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

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ADDIN EN.CITE.DATA [173]. Несмотря на то, что повышенный уровень GSH ингибировал прогрессию клеточного цикла, полное удаление тиолов из среды также препятствовало переходу клеток в S фазу. Удаление тиолов из среды культивирования лимфоцитов, препятствовало экспрессии и фосфорилированию рRb под действием IL-2. Добавление GSH, NAC и 2-меркаптоэтанола обращало этот эффект ADDIN EN.CITE <EndNote><Cite><Author>Yamauchi</Author><Year>1997</Year><RecNum>322</RecNum><DisplayText>[174]</DisplayText><record><rec-number>322</rec-number><foreign-keys><key app="EN" db-id="w2wfxafe6va9z5eev2l55aa8sxsa599eev2s">322</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Yamauchi, A.</author><author>Bloom, E. T.</author></authors></contributors><auth-address>Center for Biologics Evaluation and Research, Food and Drug Administration, Bethesda, MD 20892, USA.</auth-address><titles><title>Control of cell cycle progression in human natural killer cells through redox regulation of expression and phosphorylation of retinoblastoma gene product protein</title><secondary-title>Blood</secondary-title><alt-title>Blood</alt-title></titles><periodical><full-title>Blood</full-title><abbr-1>Blood</abbr-1></periodical><alt-periodical><full-title>Blood</full-title><abbr-1>Blood</abbr-1></alt-periodical><pages>4092-9</pages><volume>89</volume><number>11</number><edition>1997/06/01</edition><keywords><keyword>Cell Cycle</keyword><keyword>Cell Line</keyword><keyword>Gene Expression Regulation</keyword><keyword>Humans</keyword><keyword>Killer Cells, Natural/ cytology/metabolism</keyword><keyword>Oxidation-Reduction</keyword><keyword>Phosphorylation</keyword><keyword>Retinoblastoma Protein/ metabolism</keyword><keyword>Signal Transduction</keyword></keywords><dates><year>1997</year><pub-dates><date>Jun 1</date></pub-dates></dates><isbn>0006-4971 (Print)&#xD;0006-4971 (Linking)</isbn><accession-num>9166850</accession-num><urls></urls><remote-database-provider>NLM</remote-database-provider><language>eng</language></record></Cite></EndNote>[174]. Из полученных данных можно сделать вывод о том, что хотя небольшое увеличение уровня АФК необходимо для активации рRb, чрезмерное повышение прооксидантного уровня приводит к нарушению клеточного цикла.

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ADDIN EN.CITE.DATA [175]. Однако, снижение уровня О2•- с помощью темпола, препятствовало накоплению циклина А, регулятора G1/S перехода, и прогрессии через S фазу, приводя к остановке клеточного цикла в поздней G1 фазе. Удаление темпола из среды способствовало восстановлению прогрессии клеточного цикла. Эти данные указывают на необходимость присутствия О2•- для перехода клетки из G1 в S фазу. Повышенная экспрессия Emi1, ингибитора комплекса APC/Cdh1, отменяла эффект темпола. Клетки экспрессирующие Emi1, демонстрировали уровень циклина А сравнимый с контролем и отсутствие блока в G1 фазе. К сходным результатам приводило применение ингибиторов 26S протеасомы. Как было отмечено выше убиквитинирование циклина А с помощью комплекса APC/Cdh1 в течение G1 фазы препятствует переходу в S фазу. Исходя из имеющихся данных можно предположить, что О2•- играет важную роль в ингибировании APC/Cdh1 и поэтому его присутствие необходимо для перехода в S фазу. Таким образом, было показано, что повышение уровня АФК при прогрессии из G1 в S необходимо для ингибирования деградации циклина А под действием АРС PEVuZE5vdGU+PENpdGU+PEF1dGhvcj5IYXZlbnM8L0F1dGhvcj48WWVhcj4yMDA2PC9ZZWFyPjxS

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ADDIN EN.CITE.DATA [176]. Отсюда следует, что присутствие О2•- в начале G1 фазы ингибирует экспрессию циклина D1 и приводит к остановке клеточного цикла. Однако в конце G1 фазы, О2•- необходим для прогрессии из G1 в S. Кажущаяся несогласованность является лишь еще одним доказательством существования редокс-цикла внутри клеточного цикла, а также подчеркивает сложность и важность редокс-модификаций для регуляции пролиферации.

Еще один фермент S фазы, топоизомераза II, играет важную роль в поддержании целостности ДНК, путем распутывания переплетенных в процессе репликации сестринских хроматид и способствуя релаксации ДНК. Goswami et al показали, что уровень мРНК топоизомеразы варьирует в зависимости от фазы клеточного цикла достигая максимума в S фазе. Дальнейшие исследования выявили, что экспрессия топоизомеразы II регулируется за счет взаимодействия 3`-UTR последовательности мРНК с редокс-чувствительными белками [32, 57].

Фосфатаза Cdc25С, важный регулятор прогрессии клеточного цикла через G2 фазу, содержит в активном центре цистеин (Cys377) и поэтому чувствителен к изменениям редокс-статуса. Образование связи между Cys377 и Cys330 приводит к усилению связывания Cdc25С с белком 14-3-3, что препятствует перемещению Cdc25С в ядро и активации комплекса циклин В1/Cdk1 (см. Рис. 1.4) PEVuZE5vdGU+PENpdGU+PEF1dGhvcj5TYXZpdHNreTwvQXV0aG9yPjxZZWFyPjIwMDI8L1llYXI+

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ADDIN EN.CITE.DATA [148], это вероятно способствует переходу Cdc25C в более стабильное состояние и активации циклин В/Cdk1.

209554445Рисунок 1.4. Редокс-регуляция активности Cdc25C фосфатазы. Из ADDIN EN.CITE <EndNote><Cite><Author>Savitsky</Author><Year>2002</Year><RecNum>250</RecNum><DisplayText>[177]</DisplayText><record><rec-number>250</rec-number><foreign-keys><key app="EN" db-id="w2wfxafe6va9z5eev2l55aa8sxsa599eev2s">250</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Savitsky, P. A.</author><author>Finkel, T.</author></authors></contributors><auth-address>Cardiovascular Branch, NHLBI, National Institutes of Health, Bethesda, Maryland 20892-1622, USA.</auth-address><titles><title>Redox regulation of Cdc25C</title><secondary-title>J Biol Chem</secondary-title><alt-title>The Journal of biological chemistry</alt-title></titles><periodical><full-title>J Biol Chem</full-title><abbr-1>The Journal of biological chemistry</abbr-1></periodical><alt-periodical><full-title>J Biol Chem</full-title><abbr-1>The Journal of biological chemistry</abbr-1></alt-periodical><pages>20535-40</pages><volume>277</volume><number>23</number><edition>2002/04/02</edition><keywords><keyword>Cell Cycle Proteins/ metabolism</keyword><keyword>Fluorescent Antibody Technique, Indirect</keyword><keyword>G2 Phase</keyword><keyword>HeLa Cells</keyword><keyword>Humans</keyword><keyword>Hydrogen Peroxide/metabolism</keyword><keyword>Mitosis</keyword><keyword>Oxidation-Reduction</keyword><keyword>Phosphorylation</keyword><keyword>Recombinant Proteins/metabolism</keyword><keyword>cdc25 Phosphatases/ metabolism</keyword></keywords><dates><year>2002</year><pub-dates><date>Jun 7</date></pub-dates></dates><isbn>0021-9258 (Print)&#xD;0021-9258 (Linking)</isbn><accession-num>11925443</accession-num><urls></urls><electronic-resource-num>10.1074/jbc.M201589200</electronic-resource-num><remote-database-provider>NLM</remote-database-provider><language>eng</language></record></Cite></EndNote>[177] c изменениями. См. пояснения в тескте.

Chang et al. показали, что в G2 фазе активная CDK1 фосфорилирует пероксиредоксин I, внутриклеточный фермент катализирующий деградацию Н2О2, ингибируя его активность. Накопление Н2О2, в результате снижения активности пероксиредоксина I, представляется необходимым для прогрессии через G2 фазу в М ADDIN EN.CITE <EndNote><Cite><Author>Chang</Author><Year>2002</Year><RecNum>248</RecNum><DisplayText>[179]</DisplayText><record><rec-number>248</rec-number><foreign-keys><key app="EN" db-id="w2wfxafe6va9z5eev2l55aa8sxsa599eev2s">248</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Chang, T. S.</author><author>Jeong, W.</author><author>Choi, S. Y.</author><author>Yu, S.</author><author>Kang, S. W.</author><author>Rhee, S. G.</author></authors></contributors><auth-address>Laboratory of Cell Signaling, NHLBI, National Institutes of Health, Bethesda, Maryland 20892, USA.</auth-address><titles><title>Regulation of peroxiredoxin I activity by Cdc2-mediated phosphorylation</title><secondary-title>J Biol Chem</secondary-title><alt-title>The Journal of biological chemistry</alt-title></titles><periodical><full-title>J Biol Chem</full-title><abbr-1>The Journal of biological chemistry</abbr-1></periodical><alt-periodical><full-title>J Biol Chem</full-title><abbr-1>The Journal of biological chemistry</abbr-1></alt-periodical><pages>25370-6</pages><volume>277</volume><number>28</number><edition>2002/05/03</edition><keywords><keyword>Amino Acid Sequence</keyword><keyword>CDC2 Protein Kinase/ metabolism</keyword><keyword>Cell Cycle</keyword><keyword>HeLa Cells</keyword><keyword>Humans</keyword><keyword>Peroxidases/chemistry/ metabolism</keyword><keyword>Peroxiredoxins</keyword><keyword>Phosphorylation</keyword><keyword>Threonine/metabolism</keyword></keywords><dates><year>2002</year><pub-dates><date>Jul 12</date></pub-dates></dates><isbn>0021-9258 (Print)&#xD;0021-9258 (Linking)</isbn><accession-num>11986303</accession-num><urls></urls><electronic-resource-num>10.1074/jbc.M110432200</electronic-resource-num><remote-database-provider>NLM</remote-database-provider><language>eng</language></record></Cite></EndNote>[179]. Как было отмечено выше, активность MnСОД снижается по мере прогрессии клеточного цикла от G1 к М фазе, способствуя повышению уровня АФК. Повышение экспрессии MnСОД в клетках карцином усиливало формирование индуцированного радиацией G2 блока, указывая на то, что высокий уровень MnСОД препятствует прогрессии клеток через G2 фазу PEVuZE5vdGU+PENpdGU+PEF1dGhvcj5LYWxlbjwvQXV0aG9yPjxZZWFyPjIwMDY8L1llYXI+PFJl

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ADDIN EN.CITE.DATA [180]. Другой внутриклеточный антиоксидант, витамин С, также был способен индуцировать G2 блок в клетках карциномы HeLa и глиобластомы T98G человека. Индукция G2 блока под действием витамина С сопровождалась усилением экспрессии циклина В1 и снижением уровня активного Cdc25С, активатора комплекса циклин В1/CDK1 PEVuZE5vdGU+PENpdGU+PEF1dGhvcj5UaG9tYXM8L0F1dGhvcj48WWVhcj4yMDA1PC9ZZWFyPjxS

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ADDIN EN.CITE.DATA [181].

Присутствие редокс-чувствительных цистеинов в молекулах убиквитин-активирующего (Е1) и убиквитин-коньюгирующего (Е2) предполагают существование редокс-регуляции процессов деградации белка. Повышение уровня восстановленного глутатиона (GSH) ингибировало активность Е1 и Е2 PEVuZE5vdGU+PENpdGU+PEF1dGhvcj5PYmluPC9BdXRob3I+PFllYXI+MTk5ODwvWWVhcj48UmVj

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ADDIN EN.CITE.DATA [184].

Резюмируя сказанное выше, важно подчеркнуть следующее: прогрессия клеточного цикла сопровождается не только изменениями уровня циклинов и активности CDK, но и колебаниями соотношения про- и антиоксидантов внутри клетки (окислительно-восстановительного баланса). Исходя из этого, было предположено существование т.н. редокс-цикла внутри клеточного цикла и тесно с ним взаимосвязанного. Пертурбации внутриклеточного окислительно-восстановительного баланса ведут к нарушениям прогрессии клеточного цикла, указывая на возможность регуляции пролиферации через модуляцию редокс-статуса клетки.

РАЗДЕЛ 1.3.

Современное состояние знаний о противоопухолевом эффекте короткоцепочечных пептидов1.3.1. Карнозин и его производные. Общая характеристикаКарнозин представляет собой природный короткоцепочечный пептид, состоящий из двух аминокислот – -аланина и L-гистидина. В организме человека карнозин представлен во многих тканях (мышцы, мозг, печень, ткани глаза, желудок, почки, легочная ткань), достигая наиболее высокой концентрации в скелетных мышцах (~ 20 мM) и в обонятельных луковицах головного мозга (~ 2.5 мM) PEVuZE5vdGU+PENpdGU+PEF1dGhvcj5NYW5uaW9uPC9BdXRob3I+PFllYXI+MTk5MjwvWWVhcj48

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