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«Антипролиферативное действие карнозина и его производных на опухолевые клетки нейрального происхождения ...»

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ADDIN EN.CITE.DATA [27, 151, 261]. Более того, в нескольких исследованиях было продемонстрировано значительное снижение активности MnСОД в опухолевых клетках, что совпадало с повышенным внутриклеточным уровнем АФК и активной пролиферацией. Усиление экспрессии MnСОД ингибировало пролиферацию многих линий опухолевых клеток, в том числе клеток глиобастомы человека U-118 PEVuZE5vdGU+PENpdGU+PEF1dGhvcj5PYmVybGV5PC9BdXRob3I+PFllYXI+MTk3OTwvWWVhcj48

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ADDIN EN.CITE.DATA [30, 74, 75, 256, 262, 263]. В нашей работе, увеличение активности MnСОД при инкубации клеток глиобластомы с карнозином сопровождалось значительным удлинением времени удвоения популяции. Следовательно, можно предположить, что антипролиферативный эффект карнозина обусловлен его способностью усиливать экспрессию MnСОД и приводить к снижению уровня АФК.

Измерение активности цитозольной формы СОД (CuZnСОД) в контроле и после инкубации с карнозином не выявило каких-либо различий. Поскольку MnСОД представляет собой антиоксидантный фермент расположенный в матриксе митохондрий, исходя из полученных данных можно предположить, что антипролиферативный эффект карнозина является результатом изменения уровня АФК, генерируемых в митохондриях.

Интересно отметить работу Renner et al., которые показали, что уменьшение количества клеток глиобластомы в культуре под действием карнозина сопровождается снижением внутриклеточного количества АТФ и активности ЛДГ, что, по мнению авторов, являлось причиной замедления пролиферации опухолевых клеток PEVuZE5vdGU+PENpdGU+PEF1dGhvcj5SZW5uZXI8L0F1dGhvcj48WWVhcj4yMDA4PC9ZZWFyPjxS

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ADDIN EN.CITE.DATA [21, 208]. Ингибирование окислительного фосфорилирования с помощью KCN не влияло на выработку АТФ или выживаемость клеток глиобластомы, исходя из этого было предположено, что карнозин работает на уровне гликолиза, а не окислительного фосфорилирования ADDIN EN.CITE <EndNote><Cite><Author>Renner</Author><Year>2010</Year><RecNum>71</RecNum><DisplayText>[225]</DisplayText><record><rec-number>71</rec-number><foreign-keys><key app="EN" db-id="w2wfxafe6va9z5eev2l55aa8sxsa599eev2s">71</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Renner, C.</author><author>Asperger, A.</author><author>Seyffarth, A.</author><author>Meixensberger, J.</author><author>Gebhardt, R.</author><author>Gaunitz, F.

</author></authors></contributors><auth-address>Klinik und Poliklinik fur Neurochirurgie, Medizinische Fakultat der Universitat Leipzig, Leipzig, Germany.</auth-address><titles><title>Carnosine inhibits ATP production in cells from malignant glioma</title><secondary-title>Neurol Res</secondary-title><alt-title>Neurological research</alt-title></titles><periodical><full-title>Neurol Res</full-title><abbr-1>Neurological research</abbr-1></periodical><alt-periodical><full-title>Neurol Res</full-title><abbr-1>Neurological research</abbr-1></alt-periodical><pages>101-5</pages><volume>32</volume><number>1</number><edition>2009/11/17</edition><keywords><keyword>Adenosine Triphosphate/ metabolism</keyword><keyword>Antineoplastic Agents/ pharmacology</keyword><keyword>Carnosine/ pharmacology</keyword><keyword>Cell Line, Tumor</keyword><keyword>Cells, Cultured</keyword><keyword>Glioma/ drug therapy/ metabolism</keyword><keyword>Glucose/metabolism</keyword><keyword>Glycolysis/drug effects</keyword><keyword>Humans</keyword><keyword>Mitochondria/drug effects/metabolism</keyword><keyword>Organic Chemicals/pharmacology</keyword><keyword>Potassium Cyanide/pharmacology</keyword></keywords><dates><year>2010</year><pub-dates><date>Feb</date></pub-dates></dates><isbn>1743-1328 (Electronic)&#xD;0161-6412 (Linking)</isbn><accession-num>19909581</accession-num><urls></urls><electronic-resource-num>10.1179/016164109x12518779082237</electronic-resource-num><remote-database-provider>NLM</remote-database-provider><language>eng</language></record></Cite></EndNote>[225]. Недавно Sarsour et al. продемонстрировали существование взаимосвязи между гликолизом и активностью MnСОД. Понижение активности MnСОД сопровождалось усилением интенсивности поглощения глюкозы, а усиление активности MnСОД, наоборот ингибировало гликолитические процессы PEVuZE5vdGU+PENpdGU+PEF1dGhvcj5TYXJzb3VyPC9BdXRob3I+PFllYXI+MjAxMjwvWWVhcj48

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ADDIN EN.CITE.DATA [27]. Таким образом, можно предположить, что обнаруженное нами повышение активности MnСОД под действием карнозина является одним из механизмов ингибирующего действия карнозина на гликолиз, приводя к замедлению пролиферации опухолевых клеток.

Измерение активности каталазы в пробах обработанных карнозином выявило снижение ее активности в клетках глиобластомы обработанных карнозином по сравнению с контролем (Рис. 3.2.6). Снижение активности каталазы сопровождалось понижением уровня белка. Каталаза является важным участником антиоксидантной системы клетки, который катализирует реакцию разложения Н2О2 до воды и молекулярного кислорода. Таким образом, снижение активности каталазы должно приводить к повышению концентрации Н2О2, однако в нашей работе этого не наблюдалось. Более того, уровень АФК, наоборот, снижался. Возможно, это происходило потому, что изначальная активность каталазы была невелика (4 мк ед/мг). В то время как средняя активность каталазы в нормальных клетках на несколько порядков выше (примерно 5 ед/мг белка) PEVuZE5vdGU+PENpdGU+PEF1dGhvcj5MaTwvQXV0aG9yPjxZZWFyPjE5OTg8L1llYXI+PFJlY051

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ADDIN EN.CITE.DATA [148]. Понижение активности каталазы в клетках глиобластомы с 4 до 2 мк ед/мг, вероятно, не вносило значительного вклада в повышение уровня Н2О2. Кроме того, снижение уровня АФК может объясняться включением компенсаторных механизмов, например усилением активности GPx, пероксиредоксинов и т.п.

Исследование влияния карнозина на прогрессию клеточного цикла клеток РС-12 и U-118-MG выявило, что замедление пролиферации под действием карнозина сопровождается увеличением количества клеток в G2 фазе (Рис. 3.2.7). На сегодняшний день накоплен большой объем экспериментальных данных, указывающий на важность роли АФК в регуляции прогрессии клеточного цикла. Показано, что по мере прогрессии клеточного цикла от G1 к митозу происходит увеличение уровня АФК и снижение активности MnСОД. Концентрация АФК максимальна в поздней S фазе и в G2/M PEVuZE5vdGU+PENpdGU+PEF1dGhvcj5Hb3N3YW1pPC9BdXRob3I+PFllYXI+MjAwMDwvWWVhcj48

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ADDIN EN.CITE.DATA [26]. Активность MnСОД, наоборот, была максимальна в G1 фазе и постепенно снижалась по мере прогрессии через S, G2 и М фазы PEVuZE5vdGU+PENpdGU+PEF1dGhvcj5PYmVybGV5PC9BdXRob3I+PFllYXI+MTk5NTwvWWVhcj48

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ADDIN EN.CITE.DATA [27, 148, 150]. Повышение экспрессии MnСОД усиливало формирование G2 блока индуцированное действием радиации в клетках карциномы PEVuZE5vdGU+PENpdGU+PEF1dGhvcj5LYWxlbjwvQXV0aG9yPjxZZWFyPjIwMDY8L1llYXI+PFJl

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ADDIN EN.CITE.DATA [180]. Исходя из полученных нами результатов и данных литературы, мы предполагаем, что индуцированное карнозином снижение АФК и увеличение активности MnСОД приводят к нарушению внутриклеточного редокс-баланса, необходимого для прогрессии через G2 фазу (повышенный уровень АФК и низкая активность MnСОД). В результате не происходит активации редокс-зависимых регуляторов G2 фазы, что приводит к нарушению прогрессии клеточного цикла через G2 фазу.

В нашей лаборатории было также показано, что карнозин замедляет рост уровня активной формы МАР-киназы ERK1/2 в условиях окислительного стресса индуцированного активацией глутаматных рецепторов PEVuZE5vdGU+PENpdGU+PEF1dGhvcj5SeWJha292YTwvQXV0aG9yPjxZZWFyPjIwMTI8L1llYXI+

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ADDIN EN.CITE.DATA [106]. Есть данные о том, что активность ERK1/2 изменяется в зависимости от состояния редокс. Например, усиление экспрессия MnСОД подавляло активацию ERK1/2 в клетках глиобластомы человека U87, указывая на возможность регуляции активности ERK1/2 с помощью антиоксидантов PEVuZE5vdGU+PENpdGU+PEF1dGhvcj5MaTwvQXV0aG9yPjxZZWFyPjIwMTM8L1llYXI+PFJlY051

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ADDIN EN.CITE.DATA [28, 160]. Несмотря на то, что для проверки данной гипотезы, необходимо проведение множества дополнительных экспериментов, мы полагаем, что ингибирование ERK1/2 при активации MnСОД и снижении уровня АФК под действием карнозина, может быть одним из механизмов его антипролифативного эффекта.



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