<?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">vetpress</journal-id><journal-title-group><journal-title xml:lang="ru">Аграрная наука</journal-title><trans-title-group xml:lang="en"><trans-title>Agrarian science</trans-title></trans-title-group></journal-title-group><issn pub-type="ppub">0869-8155</issn><issn pub-type="epub">2686-701X</issn><publisher><publisher-name>Редакция журнала "Аграрная наука"</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="doi">10.32634/0869-8155-2025-390-01-57-70</article-id><article-id custom-type="elpub" pub-id-type="custom">vetpress-3405</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>ВЕТЕРИНАРИЯ</subject></subj-group><subj-group subj-group-type="section-heading" xml:lang="en"><subject>VETERINARY MEDICINE</subject></subj-group></article-categories><title-group><article-title>Лизосомальные катионные белки как основа клеточного и гуморального иммунитета животных: роль нейтрофильных внеклеточных ловушек в иммунном гомеостазе (обзор)</article-title><trans-title-group xml:lang="en"><trans-title>Lysosomal cationic proteins as the basis of cellular and humoral immunity of animals: the role of neutrophil extracellular traps (NETs) in immune homeostasis (review)</trans-title></trans-title-group></title-group><contrib-group><contrib contrib-type="author" corresp="yes"><contrib-id contrib-id-type="orcid">https://orcid.org/0000-0002-2326-651X</contrib-id><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Колесник</surname><given-names>Е. А.</given-names></name><name name-style="western" xml:lang="en"><surname>Kolesnik</surname><given-names>E. A.</given-names></name></name-alternatives><bio xml:lang="ru"><p>Евгений Анатольевич Колесник, доктор биологических наук, профессор кафедры физиологии, экологии человека и медико-биологических знаний</p><p>ул. Радио, 10А, стр. 2, Москва, 105005</p></bio><bio xml:lang="en"><p>Evgeniy Anatolyevich Kolesnik, Doctor of Biological Sciences, Professor of the Department of Physiology, Human Ecology and Medical and Biological Knowledge</p><p>10A/2 Radio Str., Moscow, 105005</p></bio><email xlink:type="simple">evgeniy251082@mail.ru</email><xref ref-type="aff" rid="aff-1"/></contrib><contrib contrib-type="author" corresp="yes"><contrib-id contrib-id-type="orcid">https://orcid.org/0000-0003-3818-0556</contrib-id><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Дерхо</surname><given-names>М. А.</given-names></name><name name-style="western" xml:lang="en"><surname>Derkho</surname><given-names>M. A.</given-names></name></name-alternatives><bio xml:lang="ru"><p>Марина Аркадьевна Дерхо, доктор биологических наук, профессор, заведующая кафедрой естественно-научных дисциплин</p><p>ул. им. Гагарина, 13, Троицк, 457100</p></bio><bio xml:lang="en"><p>Marina Arkadyevna Derkho, Doctor of Biological Sciences, Professor, Head of the Department of Natural Sciences</p><p>13 Gagarin Str., Troitsk, 457100</p></bio><email xlink:type="simple">derkho2010@yandex.ru</email><xref ref-type="aff" rid="aff-2"/></contrib><contrib contrib-type="author" corresp="yes"><contrib-id contrib-id-type="orcid">https://orcid.org/0000-0003-0857-5143</contrib-id><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Ребезов</surname><given-names>М. Б.</given-names></name><name name-style="western" xml:lang="en"><surname>Rebezov</surname><given-names>M. B.</given-names></name></name-alternatives><bio xml:lang="ru"><p>Максим Борисович Ребезов, доктор сельскохозяйственных наук, кандидат ветеринарных наук, профессор, главный научный сотрудник; доктор сельскохозяйственных наук, кандидат ветеринарных наук, профессор кафедры биотехнологии и пищевых продуктов</p><p>ул. им. Талалихина, 26, Москва, 109316</p><p>ул. им. Карла Либкнехта, 42, Екатеринбург, 620075</p></bio><bio xml:lang="en"><p>Maksim Borisovich Rebezov, Doctor of Agricultural Sciences, Candidate of Veterinary Sciences, Professor, Chief Researcher; Doctor of Agricultural Sciences, Candidate of Veterinary Sciences, Professor of the Department of Biotechnology and Food Products</p><p>26 Talalikhin Str., Moscow, 109316</p><p>42 Karl Liebknecht Str., Yekaterinburg, 620075</p></bio><email xlink:type="simple">rebezov@ya.ru</email><xref ref-type="aff" rid="aff-3"/></contrib></contrib-group><aff-alternatives id="aff-1"><aff xml:lang="ru"><institution>Государственный университет просвещения</institution><country>Россия</country></aff><aff xml:lang="en"><institution>Federal State University of Education</institution><country>Russian Federation</country></aff></aff-alternatives><aff-alternatives id="aff-2"><aff xml:lang="ru"><institution>Южно-Уральский государственный аграрный университет</institution><country>Россия</country></aff><aff xml:lang="en"><institution>South Ural State Agrarian University</institution><country>Russian Federation</country></aff></aff-alternatives><aff-alternatives id="aff-3"><aff xml:lang="ru"><institution>Федеральный научный центр пищевых систем&#13;
им. В.М. Горбатова Российской академии наук ; Уральский государственный аграрный университет</institution><country>Россия</country></aff><aff xml:lang="en"><institution>Gorbatov Research Center for Food Systems ; Ural State Agrarian University</institution><country>Russian Federation</country></aff></aff-alternatives><pub-date pub-type="collection"><year>2025</year></pub-date><pub-date pub-type="epub"><day>28</day><month>01</month><year>2025</year></pub-date><volume>1</volume><issue>1</issue><fpage>57</fpage><lpage>70</lpage><permissions><copyright-statement>Copyright &amp;#x00A9; Колесник Е.А., Дерхо М.А., Ребезов М.Б., 2025</copyright-statement><copyright-year>2025</copyright-year><copyright-holder xml:lang="ru">Колесник Е.А., Дерхо М.А., Ребезов М.Б.</copyright-holder><copyright-holder xml:lang="en">Kolesnik E.A., Derkho M.A., Rebezov M.B.</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.vetpress.ru/jour/article/view/3405">https://www.vetpress.ru/jour/article/view/3405</self-uri><abstract><p>Актуальность. Лизосомальные катионные белки (ЛКБ) гранулоцитарных лейкоцитов (эластаза, катепсин G, протеиназа-3, кальгранулин, кателицидины, дефензины, лактоферрин, протегрины) активны в отношении вирусов, бактерий, грибов, простейших. Отмечаются вопросы физиологических регуляторных, иммунных и патологических воздействий ЛКБ и их производных — нейтрофильных (гетерофильных) внеклеточных ловушек (НВЛ) — на патогены, здоровые клеточные и тканевые структуры организма.Результаты. Инкреция гранулоцитами ЛКБ реализуется: 1. мерокриновым типом — путем дегрануляции; 2. экзоцитозом и ложной дегрануляцией, то есть процессом декатионизации лизосом, содержащих гранулы катионных протеинов с апокриновым или голокриновым типом секреции. Декатионизация реализует экзоцитоз ЛКБ, экструзию из клетки интактных лизосом с ЛКБ, диффундирование ЛКБ через мембрану лизосом. Реакции дегрануляции лизосом с ЛКБ формируют фаголизосомы и инициируют фагоцитоз, реакции декатионизации лизосом с ЛКБ — обеспечивают формирование и функции НВЛ. НВЛ формируются нелитическим (нелизируемым) и литическим (лизируемым) путем при септическом и асептическом воспалении, при онтогенетическом развитии звеньев иммунитета. НВЛ стереотипно образуются внутрисосудисто при асептическом воспалении, оксидативном стрессе и в физиологическом режиме, при стимуляции гранулоцитов продуктами окислительного метаболизма. На модельном организме птиц (Aves) за счет применения цитохимического теста с высокочувствительным кислотно-щелочным бромфеноловым синим индикатором изучены субклеточные и клеточные проявления физиологической возрастной иммунной активности катионных протеинов кумулированных в лизосомах гранулоцитов, изучены неспецифические адаптационные реакции (НАР) позвоночных в раннем постнатальном онтогенезе. В основе формирования НАР реализуются взаимосвязи групп лейкоцитов (лимфоцитов, моноцитов и гранулоцитов) с динамикой их лизосомальных катионных белков. Метод расчета уровня активности и потенциальных возможностей гранулоцитов в фагоцитарных реакциях и при формировании НВЛ включает индексы, характеризующие направления и интенсивность иммунных реакций гранулоцитов с учетом процессов: 1. дегрануляции лизосом с ЛКБ — в инициации клеточного фагоцитарного звена; 2. декатионизации лизосом с ЛКБ — в инициации внеклеточных ловушек, участвующих в реализации гуморального звена иммунитета.</p></abstract><trans-abstract xml:lang="en"><p>Relevance. Lysosomal cationic proteins (LCP) of granulocytic leukocytes: elastase, cathepsin G, proteinase-3, calgranulin, cathelicidins, defensins, lactoferrin, protegrins are active against viruses, bacteria, fungi, protozoa. The issues of physiological regulatory, immune and pathological effects of LCP and their derivatives – neutrophil (heterophil) extracellular traps (NETs) on pathogens, healthy cellular and tissue structures of the body are noted.Results. The increment of LCP granulocytes is realized by: 1. merocrine type — by degranulation; 2. exocytosis and false degranulation, that is, the process of decationization of lysosomes containing granules of cationic proteins with apocrine or holocrine type of secretion. Decationization implements exocytosis of LCP, extrusion of intact lysosomes from the cell with LCP, and diffusion of LCP through the lysosome membrane. Lysosome degranulation reactions with LCP form phagolysosomes and initiate phagocytosis, lysosome decationization reactions with LCP ensure the formation and functions of NETs. NETs is formed by non-lytic (non-lytic) and lytic (lyzed) pathways in septic and aseptic inflammation, with the ontogenetic development of immune links. NETs is stereotypically formed intravascular during aseptic inflammation, oxidative stress and in a physiological regime, when granulocytes are stimulated by products of oxidative metabolism. Using a cytochemical test with a highly sensitive acid-base bromophenol blue indicator, subcellular and cellular manifestations of the physiological age-related immune activity of cationic proteins accumulated in granulocyte lysosomes were studied on the avian model organism (Aves), and nonspecific adaptive reactions (NAR) of vertebrates in early postnatal ontogenesis were studied. The basis for the formation of NAR is the relationship of groups of leukocytes (lymphocytes, monocytes and granulocytes) with the dynamics of their lysosomal cationic proteins. The method for calculating the level of activity and potential capabilities of granulocytes in phagocytic reactions and in the formation of .NETs includes indices characterizing the directions and intensity of immune reactions of granulocytes, taking into account the processes: 1. degranulation of lysosomes with LCP — in the initiation of the cellular phagocytic link; 2. decationization of lysosomes with LCP — in the initiation of extracellular traps involved in the implementation of the humoral link of immunity.</p></trans-abstract><kwd-group xml:lang="ru"><kwd>лизосомальные катионные белки</kwd><kwd>лизосомы</kwd><kwd>фаголизосомы</kwd><kwd>фагосомы</kwd><kwd>нейтрофильные внеклеточные ловушки</kwd><kwd>дегрануляция</kwd><kwd>декатионизация</kwd><kwd>иммунный ответ</kwd><kwd>клеточный иммунитет</kwd><kwd>гуморальный иммунитет</kwd><kwd>иммунный гомеостаз</kwd><kwd>морфология крови</kwd><kwd>гранулоциты</kwd><kwd>гетерофилы</kwd></kwd-group><kwd-group xml:lang="en"><kwd>lysosomal cationic proteins</kwd><kwd>lysosomes</kwd><kwd>phagolysosomes</kwd><kwd>phagosomes</kwd><kwd>neutrophil extracellular traps</kwd><kwd>degranulation</kwd><kwd>decationization</kwd><kwd>immune response</kwd><kwd>cellular immunity</kwd><kwd>humoral immunity</kwd><kwd>immune homeostasis</kwd><kwd>blood morphology</kwd><kwd>granulocytes</kwd><kwd>heterophils</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">Бережная Н.М. Нейтрофилы и иммунологический гомеостаз. Киев: Наукова думка. 1988; 187. ISBN 5-12-000251-X</mixed-citation><mixed-citation xml:lang="en">Berezhnaya N.M. Neutrophils and immunological homeostasis. Kyiv: Naukova dumka. 1988; 187 (in Russian). ISBN 5-12-000251-X</mixed-citation></citation-alternatives></ref><ref id="cit2"><label>2</label><citation-alternatives><mixed-citation xml:lang="ru">Borregaard N., Cowland J.B. Granules of the Human Neutrophilic Polymorphonuclear Leukocyte. Blood. 1997; 89(10): 3503-3521. https://doi.org/10.1182/blood.V89.10.3503</mixed-citation><mixed-citation xml:lang="en">Borregaard N., Cowland J.B. Granules of the Human Neutrophilic Polymorphonuclear Leukocyte. Blood. 1997; 89(10): 3503-3521. https://doi.org/10.1182/blood.V89.10.3503</mixed-citation></citation-alternatives></ref><ref id="cit3"><label>3</label><citation-alternatives><mixed-citation xml:lang="ru">Soehnlein O., Weber C., Lindbom L. Neutrophil granule proteins tune monocytic cell function. Trends in Immunology. 2009; 30(11): 538-546. https://doi.org/10.1016/j.it.2009.06.006</mixed-citation><mixed-citation xml:lang="en">Soehnlein O., Weber C., Lindbom L. Neutrophil granule proteins tune monocytic cell function. Trends in Immunology. 2009; 30(11): 538-546. https://doi.org/10.1016/j.it.2009.06.006</mixed-citation></citation-alternatives></ref><ref id="cit4"><label>4</label><citation-alternatives><mixed-citation xml:lang="ru">Пигаревский В.Е. Зернистые лейкоциты и их свойства. М.: Медицина. 1978; 127.</mixed-citation><mixed-citation xml:lang="en">Pigarevsky V.E. Granular leukocytes and their properties. Moscow: Meditsina. 1978; 127 (in Russian).</mixed-citation></citation-alternatives></ref><ref id="cit5"><label>5</label><citation-alternatives><mixed-citation xml:lang="ru">Wu Z. etal. Fumonisin B1 induces chicken heterophil extracellular traps mediated by PAD4 enzyme and P2 x 1 receptor. Poultry Science. 2022; 101(1): 101550. https://doi.org/10.10167j.psj.2021.101550</mixed-citation><mixed-citation xml:lang="en">Wu Z. et al. Fumonisin B1 induces chicken heterophil extracellular traps mediated by PAD4 enzyme and P2 x 1 receptor. Poultry Science. 2022; 101(1): 101550. https://doi.org/10.1016/j.psj.2021.101550</mixed-citation></citation-alternatives></ref><ref id="cit6"><label>6</label><citation-alternatives><mixed-citation xml:lang="ru">Chen Y etal. Citrinin stimulated heterophil extracellular trap formation in chickens. Molecular Immunology. 2022; 152: 27-34. https://doi.Org/10.1016/j.molimm.2022.09.014</mixed-citation><mixed-citation xml:lang="en">Chen Y et al . Citrinin stimulated heterophil extracellular trap formation in chickens. Molecular Immunology. 2022; 152: 27-34. https://doi.org/10.1016/j.molimm.2022.09.014</mixed-citation></citation-alternatives></ref><ref id="cit7"><label>7</label><citation-alternatives><mixed-citation xml:lang="ru">Wu H. etal. The release of FB₁-induced heterophil extracellular traps in chicken is dependent on autophagy and glycolysis. Poultry Science. 2023; 102(4): 102511. https://doi.org/10.1016/j.psj.2023.102511</mixed-citation><mixed-citation xml:lang="en">Wu H. et al. The release of FB1-induced heterophil extracellular traps in chicken is dependent on autophagy and glycolysis. Poultry Science. 2023; 102(4): 102511. https://doi.org/10.1016Zj.psj.2023.102511</mixed-citation></citation-alternatives></ref><ref id="cit8"><label>8</label><citation-alternatives><mixed-citation xml:lang="ru">Lima-Gomes Pd.S. etal. Chick heterophils release DNA extracellular traps (DETs) in vitro and in vivo upon Aspergillus fumigatus conidia exposure. Microbes and Infection. 2024; 26(3): 105261. https://doi.org/10.1016/j.micinf.2023.105261</mixed-citation><mixed-citation xml:lang="en">Lima-Gomes Pd.S. et al. Chick heterophils release DNA extracellular traps (DETs) in vitro and in vivo upon Aspergillus fumigatus conidia exposure. Microbes and Infection. 2024; 26(3): 105261. https://doi.org/10.1016/j.micinf.2023.105261</mixed-citation></citation-alternatives></ref><ref id="cit9"><label>9</label><citation-alternatives><mixed-citation xml:lang="ru">Brinkmann V., Zychlinsky A. Beneficial suicide: why neutrophils die to make NETs. Nature Reviews Microbiology. 2007; 5(8): 577-582. https://doi.org/10.1038/nrmicro1710</mixed-citation><mixed-citation xml:lang="en">Brinkmann V., Zychlinsky A. Beneficial suicide: why neutrophils die to make NETs. Nature Reviews Microbiology. 2007; 5(8): 577-582. https://doi.org/10.1038/nrmicro1710</mixed-citation></citation-alternatives></ref><ref id="cit10"><label>10</label><citation-alternatives><mixed-citation xml:lang="ru">Horwitz M., Benson K.F., Duan Z., Li F.-Q., Person R.E. Hereditary neutropenia: dogs explain human neutrophil elastase mutations. Trends in Molecular Medicine. 2004; 10(4): 163-170. https://doi.org/10.1016/j.molmed.2004.02.002</mixed-citation><mixed-citation xml:lang="en">Horwitz M., Benson K.F., Duan Z., Li F.-Q., Person R.E. Hereditary neutropenia: dogs explain human neutrophil elastase mutations. Trends in Molecular Medicine. 2004; 10(4): 163-170. https://doi.org/10.1016/j.molmed.2004.02.002</mixed-citation></citation-alternatives></ref><ref id="cit11"><label>11</label><citation-alternatives><mixed-citation xml:lang="ru">Brinkmann V. et al. Neutrophil Extracellular Traps Kill Bacteria. Science. 2004; 303(5663): 1532-1535. https://doi.org/10.1126/science.1092385</mixed-citation><mixed-citation xml:lang="en">Brinkmann V. et al. Neutrophil Extracellular Traps Kill Bacteria. Science. 2004; 303(5663): 1532-1535. https://doi.org/10.1126/science.1092385</mixed-citation></citation-alternatives></ref><ref id="cit12"><label>12</label><citation-alternatives><mixed-citation xml:lang="ru">Averhoff P, Kolbe M., Zychlinsky A., Weinrauch Y Single Residue Determines the Specificity of Neutrophil Elastase for Shigella Virulence Factors. Journal of Molecular Biology. 2008; 377(4): 1053-1066. https://doi.org/10.1016/jJmb.2007.12.034</mixed-citation><mixed-citation xml:lang="en">Averhoff P, Kolbe M., Zychlinsky A., Weinrauch Y Single Residue Determines the Specificity of Neutrophil Elastase for Shigella Virulence Factors. Journal of Molecular Biology. 2008; 377(4): 1053-1066. https://doi.org/10.1016/jJmb.2007.12.034</mixed-citation></citation-alternatives></ref><ref id="cit13"><label>13</label><citation-alternatives><mixed-citation xml:lang="ru">Urban C.F. et al. Neutrophil Extracellular Traps Contain Calprotectin, a Cytosolic Protein Complex Involved in Host Defense against Candida albicans. PLoS Pathogens. 2009; 5(10): e1000639. https://doi.org/10.1371/journal.ppat.1000639</mixed-citation><mixed-citation xml:lang="en">Urban C.F. et al. Neutrophil Extracellular Traps Contain Calprotectin, a Cytosolic Protein Complex Involved in Host Defense against Candida albicans. PLoS Pathogens. 2009; 5(10): e1000639. https://doi.org/10.1371/journal.ppat.1000639</mixed-citation></citation-alternatives></ref><ref id="cit14"><label>14</label><citation-alternatives><mixed-citation xml:lang="ru">Bianchi M., Niemiec M.J., Siler U., Urban C.F., Reichenbach J. Restoration of anti-Aspergillus defense by neutrophil extracellular traps in human chronic granulomatous disease alter gene therapy is calprotectin-dependent. The Journal of Allergy and Clinical Immunology. 2011; 127(5): 1243-1252.e7. https://doi.org/10.1016/jJaci.2011.01.021</mixed-citation><mixed-citation xml:lang="en">Bianchi M., Niemiec M.J., Siler U., Urban C.F., Reichenbach J. Restoration of anti-Aspergillus defense by neutrophil extracellular traps in human chronic granulomatous disease after gene therapy is calprotectin-dependent. The Journal of Allergy and Clinical Immunology. 2011; 127(5): 1243-1252.e7. https://doi.org/10.1016/jJaci.2011.01.021</mixed-citation></citation-alternatives></ref><ref id="cit15"><label>15</label><citation-alternatives><mixed-citation xml:lang="ru">Chen C.X.-J., Soto I., Guo Y-L., Liu Y Control of Secondary Granule Release in Neutrophils by Ral GTPase. Journal of Biological Chemistry. 2011; 286(13): 11724-11733. https://doi.org/10.1074/jbc.M110.154203</mixed-citation><mixed-citation xml:lang="en">Chen C.X.-J., Soto I., Guo Y-L., Liu Y Control of Secondary Granule Release in Neutrophils by Ral GTPase. Journal of Biological Chemistry. 2011; 286(13): 11724-11733. https://doi.org/10.1074/jbc.M110.154203</mixed-citation></citation-alternatives></ref><ref id="cit16"><label>16</label><citation-alternatives><mixed-citation xml:lang="ru">Серов В.В., Шехтер А.Б. Соединительная ткань: функциональная морфология и общая патология. М.: Медицина. 1981; 312.</mixed-citation><mixed-citation xml:lang="en">Serov V.V., Shekhter A.B. Connective tissue: functional morphology and general pathology. Moscow: Meditsina. 1981; 312 (in Russian).</mixed-citation></citation-alternatives></ref><ref id="cit17"><label>17</label><citation-alternatives><mixed-citation xml:lang="ru">Witko-Sarsat V., Rieu P, Descamps-Latscha B., Lesavre P, Halbwachs-Mecarelli L. Neutrophils: Molecules, Functions and Pathophysiological Aspects. Laboratory Investigation. 2000; 80(5): 617-653. https://doi.org/10.1038/labinvest.3780067</mixed-citation><mixed-citation xml:lang="en">Witko-Sarsat V., Rieu P, Descamps-Latscha B., Lesavre P, Halbwachs-Mecarelli L. Neutrophils: Molecules, Functions and Pathophysiological Aspects. Laboratory Investigation. 2000; 80(5): 617-653. https://doi.org/10.1038/labinvest.3780067</mixed-citation></citation-alternatives></ref><ref id="cit18"><label>18</label><citation-alternatives><mixed-citation xml:lang="ru">Soehnlein O., Lindbom L., Weber C. Mechanisms underlying neutrophil-mediated monocyte recruitment. Blood. 2009; 114(21): 4613-4623. https://doi.org/10.1182/blood-2009-06-221630</mixed-citation><mixed-citation xml:lang="en">Soehnlein O., Lindbom L., Weber C. Mechanisms underlying neutrophil-mediated monocyte recruitment. Blood. 2009; 114(21): 4613-4623. https://doi.org/10.1182/blood-2009-06-221630</mixed-citation></citation-alternatives></ref><ref id="cit19"><label>19</label><citation-alternatives><mixed-citation xml:lang="ru">Нестерова И.В., Колесникова Н.В., Чудилова Г.А., Ломтатидзе Л.В., Ковалева С.В., Евглевский А.А. Нейтрофильные гранулоциты: новый взгляд на «старых игроков» на иммунологическом поле. Иммунология. 2015; 36(4): 257-265. https://www.elibrary.ru/umhqkj</mixed-citation><mixed-citation xml:lang="en">Nesterova I.V., Kolesnikova N.V., Chudilova G.A., Lomtatidze L.V., Kovaleva S.V, Evglevsky A.A. Neutrophilic granulocytes: a new look at “old players” on the immunological field. Immunologiya. 2015; 36(4): 257-265 (in Russian). https://www.elibrary.ru/umhqkj</mixed-citation></citation-alternatives></ref><ref id="cit20"><label>20</label><citation-alternatives><mixed-citation xml:lang="ru">Mocsai A. Diverse novel functions of neutrophils in immunity, inflammation, and beyond. Journal of Experimental Medicine. 2013; 210(7): 1283-1299. https://doi.org/10.1084/jem.20122220</mixed-citation><mixed-citation xml:lang="en">Mocsai A. Diverse novel functions of neutrophils in immunity, inflammation, and beyond. Journal of Experimental Medicine. 2013; 210(7): 1283-1299. https://doi.org/10.1084/jem.20122220</mixed-citation></citation-alternatives></ref><ref id="cit21"><label>21</label><citation-alternatives><mixed-citation xml:lang="ru">Sheshachalam A., Srivastava N., Mitchell T., Lacy P, Eitzen G. Granule protein processing and regulated secretion in neutrophils. Frontiers in Immunology. 2014; 5: 448. https://doi.org/10.3389/fimmu.2014.00448</mixed-citation><mixed-citation xml:lang="en">Sheshachalam A., Srivastava N., Mitchell T., Lacy P, Eitzen G. Granule protein processing and regulated secretion in neutrophils. Frontiers in Immunology. 2014; 5: 448. https://doi.org/10.3389/fimmu.2014.00448</mixed-citation></citation-alternatives></ref><ref id="cit22"><label>22</label><citation-alternatives><mixed-citation xml:lang="ru">Bystrom J., Amin K., Bishop-Bailey D. Analysing the eosinophil cationic protein — a clue to the function of the eosinophil granulocyte Respiratory Research. 2011; 12: 10. https://doi.org/10.1186/1465-9921-12-10</mixed-citation><mixed-citation xml:lang="en">Bystrom J., Amin K., Bishop-Bailey D. Analysing the eosinophil cationic protein — a clue to the function of the eosinophil granulocyte. Respiratory Research. 2011; 12: 10. https://doi.org/10.1186/1465-9921-12-10</mixed-citation></citation-alternatives></ref><ref id="cit23"><label>23</label><citation-alternatives><mixed-citation xml:lang="ru">Clark R.A., Olsson I., Klebanoff S.J. Cytotoxicity for tumor cells of cationic proteins from human neutrophil granules. Journal of Cell Biology. 1976; 70(3): 719-723. https://doi.org/10.1083/jcb.70.3J19</mixed-citation><mixed-citation xml:lang="en">Clark R.A., Olsson I., Klebanoff S.J. Cytotoxicity for tumor cells of cationic proteins from human neutrophil granules. Journal of Cell Biology. 1976; 70(3): 719-723. https://doi.org/10.1083/jcb.70.3J19</mixed-citation></citation-alternatives></ref><ref id="cit24"><label>24</label><citation-alternatives><mixed-citation xml:lang="ru">Tal T., Sharabani M., Aviram I. Cationic proteins of neutrophil azurophilic granules: protein-protein interaction and blockade of NADPH oxidase activation. Journal of Leukocyte Biology. 1998; 63(3): 305-311. https://doi.org/10.1002/jlb.63.3.305</mixed-citation><mixed-citation xml:lang="en">Tal T., Sharabani M., Aviram I. Cationic proteins of neutrophil azurophilic granules: protein-protein interaction and blockade of NADPH oxidase activation. Journal of Leukocyte Biology. 1998; 63(3): 305-311. https://doi.org/10.1002/jlb.63.3.305</mixed-citation></citation-alternatives></ref><ref id="cit25"><label>25</label><citation-alternatives><mixed-citation xml:lang="ru">Papayannopoulos V. Neutrophil extracellular traps in immunity anc disease. Nature Reviews Immunology. 2018; 18(2): 134-147. https://doi.org/10.1038/nri.2017.105</mixed-citation><mixed-citation xml:lang="en">Papayannopoulos V. Neutrophil extracellular traps in immunity and disease. Nature Reviews Immunology. 2018; 18(2): 134-147. https://doi.org/10.1038/nri.2017.105</mixed-citation></citation-alternatives></ref><ref id="cit26"><label>26</label><citation-alternatives><mixed-citation xml:lang="ru">Thiam H.R., Wong S.L., Wagner D.D., Waterman C.M. Cellular Mechanisms of NETosis. Annual Review of Cell and Developmental Biology. 2020; 36: 191-218. https://doi.org/10.1146/annurev-ceNbio-020520-111016</mixed-citation><mixed-citation xml:lang="en">Thiam H.R., Wong S.L., Wagner D.D., Waterman C.M. Cellular Mechanisms of NETosis. Annual Review of Cell and Developmental Biology. 2020; 36: 191-218. https://doi.org/10.1146/annurev-cellbio-020520-111016</mixed-citation></citation-alternatives></ref><ref id="cit27"><label>27</label><citation-alternatives><mixed-citation xml:lang="ru">Cochrane C.G. The participation of cells in the inflammatory injury of tissue. The Journal of Investigative Dermatology. 1975; 64(5): 301-306. https://doi.org/10.1111/1523-1747.ep12512255</mixed-citation><mixed-citation xml:lang="en">Cochrane C.G. The participation of cells in the inflammatory injury of tissue. The Journal of Investigative Dermatology. 1975; 64(5): 301-306. https://doi.org/10.1111/1523-1747.ep12512255</mixed-citation></citation-alternatives></ref><ref id="cit28"><label>28</label><citation-alternatives><mixed-citation xml:lang="ru">Ranadive N.S., Cochrane C.G. Mechanism of Histamine Release from Mast Cells by Cationic Protein (Band 2) from Neutrophil Lysosomes. The Journal of Immunology. 1971; 106(2): 506-516. https://doi.org/10.4049/jimmunol.106.2.506</mixed-citation><mixed-citation xml:lang="en">Ranadive N.S., Cochrane C.G. Mechanism of Histamine Release from Mast Cells by Cationic Protein (Band 2) from Neutrophil Lysosomes. The Journal of Immunology. 1971; 106(2): 506-516. https://doi.org/10.4049/jimmunol.106.2.506</mixed-citation></citation-alternatives></ref><ref id="cit29"><label>29</label><citation-alternatives><mixed-citation xml:lang="ru">Нагоев Б.С. Очерки о нейтрофильном гранулоците. Нальчик: Эльбрус. 1986; 142.</mixed-citation><mixed-citation xml:lang="en">Nagoyev B.S. Essays on the neutrophilic granulocyte. Nalchik: Elbrus. 1986; 142 (in Russian).</mixed-citation></citation-alternatives></ref><ref id="cit30"><label>30</label><citation-alternatives><mixed-citation xml:lang="ru">Шубич М.Г. Выявление катионного белка в цитоплазме лейкоцитов с помощью бромфенолового синего. Цитология. 1974; 16(10): 1321-1322. https://www.elibrary.ru/qbthxd</mixed-citation><mixed-citation xml:lang="en">Shubich M.G. Detection of cationic proteins in the cytoplasm of leukocytes with the use of bromphenol blue. Tsitologiya. 1974; 16(10): 1321-1322 (in Russian). https://www.elibrary.ru/qbthxd</mixed-citation></citation-alternatives></ref><ref id="cit31"><label>31</label><citation-alternatives><mixed-citation xml:lang="ru">Нагоев Б.С. Качественные и количественные показатели лизосомального катионного белка лейкоцитов у здоровых людей. Лабораторное дело. 1983; (6): 6-9.</mixed-citation><mixed-citation xml:lang="en">Nagoyev B.S. Qualitative and quantitative indices of lysosomal cationic leukocyte protein in healthy persons. Laboratornoye delo. 1983; (6): 6-9 (in Russian).</mixed-citation></citation-alternatives></ref><ref id="cit32"><label>32</label><citation-alternatives><mixed-citation xml:lang="ru">Дробот Г.П., Забиякин В.А., Степанова А.Е., Смоленцев С.Ю. Динамика цитохимических показателей псевдоэозинофилов крови цесарок. Российская сельскохозяйственная наука. 2017; (1): 42-44. https://www.elibrary.ru/xtdnvf</mixed-citation><mixed-citation xml:lang="en">Drobot G.P, Zabiyakin VA., Stepanova A.E., Smolentsev S.Yu. Dynamics of cytochemical indicators of psevdoeozinofilov [sic!] blood of guinea fowl. Rossiyskaya sel'skokhozyaystvennaya nauka. 2017; (1): 42-44 (in Russian). https://www.elibrary.ru/xtdnvf</mixed-citation></citation-alternatives></ref><ref id="cit33"><label>33</label><citation-alternatives><mixed-citation xml:lang="ru">Колесник Е.А., Дерхо М.А., Лебедева И.А. Комплексная морфофизиологическая характеристика иммунного лизосомального катионного белка лейкоцитов в раннем онтогенезе бройлерных кур. Ученые записки Казанского университета. Серия: Естественные науки. 2019; 161(3): 440-458. https://doi.org/10.26907/2542-064X.2019.3.440-458</mixed-citation><mixed-citation xml:lang="en">Kolesnik E.A., Derkho M.A., Lebedeva I.A. Comprehensive morphophysiological description of the immune lysosomal cationic protein of leukocytes in the early ontogeny of broiler chickens. Uchenye Zapiski Kazanskogo Universiteta . Series: Estestvennye Nauki. 2019; 161(3): 440-458 (in Russian). https://doi.org/10.26907/2542-064X.2019.3.440-458</mixed-citation></citation-alternatives></ref><ref id="cit34"><label>34</label><citation-alternatives><mixed-citation xml:lang="ru">Pourtabrizi M., Shahtahmassebi N., Sharifmoghadam M.R. Bromophenol blue doped in nano-droplet: spectroscopy, nonlinear optical properties and Staphylococcus aureus treatment. Optical and Quantum Electronics. 2021; 53: 1. https://doi.org/10.1007/s11082-020-02634-9</mixed-citation><mixed-citation xml:lang="en">Pourtabrizi M., Shahtahmassebi N., Sharifmoghadam M.R. Bromophenol blue doped in nano-droplet: spectroscopy, nonlinear optical properties and Staphylococcus aureus treatment. Optical and Quantum Electronics. 2021; 53: 1. https://doi.org/10.1007/s11082-020-02634-9</mixed-citation></citation-alternatives></ref><ref id="cit35"><label>35</label><citation-alternatives><mixed-citation xml:lang="ru">Plaza-Garrido M., Salinas-Garcia M.C., Alba-Elena D., Martinez J.C., Camara-Artigas A. Lysozyme crystals dyed with bromophenol blue: where has the dye gone?. Acta Crystallographica Section D: Structural Biology. 2020; 76(9): 845-856. https://doi.org/10.1107/S2059798320008803</mixed-citation><mixed-citation xml:lang="en">Plaza-Garrido M., Salinas-Garcia M.C., Alba-Elena D., Martinez J.C., Camara-Artigas A. Lysozyme crystals dyed with bromophenol blue: where has the dye gone?. Acta Crystallographica Section D: Structural Biology. 2020; 76(9): 845-856. https://doi.org/10.1107/S2059798320008803</mixed-citation></citation-alternatives></ref><ref id="cit36"><label>36</label><citation-alternatives><mixed-citation xml:lang="ru">Barron A.J., Agrawal S., Lesperance D.N.A., Doucette J., Calle S., Broderick N.A. Microbiome-derived acidity protects against microbial invasion in Drosophila. Cell Reports. 2024; 43(4): 114087. https://doi.org/10.1016Zj.celrep.2024.114087</mixed-citation><mixed-citation xml:lang="en">Barron A.J., Agrawal S., Lesperance D.N.A., Doucette J., Calle S., Broderick N.A. Microbiome-derived acidity protects against microbial invasion in Drosophila. Cell Reports. 2024; 43(4): 114087. https://doi.org/10.1016/j.celrep.2024.114087</mixed-citation></citation-alternatives></ref><ref id="cit37"><label>37</label><citation-alternatives><mixed-citation xml:lang="ru">Pastore A., Badocco D., Cappellin L., Pastore P Modeling the Dichromatic Behavior of Bromophenol Blue to Enhance the Analytical Performance of pH Colorimetric Sensor Arrays. Chemosensors. 2022; 10(2): 87. https://doi.org/10.3390/chemosensors10020087</mixed-citation><mixed-citation xml:lang="en">Pastore A., Badocco D., Cappellin L., Pastore P Modeling the Dichromatic Behavior of Bromophenol Blue to Enhance the Analytical Performance of pH Colorimetric Sensor Arrays. Chemosensors. 2022; 10(2): 87. https://doi.org/10.3390/chemosensors10020087</mixed-citation></citation-alternatives></ref><ref id="cit38"><label>38</label><citation-alternatives><mixed-citation xml:lang="ru">Мазинг Ю.А. Функциональная морфология катионных белков лизосом нейтрофильных гранулоцитов. Вопросы медицинской химии. 1990; 36(6): 8-10.</mixed-citation><mixed-citation xml:lang="en">Mazing Yu.A. Functional morphology of lysosomal cationic proteins in neutrophilic granulocytes. Voprosy meditsinskoy khimii. 1990; 36(6): 8-10 (in Russian).</mixed-citation></citation-alternatives></ref><ref id="cit39"><label>39</label><citation-alternatives><mixed-citation xml:lang="ru">Chuammitri Р, Ostojic J., Andreasen C.B., Redmond S.B., Lamont S.J., Palic D. Chicken heterophil extracellular traps (HETs): Novel defense mechanism of chicken heterophils. Veterinary Immunology and Immunopathology. 2009; 129(1-2): 126-131. https://doi.org/10.1016/j.vetimm.2008.12.013</mixed-citation><mixed-citation xml:lang="en">Chuammitri P, Ostojic J., Andreasen C.B., Redmond S.B., Lamont S.J., Palic D. Chicken heterophil extracellular traps (HETs): Novel defense mechanism of chicken heterophils. Veterinary Immunology and Immunopathology. 2009; 129(1-2): 126-131. https://doi.org/10.1016/j.vetimm.2008.12.013</mixed-citation></citation-alternatives></ref><ref id="cit40"><label>40</label><citation-alternatives><mixed-citation xml:lang="ru">Jones M.P Avian Hematology. Clinics in Laboratory Medicine. 2015; 35(3): 649-659. https://doi.org/10.1016/j.cll.2015.05.013</mixed-citation><mixed-citation xml:lang="en">Jones M.P Avian Hematology. Clinics in Laboratory Medicine. 2015; 35(3): 649-659. https://doi.org/10.1016/j.cll.2015.05.013</mixed-citation></citation-alternatives></ref><ref id="cit41"><label>41</label><citation-alternatives><mixed-citation xml:lang="ru">Колесник Е.А. Цитофизиологические и математические критерии оценки фаголизосом и нейтрофильных внеклеточных ловушек в клеточном и гуморальном звеньях иммунитета. 2nd Congress of the International Society for Clinical Physiology and Pathology(ISCPP2024). Moscow. 2024; 24-26. https://doi.org/10.5281/zenodo.13739047</mixed-citation><mixed-citation xml:lang="en">Kolesnik E.A. Cytophysiological and mathematical criteria for assessing phagolysosomes and neutrophil extracellular traps in the cellular and humoral immunity. 2nd Congress of the International Society for Clinical Physiology and Pathology (ISCPP2024). Moscow. 2024; 24-26 (in Russian). https://doi.org/10.5281/zenodo.13739047</mixed-citation></citation-alternatives></ref><ref id="cit42"><label>42</label><citation-alternatives><mixed-citation xml:lang="ru">Колесник Е.А., Дерхо М.А. Об участии гипофизарно-адренокортикальных гормонов в регуляции клеточного пула крови у цыплят-бройлеров. Проблемы биологии продуктивных животных. 2018; (1): 64-74. https://doi.org/10.25687/1996-6733.prodanimbiol.2018.1.64-74</mixed-citation><mixed-citation xml:lang="en">Kolesnik E.A., Derkho M.A. About participation of pituitary-adrenocortical hormones in regulation of blood cellular pool in chicken-broilers. Problems of Productive Animal Biology. 2018; (1): 64-74 (in Russian). https://doi.org/10.25687/1996-6733.prodanimbiol.2018.1.64-74</mixed-citation></citation-alternatives></ref><ref id="cit43"><label>43</label><citation-alternatives><mixed-citation xml:lang="ru">Rada B. Neutrophil Extracellular Traps. Knaus U., Leto T. (eds.). NADPH Oxidases. Methods in Molecular Biology. New York, NY: Humana. 2019; 1982: 517-528. https://doi.org/10.1007/978-1-4939-9424-3_31</mixed-citation><mixed-citation xml:lang="en">Rada B. Neutrophil Extracellular Traps. Knaus U., Leto T. (eds.). NADPH Oxidases. Methods in Molecular Biology. New York, NY: Humana. 2019; 1982: 517-528. https://doi.org/10.1007/978-1-4939-9424-3_31</mixed-citation></citation-alternatives></ref><ref id="cit44"><label>44</label><citation-alternatives><mixed-citation xml:lang="ru">Metzler K.D., Goosmann C., Lubojemska A., Zychlinsky A., Papayannopoulos V. A Myeloperoxidase-Containing Complex Regulates Neutrophil Elastase Release and Actin Dynamics during NETosis. Cell Reports. 2014; 8(3): 883-896. https://doi.org/10.1016/j.celrep.2014.06.044</mixed-citation><mixed-citation xml:lang="en">Metzler K.D., Goosmann C., Lubojemska A., Zychlinsky A., Papayannopoulos V. A Myeloperoxidase-Containing Complex Regulates Neutrophil Elastase Release and Actin Dynamics during NETosis. Cell Reports. 2014; 8(3): 883-896. https://doi.org/10.1016/j.celrep.2014.06.044</mixed-citation></citation-alternatives></ref><ref id="cit45"><label>45</label><citation-alternatives><mixed-citation xml:lang="ru">Kharisma V.D. etal. Garcinoxanthones from Garcinia mangostana L. tackle SARS-CoV-2 infection and cytokine storm pathway inhibition: A viroinformatics study. Journal of Pharmacy and Pharmacognosy Research. 2023; 11(5): 743-756. https://doi.org/10.56499/jppres23.1650_11.5J43</mixed-citation><mixed-citation xml:lang="en">Kharisma V.D. et al. Garcinoxanthones from Garcinia mangostana L. tackle SARS-CoV-2 infection and cytokine storm pathway inhibition: A viroinformatics study. Journal of Pharmacy and Pharmacognosy Research. 2023; 11(5): 743-756. https://doi.org/10.56499/jppres23.1650_11.5J43</mixed-citation></citation-alternatives></ref><ref id="cit46"><label>46</label><citation-alternatives><mixed-citation xml:lang="ru">Колесник Е.А., Дерхо М.А., Ребезов М.Б. Формы дегенерации клеток крови, их физиологическое и клиническое значение, механизмы образования, тени клеток в мазках крови птиц. Аграрная наука. 2024; (1): 65-74. https://doi.org/10.32634/0869-8155-2024-378-1-65-74</mixed-citation><mixed-citation xml:lang="en">Kolesnik E.A., Derkho M.A., Rebezov M.B. Forms of degeneration of blood cells, their physiological and clinical significance, mechanisms of formation, shadows of cells in blood smears of birds. Agrarian science. 2024; (1): 65-74 (in Russian). https://doi.org/10.32634/0869-8155-2024-378-1-65-74</mixed-citation></citation-alternatives></ref><ref id="cit47"><label>47</label><citation-alternatives><mixed-citation xml:lang="ru">Branzk N. etal. Neutrophils sense microbe size and selectively release neutrophil extracellular traps in response to large pathogens. Nature Immunology 2014; 15(11): 1017-1025. https://doi.org/10.1038/ni.2987</mixed-citation><mixed-citation xml:lang="en">Branzk N. et al. Neutrophils sense microbe size and selectively release neutrophil extracellular traps in response to large pathogens. Nature Immunology 2014; 15(11): 1017-1025. https://doi.org/10.1038/ni.2987</mixed-citation></citation-alternatives></ref><ref id="cit48"><label>48</label><citation-alternatives><mixed-citation xml:lang="ru">Delgado-Rizo V., Martinez-Guzman M.A., Iniguez-Gutierrez L., Garcia-Orozco A., Alvarado-Navarro A., Fafutis-Morris M. Neutrophil Extracellular Traps and Its Implications in Inflammation: An Overview. Frontiers in Immunology. 2017; (8): 81. https://doi.org/10.3389/fimmu.2017.00081</mixed-citation><mixed-citation xml:lang="en">Delgado-Rizo V., Martinez-Guzman M.A., Iniguez-Gutierrez L., Garcia-Orozco A., Alvarado-Navarro A., Fafutis-Morris M. Neutrophil Extracellular Traps and Its Implications in Inflammation: An Overview. Frontiers in Immunology. 2017; (8): 81. https://doi.org/10.3389/fimmu.2017.00081</mixed-citation></citation-alternatives></ref><ref id="cit49"><label>49</label><citation-alternatives><mixed-citation xml:lang="ru">Pilsczek F.H. et al. A Novel Mechanism of Rapid Nuclear Neutrophil Extracellular Trap Formation in Response to Staphylococcus aureus. The Journal of Immunology. 2010; 185(12): 7413-7425. https://doi.org/10.4049/jimmunol.1000675</mixed-citation><mixed-citation xml:lang="en">Pilsczek F.H. et al. A Novel Mechanism of Rapid Nuclear Neutrophil Extracellular Trap Formation in Response to Staphylococcus aureus. The Journal of Immunology. 2010; 185(12): 7413-7425. https://doi.org/10.4049/jimmunol.1000675</mixed-citation></citation-alternatives></ref><ref id="cit50"><label>50</label><citation-alternatives><mixed-citation xml:lang="ru">de Bont C.M., Koopman W.J.H., Boelens W.C., Pruijn G.J.M. Stimulus-dependent chromatin dynamics, citrullination, calcium signalling and ROS production during NET formation. Biochimica et Biophysica Acta (BBA) — Molecular Cell Research. 2018; 1865(11-A): 1621-1629. https://doi.org/10.1016/j.bbamcr.2018.08.014</mixed-citation><mixed-citation xml:lang="en">de Bont C.M., Koopman W.J.H., Boelens W.C., Pruijn G.J.M. Stimulus-dependent chromatin dynamics, citrullination, calcium signalling and ROS production during NET formation. Biochimica et Biophysica Acta (BBA) — Molecular Cell Research. 2018; 1865(11-A): 1621-1629. https://doi.org/10.1016/j.bbamcr.2018.08.014</mixed-citation></citation-alternatives></ref><ref id="cit51"><label>51</label><citation-alternatives><mixed-citation xml:lang="ru">Gupta A.K., Giaglis S., Hasler P, Hahn S. Efficient Neutrophil Extracellular Trap Induction Requires Mobilization of Both Intracellular and Extracellular Calcium Pools and Is Modulated by Cyclosporine A. PloS ONE. 2014; 9(5): e97088. https://doi.org/10.1371/journal.pone.0097088</mixed-citation><mixed-citation xml:lang="en">Gupta A.K., Giaglis S., Hasler P, Hahn S. Efficient Neutrophil Extracellular Trap Induction Requires Mobilization of Both Intracellular and Extracellular Calcium Pools and Is Modulated by Cyclosporine A. PloS ONE. 2014; 9(5): e97088. https://doi.org/10.1371/journal.pone.0097088</mixed-citation></citation-alternatives></ref><ref id="cit52"><label>52</label><citation-alternatives><mixed-citation xml:lang="ru">Rossaint J. et al. Synchronized integrin engagement and chemokine activation is crucial in neutrophil extracellular trap-mediated sterile inflammation. Blood. 2014; 123(16): 2573-2584. https://doi.org/10.1182/blood-2013-07-516484</mixed-citation><mixed-citation xml:lang="en">Rossaint J. et al. Synchronized integrin engagement and chemokine activation is crucial in neutrophil extracellular trap-mediated sterile inflammation. Blood. 2014; 123(16): 2573-2584. https://doi.org/10.1182/blood-2013-07-516484</mixed-citation></citation-alternatives></ref><ref id="cit53"><label>53</label><citation-alternatives><mixed-citation xml:lang="ru">Keshari R.S. et al. Cytokines Induced Neutrophil Extracellular Traps Formation: Implication for the Inflammatory Disease Condition. PloS ONE. 2012; 7(10): e48111. https://doi.org/10.1371/journal.pone.0048111</mixed-citation><mixed-citation xml:lang="en">Keshari R.S. et al. Cytokines Induced Neutrophil Extracellular Traps Formation: Implication for the Inflammatory Disease Condition. PloS ONE. 2012; 7(10): e48111. https://doi.org/10.1371/journal.pone.0048111</mixed-citation></citation-alternatives></ref><ref id="cit54"><label>54</label><citation-alternatives><mixed-citation xml:lang="ru">Schappe M.S. et al. Chanzyme TRPM7 Mediates the Ca2+ Influx Essential for Lipopolysaccharide-Induced Toll-Like Receptor 4 Endocytosis and Macrophage Activation. Immunity. 2018; 48(1): 59-74.e5. https://doi.org/10.1016/j.immuni.2017.11.026</mixed-citation><mixed-citation xml:lang="en">Schappe M.S. et al. Chanzyme TRPM7 Mediates the Ca2+ Influx Essential for Lipopolysaccharide-Induced Toll-Like Receptor 4 Endocytosis and Macrophage Activation. Immunity. 2018; 48(1): 59-74.e5. https://doi.org/10.1016/j.immuni.2017.11.026</mixed-citation></citation-alternatives></ref><ref id="cit55"><label>55</label><citation-alternatives><mixed-citation xml:lang="ru">Wang Y et al. Histone hypercitrullination mediates chromatin decondensation and neutrophil extracellular trap formation. Journal of Cell Biology. 2009; 184(2): 205-213. https://doi.org/10.1083/jcb.200806072</mixed-citation><mixed-citation xml:lang="en">Wang Y et al. Histone hypercitrullination mediates chromatin decondensation and neutrophil extracellular trap formation. Journal of Cell Biology. 2009; 184(2): 205-213. https://doi.org/10.1083/jcb.200806072</mixed-citation></citation-alternatives></ref><ref id="cit56"><label>56</label><citation-alternatives><mixed-citation xml:lang="ru">Kenny E.F. et al. Diverse stimuli engage different neutrophil extracellular trap pathways. eLife. 2017; 6: e24437. https://doi.org/10.7554/eLife.24437</mixed-citation><mixed-citation xml:lang="en">Kenny E.F. et al. Diverse stimuli engage different neutrophil extracellular trap pathways. eLife. 2017; 6: e24437. https://doi.org/10.7554/eLife.24437</mixed-citation></citation-alternatives></ref><ref id="cit57"><label>57</label><citation-alternatives><mixed-citation xml:lang="ru">Fuchs T.A. et al. Novel cell death program leads to neutrophil extracellular traps. Journal of Cell Biology. 2007; 176(2): 231-241. https://doi.org/10.1083/jcb.200606027</mixed-citation><mixed-citation xml:lang="en">Fuchs T.A. et al. Novel cell death program leads to neutrophil extracellular traps. Journal of Cell Biology. 2007; 176(2): 231-241. https://doi.org/10.1083/jcb.200606027</mixed-citation></citation-alternatives></ref><ref id="cit58"><label>58</label><citation-alternatives><mixed-citation xml:lang="ru">Sun B. et al. Citrullination of NF-kB p65 promotes its nuclear localization and TLR-induced expression of IL-1 p and TNFa. Science Immunology. 2017; 2(12): eaal3062. https://doi.org/10.1126/sciimmunol.aal3062</mixed-citation><mixed-citation xml:lang="en">Sun B. et al. Citrullination of NF-kB p65 promotes its nuclear localization and TLR-induced expression of IL-1 в and TNFa. Science Immunology. 2017; 2(12): eaal3062. https://doi.org/10.1126/sciimmunol.aal3062</mixed-citation></citation-alternatives></ref><ref id="cit59"><label>59</label><citation-alternatives><mixed-citation xml:lang="ru">Li Y, Werth V.P., Mall M., Liu M.-L. Nuclear lamin B is crucial to the nuclear envelope integrity and extracellular trap release in neutrophils. bioRxiv. 2019; 647529. https://doi.org/10.1101/647529</mixed-citation><mixed-citation xml:lang="en">Li Y, Werth V.P., Mall M., Liu M.-L. Nuclear lamin B is crucial to the nuclear envelope integrity and extracellular trap release in neutrophils. bioRxiv. 2019; 647529. https://doi.org/10.1101/647529</mixed-citation></citation-alternatives></ref><ref id="cit60"><label>60</label><citation-alternatives><mixed-citation xml:lang="ru">Ruan J., Xia S., Liu X., Lieberman J., Wu H. Cryo-EM structure of the gasdermin A3 membrane pore. Nature. 2018; 557(7703): 62-67. https://doi.org/10.1038/s41586-018-0058-6</mixed-citation><mixed-citation xml:lang="en">Ruan J., Xia S., Liu X., Lieberman J., Wu H. Cryo-EM structure of the gasdermin A3 membrane pore. Nature. 2018; 557(7703): 62-67. https://doi.org/10.1038/s41586-018-0058-6</mixed-citation></citation-alternatives></ref><ref id="cit61"><label>61</label><citation-alternatives><mixed-citation xml:lang="ru">Chen K.W. et al. Noncanonical inflammasome signaling elicits gasdermin D-dependent neutrophil extracellular traps. Science Immunology. 2018; 3(26): eaar6676. https://doi.org/10.1126/sciimmunol.aar6676</mixed-citation><mixed-citation xml:lang="en">Chen K.W. et al. Noncanonical inflammasome signaling elicits gasdermin D-dependent neutrophil extracellular traps. Science Immunology. 2018; 3(26): eaar6676. https://doi.org/10.1126/sciimmunol.aar6676</mixed-citation></citation-alternatives></ref><ref id="cit62"><label>62</label><citation-alternatives><mixed-citation xml:lang="ru">Sollberger G. et al. Gasdermin D plays a vital role in the generation of neutrophil extracellular traps. Science Immunology. 2018; 3(26): eaar6689. https://doi.org/10.1126/sciimmunol.aar6689</mixed-citation><mixed-citation xml:lang="en">Sollberger G. et al. Gasdermin D plays a vital role in the generation of neutrophil extracellular traps. Science Immunology. 2018; 3(26): eaar6689. https://doi.org/10.1126/sciimmunol.aar6689</mixed-citation></citation-alternatives></ref><ref id="cit63"><label>63</label><citation-alternatives><mixed-citation xml:lang="ru">Renganathan B. et al. Transport and Organization of Individual Vimentin Filaments Within Dense Networks Revealed by Single Particle Tracking and 3D FIB-SEM. bioRxiv. 2024; 2024.06.10.598346. https://doi.org/10.1101/2024.06.10.598346</mixed-citation><mixed-citation xml:lang="en">Renganathan B. et al. Transport and Organization of Individual Vimentin Filaments Within Dense Networks Revealed by Single Particle Tracking and 3D FIB-SEM. bioRxiv. 2024; 2024.06.10.598346. https://doi.org/10.1101/2024.06.10.598346</mixed-citation></citation-alternatives></ref><ref id="cit64"><label>64</label><citation-alternatives><mixed-citation xml:lang="ru">Neubert E. etal. Chromatin swelling drives neutrophil extracellular trap release. Nature Communications. 2018; 9: 3767. https://doi.org/10.1038/s41467-018-06263-5</mixed-citation><mixed-citation xml:lang="en">Neubert E. et al. Chromatin swelling drives neutrophil extracellular trap release. Nature Communications. 2018; 9: 3767. https://doi.org/10.1038/s41467-018-06263-5</mixed-citation></citation-alternatives></ref><ref id="cit65"><label>65</label><citation-alternatives><mixed-citation xml:lang="ru">Giridharan S.S.P, Caplan S. MICAL-Family Proteins: Complex Regulators of the Actin Cytoskeleton. Antioxidants &amp; Redox Signaling. 2014; 20(13): 2059-2073. https://doi.org/10.1089/ars.2013.5487</mixed-citation><mixed-citation xml:lang="en">Giridharan S.S.P, Caplan S. MICAL-Family Proteins: Complex Regulators of the Actin Cytoskeleton. Antioxidants &amp; Redox Signaling. 2014; 20(13): 2059-2073. https://doi.org/10.1089/ars.2013.5487</mixed-citation></citation-alternatives></ref><ref id="cit66"><label>66</label><citation-alternatives><mixed-citation xml:lang="ru">Petretto A. etal. Neutrophil extracellular traps (NET) induced by different stimuli: A comparative proteomic analysis. PloS ONE. 2019; 14(7): e0218946. https://doi.org/10.1371/journal.pone.0218946</mixed-citation><mixed-citation xml:lang="en">Petretto A. et al. Neutrophil extracellular traps (NET) induced by different stimuli: A comparative proteomic analysis. PloS ONE. 2019; 14(7): e0218946. https://doi.org/10.1371/journal.pone.0218946</mixed-citation></citation-alternatives></ref><ref id="cit67"><label>67</label><citation-alternatives><mixed-citation xml:lang="ru">Deng W. et al. MICAL1 controls cell invasive phenotype via regulating oxidative stress in breast cancer cells. BMC Cancer. 2016; 16: 489. https://doi.org/10.1186/s12885-016-2553-1</mixed-citation><mixed-citation xml:lang="en">Deng W. et al. MICAL1 controls cell invasive phenotype via regulating oxidative stress in breast cancer cells. BMC Cancer. 2016; 16: 489. https://doi.org/10.1186/s12885-016-2553-1</mixed-citation></citation-alternatives></ref><ref id="cit68"><label>68</label><citation-alternatives><mixed-citation xml:lang="ru">Chang Y-C. et al. Group B Streptococcus Engages an Inhibitory Siglec through Sialic Acid Mimicry to Blunt Innate Immune and Inflammatory Responses In Vivo. PLoS Pathogens. 2014; 10(1): e1003846. https://doi.org/10.1371/journal.ppat.1003846</mixed-citation><mixed-citation xml:lang="en">Chang Y-C. et al. Group B Streptococcus Engages an Inhibitory Siglec through Sialic Acid Mimicry to Blunt Innate Immune and Inflammatory Responses In Vivo. PLoS Pathogens. 2014; 10(1): e1003846. https://doi.org/10.1371/journal.ppat.1003846</mixed-citation></citation-alternatives></ref><ref id="cit69"><label>69</label><citation-alternatives><mixed-citation xml:lang="ru">Secundino I. et al. Host and pathogen hyaluronan signal through human siglec-9 to suppress neutrophil activation. Journal of Molecular Medicine. 2016; 94(2): 219-233. https://doi.org/10.1007/s00109-015-1341-8</mixed-citation><mixed-citation xml:lang="en">Secundino I. et al. Host and pathogen hyaluronan signal through human siglec-9 to suppress neutrophil activation. Journal of Molecular Medicine. 2016; 94(2): 219-233. https://doi.org/10.1007/s00109-015-1341-8</mixed-citation></citation-alternatives></ref><ref id="cit70"><label>70</label><citation-alternatives><mixed-citation xml:lang="ru">Khatua B., Bhattacharya K., Mandal C. Sialoglycoproteins adsorbed by Pseudomonas aeruginosa facilitate their survival by impeding neutrophil extracellular trap through siglec-9. Journal of Leukocyte Biology. 2012; 91(4): 641-655. https://doi.org/10.1189/jlb.0511260</mixed-citation><mixed-citation xml:lang="en">Khatua B., Bhattacharya K., Mandal C. Sialoglycoproteins adsorbed by Pseudomonas aeruginosa facilitate their survival by impeding neutrophil extracellular trap through siglec-9. Journal of Leukocyte Biology. 2012; 91(4): 641-655. https://doi.org/10.1189/jlb.0511260</mixed-citation></citation-alternatives></ref><ref id="cit71"><label>71</label><citation-alternatives><mixed-citation xml:lang="ru">Beiter K., Wartha F, Albiger B., Normark S., Zychlinsky A., Henriques-Normark B. An Endonuclease Allows Streptococcus pneumoniae to Escape from Neutrophil Extracellular Traps. Current Biology 2006; 16(4): 401-407. https://doi.org/10.1016Zj.cub.2006.01.056</mixed-citation><mixed-citation xml:lang="en">Beiter K., Wartha F, Albiger B., Normark S., Zychlinsky A., Henriques-Normark B. An Endonuclease Allows Streptococcus pneumoniae to Escape from Neutrophil Extracellular Traps. Current Biology 2006; 16(4): 401-407. https://doi.org/10.1016/j.cub.2006.01.056</mixed-citation></citation-alternatives></ref><ref id="cit72"><label>72</label><citation-alternatives><mixed-citation xml:lang="ru">Juneau R.A., Stevens J.S., Apicella M.A., Criss A.K. A Thermonuclease of Neisseria gonorrhoeae Enhances Bacterial Escape From Killing by Neutrophil Extracellular Traps. The Journal of Infectious Diseases. 2015; 212(2): 316-324. https://doi.org/10.1093/infdis/jiv031</mixed-citation><mixed-citation xml:lang="en">Juneau R.A., Stevens J.S., Apicella M.A., Criss A.K. A Thermonuclease of Neisseria gonorrhoeae Enhances Bacterial Escape From Killing by Neutrophil Extracellular Traps. The Journal of Infectious Diseases. 2015; 212(2): 316-324. https://doi.org/10.1093/infdis/jiv031</mixed-citation></citation-alternatives></ref><ref id="cit73"><label>73</label><citation-alternatives><mixed-citation xml:lang="ru">Wartha F et al. Capsule and D-alanylated lipoteichoic acids protect Streptococcus pneumoniae against neutrophil extracellular traps. Cellular Microbiology. 2007; 9(5): 1162-1171. https://doi.org/10.1111/j.1462-5822.2006.00857.x</mixed-citation><mixed-citation xml:lang="en">Wartha F et al. Capsule and D-alanylated lipoteichoic acids protect Streptococcus pneumoniae against neutrophil extracellular traps. Cellular Microbiology. 2007; 9(5): 1162-1171. https://doi.org/10.1111/j.1462-5822.2006.00857.x</mixed-citation></citation-alternatives></ref><ref id="cit74"><label>74</label><citation-alternatives><mixed-citation xml:lang="ru">Воробьева Н.В., Пинегин Б.В. Нейтрофильные внеклеточные ловушки: механизмы образования, роль в норме и при патологии (обзор). Биохимия. 2014; 79(12): 1580-1591. https://elibrary.ru/tqqmsn</mixed-citation><mixed-citation xml:lang="en">Vorobjeva N.V., Pinegin B.V. Neutrophil extracellular traps: mechanisms of formation and role in health and disease. Biochemistry (Moscow). 2014; 79(12): 1286-1296. https://doi.org/10.1134/S0006297914120025</mixed-citation></citation-alternatives></ref><ref id="cit75"><label>75</label><citation-alternatives><mixed-citation xml:lang="ru">Kawabata K., Hagio T., Matsuoka S. The role of neutrophil elastase in acute lung injury. European Journal of Pharmacology. 2002; 451(1): 1-10. https://doi.org/10.1016/s0014-2999(02)02182-9</mixed-citation><mixed-citation xml:lang="en">Kawabata K., Hagio T., Matsuoka S. The role of neutrophil elastase in acute lung injury. European Journal of Pharmacology. 2002; 451(1): 1-10. https://doi.org/10.1016/s0014-2999(02)02182-9</mixed-citation></citation-alternatives></ref><ref id="cit76"><label>76</label><citation-alternatives><mixed-citation xml:lang="ru">Xu J. et al. Extracellular histones are major mediators of death in sepsis. Nature Medicine. 2009; 15(11): 1318-1321. https://doi.org/10.1038/nm.2053</mixed-citation><mixed-citation xml:lang="en">Xu J. et al. Extracellular histones are major mediators of death in sepsis. Nature Medicine. 2009; 15(11): 1318-1321. https://doi.org/10.1038/nm.2053</mixed-citation></citation-alternatives></ref><ref id="cit77"><label>77</label><citation-alternatives><mixed-citation xml:lang="ru">Thomas G.M. et al. Extracellular DNA traps are associated with the pathogenesis of TRALI in humans and mice. Blood. 2012; 119(26): 6335-6343. https://doi.org/10.1182/blood-2012-01-405183</mixed-citation><mixed-citation xml:lang="en">Thomas G.M. et al. Extracellular DNA traps are associated with the pathogenesis of TRALI in humans and mice. Blood. 2012; 119(26): 6335-6343. https://doi.org/10.1182/blood-2012-01-405183</mixed-citation></citation-alternatives></ref><ref id="cit78"><label>78</label><citation-alternatives><mixed-citation xml:lang="ru">Abrams S.T. et al. Circulating Histones Are Mediators of Trauma-associated Lung Injury. American Journal of Respiratory and Critical Care Medicine. 2013; 187(2): 160-169. https://doi.org/10.1164/rccm.201206-1037OC</mixed-citation><mixed-citation xml:lang="en">Abrams S.T. et al. Circulating Histones Are Mediators of Trauma-associated Lung Injury. American Journal of Respiratory and Critical Care Medicine. 2013; 187(2): 160-169. https://doi.org/10.1164/rccm.201206-1037OC</mixed-citation></citation-alternatives></ref><ref id="cit79"><label>79</label><citation-alternatives><mixed-citation xml:lang="ru">Poon I.K.H. et al. Phosphoinositide-mediated oligomerization of a defensin induces cell lysis. eLife. 2014; 3: e01808. https://doi.org/10.7554/eLife.01808</mixed-citation><mixed-citation xml:lang="en">Poon I.K.H. et al. Phosphoinositide-mediated oligomerization of a defensin induces cell lysis. eLife. 2014; 3: e01808. https://doi.org/10.7554/eLife.01808</mixed-citation></citation-alternatives></ref><ref id="cit80"><label>80</label><citation-alternatives><mixed-citation xml:lang="ru">Horwitz D.A., Fahmy T.M., Piccirillo C.A., La Cava A. Rebalancing Immune Homeostasis to Treat Autoimmune Diseases. Trends in Immunology. 2019; 40(10): 888-908. https://doi.org/10.1016/j.it.2019.08.003</mixed-citation><mixed-citation xml:lang="en">Horwitz D.A., Fahmy T.M., Piccirillo C.A., La Cava A. Rebalancing Immune Homeostasis to Treat Autoimmune Diseases. Trends in Immunology. 2019; 40(10): 888-908. https://doi.org/10.1016/j.it.2019.08.003</mixed-citation></citation-alternatives></ref><ref id="cit81"><label>81</label><citation-alternatives><mixed-citation xml:lang="ru">Saba H.I., Roberts H.R., Herion J.C. The Anticoagulant Activity of Lysosomal Cationic Proteins from Polymorphonuclear Leukocytes. Journal of Clinical Investigation. 1967; 46(4): 580-589. https://doi.org/10.1172/JCI105559</mixed-citation><mixed-citation xml:lang="en">Saba H.I., Roberts H.R., Herion J.C. The Anticoagulant Activity of Lysosomal Cationic Proteins from Polymorphonuclear Leukocytes. Journal of Clinical Investigation. 1967; 46(4): 580-589. https://doi.org/10.1172/JCI105559</mixed-citation></citation-alternatives></ref><ref id="cit82"><label>82</label><citation-alternatives><mixed-citation xml:lang="ru">Fuchs T.A. et al. Extracellular DNA traps promote thrombosis. Proceedings of the National Academy of Sciences. 2010; 107(36): 15880-15885. https://doi.org/10.1073/pnas.1005743107</mixed-citation><mixed-citation xml:lang="en">Fuchs T.A. et al. Extracellular DNA traps promote thrombosis. Proceedings of the National Academy of Sciences. 2010; 107(36): 15880-15885. https://doi.org/10.1073/pnas.1005743107</mixed-citation></citation-alternatives></ref><ref id="cit83"><label>83</label><citation-alternatives><mixed-citation xml:lang="ru">Brill A. et al. von Willebrand factor-mediated platelet adhesion is critical for deep vein thrombosis in mouse models. Blood. 2011; 117(4): 1400-1407. https://doi.org/10.1182/blood-2010-05-287623</mixed-citation><mixed-citation xml:lang="en">Brill A. et al. von Willebrand factor-mediated platelet adhesion is critical for deep vein thrombosis in mouse models. Blood. 2011; 117(4): 1400-1407. https://doi.org/10.1182/blood-2010-05-287623</mixed-citation></citation-alternatives></ref><ref id="cit84"><label>84</label><citation-alternatives><mixed-citation xml:lang="ru">Etulain J., Martinod K., Wong S.L., Cifuni S.M., Schattner M., Wagner D.D. P-selectin promotes neutrophil extracellular trap formation in mice. Blood. 2015; 126(2): 242-246. https://doi.org/10.1182/blood-2015-01-624023</mixed-citation><mixed-citation xml:lang="en">Etulain J., Martinod K., Wong S.L., Cifuni S.M., Schattner M., Wagner D.D. P-selectin promotes neutrophil extracellular trap formation in mice. Blood. 2015; 126(2): 242-246. https://doi.org/10.1182/blood-2015-01-624023</mixed-citation></citation-alternatives></ref><ref id="cit85"><label>85</label><citation-alternatives><mixed-citation xml:lang="ru">Monfregola J., Johnson J.L., Meijler M.M., Napolitano G., Catz S.D. MUNC13-4 Protein Regulates the Oxidative Response and Is Essential for Phagosomal Maturation and Bacterial Killing in Neutrophils. Journal of Biological Chemistry. 2012; 287(53): 44603-44618. https://doi.org/10.1074/jbc.M112.414029</mixed-citation><mixed-citation xml:lang="en">Monfregola J., Johnson J.L., Meijler M.M., Napolitano G., Catz S.D. MUNC13-4 Protein Regulates the Oxidative Response and Is Essential for Phagosomal Maturation and Bacterial Killing in Neutrophils. Journal of Biological Chemistry. 2012; 287(53): 44603-44618. https://doi.org/10.1074/jbc.M112.414029</mixed-citation></citation-alternatives></ref><ref id="cit86"><label>86</label><citation-alternatives><mixed-citation xml:lang="ru">Hakkim A. etal. Impairment of neutrophil extracellular trap degradation is associated with lupus nephritis. Proceedings of the National Academy of Sciences. 2010; 107(21): 9813-9818. https://doi.org/10.1073/pnas.0909927107</mixed-citation><mixed-citation xml:lang="en">Hakkim A. et al. Impairment of neutrophil extracellular trap degradation is associated with lupus nephritis. Proceedings of the National Academy of Sciences. 2010; 107(21): 9813-9818. https://doi.org/10.1073/pnas.0909927107</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>
