Coronary Artery Disease

Eligini, S., Porro, B., Lualdi, A., Squellerio, I., Veglia, F., Chiorino, E., Crisci, M., Garlaschè, A., Giovannardi, M., Werba, J. P., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0066945 · Cited by 54

Therapeutic Potential of the Nitrite-Generated NO Pathway in Vascular Dysfunction

Madigan, M. C., & Zuckerbraun, B. S. (2013) · Frontiers in Immunology · doi:10.3389/fimmu.2013.00174 · Cited by 51

Beneficial effects of Oridonin on myocardial ischemia/reperfusion injury: Insight gained by metabolomic approaches

Zhang, J., Zhou, Y., Sun, Y., Yan, H., Han, W., Wang, X., Wang, K., Wei, B., & Xu, X. (2019) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2019.172587 · Cited by 48

Vagal nerve stimulation reduces infarct size via a mechanism involving the alpha‐7 nicotinic acetylcholine receptor and downregulation of cardiac and vascular arginase

Kiss, A., Tratsiakovich, Y., Mahdi, A., Yang, J., Gonon, A. T., Podesser, B. K., & Pernow, J. (2017) · Acta Physiologica · doi:10.1111/apha.12861 · Cited by 47

Arginase 2 is a mediator of ischemia–reperfusion injury in the kidney through regulation of nitrosative stress

Hara, M., Torisu, K., Tomita, K., Kawai, Y., Tsuruya, K., Nakano, T., & Kitazono, T. (2020) · Kidney International · doi:10.1016/j.kint.2020.03.032 · Cited by 44

Biochemistry, pharmacology, and in vivo function of arginases

Heuser, S. K., Li, J., Pudewell, S., LoBue, A., Li, Z., & Cortese-Krott, M. M. (2024) · Pharmacological Reviews · doi:10.1124/pharmrev.124.001271 · Cited by 47

Modulating the NO generating system from a medicinal chemistry perspective: Current trends and therapeutic options in cardiovascular disease

Schade, D., Kotthaus, J., & Clement, B. (2010) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2010.02.005 · Cited by 40

Systemic Arginine Depletion After a Murine Model of Surgery or Trauma

Pribis, J. P., Zhu, X., Yoram Vodovotz, B., & Ochoa, J. B. (2011) · Journal of Parenteral and Enteral Nutrition · doi:10.1177/0148607111414579 · Cited by 38

Arginase inhibition improves coronary microvascular function and reduces infarct size following ischaemia–reperfusion in a rat model

Grönros, J., Kiss, A., Palmér, M., Jung, C., Berkowitz, D. E., & Pernow, J. (2013) · Acta Physiologica · doi:10.1111/apha.12097 · Cited by 37

Pharmacokinetics and Pharmacodynamics of Promising Arginase Inhibitors

Abdelkawy, K. S., Lack, K., & Elbarbry, F. (2016) · European Journal of Drug Metabolism and Pharmacokinetics · doi:10.1007/s13318-016-0381-y · Cited by 40

Attenuated cutaneous microvascular function in healthy young African Americans: Role of intradermal l -arginine supplementation

Kim, K., Hurr, C., Patik, J. C., & Brothers, R. M. (2018) · Microvascular Research · doi:10.1016/j.mvr.2018.02.001 · Cited by 37

Targeting Arginine in COVID-19-Induced Immunopathology and Vasculopathy

Durante, W. (2022) · Metabolites · doi:10.3390/metabo12030240 · Cited by 36

Amino acids in human nutrition and health

D’Mello, J. P. F. (2011) · CABI eBooks · doi:10.1079/9781845937980.0000 · Cited by 36

Angiotensin II-Induced Arterial Thickening, Fibrosis and Stiffening Involves Elevated Arginase Function

Bhatta, A., Yao, L., Toque, H. A., Shatanawi, A., Xu, Z., Caldwell, R. B., & Caldwell, R. W. (2015) · PLoS ONE · doi:10.1371/journal.pone.0121727 · Cited by 33

Influence of long-term treatment with glyceryl trinitrate on remote ischemic conditioning

Hauerslev, M., Mørk, S. R., Pryds, K., Contractor, H., Hansen, J., Jespersen, N. R., Johnsen, J., Heusch, G., Kleinbongard, P., Kharbanda, R. K., et al. (2018) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00114.2018 · Cited by 33

Arginase inhibition restores endothelial function in diet-induced obesity

Chung, J. H., Moon, J., Lee, Y. S., Chung, H.-K., Lee, S.-M., & Shin, M. (2014) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2014.07.083 · Cited by 31

The shifted balance of arginine metabolites in acute myocardial infarction patients and its clinical relevance

Mołek, P., Żmudzki, P., Włodarczyk, A., Nessler, J. M., & Zalewski, J. (2021) · Scientific Reports · doi:10.1038/s41598-020-80230-3 · Cited by 29

Arginase inhibition reduces infarct size via nitric oxide, protein kinase C epsilon and mitochondrial ATP-dependent K+ channels

Tratsiakovich, Y., Gonon, A. T., Krook, A., Yang, J., Shemyakin, A. S., Sjöquist, P.-O. B., & Pernow, J. (2013) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2013.04.044 · Cited by 29

Arginase as a target for treatment of myocardial ischemia-reperfusion injury

Tratsiakovich, Y., Yang, J., Gonon, A. T., Sjöquist, P.-O. B., & Pernow, J. (2013) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2013.10.040 · Cited by 29

Arginase inhibition enhances angiogenesis in endothelial cells exposed to hypoxia

Wang, L., Bhatta, A., Toque, H. A., Rojas, M., Yao, L., Xu, Z., Patel, C., Caldwell, R. B., & Caldwell, R. W. (2014) · Microvascular Research · doi:10.1016/j.mvr.2014.11.002 · Cited by 29

Arginase activity and nitric oxide levels in patients with obstructive sleep apnea syndrome

Yüksel, M., Okur, H. K., Pelin, Z., Öğünç, A. V., & Öztürk, L. (2014) · Clinics · doi:10.6061/clinics/2014(04)05 · Cited by 28

Mechanism and consequences of the shift in cardiac arginine metabolism following ischaemia and reperfusion in rats

Cabrera-Fuentes, H. A., Steinert, I., Preissner, K., Bencsik, P., Sárközy, M., Csonka, C., Ferdinandy, P., Schulz, R., Schlüter, K., Schreckenberg, R., et al. (2014) · Thrombosis and Haemostasis · doi:10.1160/th14-05-0477 · Cited by 28

Arginase induction and activation during ischemia and reperfusion and functional consequences for the heart

Schlüter, K., Schulz, R., & Schreckenberg, R. (2015) · Frontiers in Physiology · doi:10.3389/fphys.2015.00065 · Cited by 27

Role of Erythrocytes in Nitric Oxide Metabolism and Paracrine Regulation of Endothelial Function

Gajecki, D., Gawryś, J., Szahidewicz-Krupska, E., & Doroszko, A. (2022) · Antioxidants · doi:10.3390/antiox11050943 · Cited by 27

Serum levels of arginase I are associated with left ventricular function after myocardial infarction

Bekpınar, S., Gürdöl, F., Ünlüçerçi, Y., Develi-İş, S., & Yılmaz, A. (2011) · Clinical Biochemistry · doi:10.1016/j.clinbiochem.2011.06.003 · Cited by 26

The Role of Arginase and Rho Kinase in Cardioprotection from Remote Ischemic Perconditioning in Non-Diabetic and Diabetic Rat In Vivo

Kiss, A., Tratsiakovich, Y., Gonon, A. T., Fedotovskaya, O. N., Lanner, J. T., Andersson, D. C., Yang, J., & Pernow, J. (2014) · PLoS ONE · doi:10.1371/journal.pone.0104731 · Cited by 27

S-Nitrosation of arginase 1 requires direct interaction with inducible nitric oxide synthase

Dunn, J., Gutbrod, S. R., Webb, A. K., Pak, A., Jandu, S. K., Bhunia, A. K., Berkowitz, D. E., & Santhanam, L. (2011) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-011-0841-2 · Cited by 27

The effect of prolonged dietary nitrate supplementation on atherosclerosis development

Marsch, E., Theelen, T. L., Janssen, B. J., Briedé, J. J., Haenen, G. R. M. M., Senden, J. M., van Loon, L. J. C., Poeze, M., Bierau, J., Gijbels, M. J., et al. (2015) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2015.11.031 · Cited by 27

Sildenafil Protects against Myocardial Ischemia-Reperfusion Injury Following Cardiac Arrest in a Porcine Model: Possible Role of the Renin-Angiotensin System

Wang, G., Zhang, Q., Yuan, W., Wu, J., & Li, C. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms161126010 · Cited by 26

Role of Arginase 2 in Murine Retinopathy Associated with Western Diet-Induced Obesity

Atawia, R. T., Bunch, K. L., Fouda, A. Y., Lemtalsi, T., Eldahshan, W., Xu, Z., SAUL, A. B., Elmasry, K., Al‐Shabrawey, M., Caldwell, R. B., et al. (2020) · Journal of Clinical Medicine · doi:10.3390/jcm9020317 · Cited by 26

Upregulation of arginase activity contributes to intracellular ROS production induced by high glucose in H9c2 cells.

Zhou, L., Sun, C., Liu, C., Fan, Y., Zhu, H., Wu, X., Hu, L., & Li, Q. (2015) · PubMed Central · Cited by 26

Dual modulation of nitric oxide production in the heart during ischaemia/reperfusion injury and inflammation

de Prati, A. C., Podesser, B. K., Faggian, G. G., Scarabelli, T. M., Mazzucco, A., Darra, E., Rungatscher, A., Hallström, S., & Suzuki, H. (2010) · Thrombosis and Haemostasis · doi:10.1160/th09-08-0554 · Cited by 26

Vasorelaxant effects of Crataegus pentagyna: Links with arginase inhibition and phenolic profile

Bujor, A., Miron, A., Luca, S. V., Skalicka‐Woźniak, K., Silion, M., Trifan, A., Girard, C., Demougeot, C., & Totoson, P. (2020) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2020.112559 · Cited by 25

The Arginase Pathway in Neonatal Brain Hypoxia-Ischemia

Mike, J. K., Pathipati, P., Russ, J. B., Sheldon, A., & Ferriero, D. M. (2018) · Developmental Neuroscience · doi:10.1159/000496467 · Cited by 29

Norvaline Reduces Blood Pressure and Induces Diuresis in Rats with Inherited Stress‐Induced Arterial Hypertension

Gilinsky, M. A., Polityko, Y. К., Львович, М. А., Latysheva, T. V., Samson, A. O., Polis, B., & Naumenko, S. E. (2020) · BioMed Research International · doi:10.1155/2020/4935386 · Cited by 24

Requisite roles of LOX-1, JNK, and arginase in diabetes-induced endothelial vasodilator dysfunction of porcine coronary arterioles

Hein, T. W., Xu, X., Ren, Y., Xu, W., Tsai, S., Thengchaisri, N., & Kuo, L. (2019) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2019.04.015 · Cited by 24

Enteral arginase II provides ornithine for citrulline synthesis

Marini, J. C., Keller, B., Didelija, I. C., Castillo, L., & Lee, B. (2010) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00413.2010 · Cited by 23

The Nitrate–Nitrite–Nitric Oxide Pathway in Mammals

Lundberg, J. O., Weitzberg, E., Shiva, S., & Gladwin, M. T. (2011) · Humana Press eBooks · doi:10.1007/978-1-60761-616-0_3 · Cited by 26

Modulating the Bioactivity of Nitric Oxide as a Therapeutic Strategy in Cardiac Surgery

Pisarenko, O. I., & Studneva, I. M. (2020) · Journal of Surgical Research · doi:10.1016/j.jss.2020.07.022 · Cited by 30

Arginase II Contributes to the Ca 2+ /CaMKII/eNOS Axis by Regulating Ca 2+ Concentration Between the Cytosol and Mitochondria in a p32‐Dependent Manner

Koo, B., Hwang, H. M., Yi, B., Lim, H. K., Jeon, B. H., Hoe, K., Kwon, Y., Won, M., Kim, Y., Berkowitz, D. E., et al. (2018) · Journal of the American Heart Association · doi:10.1161/jaha.118.009579 · Cited by 22

Hypobaric hypoxia induced arginase expression limits nitric oxide availability and signaling in rodent heart

Singh, M., Padhy, G., Vats, P., Bhargava, K., & Sethy, N. K. (2014) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2014.01.015 · Cited by 22

There is no direct competition between arginase and nitric oxide synthase for the common substrate l-arginine.

Momma, T. Y., & Ottaviani, J. (2022) · Nitric oxide · doi:10.1016/j.niox.2022.09.002 · Cited by 19

Arginase inhibition augments nitric oxide production and facilitates left ventricular systolic function in doxorubicin-induced cardiomyopathy in mice

Toya, T., Hakuno, D., Shiraishi, Y., Kujiraoka, T., & Adachi, T. K. (2014) · Physiological Reports · doi:10.14814/phy2.12130 · Cited by 21

Arginase II protein regulates Parkin-dependent p32 degradation that contributes to Ca2+-dependent eNOS activation in endothelial cells

Koo, B., Won, M., Kim, Y., & Ryoo, S. (2021) · Cardiovascular Research · doi:10.1093/cvr/cvab163 · Cited by 20

Arginase induction and activation during ischemia and reperfusion and functional consequences for the heart

ter, K.-D. S. ⁄., Schulz, R., & Schreckenberg, R. (2015) · Frontiers in Physiology · doi:10.3389/fphys.2015.00054 · Cited by 20

Increased arginase levels contribute to impaired perfusion after cardiopulmonary resuscitation

Jung, C., Quitter, F., Lichtenauer, M., Fritzenwanger, M., Pfeil, A., Shemyakin, A. S., Franz, M., Figulla, H. R., Pfeifer, R., & Pernow, J. (2014) · European Journal of Clinical Investigation · doi:10.1111/eci.12330 · Cited by 20

Caffeic and chlorogenic acids modulate altered activity of key enzymes linked to hypertension in cyclosporine-induced hypertensive rats

Agunloye, O. M., Oboh, G., Bello, T. G., & Oyagbemi, A. A. (2020) · Journal of Basic and Clinical Physiology and Pharmacology · doi:10.1515/jbcpp-2019-0360 · Cited by 19

Increased Endothelial Inflammation, sTie-2 and Arginase Activity in Umbilical Cords Obtained from Gestational Diabetic Mothers

Giri, H., Chandel, S., DWARAKANATH, L. S., Sreekumar, S., & Dixit, M. (2013) · PLoS ONE · doi:10.1371/journal.pone.0084546 · Cited by 19

Nitric Oxide Synthetic Pathway in Patients with Microvascular Angina and Its Relations with Oxidative Stress

Porro, B., Eligini, S., Veglia, F., Lualdi, A., Squellerio, I., Fiorelli, S., Giovannardi, M., Chiorino, E., Cia, A. D., Crisci, M., et al. (2014) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2014/726539 · Cited by 19

Comparative pharmacokinetics of Nω-hydroxy-nor-L-arginine, an arginase inhibitor, after single-dose intravenous, intraperitoneal and intratracheal administration to brown Norway rats

Havlínová, Z., Babicová, A., Hroch, M., & Chládek, J. (2013) · Xenobiotica · doi:10.3109/00498254.2013.780672 · Cited by 19

Single- and multiple-dose pharmacokinetics of arginase inhibitor Nω-hydroxy-nor-L-arginine, and its effect on plasma amino acids concentrations in Wistar rats

Havlínová, Z., Hroch, M., Nagy, A., Šišpera, L., Holeček, M., & Chládek, J. (2014) · General Physiology and Biophysics · doi:10.4149/gpb_2013078 · Cited by 19

Up-regulation of arginase II contributes to pulmonary vascular endothelial cell dysfunction during experimental pulmonary embolism

Watts, J. A., Marchick, M. R., Gellar, M. A., & Kline, J. A. (2011) · Pulmonary Pharmacology & Therapeutics · doi:10.1016/j.pupt.2011.01.009 · Cited by 19

Cecropia pachystachya extract attenuated the renal lesion in 5/6 nephrectomized rats by reducing inflammation and renal arginase activity

Maquiaveli, C. D. C., da Silva, E. R., Rosa, L. C., Francescato, H. D. C., Júnior, J. F. L., da Silva, C. G. A., Casarini, D. E., Ronchi, F. A., & Coimbra, T. M. (2014) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2014.09.042 · Cited by 19

Cross-Talk Between Neutrophils and Macrophages Post-Myocardial Infarction: From Inflammatory Drivers to Therapeutic Targets

Ciortan, L., Macarie, R. D., Barbu, E., Naie, M. L., Mihaila, A. C., Serbanescu, M. A., & Butoi, E. D. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms262110575 · Cited by 21

Effect of traditional Chinese medicine on metabolism disturbance in ischemic heart diseases

Wang, A., Song, Q., Li, Y., Fang, H., Ma, X., Li, Y., Wei, B., & Pan, C. (2024) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2024.118143 · Cited by 21

L-Arginine Cardioplegia Reduces Oxidative Stress and Preserves Diastolic Function in Patients with Low Ejection Fraction Undergoing Coronary Artery Surgery

Andrews, D. T., Sutherland, J., Dawson, P., Royse, A. G., & Royse, C. F. (2012) · Anaesthesia and Intensive Care · doi:10.1177/0310057x1204000110 · Cited by 18

Increased levels of circulating arginase I in overweight compared to normal weight adolescents

Jung, C., Figulla, H. R., Lichtenauer, M., Franz, M., & Pernow, J. (2013) · Pediatric Diabetes · doi:10.1111/pedi.12054 · Cited by 18

A Novel Arginase Inhibitor Derived from Scutellavia indica Restored Endothelial Function in ApoE-Null Mice Fed a High-Cholesterol Diet

Hwang, H. M., Lee, J. H., Min, B. S., Jeon, B. H., Hoe, K., Kim, Y., & Ryoo, S. (2015) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.115.224592 · Cited by 17

Metabolic characterization of invaded cells of the pancreatic cancer cell line, PANC ‐1

Fujita, M., Imadome, K., & Imai, T. (2017) · Cancer Science · doi:10.1111/cas.13220 · Cited by 16

Arginase inhibition by rhaponticin increases L-arginine concentration that contributes to Ca2+-dependent eNOS activation

Koo, B., Lee, J., Jin, Y., Lim, H. K., & Ryoo, S. (2021) · BMB Reports · doi:10.5483/bmbrep.2021.54.10.053 · Cited by 15

Arginase 1 is upregulated at admission in patients with ST‐elevation myocardial infarction

Tengbom, J., Cederström, S., Verouhis, D., Böhm, F., Eriksson, P. O., Folkersen, L., Gabrielsen, A., Jernberg, T., Lundman, P., Persson, J., et al. (2021) · Journal of Internal Medicine · doi:10.1111/joim.13358 · Cited by 15

Circular RNA HMGCS1 sponges MIR4521 to aggravate type 2 diabetes-induced vascular endothelial dysfunction

Zhang, M., Du, G., Xie, L., Xu, Y., & Chen, W. (2024) · eLife · doi:10.7554/elife.97267 · Cited by 16

Myocardial protection by co-administration of l-arginine and tetrahydrobiopterin during ischemia and reperfusion

Tratsiakovich, Y., Gonon, A. T., Kiss, A., Yang, J., Böhm, F., Tornvall, P., Settergren, M., Channon, K. M., Sjöquist, P.-O. B., & Pernow, J. (2013) · International Journal of Cardiology · doi:10.1016/j.ijcard.2013.08.075 · Cited by 15

Arginase Inhibitor 2,3,5,4′-Tetrahydroxystilbene-2-O-β-D-Glucoside Activates Endothelial Nitric Oxide Synthase and Improves Vascular Function

Yi, B., Nguyen, M., Won, M., Kim, Y. H., & Ryoo, S. (2016) · Planta Medica · doi:10.1055/s-0042-111014 · Cited by 14

Role of arginase in vascular function

(18637399), C. L. (2024) · Figshare

Local Arginase Inhibition during Early Reperfusion Mediates Cardioprotection via Increased Nitric Oxide Production

Gonon, A. T., Jung, C., Katz, A., Westerblad, H., Shemyakin, A. S., Sjöquist, P.-O. B., Lundberg, J. O., & Pernow, J. (2012) · PLoS ONE · doi:10.1371/journal.pone.0042038 · Cited by 68

Arginase as a target for treatment of myocardial ischemia-reperfusion injury

Tratsiakovich, Y., Yang, J., Gonon, A. T., Sjöquist, P.-O. B., & Pernow, J. (2013) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2013.10.040 · Cited by 29

The importance of nitric oxide availability in myocardial ischemia-reperfusion injury : regulatory roles of arginase, L-arginine and tetrahydrobiopterin

Tratsiakovich, Y. (2016) · Figshare

Arginase inhibition reduces infarct size via nitric oxide, protein kinase C epsilon and mitochondrial ATP-dependent K+ channels

Tratsiakovich, Y., Gonon, A. T., Krook, A., Yang, J., Shemyakin, A. S., Sjöquist, P.-O. B., & Pernow, J. (2013) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2013.04.044 · Cited by 29