Arginase I is constitutively expressed in human granulocytes and participates in fungicidal activity

Nitric oxide and the immune response

Bogdan, C. (2001) · Nature Immunology · doi:10.1038/ni1001-907 · Cited by 3,447 · see citing works

Granules of the Human Neutrophilic Polymorphonuclear Leukocyte

Borregaard, N., & Cowland, J. B. (1997) · Blood · doi:10.1182/blood.v89.10.3503 · Cited by 1,514 · see citing works

Killing activity of neutrophils is mediated through activation of proteases by K+ flux

Reeves, E. P., Lu, H., Jacobs, H. L., Messina, C. G. M., Bolsover, S., Gabella, G., Potma, E. O., Warley, A., Roes, J., & Segal, A. W. (2002) · Nature · doi:10.1038/416291a · Cited by 1,153 · see citing works

Human cathelicidin, hCAP-18, is processed to the antimicrobial peptide LL-37 by extracellular cleavage with proteinase 3

Sørensen, O. E., Follin, P., Johnsen, A. H., Calafat, J., Tjabringa, G. S., Hiemstra, P. S., & Borregaard, N. (2001) · Blood · doi:10.1182/blood.v97.12.3951 · Cited by 894 · see citing works

Antigen-Specific Inhibition of CD8+ T Cell Response by Immature Myeloid Cells in Cancer Is Mediated by Reactive Oxygen Species

Kusmartsev, S. A., Nefedova, Y., Yoder, D., & Gabrilovich, D. I. (2004) · The Journal of Immunology · doi:10.4049/jimmunol.172.2.989 · Cited by 851 · see citing works

Differential Regulation of Nitric Oxide Synthase-2 and Arginase-1 by Type 1/Type 2 Cytokines In Vivo: Granulomatous Pathology Is Shaped by the Pattern of l -Arginine Metabolism

Hesse, M., Modolell, M., Flamme, A. C. L., Schito, M. L., Fuentes, J. M., Cheever, A. W., Pearce, E. J., & Wynn, T. A. (2001) · The Journal of Immunology · doi:10.4049/jimmunol.167.11.6533 · Cited by 706 · see citing works

Alternative Metabolic States in Murine Macrophages Reflected by the Nitric Oxide Synthase/Arginase Balance: Competitive Regulation by CD4+ T Cells Correlates with Th1/Th2 Phenotype

Munder, M., Eichmann, K., & Modolell, M. (1998) · The Journal of Immunology · doi:10.4049/jimmunol.160.11.5347 · Cited by 647 · 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

Th1/Th2-Regulated Expression of Arginase Isoforms in Murine Macrophages and Dendritic Cells

Munder, M., Eichmann, K., Morán, J. M., Centeno, F., Soler, G., & Modolell, M. (1999) · The Journal of Immunology · doi:10.4049/jimmunol.163.7.3771 · Cited by 561 · see citing works

Reciprocal regulation of the nitric oxide synthase/arginase balance in mouse bone marrow‐derived macrophages by TH 1 and TH 2 cytokines

Modolell, M., Corraliza, I. M., Link, F., Soler, G., & Eichmann, K. (1995) · European Journal of Immunology · doi:10.1002/eji.1830250436 · Cited by 554 · see citing works

IL-4-Induced Arginase 1 Suppresses Alloreactive T Cells in Tumor-Bearing Mice

Bronte, V., Serafini, P., Santo, C. D., Marigo, I., Tosello, V., Mazzoni, A., Segal, D. M., Staib, C., Löwel, M., Sutter, G., et al. (2003) · The Journal of Immunology · doi:10.4049/jimmunol.170.1.270 · Cited by 513 · see citing works

l -Arginine Consumption by Macrophages Modulates the Expression of CD3ζ Chain in T Lymphocytes

Rodrı́guez, P. C., Zea, A. H., DeSalvo, J., Culotta, K. S., Zabaleta, J., Quiceno, D. G., Ochoa, J. B., & Ochoa, A. C. (2003) · The Journal of Immunology · doi:10.4049/jimmunol.171.3.1232 · Cited by 494 · see citing works

Dissection of experimental asthma with DNA microarray analysis identifies arginase in asthma pathogenesis

Zimmermann, N., King, N. E., Laporte, J. D., Yang, M., Mishra, A., Pope, S. M., Muntel, E. E., Witte, D. P., Pegg, A. A., Foster, P. S., et al. (2003) · Journal of Clinical Investigation · doi:10.1172/jci17912 · Cited by 488 · see citing works

The respiratory burst of phagocytic cells is associated with a rise in vacuolar pH

Segal, A. W., Geisow, M. J., Garcia, R. C., Harper, A., & Miller, R. F. (1981) · Nature · doi:10.1038/290406a0 · Cited by 422 · see citing works

Natural Resistance to Intracellular Infections

Jabado, N., Jankowski, A., Dougaparsad, S., Picard, V., Grinstein, S., & Gros, P. (2000) · The Journal of Experimental Medicine · doi:10.1084/jem.192.9.1237 · Cited by 372 · see citing works

Metabolic fate of L-arginine in relation to microbiostatic capability of murine macrophages.

Granger, D. L., Hibbs, J. B., Perfect, J. R., & Durack, D. T. (1990) · Journal of Clinical Investigation · doi:10.1172/jci114422 · Cited by 347 · see citing works

Cutting Edge: Stat6-Dependent Substrate Depletion Regulates Nitric Oxide Production

Rutschman, R. L., Lang, R., Hesse, M., Ihle, J. N., Wynn, T. A., & Murray, P. J. (2001) · The Journal of Immunology · doi:10.4049/jimmunol.166.4.2173 · Cited by 324 · see citing works

The Inhibition of Arginase by Nω-Hydroxy- l -Arginine Controls the Growth of Leishmania Inside Macrophages

Iniesta, V., Gómez-Nieto, L. C., & Corraliza, I. (2001) · The Journal of Experimental Medicine · doi:10.1084/jem.193.6.777 · Cited by 267 · see citing works

Phagocytosis by neutrophils induces an amino acid deprivation response in <i>Saccharomyces cerevisiae</i> and <i>Candida albicans</i>

Rubin-Bejerano, I., Fraser, I., Grisafi, P., & Fink, G. R. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1834481100 · Cited by 223 · see citing works

A Simplified New Assay for Assessment of Fungal Cell Damage with the Tetrazolium Dye, (2,3)-bis-(2-Methoxy-4-Nitro-5-Sulphenyl)-(2H)-Tetrazolium-5-Carboxanilide (XTT)

Meshulam, T., Levitz, S. M., Christin, L., & Diamond, R. D. (1995) · The Journal of Infectious Diseases · doi:10.1093/infdis/172.4.1153 · Cited by 191 · 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 I Expression and Activity in Human Mononuclear Cells After Injury

Ochoa, J. B., Bernard, A. C., O’Brien, W. E., Griffen, M. M., Maley, M. E., Rockich, A. K., Tsuei, B. J., Boulanger, B. R., Kearney, P. A., & Morris, S. M. (2001) · Annals of Surgery · doi:10.1097/00000658-200103000-00014 · Cited by 168 · see citing works

l -Arginine Availability Modulates Local Nitric Oxide Production and Parasite Killing in Experimental Trypanosomiasis

Gobert, A. P., Daulouède, S., Lepoivre, M., Boucher, J. L., Bouteille, B., Buguet, A., Cespuglio, R., Veyret, B., & Vincendeau, P. (2000) · Infection and Immunity · doi:10.1128/iai.68.8.4653-4657.2000 · Cited by 167 · 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

The human arginases and arginase deficiency

Iyer, R. K., Jenkinson, C. P., Vockley, J. G., Kern, R. M., Grody, W. W., & Cederbaum, S. D. (1998) · Journal of Inherited Metabolic Disease · doi:10.1023/a:1005313809037 · Cited by 158 · see citing works

Involvement of SNAP-23 and syntaxin 6 in human neutrophil exocytosis

Martı́n-Martı́n, B., Nabokina, S. M., Blasi, J., Lazo, P. A., & Mollinedo, F. (2000) · Blood · doi:10.1182/blood.v96.7.2574 · Cited by 141 · see citing works

The Involvement of Tyrosine Kinases, Cyclic AMP/Protein Kinase A, and p38 Mitogen-Activated Protein Kinase in IL-13-Mediated Arginase I Induction in Macrophages: Its Implications in IL-13-Inhibited Nitric Oxide Production

Chang, C., Zoghi, B., Liao, J. C., & Kuo, L. (2000) · The Journal of Immunology · doi:10.4049/jimmunol.165.4.2134 · Cited by 109 · see citing works

Human Monocytes and Neutrophils Store Transforming Growth Factor-α in a Subpopulation of Cytoplasmic Granules

Calafat, J., Janssen, H., Ståhle‐Bäckdahl, M., Zuurbier, A. E. M., Knol, E. F., & Egesten, A. (1997) · Blood · doi:10.1182/blood.v90.3.1255.1255_1255_1266 · Cited by 109 · see citing works

Regulation of arginase isoforms I and II by IL-4 in cultured murine peritoneal macrophages

Louis, C. A., Mody, V. C., Henry, W. L., Reichner, J. S., & Albina, J. E. (1999) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.1999.276.1.r237 · Cited by 94 · see citing works

Arginase and autoimmune inflammation in the central nervous system

Xu, L., Hilliard, B. A., Carmody, R. J., Tsabary, G., Shin, H., Christianson, D. W., & Chen, Y. H. (2003) · Immunology · doi:10.1046/j.1365-2567.2003.01713.x · Cited by 85 · see citing works

Mechanistic and Metabolic Inferences from the Binding of Substrate Analogues and Products to Arginase,

Cox, J. D., Cama, E., Colleluori, D. M., Pèthe, S., Boucher, J., Mansuy, D., Ash, D. E., & Christianson, D. W. (2001) · Biochemistry · doi:10.1021/bi002318+ · Cited by 85 · see citing works

Role of Vesicle-Associated Membrane Protein-2, Through Q-Soluble N-Ethylmaleimide-Sensitive Factor Attachment Protein Receptor/R-Soluble N-Ethylmaleimide-Sensitive Factor Attachment Protein Receptor Interaction, in the Exocytosis of Specific and Tertiary Granules of Human Neutrophils

Mollinedo, F., Martı́n-Martı́n, B., Calafat, J., Nabokina, S. M., & Lazo, P. A. (2003) · The Journal of Immunology · doi:10.4049/jimmunol.170.2.1034 · Cited by 78 · see citing works

Divergent effects of GM‐CSF and TGFβ 1 on bone marrow‐ derived macrophage arginase‐1 activity, MCP‐1 expression, and matrix‐metalloproteinase‐12: a potential role during arteriogenesis

Jost, M. M., Ninci, E., Meder, B., Kempf, C., van Royen, N., Hua, J., Berger, B. J., Hoefer, I. E., Modolell, M., & Buschmann, I. R. (2003) · The FASEB Journal · doi:10.1096/fj.03-0071fje · Cited by 59 · see citing works

Differential expression of the two human arginase genes in hyperargininemia. Enzymatic, pathologic, and molecular analysis.

Grody, W. W., Argyle, C., Kern, R. M., Dizikes, G. J., Spector, E., Strickland, A. D., Klein, D., & Cederbaum, S. D. (1989) · Journal of Clinical Investigation · doi:10.1172/jci113923 · Cited by 58 · see citing works

Co-expression of inducible nitric oxide synthase and arginases in different human monocyte subsets. Apoptosis regulated by endogenous NO

Rouzaut, A., Subirá, M. L., de Miguel, C., Miguel, E. D. D., González, A., Santiago, E., & López-Moratalla, N. (1999) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/s0167-4889(99)00106-8 · Cited by 39 · see citing works

Arginase activity is modulated by IL-4 and HOArg in nephritic glomeruli and mesangial cells

Waddington, S. N., Tam, F. W. K., Cook, H. T., & Cattell, V. (1998) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.1998.274.3.f473 · Cited by 38 · see citing works

Induction of arginases I and II in cornea during herpes simplex virus infection

Mistry, S. K., Zheng, M., Rouse, B. T., & Morris, S. M. (2001) · Virus Research · doi:10.1016/s0168-1702(00)00243-4 · Cited by 33 · see citing works

Patterns of maturation in short-term culture of human acute myeloid leukaemic cells

Palù, G., Powles, R., Selby, P., Summersgill, B. M., & Alexander, P. M. (1979) · British Journal of Cancer · doi:10.1038/bjc.1979.252 · Cited by 31 · see citing works

Human Phagocytic Cell Responses toScedosporium apiospermum(Pseudallescheria boydii): Variable Susceptibility to Oxidative Injury

Gil‐Lamaignere, C., Roilides, E., Lyman, C. A., Simitsopoulou, M., Stergiopoulou, T., Maloukou, A., & Walsh, T. J. (2003) · Infection and Immunity · doi:10.1128/iai.71.11.6472-6478.2003 · Cited by 30 · see citing works

Purification of Arginases from Human‐Leukemic Lymphocytes and Granulocytes: Study of Their Physicochemical and Kinetic Properties

Reyero, C., & Dorner, F. (1975) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1975.tb02216.x · Cited by 25 · see citing works

Immunological Identity of the Two Different Molecular Mass Constltutive Subunits of Liver Arginase

Díez, A., Fuentes, J. M., Prada, F., Campo, M. L., & Soler, G. (1994) · Biological Chemistry Hoppe-Seyler · doi:10.1515/bchm3.1994.375.8.537 · Cited by 12 · see citing works

Delayed neutrophil apoptosis after total body irradiation in mice. The role of granulocyte-macrophage colony-stimulating factor in neutrophil function.

Escribano, S., Cuenllas, E., Gaitan, S., & Tejero, C. (1998) · PubMed · Cited by 5 · see citing works

Macrophages as regulators of tumour immunity and immunotherapy

DeNardo, D. G., & Ruffell, B. (2019) · Nature reviews. Immunology · doi:10.1038/s41577-019-0127-6 · Cited by 2,542 · see citing works

Regulation of immune responses by L-arginine metabolism

Bronte, V., & Zanovello, P. (2005) · Nature Reviews Immunology · doi:10.1038/nri1668 · Cited by 1,775 · see citing works

Metabolism via Arginase or Nitric Oxide Synthase: Two Competing Arginine Pathways in Macrophages

Rath, M., ller, I. M. ⁄., Kropf, P., Closs, E. I., & Munder, M. (2014) · Frontiers in Immunology · doi:10.3389/fimmu.2014.00532 · Cited by 1,271 · see citing works

Overview of General and Discriminating Markers of Differential Microglia Phenotypes

Jurga, A. M., Paleczna, M., & Kuter, K. Z. (2020) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2020.00198 · Cited by 1,000 · see citing works

Modulators of microglial activation and polarization after intracerebral haemorrhage

Lan, X., Han, X., Li, Q., Yang, Q.-W., & Wang, J. (2017) · Nature Reviews Neurology · doi:10.1038/nrneurol.2017.69 · Cited by 819 · see citing works

Arginase-Producing Myeloid Suppressor Cells in Renal Cell Carcinoma Patients: A Mechanism of Tumor Evasion

Zea, A. H., Rodrı́guez, P. C., Atkins, M. B., Hernandez, C., Signoretti, S., Zabaleta, J., McDermott, D. F., Quiceno, D. G., Youmans, A. J., O’Neill, A., et al. (2005) · Cancer Research · doi:10.1158/0008-5472.can-04-4505 · Cited by 852 · see citing works

Diversity and dialogue in immunity to helminths

Allen, J. E., & Maizels, R. M. (2011) · Nature reviews. Immunology · doi:10.1038/nri2992 · Cited by 831 · see citing works

A subset of neutrophils in human systemic inflammation inhibits T cell responses through Mac-1

Pillay, J., Kamp, V. M., van Hoffen, E., Visser, T., Tak, T., Lammers, J. J., Ulfman, L. H., Leenen, L. P. H., Pickkers, P., & Koenderman, L. (2011) · Journal of Clinical Investigation · doi:10.1172/jci57990 · Cited by 829 · see citing works

Krüppel-like factor 4 regulates macrophage polarization

Liao, X., Sharma, N., Kapadia, F., Zhou, G., Lu, Y., Hong, H., Paruchuri, K., Mahabeleshwar, G. H., Dalmas, E., Venteclef, N., et al. (2011) · Journal of Clinical Investigation · doi:10.1172/jci45444 · Cited by 778 · see citing works

Arginase I–Producing Myeloid-Derived Suppressor Cells in Renal Cell Carcinoma Are a Subpopulation of Activated Granulocytes

Rodrı́guez, P. C., Ernstoff, M. S., Hernandez, C., Atkins, M. B., Zabaleta, J., Sierra, R. A., & Ochoa, A. C. (2009) · Cancer Research · doi:10.1158/0008-5472.can-08-1921 · Cited by 774 · see citing works

Neutrophil granules: a library of innate immunity proteins

Borregaard, N., Sørensen, O. E., & Theilgaard‐Mönch, K. (2007) · Trends in Immunology · doi:10.1016/j.it.2007.06.002 · Cited by 735 · see citing works

Arginine regulation by myeloid derived suppressor cells and tolerance in cancer: mechanisms and therapeutic perspectives

Rodrı́guez, P. C., & Ochoa, A. C. (2008) · Immunological Reviews · doi:10.1111/j.1600-065x.2008.00608.x · Cited by 722 · see citing works

Arginase: an emerging key player in the mammalian immune system

Munder, M. (2009) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2009.00291.x · Cited by 701 · see citing works

Neutrophils: Between Host Defence, Immune Modulation, and Tissue Injury

Krüger, P., Saffarzadeh, M., Weber, A. N. R., Rieber, N. P., Radsak, M. P., von Bernuth, H., Benarafa, C., Roos, D., Skokowa, J., & Hartl, D. (2015) · PLoS Pathogens · doi:10.1371/journal.ppat.1004651 · Cited by 663 · see citing works

Macrophage phenotypes during tissue repair

Novak, M. L., & Koh, T. J. (2013) · Journal of Leukocyte Biology · doi:10.1189/jlb.1012512 · Cited by 658 · see citing works

Arginine Metabolism: Boundaries of Our Knowledge

Morris, S. M. (2007) · Journal of Nutrition · doi:10.1093/jn/137.6.1602s · Cited by 640 · see citing works

Arginase I in myeloid suppressor cells is induced by COX-2 in lung carcinoma

Rodrı́guez, P. C., Hernandez, C. P., Quiceno, D. G., Dubinett, S. M., Zabaleta, J., Ochoa, J. B., Gilbert, J., & Ochoa, A. C. (2005) · The Journal of Experimental Medicine · doi:10.1084/jem.20050715 · Cited by 609 · see citing works

Obstacles and opportunities for understanding macrophage polarization

Murray, P. J., & Wynn, T. A. (2011) · Journal of Leukocyte Biology · doi:10.1189/jlb.0710409 · Cited by 565 · see citing works

Wound Macrophages as Key Regulators of Repair

Brancato, S. K., & Albina, J. E. (2011) · The American Journal of Pathology · doi:10.1016/j.ajpath.2010.08.003 · Cited by 508 · see citing works

Arginase, Prostaglandins, and Myeloid-Derived Suppressor Cells in Renal Cell Carcinoma

Ochoa, A. C., Zea, A. H., Hernandez, C., & Rodrı́guez, P. C. (2007) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-06-2197 · Cited by 489 · see citing works

Inhibition of arginase by CB-1158 blocks myeloid cell-mediated immune suppression in the tumor microenvironment

Steggerda, S. M., Bennett, M. K., Chen, J., Emberley, E. D., Huang, T. C., Janes, J. R., Li, W., MacKinnon, A. L., Makkouk, A., Marguier, G. M., et al. (2017) · Journal for ImmunoTherapy of Cancer · doi:10.1186/s40425-017-0308-4 · Cited by 488 · see citing works

The phenotype of murine wound macrophages

Daley, J. M., Brancato, S. K., Thomay, A. A., Reichner, J. S., & Albina, J. E. (2009) · Journal of Leukocyte Biology · doi:10.1189/jlb.0409236 · Cited by 452 · see citing works

Myeloid Cell-Derived Arginase in Cancer Immune Response

Grzywa, T. M., Sosnowska, A., Matryba, P., Rydzyńska, Z., Jasiński, M., Nowis, D., & Gołąb, J. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.00938 · Cited by 434 · see citing works

Suppression of T-cell functions by human granulocyte arginase

Munder, M. (2006) · Blood · doi:10.1182/blood-2006-11-010389 · Cited by 417 · see citing works

Immune suppression by neutrophils and granulocytic myeloid-derived suppressor cells: similarities and differences

Pillay, J., Tak, T., Kamp, V. M., & Koenderman, L. (2013) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-013-1286-4 · Cited by 376 · see citing works

Liver ischaemia–reperfusion injury: a new understanding of the role of innate immunity

Hirao, H., Nakamura, K., & Kupiec‐Weglinski, J. W. (2021) · Nature Reviews Gastroenterology & Hepatology · doi:10.1038/s41575-021-00549-8 · Cited by 375 · see citing works

Neutrophil Degranulation, Plasticity, and Cancer Metastasis

Mollinedo, F. (2019) · Trends in Immunology · doi:10.1016/j.it.2019.01.006 · Cited by 348 · see citing works

Neutrophil phenotypes and functions in cancer: A consensus statement

Quail, D. F., Amulic, B., Aziz, M., Barnes, B. J., Eruslanov, E. B., Fridlender, Z. G., Goodridge, H. S., Granot, Z., Hidalgo, A., Huttenlocher, A., et al. (2022) · The Journal of Experimental Medicine · doi:10.1084/jem.20220011 · Cited by 336 · see citing works

A human promyelocytic-like population is responsible for the immune suppression mediated by myeloid-derived suppressor cells

Solito, S., Falisi, E., Diaz-Montero, C. M., Doni, A., Pinton, L., Rosato, A., Francescato, S., Basso, G., Zanovello, P., Onicescu, G., et al. (2011) · Blood · doi:10.1182/blood-2010-12-325753 · Cited by 337 · see citing works

OsteoMacs: Key players around bone biomaterials

Miron, R. J., & Bosshardt, D. D. (2015) · Biomaterials · doi:10.1016/j.biomaterials.2015.12.017 · Cited by 321 · see citing works

Metabolism of L-Arginine by Myeloid-Derived Suppressor Cells in Cancer: Mechanisms of T cell suppression and Therapeutic Perspectives

Raber, P. L., Ochoa, A. C., & Rodrı́guez, P. C. (2012) · Immunological Investigations · doi:10.3109/08820139.2012.680634 · Cited by 322 · see citing works

Control of immune response by amino acid metabolism

Grohmann, U., & Bronte, V. (2010) · Immunological Reviews · doi:10.1111/j.1600-065x.2010.00915.x · Cited by 311 · see citing works

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 311 · see citing works

IL4Rα+ Myeloid-Derived Suppressor Cell Expansion in Cancer Patients

Mandruzzato, S., Solito, S., Falisi, E., Francescato, S., Chiarion‐Sileni, V., D, S. M. M., Zanon, A., Rossi, C. R., Nitti, D., Bronte, V., et al. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0803831 · Cited by 302 · see citing works

Arginase-1 and Ym1 are markers for murine, but not human, alternatively activated myeloid cells

Raes, G., Van den Bergh, R., De Baetselier, P., & Ghassabeh, G. H. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.174.11.6561 · Cited by 302 · see citing works

Ammonium metabolism in humans

Adeva‐Andany, M. M., Souto, G., Blanco, N., & Donapetry, C. (2012) · Metabolism · doi:10.1016/j.metabol.2012.07.007 · Cited by 299 · see citing works

Arginase and polyamine synthesis are key factors in the regulation of experimental leishmaniasis in vivo

Kropf, P., Fuentes, J. M., Fähnrich, E., Arpa, L., Herath, S., Weber, V., Soler, G., Celada, A., Modolell, M., & Müller, I. (2005) · The FASEB Journal · doi:10.1096/fj.04-3416fje · Cited by 297 · see citing works

Metabolic regulation of hepatitis B immunopathology by myeloid-derived suppressor cells

Pallett, L. J., Gill, U. S., Quaglia, A., Sinclair, L. V., Jover‐Cobos, M., Schurich, A., Singh, K. P., Thomas, N., Das, A., Chen, A., et al. (2015) · Nature Medicine · doi:10.1038/nm.3856 · Cited by 280 · see citing works

Polymorphonuclear neutrophils and T lymphocytes: strange bedfellows or brothers in arms?

Müller, I., Munder, M., Kropf, P., & Hänsch, G. M. (2009) · Trends in Immunology · doi:10.1016/j.it.2009.07.007 · Cited by 275 · see citing works

Alternative activation is an innate response to injury that requires CD4+ T cells to be sustained during chronic infection

Loke, P., Gallagher, I., Nair, M. G., Zang, X., Brombacher, F., Mohrs, M., Allison, J. P., & Allen, J. E. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.179.6.3926 · Cited by 274 · see citing works

Differences in innate immune response between man and mouse

Zschaler, J., Schlorke, D., & Arnhold, J. (2014) · Critical Reviews in Immunology · doi:10.1615/critrevimmunol.2014011600 · Cited by 258 · see citing works

Human myeloperoxidase in innate and acquired immunity

Arnhold, J., & Flemmig, J. (2010) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2010.04.008 · Cited by 251 · see citing works

How Neutrophils Shape Adaptive Immune Responses

Leliefeld, P. H. C., Koenderman, L., & Pillay, J. (2015) · Frontiers in Immunology · doi:10.3389/fimmu.2015.00471 · Cited by 247 · see citing works

Early Expansion of Circulating Granulocytic Myeloid-derived Suppressor Cells Predicts Development of Nosocomial Infections in Patients with Sepsis

Uhel, F., Azzaoui, I., Grégoire, M., Pangault, C., Dulong, J., Tadié, J., Gacouin, A., Camus, C., Cynober, L., Fest, T., et al. (2017) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.201606-1143oc · Cited by 244 · see citing works

Phenotype, function and clinical implications of myeloid-derived suppressor cells in cancer patients

Filipazzi, P., Huber, V., & Rivoltini, L. (2011) · Cancer Immunology Immunotherapy · doi:10.1007/s00262-011-1161-9 · Cited by 244 · see citing works

Arginase-1

Yan, B. C., Gong, C., Song, J. Y., Krausz, T. N., Tretiakova, M., Hyjek, E. M., Al‐Ahmadie, H. A., Alves, V. A. F., Xiao, S., Anders, R. A., et al. (2010) · The American Journal of Surgical Pathology · doi:10.1097/pas.0b013e3181e5dffa · Cited by 229 · see citing works

Neutrophils in cancer

Treffers, L. W., Hiemstra, I. H., Kuijpers, T. W., van den Berg, T. K., & Matlung, H. L. (2016) · Immunological Reviews · doi:10.1111/imr.12444 · Cited by 204 · see citing works

IL‐8 induces exocytosis of arginase 1 by neutrophil polymorphonuclears in nonsmall cell lung cancer

Rotondo, R., Barisione, G., Mastracci, L., Grossi, F., Orengo, A. M., Costa, R., Truini, M., Fabbi, M., Ferrini, S., & Barbieri, O. (2009) · International Journal of Cancer · doi:10.1002/ijc.24448 · Cited by 198 · see citing works

Neutrophil Degranulation and Immunosuppression in Patients with GBM: Restoration of Cellular Immune Function by Targeting Arginase I

Sippel, T. R., White, J., Nag, K., Tsvankin, V., Klaassen, M., Kleinschmidt-DeMasters, B. K., & Waziri, A. E. (2011) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-11-1107 · Cited by 198 · see citing works

Characterization of polarized THP-1 macrophages and polarizing ability of LPS and food compounds

Chanput, W. P., Mes, J. J., Savelkoul, H. F. J., & Wichers, H. J. (2012) · Food & Function · doi:10.1039/c2fo30156c · Cited by 190 · see citing works

Alternative activation deprives macrophages of a coordinated defense program to Mycobacterium tuberculosis

Kahnert, A., Seiler, P. J., Stein, M., Bandermann, S., Hahnke, K., Mollenkopf, H., & Kaufmann, S. H. E. (2006) · European Journal of Immunology · doi:10.1002/eji.200535496 · Cited by 187 · see citing works

Distinct Functions of Neutrophil in Cancer and Its Regulation

Granot, Z., & Jabłońska, J. (2015) · Mediators of Inflammation · doi:10.1155/2015/701067 · Cited by 178 · see citing works

Arginase 1 is a key driver of immune suppression in pancreatic cancer

Menjivar, R. E., Nwosu, Z. C., Du, W., Donahue, K. L., Hong, H. S., Espinoza, C. E., Brown, K. L., Velez-Delgado, A., Yan, W., Lima, F., et al. (2023) · eLife · doi:10.7554/elife.80721 · Cited by 180 · see citing works

The role of efferocytosis‐fueled macrophage metabolism in the resolution of inflammation

Schilperoort, M., Ngai, D., Sukka, S. R., Avrampou, K., Shi, H., & Tabas, I. A. (2023) · Immunological Reviews · doi:10.1111/imr.13214 · Cited by 181 · see citing works

On the armament and appearances of human myeloid-derived suppressor cells

Poschke, I. C., & Kiessling, R. W. (2012) · Clinical Immunology · doi:10.1016/j.clim.2012.06.003 · Cited by 176 · see citing works

“Of Mice and Men”: Arginine Metabolism in Macrophages

Thomas, A. C., & Mattila, J. T. (2014) · Frontiers in Immunology · doi:10.3389/fimmu.2014.00479 · Cited by 175 · see citing works

Low-density granulocytes activate T cells and demonstrate a non-suppressive role in systemic lupus erythematosus

Rahman, S., Sagar, D., Hanna, R. N., Lightfoot, Y. L., Mistry, P., Smith, C. K., Manna, Z. G., Hasni, S., Siegel, R. M., Sanjuán, M. A. F., et al. (2019) · Annals of the Rheumatic Diseases · doi:10.1136/annrheumdis-2018-214620 · Cited by 170 · see citing works

Arginase activity mediates reversible T cell hyporesponsiveness in human pregnancy

Kropf, P., Baud, D., Marshall, S. E., Munder, M., Mosley, A. J., Fuentes, J. M., Bangham, C. R. M., Taylor, G. P., Herath, S., Choi, B., et al. (2007) · European Journal of Immunology · doi:10.1002/eji.200636542 · Cited by 164 · see citing works

Multifactorial Etiology of Gastric Cancer

Zabaleta, J. (2012) · Methods in molecular biology · doi:10.1007/978-1-61779-612-8_26 · Cited by 156 · see citing works

Macrophage PTEN Regulates Expression and Secretion of Arginase I Modulating Innate and Adaptive Immune Responses

Sahin, E., Haubenwallner, S., Kuttke, M., Kollmann, I., Halfmann, A., Dohnal, A. M., Chen, L., Cheng, P. P., Hoesel, B., Einwallner, E., et al. (2014) · The Journal of Immunology · doi:10.4049/jimmunol.1302167 · Cited by 155 · see citing works

Mouse versus Human Neutrophils in Cancer: A Major Knowledge Gap

Eruslanov, E. B., Singhal, S. K., & Albelda, S. Μ. (2017) · Trends in cancer · doi:10.1016/j.trecan.2016.12.006 · Cited by 148 · see citing works

Arginase 1 is expressed in myelocytes/metamyelocytes and localized in gelatinase granules of human neutrophils

Jacobsen, L. C., Theilgaard‐Mönch, K., Christensen, E., & Borregaard, N. (2006) · Blood · doi:10.1182/blood-2006-06-032599 · Cited by 147 · see citing works

Arginase and pulmonary diseases

Maarsingh, H., Pera, T., & Meurs, H. (2008) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/s00210-008-0286-7 · Cited by 145 · see citing works

Arginine Transport via Cationic Amino Acid Transporter 2 Plays a Critical Regulatory Role in Classical or Alternative Activation of Macrophages

Yeramian, A., Jaular, L. M., Serrat, N., Arpa, L., Soler, C., Bertran, J., McLeod, C., Palacı́n, M., Modolell, M., Lloberas, J., et al. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.176.10.5918 · Cited by 144 · see citing works

The defensive alliance between neutrophils and NK cells as a novel arm of innate immunity

Costantini, C., & Cassatella, M. A. (2010) · Journal of Leukocyte Biology · doi:10.1189/jlb.0510250 · Cited by 141 · see citing works

Exocytosis of azurophil and arginase 1-containing granules by activated polymorphonuclear neutrophils is required to inhibit T lymphocyte proliferation

Rotondo, R., Bertolotto, M. B., Barisione, G., Astigiano, S., Mandruzzato, S., Ottonello, L. C., Dallegri, F., Bronte, V., Ferrini, S., & Barbieri, O. (2011) · Journal of Leukocyte Biology · doi:10.1189/jlb.1109737 · Cited by 139 · see citing works

Regulation of NK Cell Function by Human Granulocyte Arginase

Oberlies, J., Watzl, C., Giese, T., Luckner, C., Kropf, P., Müller, I., Ho, A. D., & Munder, M. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0803523 · Cited by 139 · see citing works

Macrophage functions in wound healing

Kloc, M., Ghobrial, R. M., Wosik, J., Lewicka, A., Lewicki, S., & Kubiak, J. Z. (2018) · Journal of Tissue Engineering and Regenerative Medicine · doi:10.1002/term.2772 · Cited by 131 · see citing works

Attributes of alternatively activated (M2) macrophages

Shrivastava, R., & Shukla, N. (2019) · Life Sciences · doi:10.1016/j.lfs.2019.03.062 · Cited by 130 · see citing works

The roles of arginases and arginine in immunity

Canè, S., Geiger, R., & Bronte, V. (2024) · Nature reviews. Immunology · doi:10.1038/s41577-024-01098-2 · Cited by 135 · see citing works

Characterization of a Novel Population of Low-Density Granulocytes Associated with Disease Severity in HIV-1 Infection

Cloke, T., Munder, M., Taylor, G. P., Müller, I., & Kropf, P. (2012) · PLoS ONE · doi:10.1371/journal.pone.0048939 · Cited by 125 · see citing works

Activated neutrophils exert myeloid-derived suppressor cell activity damaging T cells beyond repair

Aarts, C. E. M., Hiemstra, I. H., Béguin, E. P., Hoogendijk, A. J., Bouchmal, S., van Houdt, M., Tool, A. T. J., Mul, E. P. J., Jansen, M. H., Janssen, H., et al. (2019) · Blood Advances · doi:10.1182/bloodadvances.2019031609 · Cited by 125 · see citing works

Candida albicans Chitin Increases Arginase-1 Activity in Human Macrophages, with an Impact on Macrophage Antimicrobial Functions

Wagener, J., MacCallum, D. M., Brown, G. D., & Gow, N. A. R. (2017) · mBio · doi:10.1128/mbio.01820-16 · Cited by 123 · 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

The Role of Leishmania Proteophosphoglycans in Sand Fly Transmission and Infection of the Mammalian Host

Rogers, M. E. (2012) · Frontiers in Microbiology · doi:10.3389/fmicb.2012.00223 · Cited by 122 · see citing works

Rapid Host Defense against Aspergillus fumigatus Involves Alveolar Macrophages with a Predominance of Alternatively Activated Phenotype

Bhatia, S., Fei, M., Yarlagadda, M., Qi, Z., Akira, S., Saijo, S., Iwakura, Y., van Rooijen, N., Gibson, G. A., Croix, C. M. S., et al. (2011) · PLoS ONE · doi:10.1371/journal.pone.0015943 · Cited by 119 · see citing works

Induction of human IL-10-producing neutrophils by LPS-stimulated Treg cells and IL-10

Lewkowicz, N., Mycko, M. P., Przygodzka, P., Ćwiklińska, H., Cichalewska, M., Matysiak, M., Selmaj, K. W., & Lewkowicz, P. (2015) · Mucosal Immunology · doi:10.1038/mi.2015.66 · Cited by 116 · see citing works

A role for IL‐18 in protective immunity against <i>Mycobacterium tuberculosis</i>

Schneider, B. E., Korbel, D., Hagens, K., Koch, M., Raupach, B., Enders, J., Kaufmann, S. H. E., Mittrücker, H., & Schaible, U. E. (2010) · European Journal of Immunology · doi:10.1002/eji.200939583 · Cited by 115 · see citing works

Targeting and exploitation of tumor-associated neutrophils to enhance immunotherapy and drug delivery for cancer treatment

Zhang, Y., Liu, G., Sun, M., & Lü, X. (2020) · Cancer Biology and Medicine · doi:10.20892/j.issn.2095-3941.2019.0372 · Cited by 111 · see citing works

Tumor metabolism as modulator of immune response and tumor progression

Gottfried, E., Kreutz, M. P., & Mackensen, A. (2012) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2012.02.009 · Cited by 112 · see citing works

A Method for Identification and Analysis of Non-Overlapping Myeloid Immunophenotypes in Humans

Gustafson, M. P., Lin, Y., Maas, M. L., Keulen, V. P. V., Johnston, P. B., Peikert, T., Gastineau, D. A., & Dietz, A. B. (2015) · PLoS ONE · doi:10.1371/journal.pone.0121546 · Cited by 111 · see citing works

Cofilin: a redox sensitive mediator of actin dynamics during T‐cell activation and migration

Samstag, Y., John, I., & Wabnitz, G. H. (2013) · Immunological Reviews · doi:10.1111/imr.12115 · Cited by 108 · see citing works

Arginase-1 deficiency

Sin, Y. Y., Baron, G., Schulze, A., & Funk, C. D. (2015) · Journal of Molecular Medicine · doi:10.1007/s00109-015-1354-3 · Cited by 103 · see citing works

Local Suppression of T Cell Responses by Arginase-Induced L-Arginine Depletion in Nonhealing Leishmaniasis

Modolell, M., Choi, B., Ryan, R. O., Hancock, M., Titus, R. G., Abebe, T., Hailu, A., Müller, I., Rogers, M. E., Bangham, C. R. M., et al. (2009) · PLoS neglected tropical diseases · doi:10.1371/journal.pntd.0000480 · Cited by 102 · see citing works

Reconstitution of T Cell Proliferation under Arginine Limitation: Activated Human T Cells Take Up Citrulline via L-Type Amino Acid Transporter 1 and Use It to Regenerate Arginine after Induction of Argininosuccinate Synthase Expression

Werner, A., Koschke, M., Leuchtner, N., Luckner‐Minden, C., Habermeier, A., Rupp, J., Heinrich, C., Conradi, R., Closs, E. I., & Munder, M. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.00864 · Cited by 98 · see citing works

Alternatively Activated and Immunoregulatory Monocytes in Human Filarial Infections

Babu, S., Kumaraswami, V., & Nutman, T. B. (2009) · The Journal of Infectious Diseases · doi:10.1086/599090 · Cited by 95 · see citing works

IL-35 induces N2 phenotype of neutrophils to promote tumor growth

Zou, J.-M., Qin, J., Li, Y., Wang, Y., Li, D., Shu, Y., Luo, C., Wang, S., Chi, G., Guo, F., et al. (2017) · Oncotarget · doi:10.18632/oncotarget.16819 · Cited by 95 · see citing works

Depletion of L -arginine induces autophagy as a cytoprotective response to endoplasmic reticulum stress in human T lymphocytes

García‐Navas, R., Munder, M., & Mollinedo, F. (2012) · Autophagy · doi:10.4161/auto.21315 · Cited by 91 · see citing works

Expression patterns of the immunomodulatory enzyme arginase 1 in blood, lymph nodes and tumor tissue of early-stage breast cancer patients

de Boniface, J., Mao, Y., Schmidt‐Mende, J., Kiessling, R. W., & Poschke, I. C. (2012) · OncoImmunology · doi:10.4161/onci.21678 · Cited by 91 · see citing works

Differential impact of l -arginine deprivation on the activation and effector functions of T cells and macrophages

Choi, B.-S., Martinez-Falero, I. C., Corset, C., Munder, M., Modolell, M., Müller, I., & Kropf, P. (2008) · Journal of Leukocyte Biology · doi:10.1189/jlb.0508310 · Cited by 90 · see citing works

The effect of short-chain fatty acids on M2 macrophages polarizationin vitroandin vivo

Huang, C., Du, W., Ni, Y., Lan, G., & Shi, G. (2021) · Clinical & Experimental Immunology · doi:10.1093/cei/uxab028 · Cited by 89 · see citing works

MAP Kinase Phosphatase-2 Plays a Critical Role in Response to Infection by Leishmania mexicana

Al-Mutairi, M. S., Cadalbert, L. C., McGachy, H. A., Shweash, M., Schroeder, J., Kurnik‐Łucka, M., Sloss, C. M., Bryant, C. E., Alexander, J. K., & Plevin, R. J. (2010) · PLoS Pathogens · doi:10.1371/journal.ppat.1001192 · Cited by 89 · see citing works

Metabolism in the Tumor Microenvironment

Lau, A. N., & Heiden, M. G. V. (2019) · Annual Review of Cancer Biology · doi:10.1146/annurev-cancerbio-030419-033333 · Cited by 89 · see citing works

Myeloid Derived Suppressor Cells (MDSCs) Are Increased and Exert Immunosuppressive Activity Together with Polymorphonuclear Leukocytes (PMNs) in Chronic Myeloid Leukemia Patients

Giallongo, C., Parrinello, N. L., Tibullo, D., Cava, P. L., Romano, A., Chiarenza, A., Barbagallo, I. A., Palumbo, G. A., Stagno, F., Vigneri, P. G., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0101848 · Cited by 87 · see citing works

Arginase in Parasitic Infections: Macrophage Activation, Immunosuppression, and Intracellular Signals

Stempin, C. C., Dulgerian, L. R., Garrido, V. V., & Cerbán, F. M. (2009) · BioMed Research International · doi:10.1155/2010/683485 · Cited by 86 · see citing works

Role of Arginase 1 from Myeloid Cells in Th2-Dominated Lung Inflammation

Barron, L., Smith, A. M., Kasmi, K. C. E., Qualls, J. E., Huang, X., Cheever, A. W., Borthwick, L. A., Wilson, M. S., Murray, P. J., & Wynn, T. A. (2013) · PLoS ONE · doi:10.1371/journal.pone.0061961 · Cited by 84 · see citing works

Characterization of Neutrophil Subsets in Healthy Human Pregnancies

Ssemaganda, A., Kindinger, L. M., Bergin, P. J., Nielsen, L., Mpendo, J., Ssetaala, A., Kiwanuka, N., Munder, M., Teoh, T. G., Kropf, P., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0085696 · Cited by 82 · see citing works

Induced arginine transport via cationic amino acid transporter‐1 is necessary for human T‐cell proliferation

Werner, A., Amann, E., Schnitzius, V., Habermeier, A., Luckner‐Minden, C., Leuchtner, N., Rupp, J., Closs, E. I., & Munder, M. (2015) · European Journal of Immunology · doi:10.1002/eji.201546047 · Cited by 82 · see citing works

Transcriptional regulation of macrophage arginase 1 expression and its role in atherosclerosis

Pourcet, B., & Pineda‐Torra, I. (2013) · Trends in Cardiovascular Medicine · doi:10.1016/j.tcm.2012.10.003 · Cited by 82 · see citing works

Arginine metabolism in myeloid cells in health and disease

Karadima, E., Chavakis, T., & Alexaki, V. I. (2025) · Seminars in Immunopathology · doi:10.1007/s00281-025-01038-9 · Cited by 82 · see citing works

From bloodjournal.hematologylibrary.org at PENN STATE UNIVERSITY on February 23, 2013. For personal use only.

Munder, M., Mollinedo, F., Calafat, J., Canchado, J., Gil-lamaignere, C., Fuentes, M., Luckner, C., Doschko, G., Soler, G., Eichmann, K., et al. (2004)

Untersuchungen zur Regulation des Enzyms Arginase in humanen Granulozyten

Doschko, G. U. M. (2004)

Human eosinophil granulocytes do not express the enzyme arginase

Luckner‐Minden, C., Fischer, I., Langhans, C., Schiller, M. R., Kropf, P., Müller, I., Hohlfeld, J. M., Ho, A. D., & Munder, M. (2010) · Journal of Leukocyte Biology · doi:10.1189/jlb.1109741 · Cited by 15 · see citing works

Arginase 1 is expressed in myelocytes/metamyelocytes and localized in gelatinase granules of human neutrophils

Jacobsen, L. C., Theilgaard‐Mönch, K., Christensen, E., & Borregaard, N. (2006) · Blood · doi:10.1182/blood-2006-06-032599 · Cited by 147 · see citing works

Arginase: an emerging key player in the mammalian immune system

Munder, M. (2009) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2009.00291.x · Cited by 701 · see citing works