<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE article PUBLIC "-//NLM//DTD JATS (Z39.96) Journal Publishing DTD v1.3 20210610//EN" "JATS-journalpublishing1-3.dtd">
<article article-type="research-article" dtd-version="1.3" xmlns:mml="http://www.w3.org/1998/Math/MathML" xmlns:xlink="http://www.w3.org/1999/xlink" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xml:lang="ru"><front><journal-meta><journal-id journal-id-type="publisher-id">mimmun</journal-id><journal-title-group><journal-title xml:lang="ru">Медицинская иммунология</journal-title><trans-title-group xml:lang="en"><trans-title>Medical Immunology (Russia)</trans-title></trans-title-group></journal-title-group><issn pub-type="ppub">1563-0625</issn><issn pub-type="epub">2313-741X</issn><publisher><publisher-name>SPb RAACI</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="doi">10.15789/1563-0625-2015-4-303-318</article-id><article-id custom-type="elpub" pub-id-type="custom">mimmun-922</article-id><article-categories><subj-group subj-group-type="heading"><subject>Research Article</subject></subj-group><subj-group subj-group-type="section-heading" xml:lang="ru"><subject>ОБЗОРЫ</subject></subj-group><subj-group subj-group-type="section-heading" xml:lang="en"><subject>REVIEWS</subject></subj-group></article-categories><title-group><article-title>ИММУНОСУПРЕССОРНЫЕ ЭФФЕКТЫ АРГИНИНДЕИМИНАЗЫ STREPTOCOCCUS PYOGENES</article-title><trans-title-group xml:lang="en"><trans-title>IMMUNOSUPPRESSIVE EFFECTS OF ARGININE DEIMINASE FROM STREPTOCOCCUS PYOGENES</trans-title></trans-title-group></title-group><contrib-group><contrib contrib-type="author" corresp="yes"><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Старикова</surname><given-names>Э. А.</given-names></name><name name-style="western" xml:lang="en"><surname>Starikova</surname><given-names>E. A.</given-names></name></name-alternatives><bio xml:lang="ru"/><bio xml:lang="en"/><email xlink:type="simple">Starickova@yandex.ru</email><xref ref-type="aff" rid="aff-1"/></contrib><contrib contrib-type="author" corresp="yes"><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Соколов</surname><given-names>А. В.</given-names></name><name name-style="western" xml:lang="en"><surname>Sokolov</surname><given-names>A. V.</given-names></name></name-alternatives><bio xml:lang="ru"/><bio xml:lang="en"/><xref ref-type="aff" rid="aff-1"/></contrib><contrib contrib-type="author" corresp="yes"><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Бурова</surname><given-names>Л. А.</given-names></name><name name-style="western" xml:lang="en"><surname>Burova</surname><given-names>L. A.</given-names></name></name-alternatives><bio xml:lang="ru"/><bio xml:lang="en"/><xref ref-type="aff" rid="aff-1"/></contrib><contrib contrib-type="author" corresp="yes"><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Фрейдлин</surname><given-names>И. С.</given-names></name><name name-style="western" xml:lang="en"><surname>Freidlin</surname><given-names>I. S.</given-names></name></name-alternatives><bio xml:lang="ru"/><bio xml:lang="en"/><xref ref-type="aff" rid="aff-1"/></contrib></contrib-group><aff-alternatives id="aff-1"><aff xml:lang="ru"><institution>ФГБНУ «Институт экспериментальной медицины», Санкт-Петербург, Россия</institution><country>Россия</country></aff><aff xml:lang="en"><institution>Research Institute of Experimental Medicine, North-Western Branch, Russian Academy of Sciences, St. Petersburg, Russian Federation</institution><country>Russian Federation</country></aff></aff-alternatives><pub-date pub-type="collection"><year>2015</year></pub-date><pub-date pub-type="epub"><day>07</day><month>10</month><year>2015</year></pub-date><volume>17</volume><issue>4</issue><fpage>303</fpage><lpage>318</lpage><permissions><copyright-statement>Copyright &amp;#x00A9; Старикова Э.А., Соколов А.В., Бурова Л.А., Фрейдлин И.С., 2015</copyright-statement><copyright-year>2015</copyright-year><copyright-holder xml:lang="ru">Старикова Э.А., Соколов А.В., Бурова Л.А., Фрейдлин И.С.</copyright-holder><copyright-holder xml:lang="en">Starikova E.A., Sokolov A.V., Burova L.A., Freidlin I.S.</copyright-holder><license xml:lang="ru" license-type="creative-commons-attribution" xlink:href="https://creativecommons.org/licenses/by/4.0/" xlink:type="simple"><license-p>Данная работа распространяется под лицензией Creative Commons Attribution 4.0.</license-p></license><license xml:lang="en" license-type="creative-commons-attribution" xlink:href="https://creativecommons.org/licenses/by/4.0/" xlink:type="simple"><license-p>This work is licensed under a Creative Commons Attribution 4.0 License.</license-p></license></permissions><self-uri xlink:href="https://www.mimmun.ru/mimmun/article/view/922">https://www.mimmun.ru/mimmun/article/view/922</self-uri><abstract><p>Многие патогенные микроорганизмы используют метаболические пути аргинина для успешной диссеминации. Бактериальная аргининдеиминаза гидролизует аргинин с образованием одной молекулы аммиака и двух молекул АТФ. Активность фермента способствует улучшению выживаемости патогенных бактерий в условиях пониженной кислотности в очаге инфекции или в фаголизосомах, в анаэробных условиях, а также приводит к дефициту аргинина. Метаболизм аргинина играет важную роль в регуляции функций клеток иммунной системы. У млекопитающих аргинин является субстратом ферментов NOS и аргиназы. Деплеция аргинина является одним из механимов иммуносупресии. В обзоре проводится анализ данных литературы о влиянии стрептококковой аргинидеиминазы на метаболизм аргинина эукариотических клеток, а также обсуждается иммуносупрессорное действие фермента.</p></abstract><trans-abstract xml:lang="en"/><kwd-group xml:lang="ru"><kwd>аргининдеиминаза</kwd><kwd>Streptococcus pyogenes</kwd><kwd>иммуносупрессия</kwd></kwd-group><kwd-group xml:lang="en"><kwd>arginine deiminase</kwd><kwd>Streptococcus pyogenes</kwd><kwd>immunosuppression</kwd></kwd-group></article-meta></front><back><ref-list><title>References</title><ref id="cit1"><label>1</label><citation-alternatives><mixed-citation xml:lang="ru">Amber I.J., Hibbs J.B.Jr., Parker C.J., Johnson B.B., Taintor R.R., Vavrin Z. Activated macrophage conditioned medium: identiﬁcation of the soluble factors inducing cytotoxicity and the L-arginine dependent eﬀector mechanism. J. Leukoc. Biol., 1991, Vol. 49, no. 6, pp. 610-620.</mixed-citation><mixed-citation xml:lang="en">Amber I.J., Hibbs J.B.Jr., Parker C.J., Johnson B.B., Taintor R.R., Vavrin Z. Activated macrophage conditioned medium: identiﬁcation of the soluble factors inducing cytotoxicity and the L-arginine dependent eﬀector mechanism. J. Leukoc. Biol., 1991, Vol. 49, no. 6, pp. 610-620.</mixed-citation></citation-alternatives></ref><ref id="cit2"><label>2</label><citation-alternatives><mixed-citation xml:lang="ru">Aulak K.S., Miyagi M., Yan L., West K.A., Massillon D., Crabb J.W., Stuehr D.J. Proteomic method identiﬁes proteins nitrated in vivo during inﬂammatory challenge. Proc. Natl Acad. Sci. USA, 2001, Vol. 98, pp. 12056-12061.</mixed-citation><mixed-citation xml:lang="en">Aulak K.S., Miyagi M., Yan L., West K.A., Massillon D., Crabb J.W., Stuehr D.J. Proteomic method identiﬁes proteins nitrated in vivo during inﬂammatory challenge. Proc. Natl Acad. Sci. USA, 2001, Vol. 98, pp. 12056-12061.</mixed-citation></citation-alternatives></ref><ref id="cit3"><label>3</label><citation-alternatives><mixed-citation xml:lang="ru">Bahri S., Zerrouk N., Aussel C., Moinard C., Crenn P., Curis E., Chaumeil J.C., Cynober L., Sfar S. Citrulline: from metabolism to therapeutic use. Nutrition, 2013, Vol. 29, no. 3, pp. 479-484.</mixed-citation><mixed-citation xml:lang="en">Bahri S., Zerrouk N., Aussel C., Moinard C., Crenn P., Curis E., Chaumeil J.C., Cynober L., Sfar S. Citrulline: from metabolism to therapeutic use. Nutrition, 2013, Vol. 29, no. 3, pp. 479-484.</mixed-citation></citation-alternatives></ref><ref id="cit4"><label>4</label><citation-alternatives><mixed-citation xml:lang="ru">Baydoun A.R., Bogle R.G., Pearson J.D., Mann G.E. Discrimination between citrulline and arginine transport in activated murine macrophages: inefficient synthesis of NO from recycling citrulline to arginine. Br. J. Pharmacol., 1994, Vol. 112, pp. 487-492.</mixed-citation><mixed-citation xml:lang="en">Baydoun A.R., Bogle R.G., Pearson J.D., Mann G.E. Discrimination between citrulline and arginine transport in activated murine macrophages: inefficient synthesis of NO from recycling citrulline to arginine. Br. J. Pharmacol., 1994, Vol. 112, pp. 487-492.</mixed-citation></citation-alternatives></ref><ref id="cit5"><label>5</label><citation-alternatives><mixed-citation xml:lang="ru">Baylis C. Nitric oxide deﬁciency in chronic kidney disease. Am. J. Physiol. Renal. Physiol., 2008, Vol. 294, Vol. 1, pp. 1-9.</mixed-citation><mixed-citation xml:lang="en">Baylis C. Nitric oxide deﬁciency in chronic kidney disease. Am. J. Physiol. Renal. Physiol., 2008, Vol. 294, Vol. 1, pp. 1-9.</mixed-citation></citation-alternatives></ref><ref id="cit6"><label>6</label><citation-alternatives><mixed-citation xml:lang="ru">Beloussow K., Wang L., Wu J., Ann D., Shen W.C. Recombinant arginine deiminase as a potential anti-angiogenic agent. Cancer. Lett., 2002, Vol. 183, Vol. 2, pp. 155-162.</mixed-citation><mixed-citation xml:lang="en">Beloussow K., Wang L., Wu J., Ann D., Shen W.C. Recombinant arginine deiminase as a potential anti-angiogenic agent. Cancer. Lett., 2002, Vol. 183, Vol. 2, pp. 155-162.</mixed-citation></citation-alternatives></ref><ref id="cit7"><label>7</label><citation-alternatives><mixed-citation xml:lang="ru">Biswas S.K., Mantovani A. Orchestration of metabolism by macrophages. Cell Metab., 2012, Vol. 15, no. 4, pp. 432-437.</mixed-citation><mixed-citation xml:lang="en">Biswas S.K., Mantovani A. Orchestration of metabolism by macrophages. Cell Metab., 2012, Vol. 15, no. 4, pp. 432-437.</mixed-citation></citation-alternatives></ref><ref id="cit8"><label>8</label><citation-alternatives><mixed-citation xml:lang="ru">Bobermin L.D., Quincozes-Santos A., Guerra M.C., Leite M.C., Souza D.O., Goncalves C.-A., Gottfried C. Resveratrol Prevents Ammonia Toxicity in Astroglial Cells. PLOS., 2012, Vol. 7, e52164.</mixed-citation><mixed-citation xml:lang="en">Bobermin L.D., Quincozes-Santos A., Guerra M.C., Leite M.C., Souza D.O., Goncalves C.-A., Gottfried C. Resveratrol Prevents Ammonia Toxicity in Astroglial Cells. PLOS., 2012, Vol. 7, e52164.</mixed-citation></citation-alternatives></ref><ref id="cit9"><label>9</label><citation-alternatives><mixed-citation xml:lang="ru">Bogdan C. Nitric oxide synthase in innate and adaptive immunity: an update. Trends Immunol., 2015, Vol. 36, no. 3, pp. 161-178.</mixed-citation><mixed-citation xml:lang="en">Bogdan C. Nitric oxide synthase in innate and adaptive immunity: an update. Trends Immunol., 2015, Vol. 36, no. 3, pp. 161-178.</mixed-citation></citation-alternatives></ref><ref id="cit10"><label>10</label><citation-alternatives><mixed-citation xml:lang="ru">Brasse-Lagnel C., Fairand A., Lavoinne A., Husson A. Glutamine stimulates argininosuccinate synthetase gene expression through cytosolic O-glycosylation of Sp1 in Caco-2 cells. J. Biol. Chem., 2003, Vol. 278, pp. 52504-52510.</mixed-citation><mixed-citation xml:lang="en">Brasse-Lagnel C., Fairand A., Lavoinne A., Husson A. Glutamine stimulates argininosuccinate synthetase gene expression through cytosolic O-glycosylation of Sp1 in Caco-2 cells. J. Biol. Chem., 2003, Vol. 278, pp. 52504-52510.</mixed-citation></citation-alternatives></ref><ref id="cit11"><label>11</label><citation-alternatives><mixed-citation xml:lang="ru">Bronte V., Zanovello P. Regulation of immune responses by L-arginine metabolism. Nat. Rev. Immunol., 2005, Vol. 5, no. 8, pp. 641-654.</mixed-citation><mixed-citation xml:lang="en">Bronte V., Zanovello P. Regulation of immune responses by L-arginine metabolism. Nat. Rev. Immunol., 2005, Vol. 5, no. 8, pp. 641-654.</mixed-citation></citation-alternatives></ref><ref id="cit12"><label>12</label><citation-alternatives><mixed-citation xml:lang="ru">Bronte V., Seraﬁni P., De Santo C., Marigo I., Tosello V., Mazzoni A., Segal D.M., Staib C., Lowel M., Sutter G., Colombo M.P., Zanovello P. IL-4-induced arginase 1 suppresses alloreactive T cells in tumor-bearing mice. J. Immunol., 2003, Vol. 170, pp. 270-278.</mixed-citation><mixed-citation xml:lang="en">Bronte V., Seraﬁni P., De Santo C., Marigo I., Tosello V., Mazzoni A., Segal D.M., Staib C., Lowel M., Sutter G., Colombo M.P., Zanovello P. IL-4-induced arginase 1 suppresses alloreactive T cells in tumor-bearing mice. J. Immunol., 2003, Vol. 170, pp. 270-278.</mixed-citation></citation-alternatives></ref><ref id="cit13"><label>13</label><citation-alternatives><mixed-citation xml:lang="ru">Casiano-Colon A., Marquis R.E. Role of the arginine deiminase system in protecting oral bacteria and an enzymatic basis for acid tolerance. Appl. Environ. Microbiol., 1988, Vol. 54, no. 6, pp. 1318-1324.</mixed-citation><mixed-citation xml:lang="en">Casiano-Colon A., Marquis R.E. Role of the arginine deiminase system in protecting oral bacteria and an enzymatic basis for acid tolerance. Appl. Environ. Microbiol., 1988, Vol. 54, no. 6, pp. 1318-1324.</mixed-citation></citation-alternatives></ref><ref id="cit14"><label>14</label><citation-alternatives><mixed-citation xml:lang="ru">Chen F., Lucas R., Fulton D. The subcellular compartmentalization of arginine metabolizing enzymes and their role in endothelial dysfunction. Front. Immunol., 2013, Vol. 4, no. 184.</mixed-citation><mixed-citation xml:lang="en">Chen F., Lucas R., Fulton D. The subcellular compartmentalization of arginine metabolizing enzymes and their role in endothelial dysfunction. Front. Immunol., 2013, Vol. 4, no. 184.</mixed-citation></citation-alternatives></ref><ref id="cit15"><label>15</label><citation-alternatives><mixed-citation xml:lang="ru">Closs E.I., Simon A., Vekony N., Rotmann A. Plasma membrane transporters for arginine. J. Nutr., 2004, Vol. 134, no. 10, pp. 2752S-2759.</mixed-citation><mixed-citation xml:lang="en">Closs E.I., Simon A., Vekony N., Rotmann A. Plasma membrane transporters for arginine. J. Nutr., 2004, Vol. 134, no. 10, pp. 2752S-2759.</mixed-citation></citation-alternatives></ref><ref id="cit16"><label>16</label><citation-alternatives><mixed-citation xml:lang="ru">Cole C., Thomas S., Filak H., Henson P.M., Lenz L.L. Nitric oxide increases susceptibility of toll-like receptor-activated macrophages to spreading Listeria monocytogenes. Immunity, 2012, Vol. 36, no. 5, pp. 807-820.</mixed-citation><mixed-citation xml:lang="en">Cole C., Thomas S., Filak H., Henson P.M., Lenz L.L. Nitric oxide increases susceptibility of toll-like receptor-activated macrophages to spreading Listeria monocytogenes. Immunity, 2012, Vol. 36, no. 5, pp. 807-820.</mixed-citation></citation-alternatives></ref><ref id="cit17"><label>17</label><citation-alternatives><mixed-citation xml:lang="ru">Cullen M.E., Yuen A.H., Felkin L.E., Smolenski R.T., Hall J.L., Grindle S., Miller L.W., Birks E.J., Yacoub M.H., Barton P.J. Myocardial expression of the arginine:glycine amidinotransferase gene is elevated in heart failure and normalized aﬅer recovery: potential implications for local creatine synthesis. Circulation, 2006, Vol. 114, pp. 16-20.</mixed-citation><mixed-citation xml:lang="en">Cullen M.E., Yuen A.H., Felkin L.E., Smolenski R.T., Hall J.L., Grindle S., Miller L.W., Birks E.J., Yacoub M.H., Barton P.J. Myocardial expression of the arginine:glycine amidinotransferase gene is elevated in heart failure and normalized aﬅer recovery: potential implications for local creatine synthesis. Circulation, 2006, Vol. 114, pp. 16-20.</mixed-citation></citation-alternatives></ref><ref id="cit18"><label>18</label><citation-alternatives><mixed-citation xml:lang="ru">Cunin R.N. Glansdorﬀ A.P., Stalon V. Biosynthesis and metabolism of arginine in bacteria. Microbiol. Rev., 1986, Vol. 50, pp. 314-352.</mixed-citation><mixed-citation xml:lang="en">Cunin R.N. Glansdorﬀ A.P., Stalon V. Biosynthesis and metabolism of arginine in bacteria. Microbiol. Rev., 1986, Vol. 50, pp. 314-352.</mixed-citation></citation-alternatives></ref><ref id="cit19"><label>19</label><citation-alternatives><mixed-citation xml:lang="ru">Cusumano Z.T., Watson M.E.Jr., Caparon M.G. Streptococcus pyogenes arginine and citrulline catabolism promotes infection and modulates innate immunity. Infect. Immun., 2014, Vol. 82, no. 1, pp. 233-242.</mixed-citation><mixed-citation xml:lang="en">Cusumano Z.T., Watson M.E.Jr., Caparon M.G. Streptococcus pyogenes arginine and citrulline catabolism promotes infection and modulates innate immunity. Infect. Immun., 2014, Vol. 82, no. 1, pp. 233-242.</mixed-citation></citation-alternatives></ref><ref id="cit20"><label>20</label><citation-alternatives><mixed-citation xml:lang="ru">Das P., Lahiri A., Lahiri A. and Chakravortty D. Modulation of the Arginase Pathway in the Context of Microbial Pathogenesis: A Metabolic Enzyme Moonlighting as an Immune Modulator. PLoS Pathog., 2010, Vol. 6, no. 6.</mixed-citation><mixed-citation xml:lang="en">Das P., Lahiri A., Lahiri A. and Chakravortty D. Modulation of the Arginase Pathway in the Context of Microbial Pathogenesis: A Metabolic Enzyme Moonlighting as an Immune Modulator. PLoS Pathog., 2010, Vol. 6, no. 6.</mixed-citation></citation-alternatives></ref><ref id="cit21"><label>21</label><citation-alternatives><mixed-citation xml:lang="ru">de Jonge W.J., Kwikkers K.L., te Velde A.A., van Deventer S.J., Nolte M.A., Mebius R.E., Ruijter J.M., Lamers M.C., Lamers W.H. Arginine deﬁciency aﬀects early B cell maturation and lymphoid organ development in transgenic mice. J. Clin. Invest., 2002, Vol. 110, no. 10, pp. 1539-1548.</mixed-citation><mixed-citation xml:lang="en">de Jonge W.J., Kwikkers K.L., te Velde A.A., van Deventer S.J., Nolte M.A., Mebius R.E., Ruijter J.M., Lamers M.C., Lamers W.H. Arginine deﬁciency aﬀects early B cell maturation and lymphoid organ development in transgenic mice. J. Clin. Invest., 2002, Vol. 110, no. 10, pp. 1539-1548.</mixed-citation></citation-alternatives></ref><ref id="cit22"><label>22</label><citation-alternatives><mixed-citation xml:lang="ru">Degnan B.A., Fontaine M.C., Doebereiner A.H., Lee J.J., Mastroeni P., Dougan G., Goodacre J.A., Kehoe M.A. Characterization of an isogenic mutant of Streptococcus pyogenes Manfredo lacking the ability to make streptococcal acid glycoprotein. Infect. Immun., 2000, Vol. 68, no. 5, pp. 2441-2448.</mixed-citation><mixed-citation xml:lang="en">Degnan B.A., Fontaine M.C., Doebereiner A.H., Lee J.J., Mastroeni P., Dougan G., Goodacre J.A., Kehoe M.A. Characterization of an isogenic mutant of Streptococcus pyogenes Manfredo lacking the ability to make streptococcal acid glycoprotein. Infect. Immun., 2000, Vol. 68, no. 5, pp. 2441-2448.</mixed-citation></citation-alternatives></ref><ref id="cit23"><label>23</label><citation-alternatives><mixed-citation xml:lang="ru">Degnan B.A., Palmer J.M., Robson T., Jones C.E., Fischer M., Glanville M., Mellor G.D., Diamond A.G., Kehoe M.A., Goodacre J.A. Inhibition of human peripheral blood mononuclear cell proliferation by Streptococcus pyogenes cell extract is associated with arginine deiminase activity. Infect Immun., 1998, Vol. 66, no. 7, pp. 3050-3058.</mixed-citation><mixed-citation xml:lang="en">Degnan B.A., Palmer J.M., Robson T., Jones C.E., Fischer M., Glanville M., Mellor G.D., Diamond A.G., Kehoe M.A., Goodacre J.A. Inhibition of human peripheral blood mononuclear cell proliferation by Streptococcus pyogenes cell extract is associated with arginine deiminase activity. Infect Immun., 1998, Vol. 66, no. 7, pp. 3050-3058.</mixed-citation></citation-alternatives></ref><ref id="cit24"><label>24</label><citation-alternatives><mixed-citation xml:lang="ru">Deignan J.L., Livesay J.C., Yoo P.K., Goodman S.I., O’Brien W.E., Iyer R.K., Cederbaum S.D., Grody W.W. Ornithine deﬁciency in the arginase double knockout mouse. Mol. Genet. Metab., 2006, Vol. 89, pp. 87-96.</mixed-citation><mixed-citation xml:lang="en">Deignan J.L., Livesay J.C., Yoo P.K., Goodman S.I., O’Brien W.E., Iyer R.K., Cederbaum S.D., Grody W.W. Ornithine deﬁciency in the arginase double knockout mouse. Mol. Genet. Metab., 2006, Vol. 89, pp. 87-96.</mixed-citation></citation-alternatives></ref><ref id="cit25"><label>25</label><citation-alternatives><mixed-citation xml:lang="ru">Durante W. Role of arginase in vessel wall remodeling. Front. Immunol., 2013, Vol. 4, no. 111.</mixed-citation><mixed-citation xml:lang="en">Durante W. Role of arginase in vessel wall remodeling. Front. Immunol., 2013, Vol. 4, no. 111.</mixed-citation></citation-alternatives></ref><ref id="cit26"><label>26</label><citation-alternatives><mixed-citation xml:lang="ru">Erez A. Argininosuccinic aciduria: from a monogenic to a complex disorder. Genet. Med. 2013, Vol. 15, no. 4, pp. 251-257.</mixed-citation><mixed-citation xml:lang="en">Erez A. Argininosuccinic aciduria: from a monogenic to a complex disorder. Genet. Med. 2013, Vol. 15, no. 4, pp. 251-257.</mixed-citation></citation-alternatives></ref><ref id="cit27"><label>27</label><citation-alternatives><mixed-citation xml:lang="ru">Fingar D.C., Richardson C.J., Tee A.R., Cheatham L., Tsou C., Blenis J. mTOR Controls Cell Cycle Progression through Its Cell Growth Eﬀectors S6K1 and 4E-BP1/Eukaryotic Translation Initiation Factor 4E. Molecular and Cellular Biology., 2004, Vol. 24, no. 1, pp. 200-216.</mixed-citation><mixed-citation xml:lang="en">Fingar D.C., Richardson C.J., Tee A.R., Cheatham L., Tsou C., Blenis J. mTOR Controls Cell Cycle Progression through Its Cell Growth Eﬀectors S6K1 and 4E-BP1/Eukaryotic Translation Initiation Factor 4E. Molecular and Cellular Biology., 2004, Vol. 24, no. 1, pp. 200-216.</mixed-citation></citation-alternatives></ref><ref id="cit28"><label>28</label><citation-alternatives><mixed-citation xml:lang="ru">Gabrilovich D. Mechanisms and functional signiﬁcance of tumour-induced dendritic-cell defects. Nat. Rev. Immunol., 2004, Vol. 4, pp. 941-952.</mixed-citation><mixed-citation xml:lang="en">Gabrilovich D. Mechanisms and functional signiﬁcance of tumour-induced dendritic-cell defects. Nat. Rev. Immunol., 2004, Vol. 4, pp. 941-952.</mixed-citation></citation-alternatives></ref><ref id="cit29"><label>29</label><citation-alternatives><mixed-citation xml:lang="ru">Gabrilovich D.I., Nagaraj S. Myeloid-derived suppressor cells as regulators of the immune system. Nat. Rev. Immunol., 2009, Vol. 9, no. 3, pp. 162-174.</mixed-citation><mixed-citation xml:lang="en">Gabrilovich D.I., Nagaraj S. Myeloid-derived suppressor cells as regulators of the immune system. Nat. Rev. Immunol., 2009, Vol. 9, no. 3, pp. 162-174.</mixed-citation></citation-alternatives></ref><ref id="cit30"><label>30</label><citation-alternatives><mixed-citation xml:lang="ru">Ghosh P., Sica A., Young H.A., Ye J., Franco J.L., Wiltrout R.H., Longo D.L., Rice N.R., Komschlies K.L. Alterations in NF kappa B/Rel family proteins in splenic T-cells from tumor-bearing mice and reversal following therapy. Cancer. Res., 1994, Vol. 54, pp. 2969-2972.</mixed-citation><mixed-citation xml:lang="en">Ghosh P., Sica A., Young H.A., Ye J., Franco J.L., Wiltrout R.H., Longo D.L., Rice N.R., Komschlies K.L. Alterations in NF kappa B/Rel family proteins in splenic T-cells from tumor-bearing mice and reversal following therapy. Cancer. Res., 1994, Vol. 54, pp. 2969-2972.</mixed-citation></citation-alternatives></ref><ref id="cit31"><label>31</label><citation-alternatives><mixed-citation xml:lang="ru">Goldmann O., Rohde M., Chhatwal G.S., Medina E. Role of macrophages in host resistance to group A streptococci. Infect. Immun., 2004, Vol. 72, pp. 2956-2963.</mixed-citation><mixed-citation xml:lang="en">Goldmann O., Rohde M., Chhatwal G.S., Medina E. Role of macrophages in host resistance to group A streptococci. Infect. Immun., 2004, Vol. 72, pp. 2956-2963.</mixed-citation></citation-alternatives></ref><ref id="cit32"><label>32</label><citation-alternatives><mixed-citation xml:lang="ru">Gong H., Zolzer F., von Recklinghausen G., Havers W., Schweigerer L. Arginine deiminase inhibits proliferation of human leukemia cells more potently than asparaginase by inducing cell cycle arrest and apoptosis. Leukemia., 2000, Vol. 14, pp. 826-829.</mixed-citation><mixed-citation xml:lang="en">Gong H., Zolzer F., von Recklinghausen G., Havers W., Schweigerer L. Arginine deiminase inhibits proliferation of human leukemia cells more potently than asparaginase by inducing cell cycle arrest and apoptosis. Leukemia., 2000, Vol. 14, pp. 826-829.</mixed-citation></citation-alternatives></ref><ref id="cit33"><label>33</label><citation-alternatives><mixed-citation xml:lang="ru">Goodwin B.L., Solomonson L.P., Eichler D.C. Argininosuccinate Synthase Expression Is Required to Maintain Nitric Oxide Production and Cell Viability in Aortic Endothelial Cells. J. Biol Chem., 2004, Vol. 279, no. 18, pp. 18353-18360.</mixed-citation><mixed-citation xml:lang="en">Goodwin B.L., Solomonson L.P., Eichler D.C. Argininosuccinate Synthase Expression Is Required to Maintain Nitric Oxide Production and Cell Viability in Aortic Endothelial Cells. J. Biol Chem., 2004, Vol. 279, no. 18, pp. 18353-18360.</mixed-citation></citation-alternatives></ref><ref id="cit34"><label>34</label><citation-alternatives><mixed-citation xml:lang="ru">Gordon S., Taylor P.R. Monocyte and macrophage heterogeneity. Nature Rev. Immunol., 2005, Vol. 5, pp. 953-964.</mixed-citation><mixed-citation xml:lang="en">Gordon S., Taylor P.R. Monocyte and macrophage heterogeneity. Nature Rev. Immunol., 2005, Vol. 5, pp. 953-964.</mixed-citation></citation-alternatives></ref><ref id="cit35"><label>35</label><citation-alternatives><mixed-citation xml:lang="ru">Granger D.L., Hibbs J.B., Perfect Jr.J.R., Durack D.T. Speciﬁc amino acid (L-arginine) requirement for the microbiostatic activity of murine macrophages. J. Clin. Invest., 1988, Vol. 81, no. 4, pp. 1129-1136.</mixed-citation><mixed-citation xml:lang="en">Granger D.L., Hibbs J.B., Perfect Jr.J.R., Durack D.T. Speciﬁc amino acid (L-arginine) requirement for the microbiostatic activity of murine macrophages. J. Clin. Invest., 1988, Vol. 81, no. 4, pp. 1129-1136.</mixed-citation></citation-alternatives></ref><ref id="cit36"><label>36</label><citation-alternatives><mixed-citation xml:lang="ru">Gross T.J., Kremens K., Powers L.S., Brink B., Knutson T., Domann F.E. Epigenetic silencing of the human NOS2 gene: rethinking the role of nitric oxide in human macrophage inﬂammatory responses. J. Immunol., 2014, Vol. 192, no. 5, pp. 2326-2338.</mixed-citation><mixed-citation xml:lang="en">Gross T.J., Kremens K., Powers L.S., Brink B., Knutson T., Domann F.E. Epigenetic silencing of the human NOS2 gene: rethinking the role of nitric oxide in human macrophage inﬂammatory responses. J. Immunol., 2014, Vol. 192, no. 5, pp. 2326-2338.</mixed-citation></citation-alternatives></ref><ref id="cit37"><label>37</label><citation-alternatives><mixed-citation xml:lang="ru">Guei T.R., Liu M.C., Yang C.P., Su T.S. Identiﬁcation of a liver-speciﬁc cAMP response element in the human argininosuccinate synthetase gene. Biochem. Biophys. Res. Commun., 2008, Vol. 377, pp. 257-261.</mixed-citation><mixed-citation xml:lang="en">Guei T.R., Liu M.C., Yang C.P., Su T.S. Identiﬁcation of a liver-speciﬁc cAMP response element in the human argininosuccinate synthetase gene. Biochem. Biophys. Res. Commun., 2008, Vol. 377, pp. 257-261.</mixed-citation></citation-alternatives></ref><ref id="cit38"><label>38</label><citation-alternatives><mixed-citation xml:lang="ru">Hammermann R., Bliesener N., Mossner J., Klasen S., Wiesinger H., Wessler I., Race K. Inability of rat alveolar macrophages to recycle L-citrulline to L-arginine despite induction of argininosuccinate synthetase mRNA and protein, and inhibition of nitric oxide synthesis by exogenous L-citrulline. Naunyn-Schmiedeberg´s Arch. Pharmacol., 1998, Vol. 358, pp. 601-607.</mixed-citation><mixed-citation xml:lang="en">Hammermann R., Bliesener N., Mossner J., Klasen S., Wiesinger H., Wessler I., Race K. Inability of rat alveolar macrophages to recycle L-citrulline to L-arginine despite induction of argininosuccinate synthetase mRNA and protein, and inhibition of nitric oxide synthesis by exogenous L-citrulline. Naunyn-Schmiedeberg´s Arch. Pharmacol., 1998, Vol. 358, pp. 601-607.</mixed-citation></citation-alternatives></ref><ref id="cit39"><label>39</label><citation-alternatives><mixed-citation xml:lang="ru">Hecker M., Sessa W.C., Harris H.J., Anggard E.E., Vane J.R. The metabolism of L-arginine and its signiﬁcance for endotheliumderived relaxing factor: cultured endothelial cells recycle Lcitrulline to L-arginine. Proc. Natl. Acad. Sci. USA, 1990, Vol. 87, pp. 8612-8616.</mixed-citation><mixed-citation xml:lang="en">Hecker M., Sessa W.C., Harris H.J., Anggard E.E., Vane J.R. The metabolism of L-arginine and its signiﬁcance for endotheliumderived relaxing factor: cultured endothelial cells recycle Lcitrulline to L-arginine. Proc. Natl. Acad. Sci. USA, 1990, Vol. 87, pp. 8612-8616.</mixed-citation></citation-alternatives></ref><ref id="cit40"><label>40</label><citation-alternatives><mixed-citation xml:lang="ru">Heid M.E., Keyel P.A., Kamga C., Shiva S., Watkins S.C., Salter R.D. Mitochondrial reactive oxygen species induces NLRP3-dependent lysosomal damage and inﬂammasome activation. J. Immunol., 2013, Vol. 191, no. 10, pp. 5230-5238.</mixed-citation><mixed-citation xml:lang="en">Heid M.E., Keyel P.A., Kamga C., Shiva S., Watkins S.C., Salter R.D. Mitochondrial reactive oxygen species induces NLRP3-dependent lysosomal damage and inﬂammasome activation. J. Immunol., 2013, Vol. 191, no. 10, pp. 5230-5238.</mixed-citation></citation-alternatives></ref><ref id="cit41"><label>41</label><citation-alternatives><mixed-citation xml:lang="ru">Henningham A., Ericsson D.J., Langer K., Casey L.W., Jovcevski B., Chhatwal G.S., Aquilina J.A., Batzloﬀ M.R., Kobe B., Walker M.J. Structure-informed design of an enzymatically inactive vaccine component for group A Streptococcus. M. Bio, 2013, Vol. 4, no. 4.</mixed-citation><mixed-citation xml:lang="en">Henningham A., Ericsson D.J., Langer K., Casey L.W., Jovcevski B., Chhatwal G.S., Aquilina J.A., Batzloﬀ M.R., Kobe B., Walker M.J. Structure-informed design of an enzymatically inactive vaccine component for group A Streptococcus. M. Bio, 2013, Vol. 4, no. 4.</mixed-citation></citation-alternatives></ref><ref id="cit42"><label>42</label><citation-alternatives><mixed-citation xml:lang="ru">Hibbs J.B.Jr., Vavrin Z., Taintor R.R. L-arginine is required for expression of the activated macrophage eﬀector mechanism causing selective metabolic inhibition in target cells. J. Immunol., 1987, Vol. 138, no. 2, pp. 550-565.</mixed-citation><mixed-citation xml:lang="en">Hibbs J.B.Jr., Vavrin Z., Taintor R.R. L-arginine is required for expression of the activated macrophage eﬀector mechanism causing selective metabolic inhibition in target cells. J. Immunol., 1987, Vol. 138, no. 2, pp. 550-565.</mixed-citation></citation-alternatives></ref><ref id="cit43"><label>43</label><citation-alternatives><mixed-citation xml:lang="ru">Hibbs J.B.Jr., Taintor R.R., Vavrin Z., Rachlin E.M. Nitric oxide: a cytotoxic activated macrophage eﬀector molecule. Biochem. Biophys. Res. Commun., 1988, Vol. 157, pp. 87-94.</mixed-citation><mixed-citation xml:lang="en">Hibbs J.B.Jr., Taintor R.R., Vavrin Z., Rachlin E.M. Nitric oxide: a cytotoxic activated macrophage eﬀector molecule. Biochem. Biophys. Res. Commun., 1988, Vol. 157, pp. 87-94.</mixed-citation></citation-alternatives></ref><ref id="cit44"><label>44</label><citation-alternatives><mixed-citation xml:lang="ru">Item C.B., Stockler-Ipsiroglu S., Stromberger C., Muhl A., Alessandri M.G., Bianchi M.C., Tosetti M., Fornai F., Cioni G. Arginine:glycine amidinotransferase deﬁciency: the third inborn error of creatine metabolism in humans. Am. J. Hum. Genet. 2001, Vol. 69, no. 5, pp. 1127-1133.</mixed-citation><mixed-citation xml:lang="en">Item C.B., Stockler-Ipsiroglu S., Stromberger C., Muhl A., Alessandri M.G., Bianchi M.C., Tosetti M., Fornai F., Cioni G. Arginine:glycine amidinotransferase deﬁciency: the third inborn error of creatine metabolism in humans. Am. J. Hum. Genet. 2001, Vol. 69, no. 5, pp. 1127-1133.</mixed-citation></citation-alternatives></ref><ref id="cit45"><label>45</label><citation-alternatives><mixed-citation xml:lang="ru">Iyer R.K., Yoo P.K., Kern R.M., Rozengurt N., Tsoa R., O’Brien W.E., Yu H., Grody W.W., Cederbaum S.D. Mouse model for human arginase deﬁciency. Mol. Cell. Biol., 2002, Vol. 22, no. 13, pp. 4491-4498.</mixed-citation><mixed-citation xml:lang="en">Iyer R.K., Yoo P.K., Kern R.M., Rozengurt N., Tsoa R., O’Brien W.E., Yu H., Grody W.W., Cederbaum S.D. Mouse model for human arginase deﬁciency. Mol. Cell. Biol., 2002, Vol. 22, no. 13, pp. 4491-4498.</mixed-citation></citation-alternatives></ref><ref id="cit46"><label>46</label><citation-alternatives><mixed-citation xml:lang="ru">Iyo A.H., Zhu M.Y., Ordway G.A., Regunathan S. Expression of arginine decarboxylase in brain regions and neuronal cells. J. Neurochem., 2006, Vol. 96, no. 4, pp. 1042-1050.</mixed-citation><mixed-citation xml:lang="en">Iyo A.H., Zhu M.Y., Ordway G.A., Regunathan S. Expression of arginine decarboxylase in brain regions and neuronal cells. J. Neurochem., 2006, Vol. 96, no. 4, pp. 1042-1050.</mixed-citation></citation-alternatives></ref><ref id="cit47"><label>47</label><citation-alternatives><mixed-citation xml:lang="ru">Jayasekera J.P., Vinuesa, C.G., Karupiah, G., King, N.J.C. Enhanced antiviral antibody secretion and attenuated immunopathology during inﬂuenza virus infection in nitric oxide synthase-2-deﬁcient mice. J. Gen. Virol., 2006, no. 87, pp. 3361-3371.</mixed-citation><mixed-citation xml:lang="en">Jayasekera J.P., Vinuesa, C.G., Karupiah, G., King, N.J.C. Enhanced antiviral antibody secretion and attenuated immunopathology during inﬂuenza virus infection in nitric oxide synthase-2-deﬁcient mice. J. Gen. Virol., 2006, no. 87, pp. 3361-3371.</mixed-citation></citation-alternatives></ref><ref id="cit48"><label>48</label><citation-alternatives><mixed-citation xml:lang="ru">Kanaoka M., Kawanaka T.C., Negoro Y., Fukita K.T., Agui H. Cloning and expression of the antitumor glycoprotein gene of Streptococcus pyogenes Su in Escherichia coli. Agric. Biol. Chem., 1987, Vol. 51, pp. 2641-2648.</mixed-citation><mixed-citation xml:lang="en">Kanaoka M., Kawanaka T.C., Negoro Y., Fukita K.T., Agui H. Cloning and expression of the antitumor glycoprotein gene of Streptococcus pyogenes Su in Escherichia coli. Agric. Biol. Chem., 1987, Vol. 51, pp. 2641-2648.</mixed-citation></citation-alternatives></ref><ref id="cit49"><label>49</label><citation-alternatives><mixed-citation xml:lang="ru">Kapp K., Prufer S., Michel C.S., Habermeier A., Luckner-Minden C., Giese T., Bomalaski J., Langhans C.D., Kropf P., Muller I., Closs E.I., Radsak M.P., Munder M. Granulocyte functions are independent of arginine availability. J. Leukoc. Biol., 2014, Vol. 96, no. 6, pp. 1047-1053.</mixed-citation><mixed-citation xml:lang="en">Kapp K., Prufer S., Michel C.S., Habermeier A., Luckner-Minden C., Giese T., Bomalaski J., Langhans C.D., Kropf P., Muller I., Closs E.I., Radsak M.P., Munder M. Granulocyte functions are independent of arginine availability. J. Leukoc. Biol., 2014, Vol. 96, no. 6, pp. 1047-1053.</mixed-citation></citation-alternatives></ref><ref id="cit50"><label>50</label><citation-alternatives><mixed-citation xml:lang="ru">Kim R.H., Coates J.M., Bowles T.L., McNerney G.P., Sutcliﬀe J., Jung J.U., Gandour-Edwards R., Chuang F.Y., Bold R.J., Kung H.J. Arginine deiminase as a novel therapy for prostate cancer induces autophagy and caspase-independent apoptosis. Cancer. Res., 2009, Vol. 69, pp. 700-708.</mixed-citation><mixed-citation xml:lang="en">Kim R.H., Coates J.M., Bowles T.L., McNerney G.P., Sutcliﬀe J., Jung J.U., Gandour-Edwards R., Chuang F.Y., Bold R.J., Kung H.J. Arginine deiminase as a novel therapy for prostate cancer induces autophagy and caspase-independent apoptosis. Cancer. Res., 2009, Vol. 69, pp. 700-708.</mixed-citation></citation-alternatives></ref><ref id="cit51"><label>51</label><citation-alternatives><mixed-citation xml:lang="ru">Komada Y., Zhang X.L., Zhou Y.W., Ido M., Azuma E. Apoptotic cell death of human T lymphoblastoid cells induced by arginine deiminase. Int. J. Hematol., 1997, Vol. 65, no. 2, pp. 129-141.</mixed-citation><mixed-citation xml:lang="en">Komada Y., Zhang X.L., Zhou Y.W., Ido M., Azuma E. Apoptotic cell death of human T lymphoblastoid cells induced by arginine deiminase. Int. J. Hematol., 1997, Vol. 65, no. 2, pp. 129-141.</mixed-citation></citation-alternatives></ref><ref id="cit52"><label>52</label><citation-alternatives><mixed-citation xml:lang="ru">Kuo M.T., Savaraj N., Feun L.G. Targeted cellular metabolism for cancer chemotherapy with recombinant arginine-degrading enzymes. Oncotarget., 2010, Vol. 1, no. 4, pp. 246-251.</mixed-citation><mixed-citation xml:lang="en">Kuo M.T., Savaraj N., Feun L.G. Targeted cellular metabolism for cancer chemotherapy with recombinant arginine-degrading enzymes. Oncotarget., 2010, Vol. 1, no. 4, pp. 246-251.</mixed-citation></citation-alternatives></ref><ref id="cit53"><label>53</label><citation-alternatives><mixed-citation xml:lang="ru">Landau G., Bercovich Z., Park M.H., Kahana C. The Role of Polyamines in Supporting Growth of Mammalian Cells Is Mediated through Their Requirement for Translation Initiation and Elongation. Biol. Chem., 2010, Vol. 285, no. 17, pp. 12474-12481.</mixed-citation><mixed-citation xml:lang="en">Landau G., Bercovich Z., Park M.H., Kahana C. The Role of Polyamines in Supporting Growth of Mammalian Cells Is Mediated through Their Requirement for Translation Initiation and Elongation. Biol. Chem., 2010, Vol. 285, no. 17, pp. 12474-12481.</mixed-citation></citation-alternatives></ref><ref id="cit54"><label>54</label><citation-alternatives><mixed-citation xml:lang="ru">Laplante M., Sabatini D.M. mTOR signaling in growth control and disease. Cell, 2014, Vol. 149, pp. 274-293.</mixed-citation><mixed-citation xml:lang="en">Laplante M., Sabatini D.M. mTOR signaling in growth control and disease. Cell, 2014, Vol. 149, pp. 274-293.</mixed-citation></citation-alternatives></ref><ref id="cit55"><label>55</label><citation-alternatives><mixed-citation xml:lang="ru">LeBien T.W. Arginine: an unusual dietary requirement of pre-B lymphocytes? J. Clin. Invest., 2002, Vol. 11, pp. 1411-1413.</mixed-citation><mixed-citation xml:lang="en">LeBien T.W. Arginine: an unusual dietary requirement of pre-B lymphocytes? J. Clin. Invest., 2002, Vol. 11, pp. 1411-1413.</mixed-citation></citation-alternatives></ref><ref id="cit56"><label>56</label><citation-alternatives><mixed-citation xml:lang="ru">Lee S.W., Heonsik C., Eun S.-Y., Fukuyama S., Croﬅ M. Nitric oxide modulates TGF-beta-directive signals to suppress Foxp3+ regulatory T cell diﬀerentiation and potentiate Th1 development. J. Immunol., 2011, Vol. 186, pp. 6972-6980.</mixed-citation><mixed-citation xml:lang="en">Lee S.W., Heonsik C., Eun S.-Y., Fukuyama S., Croﬅ M. Nitric oxide modulates TGF-beta-directive signals to suppress Foxp3+ regulatory T cell diﬀerentiation and potentiate Th1 development. J. Immunol., 2011, Vol. 186, pp. 6972-6980.</mixed-citation></citation-alternatives></ref><ref id="cit57"><label>57</label><citation-alternatives><mixed-citation xml:lang="ru">Li H., Meininger C.J., Hawker J.R.Jr, Haynes T.E., Kepka-Lenhart D., Mistry S.K. Regulatory role of arginase I and II in nitric oxide, polyamine, and proline syntheses in endothelial cells. Am. J. Physiol. Endocrinol. Metab., 2001, Vol. 280, no. 1, pp. 75-82.</mixed-citation><mixed-citation xml:lang="en">Li H., Meininger C.J., Hawker J.R.Jr, Haynes T.E., Kepka-Lenhart D., Mistry S.K. Regulatory role of arginase I and II in nitric oxide, polyamine, and proline syntheses in endothelial cells. Am. J. Physiol. Endocrinol. Metab., 2001, Vol. 280, no. 1, pp. 75-82.</mixed-citation></citation-alternatives></ref><ref id="cit58"><label>58</label><citation-alternatives><mixed-citation xml:lang="ru">Li H., Meininger C.J., Kelly K.A., Hawker J.R. Jr, Morris S.M. Jr, Wu G. Activities of arginase I and II are limiting for endothelial cell proliferation. Am. J. Physiol. Regul. Integr. Comp. Physiol., 2002, Vol. 282, no. 1, pp. 64-69.</mixed-citation><mixed-citation xml:lang="en">Li H., Meininger C.J., Kelly K.A., Hawker J.R. Jr, Morris S.M. Jr, Wu G. Activities of arginase I and II are limiting for endothelial cell proliferation. Am. J. Physiol. Regul. Integr. Comp. Physiol., 2002, Vol. 282, no. 1, pp. 64-69.</mixed-citation></citation-alternatives></ref><ref id="cit59"><label>59</label><citation-alternatives><mixed-citation xml:lang="ru">Mattila J.T., Thomas A.C. Nitric oxide synthase: non-canonical expression patterns. Front. Immunol., 2014, Vol. 9, no. 5, p. 478.</mixed-citation><mixed-citation xml:lang="en">Mattila J.T., Thomas A.C. Nitric oxide synthase: non-canonical expression patterns. Front. Immunol., 2014, Vol. 9, no. 5, p. 478.</mixed-citation></citation-alternatives></ref><ref id="cit60"><label>60</label><citation-alternatives><mixed-citation xml:lang="ru">Miescher S., Whiteside T.L., Carrel S., von Fliedner V. Functional properties of tumor-inﬁltrating and blood lymphocytes in patients with solid tumors: eﬀects of tumor cells and their supernatants on proliferative responses of lymphocytes. J. Immunol., 1986, Vol. 136, pp. 1899-1907.</mixed-citation><mixed-citation xml:lang="en">Miescher S., Whiteside T.L., Carrel S., von Fliedner V. Functional properties of tumor-inﬁltrating and blood lymphocytes in patients with solid tumors: eﬀects of tumor cells and their supernatants on proliferative responses of lymphocytes. J. Immunol., 1986, Vol. 136, pp. 1899-1907.</mixed-citation></citation-alternatives></ref><ref id="cit61"><label>61</label><citation-alternatives><mixed-citation xml:lang="ru">Mishalian I., Ordan M., Peled A., Maly A., Eichenbaum M.B., Ravins M., Aychek T., Jung S., Hanski E. Recruited macrophages control dissemination of group A streptococcus from infected soﬅ tissues. J. Immunol., 2011, Vol. 187, pp. 6022-6031.</mixed-citation><mixed-citation xml:lang="en">Mishalian I., Ordan M., Peled A., Maly A., Eichenbaum M.B., Ravins M., Aychek T., Jung S., Hanski E. Recruited macrophages control dissemination of group A streptococcus from infected soﬅ tissues. J. Immunol., 2011, Vol. 187, pp. 6022-6031.</mixed-citation></citation-alternatives></ref><ref id="cit62"><label>62</label><citation-alternatives><mixed-citation xml:lang="ru">Miyazaki K., Takaku H., Umeda M., Fujita T., Huang W., Kimura T., Yamashita J. and Horio T. Potent Growth Inhibition of Human Tumor Cells in Culture by Arginine Deiminase Puriﬁed from a Culture Medium of a Mycoplasma-infected Cell Line. Cancer Research, 1990, Vol. 50, pp. 4522-4527.</mixed-citation><mixed-citation xml:lang="en">Miyazaki K., Takaku H., Umeda M., Fujita T., Huang W., Kimura T., Yamashita J. and Horio T. Potent Growth Inhibition of Human Tumor Cells in Culture by Arginine Deiminase Puriﬁed from a Culture Medium of a Mycoplasma-infected Cell Line. Cancer Research, 1990, Vol. 50, pp. 4522-4527.</mixed-citation></citation-alternatives></ref><ref id="cit63"><label>63</label><citation-alternatives><mixed-citation xml:lang="ru">Mizoguchi H., O’Shea J.J., Longo D.L., Loeffler C.M., McVicar D.W., Ochoa A.C. Alterations in signal transduction molecules in T lymphocytes from tumor-bearing mice. Science, 1992, Vol. 258, pp. 1795-1798.</mixed-citation><mixed-citation xml:lang="en">Mizoguchi H., O’Shea J.J., Longo D.L., Loeffler C.M., McVicar D.W., Ochoa A.C. Alterations in signal transduction molecules in T lymphocytes from tumor-bearing mice. Science, 1992, Vol. 258, pp. 1795-1798.</mixed-citation></citation-alternatives></ref><ref id="cit64"><label>64</label><citation-alternatives><mixed-citation xml:lang="ru">Morris S.M.Jr. Arginases and arginine deﬁciency syndromes. Curr. Opin. Clin. Nutr. Metab. Care, 2012, Vol. 15, no. 1, pp. 64-70.</mixed-citation><mixed-citation xml:lang="en">Morris S.M.Jr. Arginases and arginine deﬁciency syndromes. Curr. Opin. Clin. Nutr. Metab. Care, 2012, Vol. 15, no. 1, pp. 64-70.</mixed-citation></citation-alternatives></ref><ref id="cit65"><label>65</label><citation-alternatives><mixed-citation xml:lang="ru">Morris S.M.Jr. Recent advances in arginine metabolism: roles and regulation of the arginases. British Journal of Pharmacology, 2009, Vol. 157, no. 6, pp. 922-930.</mixed-citation><mixed-citation xml:lang="en">Morris S.M.Jr. Recent advances in arginine metabolism: roles and regulation of the arginases. British Journal of Pharmacology, 2009, Vol. 157, no. 6, pp. 922-930.</mixed-citation></citation-alternatives></ref><ref id="cit66"><label>66</label><citation-alternatives><mixed-citation xml:lang="ru">Morris S.M.Jr. Regulation of enzymes of the urea cycle and arginine metabolism. Annu. Rev. Nutr., 2002, Vol. 22, pp. 87-105.</mixed-citation><mixed-citation xml:lang="en">Morris S.M.Jr. Regulation of enzymes of the urea cycle and arginine metabolism. Annu. Rev. Nutr., 2002, Vol. 22, pp. 87-105.</mixed-citation></citation-alternatives></ref><ref id="cit67"><label>67</label><citation-alternatives><mixed-citation xml:lang="ru">Morrison R.F., Seidel E.R. Vascular endothelial cell proliferation: regulation of cellular polyamines. Cardiovasc. Res., 1995, Vol. 29, no. 6, pp. 841-847.</mixed-citation><mixed-citation xml:lang="en">Morrison R.F., Seidel E.R. Vascular endothelial cell proliferation: regulation of cellular polyamines. Cardiovasc. Res., 1995, Vol. 29, no. 6, pp. 841-847.</mixed-citation></citation-alternatives></ref><ref id="cit68"><label>68</label><citation-alternatives><mixed-citation xml:lang="ru">Morrow K., Hernandez C.P., Raber P., Del Valle L., Wilk A.M., Majumdar S., Wyczechowska D., Reiss K., Rodriguez P.C. Anti-leukemic mechanisms of pegylated arginase I in acute lymphoblastic T-cell leukemia. Leukemia, 2013, Vol. 27, no. 3, pp. 569-577.</mixed-citation><mixed-citation xml:lang="en">Morrow K., Hernandez C.P., Raber P., Del Valle L., Wilk A.M., Majumdar S., Wyczechowska D., Reiss K., Rodriguez P.C. Anti-leukemic mechanisms of pegylated arginase I in acute lymphoblastic T-cell leukemia. Leukemia, 2013, Vol. 27, no. 3, pp. 569-577.</mixed-citation></citation-alternatives></ref><ref id="cit69"><label>69</label><citation-alternatives><mixed-citation xml:lang="ru">Munder M., Mollinedo F., Calafat J., Canchado J., Gil-Lamaignere C., Fuentes J.M., Luckner C., Doschko G., Soler G., Eichmann K., Muller F.M., Ho A.D., Goerner M., Modolell M. Arginase I is constitutively expressed in human granulocytes and participates in fungicidal activity. Blood, 2005, Vol. 105, no. 6, pp. 2549-2556.</mixed-citation><mixed-citation xml:lang="en">Munder M., Mollinedo F., Calafat J., Canchado J., Gil-Lamaignere C., Fuentes J.M., Luckner C., Doschko G., Soler G., Eichmann K., Muller F.M., Ho A.D., Goerner M., Modolell M. Arginase I is constitutively expressed in human granulocytes and participates in fungicidal activity. Blood, 2005, Vol. 105, no. 6, pp. 2549-2556.</mixed-citation></citation-alternatives></ref><ref id="cit70"><label>70</label><citation-alternatives><mixed-citation xml:lang="ru">Murohara T., Asahara T., Silver M., Bauters C., Masuda H., Kalka C., Kearney M., Chen D., Symes J.F., Fishman M.C., Huang P.L., Isner J.M. Nitric oxide synthase modulates angiogenesis in response to tissue ischemia. J. Clin. Invest., 1998, Vol. 101, pp. 2567-2578.</mixed-citation><mixed-citation xml:lang="en">Murohara T., Asahara T., Silver M., Bauters C., Masuda H., Kalka C., Kearney M., Chen D., Symes J.F., Fishman M.C., Huang P.L., Isner J.M. Nitric oxide synthase modulates angiogenesis in response to tissue ischemia. J. Clin. Invest., 1998, Vol. 101, pp. 2567-2578.</mixed-citation></citation-alternatives></ref><ref id="cit71"><label>71</label><citation-alternatives><mixed-citation xml:lang="ru">Murray P.J., Wynn T.A. Obstacles and opportunities for understanding macrophage polarization. J. Leukoc. Biol., 2011, Vol. 89, no. 4, pp. 557-563.</mixed-citation><mixed-citation xml:lang="en">Murray P.J., Wynn T.A. Obstacles and opportunities for understanding macrophage polarization. J. Leukoc. Biol., 2011, Vol. 89, no. 4, pp. 557-563.</mixed-citation></citation-alternatives></ref><ref id="cit72"><label>72</label><citation-alternatives><mixed-citation xml:lang="ru">Nobbs A.H., Lamont R.J., Jenkinson H.F. Streptococcus Adherence and Colonization. Microbiology and Molecular Biology Reviews, 2009, Vol. 73, no. 3, pp. 407-450.</mixed-citation><mixed-citation xml:lang="en">Nobbs A.H., Lamont R.J., Jenkinson H.F. Streptococcus Adherence and Colonization. Microbiology and Molecular Biology Reviews, 2009, Vol. 73, no. 3, pp. 407-450.</mixed-citation></citation-alternatives></ref><ref id="cit73"><label>73</label><citation-alternatives><mixed-citation xml:lang="ru">Noh E.J., Kang S.W., Shin Y.J., Kim D.C., Park I.S., Kim M.Y., Chun B.G., Min B.H. Characterization of mycoplasma arginine deiminase expressed in E. coli and its inhibitory regulation of nitric oxide synthesis. Mol. Cells, 2002, Vol. 28, no. 13, no. 1, pp. 137-143.</mixed-citation><mixed-citation xml:lang="en">Noh E.J., Kang S.W., Shin Y.J., Kim D.C., Park I.S., Kim M.Y., Chun B.G., Min B.H. Characterization of mycoplasma arginine deiminase expressed in E. coli and its inhibitory regulation of nitric oxide synthesis. Mol. Cells, 2002, Vol. 28, no. 13, no. 1, pp. 137-143.</mixed-citation></citation-alternatives></ref><ref id="cit74"><label>74</label><citation-alternatives><mixed-citation xml:lang="ru">Norenberg M.D. Oxidative and nitrosative stress in ammonia neurotoxicity. Hepatology, 2003, Vol. 37, pp. 245-248.</mixed-citation><mixed-citation xml:lang="en">Norenberg M.D. Oxidative and nitrosative stress in ammonia neurotoxicity. Hepatology, 2003, Vol. 37, pp. 245-248.</mixed-citation></citation-alternatives></ref><ref id="cit75"><label>75</label><citation-alternatives><mixed-citation xml:lang="ru">Oberlies J., Watzl C., Giese T., Luckner C., Kropf P., Müller I., Ho A.D., Munder M. Regulation of NK cell function by human granulocyte arginase. J. Immunol., 2009, Vol. 182, no. 9, pp. 5259-5267.</mixed-citation><mixed-citation xml:lang="en">Oberlies J., Watzl C., Giese T., Luckner C., Kropf P., Müller I., Ho A.D., Munder M. Regulation of NK cell function by human granulocyte arginase. J. Immunol., 2009, Vol. 182, no. 9, pp. 5259-5267.</mixed-citation></citation-alternatives></ref><ref id="cit76"><label>76</label><citation-alternatives><mixed-citation xml:lang="ru">Obermajer N., Wong J.L., Edwards R.P., Chen K., Scott M., Khader S., Kolls J.K., Kunle Odunsi, Billiar T.R. and Kalinski P. Induction and stability of human Th17 cells require endogenous NOS2 and cGMP-dependent NO signaling. J. Exp. Med., 2013, Vol. 210, pp. 1433-1445.</mixed-citation><mixed-citation xml:lang="en">Obermajer N., Wong J.L., Edwards R.P., Chen K., Scott M., Khader S., Kolls J.K., Kunle Odunsi, Billiar T.R. and Kalinski P. Induction and stability of human Th17 cells require endogenous NOS2 and cGMP-dependent NO signaling. J. Exp. Med., 2013, Vol. 210, pp. 1433-1445.</mixed-citation></citation-alternatives></ref><ref id="cit77"><label>77</label><citation-alternatives><mixed-citation xml:lang="ru">Papapetropoulos A., Garcia-Cardena G., Madri J.A., Sessa W.C. Nitric oxide production contributes to the angiogenic properties of vascular endothelial growth factor in human endothelial cells. J. Clin. Invest., 1997, Vol. 100, no. 12, pp. 3131-3139.</mixed-citation><mixed-citation xml:lang="en">Papapetropoulos A., Garcia-Cardena G., Madri J.A., Sessa W.C. Nitric oxide production contributes to the angiogenic properties of vascular endothelial growth factor in human endothelial cells. J. Clin. Invest., 1997, Vol. 100, no. 12, pp. 3131-3139.</mixed-citation></citation-alternatives></ref><ref id="cit78"><label>78</label><citation-alternatives><mixed-citation xml:lang="ru">Park I.-S., Kang S.-W., Shin Y.-J., Chae K.-Y., Park M.-O., Kim M.-Y., Wheatley D.N., Min B.-H. Arginine deiminase: a potential inhibitor of angiogenesis and tumour growth. British Journal of Cancer, 2003, Vol. 89, pp. 907-914.</mixed-citation><mixed-citation xml:lang="en">Park I.-S., Kang S.-W., Shin Y.-J., Chae K.-Y., Park M.-O., Kim M.-Y., Wheatley D.N., Min B.-H. Arginine deiminase: a potential inhibitor of angiogenesis and tumour growth. British Journal of Cancer, 2003, Vol. 89, pp. 907-914.</mixed-citation></citation-alternatives></ref><ref id="cit79"><label>79</label><citation-alternatives><mixed-citation xml:lang="ru">Pekarek L.A., Starr B.A., Toledano A.Y., Schreiber H. Inhibition of tumor growth by elimination of granulocytes. J. Exp. Med., 1995, Vol. 181, pp. 435-440.</mixed-citation><mixed-citation xml:lang="en">Pekarek L.A., Starr B.A., Toledano A.Y., Schreiber H. Inhibition of tumor growth by elimination of granulocytes. J. Exp. Med., 1995, Vol. 181, pp. 435-440.</mixed-citation></citation-alternatives></ref><ref id="cit80"><label>80</label><citation-alternatives><mixed-citation xml:lang="ru">Pernow J., Jung C. Arginase as a potential targetin the treatment of cardiovascular disease: reversal of arginine steal? Cardiovasc. Res., 2013, Vol. 98, no. 3, pp. 334-343.</mixed-citation><mixed-citation xml:lang="en">Pernow J., Jung C. Arginase as a potential targetin the treatment of cardiovascular disease: reversal of arginine steal? Cardiovasc. Res., 2013, Vol. 98, no. 3, pp. 334-343.</mixed-citation></citation-alternatives></ref><ref id="cit81"><label>81</label><citation-alternatives><mixed-citation xml:lang="ru">Phillips M.M., Sheaﬀ M.T., Szlosarek P.W. Targeting arginine-dependent cancers with arginine-degrading enzymes: opportunities and challenges. Cancer. Res. Treat., 2013, Vol. 45, no. 4, pp. 251-562.</mixed-citation><mixed-citation xml:lang="en">Phillips M.M., Sheaﬀ M.T., Szlosarek P.W. Targeting arginine-dependent cancers with arginine-degrading enzymes: opportunities and challenges. Cancer. Res. Treat., 2013, Vol. 45, no. 4, pp. 251-562.</mixed-citation></citation-alternatives></ref><ref id="cit82"><label>82</label><citation-alternatives><mixed-citation xml:lang="ru">Raber P., Ochoa A.C., Rodriguez P.C. Metabolism of L-Arginine by Myeloid-Derived Suppressor Cells in Cancer: Mechanisms of T cell suppression and Therapeutic Perspectives. Immunol. Invest., 2012, Vol. 41, no. 6-7, pp. 614-634.</mixed-citation><mixed-citation xml:lang="en">Raber P., Ochoa A.C., Rodriguez P.C. Metabolism of L-Arginine by Myeloid-Derived Suppressor Cells in Cancer: Mechanisms of T cell suppression and Therapeutic Perspectives. Immunol. Invest., 2012, Vol. 41, no. 6-7, pp. 614-634.</mixed-citation></citation-alternatives></ref><ref id="cit83"><label>83</label><citation-alternatives><mixed-citation xml:lang="ru">Rabier D., Kamoun P. Metabolism of citrulline in man. Amino Acid., 1995, Vol. 9, pp. 299-316.</mixed-citation><mixed-citation xml:lang="en">Rabier D., Kamoun P. Metabolism of citrulline in man. Amino Acid., 1995, Vol. 9, pp. 299-316.</mixed-citation></citation-alternatives></ref><ref id="cit84"><label>84</label><citation-alternatives><mixed-citation xml:lang="ru">Racke K., Warnken M. L-Arginine Metabolic Pathways. The Open Nitric Oxide Journal, 2010, Vol. 2, pp. 9-19.</mixed-citation><mixed-citation xml:lang="en">Racke K., Warnken M. L-Arginine Metabolic Pathways. The Open Nitric Oxide Journal, 2010, Vol. 2, pp. 9-19.</mixed-citation></citation-alternatives></ref><ref id="cit85"><label>85</label><citation-alternatives><mixed-citation xml:lang="ru">Raijman L. Citrulline synthesis in rat tissues and liver content of carbamoyl phosphate and ornithine. Biochem. J., 1974, Vol. 138, pp. 225-232.</mixed-citation><mixed-citation xml:lang="en">Raijman L. Citrulline synthesis in rat tissues and liver content of carbamoyl phosphate and ornithine. Biochem. J., 1974, Vol. 138, pp. 225-232.</mixed-citation></citation-alternatives></ref><ref id="cit86"><label>86</label><citation-alternatives><mixed-citation xml:lang="ru">Ramirez M., Wek R.C., Vazquez de Aldana C.R., Jackson B.M., Freeman B., Hinnebusch A.G. Mutations activating the yeast eIF-2 alpha kinase GCN2: isolation of alleles altering the domain related to histidyl-tRNA synthetases. Mol. Cell. Biol., 1992, Vol. 12, no. 12, pp. 5801-5815.</mixed-citation><mixed-citation xml:lang="en">Ramirez M., Wek R.C., Vazquez de Aldana C.R., Jackson B.M., Freeman B., Hinnebusch A.G. Mutations activating the yeast eIF-2 alpha kinase GCN2: isolation of alleles altering the domain related to histidyl-tRNA synthetases. Mol. Cell. Biol., 1992, Vol. 12, no. 12, pp. 5801-5815.</mixed-citation></citation-alternatives></ref><ref id="cit87"><label>87</label><citation-alternatives><mixed-citation xml:lang="ru">Rato C., Amirova S.R., Declan G.B., Stansﬁeld I., Wallace H.M. Translational recoding as a feedback controller: systems approaches reveal polyamine-speciﬁc eﬀects on the antizyme ribosomal frameshiﬅ. Nucleic Acids Res., 2011, Vol. 39, no. 11, pp. 4587-4597.</mixed-citation><mixed-citation xml:lang="en">Rato C., Amirova S.R., Declan G.B., Stansﬁeld I., Wallace H.M. Translational recoding as a feedback controller: systems approaches reveal polyamine-speciﬁc eﬀects on the antizyme ribosomal frameshiﬅ. Nucleic Acids Res., 2011, Vol. 39, no. 11, pp. 4587-4597.</mixed-citation></citation-alternatives></ref><ref id="cit88"><label>88</label><citation-alternatives><mixed-citation xml:lang="ru">Rodriguez P.C., Zea A.H., DeSalvo J., Culotta K.S., Zabaleta J., Quiceno D.G., Ochoa J.B., Ochoa A.C. L-arginine consumption by macrophages modulates the expression of CD3 zeta chain in T lymphocytes. J. Immunol., 2003, Vol. 171, no. 3, pp. 1232-1239.</mixed-citation><mixed-citation xml:lang="en">Rodriguez P.C., Zea A.H., DeSalvo J., Culotta K.S., Zabaleta J., Quiceno D.G., Ochoa J.B., Ochoa A.C. L-arginine consumption by macrophages modulates the expression of CD3 zeta chain in T lymphocytes. J. Immunol., 2003, Vol. 171, no. 3, pp. 1232-1239.</mixed-citation></citation-alternatives></ref><ref id="cit89"><label>89</label><citation-alternatives><mixed-citation xml:lang="ru">Saha S., Kashina A. Posttranslational Arginylation as a Global Biological Regulator. Dev. Biol., 2011, Vol. 358, no. 1, pp. 1-8.</mixed-citation><mixed-citation xml:lang="en">Saha S., Kashina A. Posttranslational Arginylation as a Global Biological Regulator. Dev. Biol., 2011, Vol. 358, no. 1, pp. 1-8.</mixed-citation></citation-alternatives></ref><ref id="cit90"><label>90</label><citation-alternatives><mixed-citation xml:lang="ru">Saini A.S., Shenoy G.N., Rath S., Bal V., George A. Inducible nitric oxide synthase is a major intermediate in signaling pathways for the survival of plasma cells. Nat. Immunol., 2014, Vol. 15, pp. 275-282.</mixed-citation><mixed-citation xml:lang="en">Saini A.S., Shenoy G.N., Rath S., Bal V., George A. Inducible nitric oxide synthase is a major intermediate in signaling pathways for the survival of plasma cells. Nat. Immunol., 2014, Vol. 15, pp. 275-282.</mixed-citation></citation-alternatives></ref><ref id="cit91"><label>91</label><citation-alternatives><mixed-citation xml:lang="ru">Santhanam L., Lim H.K., Lim H.K., Miriel V., Brown T., Patel M., Balanson S., Ryoo S., Anderson M., Irani K., Khanday F., Di Costanzo L., Nyhan D., Hare J.M., Christianson D.W., Rivers R., Shoukas A., Berkowitz D.E. Inducible NO synthase dependent S-nitrosylation and activation of arginase1 contribute to age-related endothelial dysfunction. Circ. Res., 2007, Vol. 101, pp. 692-702.</mixed-citation><mixed-citation xml:lang="en">Santhanam L., Lim H.K., Lim H.K., Miriel V., Brown T., Patel M., Balanson S., Ryoo S., Anderson M., Irani K., Khanday F., Di Costanzo L., Nyhan D., Hare J.M., Christianson D.W., Rivers R., Shoukas A., Berkowitz D.E. Inducible NO synthase dependent S-nitrosylation and activation of arginase1 contribute to age-related endothelial dysfunction. Circ. Res., 2007, Vol. 101, pp. 692-702.</mixed-citation></citation-alternatives></ref><ref id="cit92"><label>92</label><citation-alternatives><mixed-citation xml:lang="ru">Savaraj N., You M., Wu C., Wangpaichitr M., Kuo M.T., Feun L.G. Arginine deprivation, autophagy, apoptosis (AAA) for the treatment of melanoma. Curr. Mol. Med., 2010, Vol. 10, pp. 405-412.</mixed-citation><mixed-citation xml:lang="en">Savaraj N., You M., Wu C., Wangpaichitr M., Kuo M.T., Feun L.G. Arginine deprivation, autophagy, apoptosis (AAA) for the treatment of melanoma. Curr. Mol. Med., 2010, Vol. 10, pp. 405-412.</mixed-citation></citation-alternatives></ref><ref id="cit93"><label>93</label><citation-alternatives><mixed-citation xml:lang="ru">Schneemann M., Schoeden G. Macrophage biology and immunology: man is not a mouse. J. Leukoc. Biol., 2007, Vol. 81, no. 3, p. 579.</mixed-citation><mixed-citation xml:lang="en">Schneemann M., Schoeden G. Macrophage biology and immunology: man is not a mouse. J. Leukoc. Biol., 2007, Vol. 81, no. 3, p. 579.</mixed-citation></citation-alternatives></ref><ref id="cit94"><label>94</label><citation-alternatives><mixed-citation xml:lang="ru">Schneemann M., Schoedon G. Species diﬀerences in macrophage NO production are important. Nat. Immunol., 2002, Vol. 3, no. 2, p. 102.</mixed-citation><mixed-citation xml:lang="en">Schneemann M., Schoedon G. Species diﬀerences in macrophage NO production are important. Nat. Immunol., 2002, Vol. 3, no. 2, p. 102.</mixed-citation></citation-alternatives></ref><ref id="cit95"><label>95</label><citation-alternatives><mixed-citation xml:lang="ru">Scotton C.J., Martinez F.O., Smelt M.J., Sironi M., Locati M., Mantovani A., Sozzani S. Transcriptional proﬁling reveals complex regulation of the monocyte IL-1β system by IL-13. J. Immunol., 2005, Vol. 174, pp. 834-845.</mixed-citation><mixed-citation xml:lang="en">Scotton C.J., Martinez F.O., Smelt M.J., Sironi M., Locati M., Mantovani A., Sozzani S. Transcriptional proﬁling reveals complex regulation of the monocyte IL-1β system by IL-13. J. Immunol., 2005, Vol. 174, pp. 834-845.</mixed-citation></citation-alternatives></ref><ref id="cit96"><label>96</label><citation-alternatives><mixed-citation xml:lang="ru">Takahashi Y., Mai M., Nishioka K. alpha-diﬂuoromethylornithine induces apoptosis as well as anti-angiogenesis in the inhibition of tumor growth and metastasis in a human gastric cancer model. Int. J. Cancer, 2000, Vol. 85, no. 2, pp. 243-247.</mixed-citation><mixed-citation xml:lang="en">Takahashi Y., Mai M., Nishioka K. alpha-diﬂuoromethylornithine induces apoptosis as well as anti-angiogenesis in the inhibition of tumor growth and metastasis in a human gastric cancer model. Int. J. Cancer, 2000, Vol. 85, no. 2, pp. 243-247.</mixed-citation></citation-alternatives></ref><ref id="cit97"><label>97</label><citation-alternatives><mixed-citation xml:lang="ru">Takaku H., Takase M., Abe S., Hayashi H., Miyazaki K. In vivo antitumour activity of arginine deiminase puriﬁed from Mycoplasma arginine. Int. J. Cancer, 1992, Vol. 51, pp. 244-249.</mixed-citation><mixed-citation xml:lang="en">Takaku H., Takase M., Abe S., Hayashi H., Miyazaki K. In vivo antitumour activity of arginine deiminase puriﬁed from Mycoplasma arginine. Int. J. Cancer, 1992, Vol. 51, pp. 244-249.</mixed-citation></citation-alternatives></ref><ref id="cit98"><label>98</label><citation-alternatives><mixed-citation xml:lang="ru">Tasaki T., Kwon Y.T. The mammalian N-end rule pathway: new insights into its components and physiological roles. Trends Biochem. Sci., 2007, Vol. 32, no. 11, pp. 520-528.</mixed-citation><mixed-citation xml:lang="en">Tasaki T., Kwon Y.T. The mammalian N-end rule pathway: new insights into its components and physiological roles. Trends Biochem. Sci., 2007, Vol. 32, no. 11, pp. 520-528.</mixed-citation></citation-alternatives></ref><ref id="cit99"><label>99</label><citation-alternatives><mixed-citation xml:lang="ru">Tezuka H., Abe Y., Iwata M., Takeuchi H., Ishikawa H., Matsushita M., Shiohara T., Akira S., Ohteki T. Regulation of IgA production by naturally occurring TNF/iNOS-producing dendritic cell. Nature, 2007, Vol. 448, pp. 929-933.</mixed-citation><mixed-citation xml:lang="en">Tezuka H., Abe Y., Iwata M., Takeuchi H., Ishikawa H., Matsushita M., Shiohara T., Akira S., Ohteki T. Regulation of IgA production by naturally occurring TNF/iNOS-producing dendritic cell. Nature, 2007, Vol. 448, pp. 929-933.</mixed-citation></citation-alternatives></ref><ref id="cit100"><label>100</label><citation-alternatives><mixed-citation xml:lang="ru">Thomas A.C., Mattila J.T. “Of mice and men”: arginine metabolism in macrophages. Front Immunol., 2014, Vol. 5, p. 479.</mixed-citation><mixed-citation xml:lang="en">Thomas A.C., Mattila J.T. “Of mice and men”: arginine metabolism in macrophages. Front Immunol., 2014, Vol. 5, p. 479.</mixed-citation></citation-alternatives></ref><ref id="cit101"><label>101</label><citation-alternatives><mixed-citation xml:lang="ru">Thomas J.B., Holtsberg F.W., Ensor C.M., Bomalaski J.S., Clark M.A. Enzymic degradation of plasma arginine using arginine deiminase inhibits nitric oxide production and protects mice from the lethal eﬀects of tumour necrosis factor alpha and endotoxin. Biochem. J., 2002, Vol. 363, pp. 581-587.</mixed-citation><mixed-citation xml:lang="en">Thomas J.B., Holtsberg F.W., Ensor C.M., Bomalaski J.S., Clark M.A. Enzymic degradation of plasma arginine using arginine deiminase inhibits nitric oxide production and protects mice from the lethal eﬀects of tumour necrosis factor alpha and endotoxin. Biochem. J., 2002, Vol. 363, pp. 581-587.</mixed-citation></citation-alternatives></ref><ref id="cit102"><label>102</label><citation-alternatives><mixed-citation xml:lang="ru">Tumurkhuu G., Koide N., Dagvadorj J., Noman A.S.M., Khuda I.I.-E., Naiki Y., Komatsu T., Yoshida T., Yokochi T. B1 cells produce nitric oxide in response to a series of toll-like receptor ligands. Cell. Immunol., 2010, Vol. 261, pp. 122-127.</mixed-citation><mixed-citation xml:lang="en">Tumurkhuu G., Koide N., Dagvadorj J., Noman A.S.M., Khuda I.I.-E., Naiki Y., Komatsu T., Yoshida T., Yokochi T. B1 cells produce nitric oxide in response to a series of toll-like receptor ligands. Cell. Immunol., 2010, Vol. 261, pp. 122-127.</mixed-citation></citation-alternatives></ref><ref id="cit103"><label>103</label><citation-alternatives><mixed-citation xml:lang="ru">Villalobo A. Nitric oxide and cell proliferation. FEBS J., 2006, Vol. 273, no. 11, pp. 2329-2344.</mixed-citation><mixed-citation xml:lang="en">Villalobo A. Nitric oxide and cell proliferation. FEBS J., 2006, Vol. 273, no. 11, pp. 2329-2344.</mixed-citation></citation-alternatives></ref><ref id="cit104"><label>104</label><citation-alternatives><mixed-citation xml:lang="ru">Wakabayashi Y., Yamada E., Yoshida T., Takahashi H. Arginine becomes an essential amino acid aﬅer massive resection of rat small intestine. J. Biol. Chem., 1994, Vol. 269, no. 51, pp. 32667-32671.</mixed-citation><mixed-citation xml:lang="en">Wakabayashi Y., Yamada E., Yoshida T., Takahashi H. Arginine becomes an essential amino acid aﬅer massive resection of rat small intestine. J. Biol. Chem., 1994, Vol. 269, no. 51, pp. 32667-32671.</mixed-citation></citation-alternatives></ref><ref id="cit105"><label>105</label><citation-alternatives><mixed-citation xml:lang="ru">Wek R.C., Ramirez M., Jackson B.M., Hinnebusch A.G. Identiﬁcation of positive-acting domains in GCN2 protein kinase required for translational activation of GCN4 expressio. Mol. Cell. Biol., 1990, Vol. 10, no. 6, pp. 2820-2831.</mixed-citation><mixed-citation xml:lang="en">Wek R.C., Ramirez M., Jackson B.M., Hinnebusch A.G. Identiﬁcation of positive-acting domains in GCN2 protein kinase required for translational activation of GCN4 expressio. Mol. Cell. Biol., 1990, Vol. 10, no. 6, pp. 2820-2831.</mixed-citation></citation-alternatives></ref><ref id="cit106"><label>106</label><citation-alternatives><mixed-citation xml:lang="ru">Wek S.A., Zhu S., Wek R.C. The histidyl-tRNA synthetase-related sequence in the eIF-2 alpha protein kinase GCN2 interacts with tRNA and is required for activation in response to starvation for diﬀerent amino acids. Mol. Cell. Biol., 1995, Vol. 8, pp. 4497-5506.</mixed-citation><mixed-citation xml:lang="en">Wek S.A., Zhu S., Wek R.C. The histidyl-tRNA synthetase-related sequence in the eIF-2 alpha protein kinase GCN2 interacts with tRNA and is required for activation in response to starvation for diﬀerent amino acids. Mol. Cell. Biol., 1995, Vol. 8, pp. 4497-5506.</mixed-citation></citation-alternatives></ref><ref id="cit107"><label>107</label><citation-alternatives><mixed-citation xml:lang="ru">Whiteside T.L., Rabinowich H. The role of Fas/FasL in immunosuppression induced by human tumors. Cancer Immunol Immunother., 1998, Vol. 46, pp. 175-184.</mixed-citation><mixed-citation xml:lang="en">Whiteside T.L., Rabinowich H. The role of Fas/FasL in immunosuppression induced by human tumors. Cancer Immunol Immunother., 1998, Vol. 46, pp. 175-184.</mixed-citation></citation-alternatives></ref><ref id="cit108"><label>108</label><citation-alternatives><mixed-citation xml:lang="ru">Windmueller H.G., Spaeth A.E. Source and fate of circulating citrulline. Am. J. Physiol., 1981, Vol. 241, pp. 473-480.</mixed-citation><mixed-citation xml:lang="en">Windmueller H.G., Spaeth A.E. Source and fate of circulating citrulline. Am. J. Physiol., 1981, Vol. 241, pp. 473-480.</mixed-citation></citation-alternatives></ref><ref id="cit109"><label>109</label><citation-alternatives><mixed-citation xml:lang="ru">Winterhoﬀ N., Goethe R., Gruening P., Rohde M., Kalisz H., Smith H.E., Valentin-Weigand P. Identiﬁcation and characterization of two temperature-induced surface-associated proteins of Streptococcus suis with high homologies to members of the Arginine Deiminase system of Streptococcus pyogenes. J. Bacteriol., 2002, Vol. 184, no. 24, pp. 6768-6776.</mixed-citation><mixed-citation xml:lang="en">Winterhoﬀ N., Goethe R., Gruening P., Rohde M., Kalisz H., Smith H.E., Valentin-Weigand P. Identiﬁcation and characterization of two temperature-induced surface-associated proteins of Streptococcus suis with high homologies to members of the Arginine Deiminase system of Streptococcus pyogenes. J. Bacteriol., 2002, Vol. 184, no. 24, pp. 6768-6776.</mixed-citation></citation-alternatives></ref><ref id="cit110"><label>110</label><citation-alternatives><mixed-citation xml:lang="ru">Wirawan E., Vanden Berghe T., Lippens S., Agostinis P., Vandenabeele P. Autophagy: for better or for worse. Cell Res., 2012, Vol. 1, no. 43-61.</mixed-citation><mixed-citation xml:lang="en">Wirawan E., Vanden Berghe T., Lippens S., Agostinis P., Vandenabeele P. Autophagy: for better or for worse. Cell Res., 2012, Vol. 1, no. 43-61.</mixed-citation></citation-alternatives></ref><ref id="cit111"><label>111</label><citation-alternatives><mixed-citation xml:lang="ru">Witte M.B., Barbul A. Arginine physiology and its implication for wound healing. Wound Repair Regen., 2003, Vol. 11, pp. 419-423.</mixed-citation><mixed-citation xml:lang="en">Witte M.B., Barbul A. Arginine physiology and its implication for wound healing. Wound Repair Regen., 2003, Vol. 11, pp. 419-423.</mixed-citation></citation-alternatives></ref><ref id="cit112"><label>112</label><citation-alternatives><mixed-citation xml:lang="ru">Wu G., Brosnan N.T. Macrophages can convert citrulline into arginine. Biochem. J., 1992, Vol. 281, pp. 45-48. 113. Wynn T.A., Chawla A. and Pollard J.W. Macrophage biology in development, homeostasis and disease. Nature, 2013. Vol. 496, pp. 445-456.</mixed-citation><mixed-citation xml:lang="en">Wu G., Brosnan N.T. Macrophages can convert citrulline into arginine. Biochem. J., 1992, Vol. 281, pp. 45-48. 113. Wynn T.A., Chawla A. and Pollard J.W. Macrophage biology in development, homeostasis and disease. Nature, 2013. Vol. 496, pp. 445-456.</mixed-citation></citation-alternatives></ref><ref id="cit113"><label>113</label><citation-alternatives><mixed-citation xml:lang="ru">Xia Y., Roman L.J., Masters B.S., Zweier J.L. Inducible nitric-oxide synthase generates superoxide from the reductase domain. J. Biol. Chem., 1998, Vol. 273, pp. 22635-22639.</mixed-citation><mixed-citation xml:lang="en">Xia Y., Roman L.J., Masters B.S., Zweier J.L. Inducible nitric-oxide synthase generates superoxide from the reductase domain. J. Biol. Chem., 1998, Vol. 273, pp. 22635-22639.</mixed-citation></citation-alternatives></ref><ref id="cit114"><label>114</label><citation-alternatives><mixed-citation xml:lang="ru">Yang J., Zhang R., Lu G., Shen Y., Peng L., Zhu C., Cui M., Wang W., Arnaboldi P., Tang M., Gupta M., Qi C. F., Jayaraman P., Zhu H., Jiang B., Chen S.-h., He J.C., Ting A.T., Zhou M.-MKuchroo V.K., Morse H.C., III, Ozato K., Sikora A.G., Xiong H. T cell-derived inducible nitric oxide synthase switches oﬀ Th17 cell diﬀerentiation. J. Exp. Med., 2013, Vol. 210, pp. 1447-1462.</mixed-citation><mixed-citation xml:lang="en">Yang J., Zhang R., Lu G., Shen Y., Peng L., Zhu C., Cui M., Wang W., Arnaboldi P., Tang M., Gupta M., Qi C. F., Jayaraman P., Zhu H., Jiang B., Chen S.-h., He J.C., Ting A.T., Zhou M.-MKuchroo V.K., Morse H.C., III, Ozato K., Sikora A.G., Xiong H. T cell-derived inducible nitric oxide synthase switches oﬀ Th17 cell diﬀerentiation. J. Exp. Med., 2013, Vol. 210, pp. 1447-1462.</mixed-citation></citation-alternatives></ref><ref id="cit115"><label>115</label><citation-alternatives><mixed-citation xml:lang="ru">Yoshida J., Takamura S., Suzuki S. Cell growth inhibitory action of SAGP, an antitumor glycoprotein from Streptococcus pyogenes (Su strain). Jpn. J. Pharmacol., 1987, Vol. 5, no. 2, pp. 143-147.</mixed-citation><mixed-citation xml:lang="en">Yoshida J., Takamura S., Suzuki S. Cell growth inhibitory action of SAGP, an antitumor glycoprotein from Streptococcus pyogenes (Su strain). Jpn. J. Pharmacol., 1987, Vol. 5, no. 2, pp. 143-147.</mixed-citation></citation-alternatives></ref><ref id="cit116"><label>116</label><citation-alternatives><mixed-citation xml:lang="ru">Yoshida J., Takamura S., Nishio M. Characterization of a streptococcal antitumor glycoprotein (SAGP). Life Sci., 11998, Vol. 2, no. 12, pp. 1043-1053.</mixed-citation><mixed-citation xml:lang="en">Yoshida J., Takamura S., Nishio M. Characterization of a streptococcal antitumor glycoprotein (SAGP). Life Sci., 11998, Vol. 2, no. 12, pp. 1043-1053.</mixed-citation></citation-alternatives></ref><ref id="cit117"><label>117</label><citation-alternatives><mixed-citation xml:lang="ru">Zea A.H., Rodriguez P.C., Culotta K.S., Hernandez C.P., DeSalvo J., Ochoa J.B., Park H.J., Zabaleta J., Ochoa A.C. l-Arginine modulates CD3zeta expression and T cell function in activated human T lymphocytes. Cell Immunol., 2004, Vol. 232, pp. 21-31.</mixed-citation><mixed-citation xml:lang="en">Zea A.H., Rodriguez P.C., Culotta K.S., Hernandez C.P., DeSalvo J., Ochoa J.B., Park H.J., Zabaleta J., Ochoa A.C. l-Arginine modulates CD3zeta expression and T cell function in activated human T lymphocytes. Cell Immunol., 2004, Vol. 232, pp. 21-31.</mixed-citation></citation-alternatives></ref><ref id="cit118"><label>118</label><citation-alternatives><mixed-citation xml:lang="ru">Zhang R., Wang L., Zhang L., Chen J., Zhu Z., Zhang Z., Chopp M. Nitric oxide enhances angiogenesis via the synthesis of vascular endothelial growth factor and cGMP aﬅer stroke in the rat. Circ. Res., 2003, Vol. 92, pp. 308-313.</mixed-citation><mixed-citation xml:lang="en">Zhang R., Wang L., Zhang L., Chen J., Zhu Z., Zhang Z., Chopp M. Nitric oxide enhances angiogenesis via the synthesis of vascular endothelial growth factor and cGMP aﬅer stroke in the rat. Circ. Res., 2003, Vol. 92, pp. 308-313.</mixed-citation></citation-alternatives></ref><ref id="cit119"><label>119</label><citation-alternatives><mixed-citation xml:lang="ru">Zharikov S., Krotova K., Hu H., Baylis C., Johnson R.J., Block E.R., Patel J. Uric acid decreases NO production and increases arginase activity in cultured pulmonary artery endothelial cells. Am. J. Physiol. Cell. Physiol., 2008, Vol. 295, pp. 1183-1190.</mixed-citation><mixed-citation xml:lang="en">Zharikov S., Krotova K., Hu H., Baylis C., Johnson R.J., Block E.R., Patel J. Uric acid decreases NO production and increases arginase activity in cultured pulmonary artery endothelial cells. Am. J. Physiol. Cell. Physiol., 2008, Vol. 295, pp. 1183-1190.</mixed-citation></citation-alternatives></ref><ref id="cit120"><label>120</label><citation-alternatives><mixed-citation xml:lang="ru">Zhu M.Y., Iyo A., Piletz J.E., Regunathan S. Expression of human arginine decarboxylase, the biosynthetic enzyme for agmatine. Biochim. Biophys. Acta, 2004, Vol. 1670, no. 2, pp. 156-164.</mixed-citation><mixed-citation xml:lang="en">Zhu M.Y., Iyo A., Piletz J.E., Regunathan S. Expression of human arginine decarboxylase, the biosynthetic enzyme for agmatine. Biochim. Biophys. Acta, 2004, Vol. 1670, no. 2, pp. 156-164.</mixed-citation></citation-alternatives></ref><ref id="cit121"><label>121</label><citation-alternatives><mixed-citation xml:lang="ru">Zhuo W., Song X., Zhou H., Luo Y. Arginine deiminase modulates endothelial tip cells via excessive synthesis of reactive oxygen species. Biochem. Soc. Trans., 2011, Vol. 5, pp. 1376-1381.</mixed-citation><mixed-citation xml:lang="en">Zhuo W., Song X., Zhou H., Luo Y. Arginine deiminase modulates endothelial tip cells via excessive synthesis of reactive oxygen species. Biochem. Soc. Trans., 2011, Vol. 5, pp. 1376-1381.</mixed-citation></citation-alternatives></ref></ref-list><fn-group><fn fn-type="conflict"><p>The authors declare that there are no conflicts of interest present.</p></fn></fn-group></back></article>
