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<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">nbsprot</journal-id><journal-title-group><journal-title xml:lang="ru">Вестник войск РХБ защиты</journal-title><trans-title-group xml:lang="en"><trans-title>Journal of NBC Protection Corps</trans-title></trans-title-group></journal-title-group><issn pub-type="ppub">2587-5728</issn><issn pub-type="epub">3034-2791</issn><publisher><publisher-name>27 Научный центр</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="doi">10.35825/2587-5728-2019-3-2-117-136</article-id><article-id custom-type="edn" pub-id-type="custom">qbguzu</article-id><article-id custom-type="elpub" pub-id-type="custom">nbsprot-239</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>Биологическая безопасность и защита от биологических угроз</subject></subj-group><subj-group subj-group-type="section-heading" xml:lang="en"><subject>Biological Security and Protection against Biological Threats</subject></subj-group></article-categories><title-group><article-title>Нейро- и кардиотоксины актиний: структура, функция и перспективы применения в научной и медицинской практике</article-title><trans-title-group xml:lang="en"><trans-title>Neuro- and Cardiotoxins from Sea Anemones: Structure, Function and Potential of Application in Research and Medical Practice</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>Калина</surname><given-names>Р. С.</given-names></name><name name-style="western" xml:lang="en"><surname>Kalina</surname><given-names>R. S.</given-names></name></name-alternatives><bio xml:lang="ru"><p>Калина Римма Сергеевна. Младший научный сотрудник </p><p>Проспект 100-летия Владивостока, д. 159, г. Владивосток, 690022</p></bio><bio xml:lang="en"><p>Rimma Sergeevna Kalina. Junior Researcher </p><p>Prospect 100-let Vladivostoky 159, Vladivostok 690022</p></bio><email xlink:type="simple">kalinarimma@gmail.com</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>Монастырная</surname><given-names>М. М.</given-names></name><name name-style="western" xml:lang="en"><surname>Monastyrnaya</surname><given-names>M. M.</given-names></name></name-alternatives><bio xml:lang="ru"><p>Монастырная Маргарита Михайловна. Ведущий научный сотрудник, д-р хим. наук</p><p>Проспект 100-летия Владивостока, д. 159, г. Владивосток, 690022</p></bio><bio xml:lang="en"><p>Margarita Michailovna Monastyrnaya. Leading Researcher, Doctor of Chemical Sciences</p><p>Prospect 100-let Vladivostoky 159, Vladivostok 690022</p></bio><xref ref-type="aff" rid="aff-1"/></contrib></contrib-group><aff-alternatives id="aff-1"><aff xml:lang="ru"><institution>Тихоокеанский институт биоорганической химии им Г.Б. Елякова ДВО РАН (ТИБОХ ДВО РАН)</institution><country>Россия</country></aff><aff xml:lang="en"><institution>G.B. Elyakov Pacific Institute of Bioorganic Chemistry, Far Eastern Branch of the Russian Academy of Sciences</institution><country>Russian Federation</country></aff></aff-alternatives><pub-date pub-type="collection"><year>2019</year></pub-date><pub-date pub-type="epub"><day>10</day><month>07</month><year>2023</year></pub-date><volume>3</volume><issue>2</issue><fpage>117</fpage><lpage>136</lpage><permissions><copyright-statement>Copyright &amp;#x00A9; Калина Р.С., Монастырная М.М., 2023</copyright-statement><copyright-year>2023</copyright-year><copyright-holder xml:lang="ru">Калина Р.С., Монастырная М.М.</copyright-holder><copyright-holder xml:lang="en">Kalina R.S., Monastyrnaya M.M.</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.nbsprot.ru/jour/article/view/239">https://www.nbsprot.ru/jour/article/view/239</self-uri><abstract><p>Актинии повсеместно распространены в Мировом океане и представляют собой древнейшие активно-ядовитые организмы. Их основной инструмент нападения на других животных – нематоцисты, жалящие органеллы, внутри которых заключена свернутая полая нить с ядовитым острием на конце. Для привлечения потенциальных жертв они используют флуоресцентные белки, ставшие отдельным объектом исследования в качестве генетически кодируемых маркеров для наблюдения за активностью промоторов генов. Ядовитый секрет актиний характеризуется наличием максимального количества пептидов различных структурных классов и пространственных структур среди изученных наземных и морских организмов (пчелы, пауки, скорпионы, змеи, моллюски конусы и др.), что затрудняет его идентификацию и дифференциацию от ядов животных других таксонов, если неизвестен конкретный источник его происхождения. Токсичность некоторых биологически активных пептидов актиний (RpI, RpIII) при внутривенном введении экспериментальным животным сравнима с токсичностью наиболее известных и опасных представителей природных токсинов, имеющих сходный механизм действия (альфа-гемолизин и тетродотоксин), или боевых отравляющих веществ, таких как зарин и синильная кислота. По токсическому действию биологически активные пептиды актиний в основном можно отнести к нейротоксинам, поскольку они оказывают влияние на функционирование натриевых каналов в клетках нервной системы животных. Кардиотоксическое действие секрета актиний обусловлено специфичностью взаимодействия отдельных, входящих в его состав, нейротоксинов с одним из подтипов натриевых каналов мышечных клеток, характерных для тканей сердца. Основными способами идентификации нейротоксинов актиний в образцах, например, при расследовании биопреступлений, могут быть секвенирование по методу Эдмана или методы тандемной масс-спектрометрии (анализ фрагментов молекулы токсина для установления его структуры). Дальнейшее изучение механизмов взаимодействия нейротоксинов актиний с ионными каналами клеток нервной и мышечной систем способно привести к созданию препаратов для лечения каналопатий и антидотов широко спектра действия, блокирующих токсины, воздействующие на натриевые каналы.</p></abstract><trans-abstract xml:lang="en"><p>Sea anemones are well-spread everywhere in the World Ocean and represent the most ancient active poisonous organisms. Their main instrument of attack on other animals are the nematocysts – stinging organelles with the curtailed hollow thread with poisonous edge on the end. In order to attract their potential victims, they use fluorescent proteins. These proteins became a separate object of research as genetically coded markers for the observation of activity of promotors of genes. The poisonous secret of sea anemones is characterized by the presence of maximum number of peptides of various structural classes and spatial structures among the studied land and marine organisms (bees, spiders, scorpions, snakes ect.). This fact complicates the identification of sea anemones' secret and its differentiation from poisons of animals of other taxons, if the concrete source of its origin is unknown. The toxicity of some biologically active sea anemone peptides (RpI, RpIII) at intravenous administration to experimental animals is comparable with that of the most well-known and dangerous representatives of natural toxins with the similar mechanism of action (an alpha-hemolysine and tetrodotoxin), or chemical warfare agents, such as sarin and hydrogen cyanide. Based on their toxic effect, the biologically active sea anemone peptides generally can be classified as neurotoxins due to their impact on the functioning of sodium channels in the cells of the nervous system of animals. Cardiotoxic effect of sea anemone secret is caused by the specificity of interaction between its separate neurotoxins and one of the sub-types of sodium channels of muscle cells, characteristic for heart tissues. The main ways of identification of sea anemone neurotoxins in samples (for example, during the investigation of biological crimes) can be sequence by Edman`s method or tandem mass spectrometry (the analysis of fragments of toxin molecule for the establishment of its structure). Further study on the mechanisms of interaction between the sea anemone neurotoxins and the ion channels of the cells of nervous and muscular systems may result in the creation of medicines for treatment of channelopathy, as well as pluripotential antidotes, blocking the toxins, that influence on sodium channels.</p></trans-abstract><kwd-group xml:lang="ru"><kwd>актинии</kwd><kwd>антидот</kwd><kwd>биопреступление</kwd><kwd>зарин</kwd><kwd>ионный канал</kwd><kwd>кардиотоксин</kwd><kwd>нейропептид</kwd><kwd>нейротоксин</kwd><kwd>нематоцист</kwd><kwd>нефротоксичность</kwd><kwd>секвенирование по методу Эдмана</kwd><kwd>синильная кислота</kwd><kwd>стрекательная клетка</kwd><kwd>тандемная масс-спектрометрия</kwd><kwd>тетродоксин</kwd><kwd>флуоресцентный белок</kwd><kwd>цитолизин</kwd></kwd-group><kwd-group xml:lang="en"><kwd>sea anemones</kwd><kwd>antidote</kwd><kwd>biological crime</kwd><kwd>sarin</kwd><kwd>ion channel</kwd><kwd>cardiotoxin</kwd><kwd>neuropeptide</kwd><kwd>neurotoxin</kwd><kwd>nematocyst</kwd><kwd>nephrotoxicity</kwd><kwd>sequence by Edman's method</kwd><kwd>hydrogen cyanide</kwd><kwd>thread cell</kwd><kwd>tandem mass-spectrometry</kwd><kwd>tetrodotoxin</kwd><kwd>fluorescent protein</kwd><kwd>cytolysin</kwd></kwd-group><funding-group><funding-statement xml:lang="ru">Исследование выполнено при финансовой поддержке РФФИ в рамках научного проекта № 18-04-00631.</funding-statement></funding-group></article-meta></front><back><ref-list><title>References</title><ref id="cit1"><label>1</label><citation-alternatives><mixed-citation xml:lang="ru">Rentzsch F., Layden M., Manuel M. 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