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

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ADDIN EN.CITE.DATA [155, 157]. Интересно отметить, что молекула малой ГТФазы Ras, активатора ERK1/2, содержит редокс-чувствительные цистеины PEVuZE5vdGU+PENpdGU+PEF1dGhvcj5DaHU8L0F1dGhvcj48WWVhcj4yMDA0PC9ZZWFyPjxSZWNO

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ADDIN EN.CITE.DATA [158]. Модификации цистеинов в молекуле Ras под действием Н2О2 может быть одним из механизмов редокс-регуляции ERK1/2 PEVuZE5vdGU+PENpdGU+PEF1dGhvcj5OaXNoaWRhPC9BdXRob3I+PFllYXI+MjAwMjwvWWVhcj48

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ADDIN EN.CITE.DATA [159]. Ингибирование образования Н2О2 с помощью NAC или GSH, а также усиление экспрессии MnСОД препятствовало активации ERK1/2 и дальнейшей передачи сигнала от рецепторов факторов роста к ядру PEVuZE5vdGU+PENpdGU+PEF1dGhvcj5MYXVyZW50PC9BdXRob3I+PFllYXI+MjAwNTwvWWVhcj48

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ADDIN EN.CITE.DATA [28, 160].

Рисунок 1.3.

Примеры редокс-регулируемых модификаций в молекулах белков. Из PEVuZE5vdGU+PENpdGU+PEF1dGhvcj5Db25vdXI8L0F1dGhvcj48WWVhcj4yMDA0PC9ZZWFyPjxS

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ADDIN EN.CITE.DATA [149] с изменениями. (А) Обратимое глутатионилирование остатка цистеина. (Б) Образование дисульфидной связи в молекуле тиоредоксина. (В) Взаимодействие электрона с изоаллоксазиновой сопряжённой циклической системой флавина – кофактора белка электронно-транспортной цепи. (Г) Окисленная иона железа в составе гемма. (Д) Диссоциация окисленного переходного металла (Х) из металлсвязывающего домена белка.

В нескольких независимых лабораториях было показано, что ДНК-связывающий домен некоторых факторов транксрипции (р53, NF-kB, AP-1, c-Myb, Ets, Sp-1, Egr-1 и др.) содержит консервативные цистеины, замещение или удаление которых приводит к нарушению редокс-регуляции и изменению активности/функции белка (см. ADDIN EN.CITE <EndNote><Cite><Author>Sun</Author><Year>1996</Year><RecNum>313</RecNum><DisplayText>[161]</DisplayText><record><rec-number>313</rec-number><foreign-keys><key app="EN" db-id="w2wfxafe6va9z5eev2l55aa8sxsa599eev2s">313</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Sun, Y.</author><author>Oberley, L. W.</author></authors></contributors><auth-address>Department of Cancer Research, Parke-Davis Pharmaceutical Research, Division of Warner-Lambert Company, Ann Arbor, MI 48105, USA.</auth-address><titles><title>Redox regulation of transcriptional activators</title><secondary-title>Free Radic Biol Med</secondary-title><alt-title>Free radical biology &amp; medicine</alt-title></titles><periodical><full-title>Free Radic Biol Med</full-title><abbr-1>Free radical biology &amp; medicine</abbr-1></periodical><alt-periodical><full-title>Free Radic Biol Med</full-title><abbr-1>Free radical biology &amp; medicine</abbr-1></alt-periodical><pages>335-48</pages><volume>21</volume><number>3</number><edition>1996/01/01</edition><keywords><keyword>Animals</keyword><keyword>Binding Sites</keyword><keyword>DNA/metabolism</keyword><keyword>Humans</keyword><keyword>NF-kappa B/chemistry/metabolism</keyword><keyword>Oxidation-Reduction</keyword><keyword>Transcription Factor AP-1/chemistry/metabolism</keyword><keyword>Transcription Factors/chemistry/metabolism</keyword><keyword>Tumor Suppressor Protein p53/chemistry/metabolism</keyword></keywords><dates><year>1996</year></dates><isbn>0891-5849 (Print)&#xD;0891-5849 (Linking)</isbn><accession-num>8855444</accession-num><urls></urls><remote-database-provider>NLM</remote-database-provider><language>eng</language></record></Cite></EndNote>[161] и ссылки в нем). Например, замещение консервативных цистеинов в молекуле опухолевого супрессора р53 приводит к снижению его ДНК-связывающих способностей. Неспособный связываться с ДНК белок не может выполнять свои функции фактора транскрипции и опухолевого супрессора, что часто приводит к трансформации клетки и чрезмерной пролиферации PEVuZE5vdGU+PENpdGU+PEF1dGhvcj5DaG88L0F1dGhvcj48WWVhcj4xOTk0PC9ZZWFyPjxSZWNO

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ZT4A

ADDIN EN.CITE.DATA [162, 163]. Сходным образом замещение цистеинов в молекулах NF-kB и АР-1 и нарушение их редокс-регуляции способствует абберантной пролиферации и развитию опухолей PEVuZE5vdGU+PENpdGU+PEF1dGhvcj5Ub2xlZGFubzwvQXV0aG9yPjxZZWFyPjE5OTE8L1llYXI+

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ADDIN EN.CITE.DATA [164, 165].

Показано, что промотор циклина D1, важного регулятора прогрессии клетки через G1 фазу, содержит сайты связывания редок-регулируемых факторов транскрипции, таких как NF-kB, AP-1, Sp-1 и др, то есть экспрессия циклина D1 зависит от состояния внутриклеточного редокс-статуса ADDIN EN.CITE <EndNote><Cite><Author>Burch</Author><Year>2005</Year><RecNum>307</RecNum><DisplayText>[166]</DisplayText><record><rec-number>307</rec-number><foreign-keys><key app="EN" db-id="w2wfxafe6va9z5eev2l55aa8sxsa599eev2s">307</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Burch, P. M.</author><author>Heintz, N. H.</author></authors></contributors><auth-address>Environmental Pathology Program and Vermont Cancer Center, University of Vermont College of Medicine, Burlington, VT 05405, USA.</auth-address><titles><title>Redox regulation of cell-cycle re-entry: cyclin D1 as a primary target for the mitogenic effects of reactive oxygen and nitrogen species</title><secondary-title>Antioxid Redox Signal</secondary-title><alt-title>Antioxidants &amp; redox signaling</alt-title></titles><periodical><full-title>Antioxid Redox Signal</full-title><abbr-1>Antioxidants &amp; redox signaling</abbr-1></periodical><alt-periodical><full-title>Antioxid Redox Signal</full-title><abbr-1>Antioxidants &amp; redox signaling</abbr-1></alt-periodical><pages>741-51</pages><volume>7</volume><number>5-6</number><edition>2005/05/14</edition><keywords><keyword>Animals</keyword><keyword>Cell Cycle</keyword><keyword>Cyclin D1/ metabolism</keyword><keyword>Humans</keyword><keyword>Mitogens/ metabolism</keyword><keyword>Reactive Nitrogen Species/ metabolism</keyword><keyword>Reactive Oxygen Species/ metabolism</keyword><keyword>Signal Transduction</keyword></keywords><dates><year>2005</year><pub-dates><date>May-Jun</date></pub-dates></dates><isbn>1523-0864 (Print)&#xD;1523-0864 (Linking)</isbn><accession-num>15890020</accession-num><urls></urls><electronic-resource-num>10.1089/ars.2005.7.741</electronic-resource-num><remote-database-provider>NLM</remote-database-provider><language>eng</language></record></Cite></EndNote>[166]. В условиях окислительного стресса происходит глутатионилирование c-Jun, одной из субъединиц АР-1, по Cys269, который находится в сайте связывания ДНК. Глутатионилирование ДНК-связывающего домена ингибирует активность АР-1 и репрессирует экспрессию циклина D1. В опухолевых клетках часто происходит мутация Cys269 и его замена на серин, что приводит к потере редокс-регуляции и абберантной пролиферации PEVuZE5vdGU+PENpdGU+PEF1dGhvcj5LbGF0dDwvQXV0aG9yPjxZZWFyPjE5OTk8L1llYXI+PFJl

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ADDIN EN.CITE.DATA [167]. Чувствительность к состоянию редокс-статуса была также показана для c-Myb и NF-Y, регулирующим транскрипцию циклинов В1 и А. Фактор транскрипции b-Myb содержит семь редокс-чувствительных цистеинов. Смещение окислительно-восстановительного равновесия в более окисленное состояние с помощью окислителя диамида значительно снижало активность b-Myb, приводя к нарушению связывания транскрипционного фактора с ДНК. Интересно отметить, что повышенный уровень b-Myb часто встречается в опухолевых клетках. Как отмечалось выше, большинство опухолевых клеток характеризуется повышенным содержанием АФК, что возможно и приводит к нарушению регуляции пролиферации с помощью b-myb PEVuZE5vdGU+PENpdGU+PEF1dGhvcj5CZXJnaG9sdHo8L0F1dGhvcj48WWVhcj4yMDAxPC9ZZWFy

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ADDIN EN.CITE.DATA [168]. Фактор транскрипции NF-Y на 30% существует в виде неактивных димеров. Добавление восстановителя, дитиотреитола, к NF-Y способствовало усилению связывания NF-Y с ДНК. Замещение Cys85 и Cys89 в молекуле NF-Y на серины приводило к тому, что NF-Y присутствовал только в форме мономеров и его активность не зависела от дитиотреитола PEVuZE5vdGU+PENpdGU+PEF1dGhvcj5OYWtzaGF0cmk8L0F1dGhvcj48WWVhcj4xOTk2PC9ZZWFy

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ADDIN EN.CITE.DATA [169].

Рисунок 1.3.

Редокс-регуляция клеточного цикла. Из ADDIN EN.CITE <EndNote><Cite><Author>Sarsour</Author><Year>2009</Year><RecNum>19</RecNum><DisplayText>[152]</DisplayText><record><rec-number>19</rec-number><foreign-keys><key app="EN" db-id="w2wfxafe6va9z5eev2l55aa8sxsa599eev2s">19</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Sarsour, E. H.</author><author>Kumar, M. G.</author><author>Chaudhuri, L.</author><author>Kalen, A. L.</author><author>Goswami, P. C.</author></authors></contributors><auth-address>Free Radical and Radiation Biology Program, Department of Radiation Oncology, University of Iowa, Iowa City, Iowa, USA.</auth-address><titles><title>Redox control of the cell cycle in health and disease</title><secondary-title>Antioxid Redox Signal</secondary-title><alt-title>Antioxidants &amp; redox signaling</alt-title></titles><periodical><full-title>Antioxid Redox Signal</full-title><abbr-1>Antioxidants &amp; redox signaling</abbr-1></periodical><alt-periodical><full-title>Antioxid Redox Signal</full-title><abbr-1>Antioxidants &amp; redox signaling</abbr-1></alt-periodical><pages>2985-3011</pages><volume>11</volume><number>12</number><edition>2009/06/10</edition><keywords><keyword>Animals</keyword><keyword>Cell Cycle</keyword><keyword>Disease</keyword><keyword>Humans</keyword><keyword>Oxidation-Reduction</keyword></keywords><dates><year>2009</year><pub-dates><date>Dec</date></pub-dates></dates><isbn>1557-7716 (Electronic)&#xD;1523-0864 (Linking)</isbn><accession-num>19505186</accession-num><urls></urls><custom2>PMC2783918</custom2><custom6>Nihms145947</custom6><electronic-resource-num>10.1089/ars.2009.2513</electronic-resource-num><remote-database-provider>NLM</remote-database-provider><language>eng</language></record></Cite></EndNote>[152] с изменениями, см. пояснения в тексте.

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ADDIN EN.CITE.DATA [170]. Полученные данные указывали на необходимость присутствия небольших количеств Н2О2 для перехода клеток из G1 в S фазу клеточного цикла.

Подобно действию NAC, усиление экспрессии каталазы или GPx, катализаторов разложения Н2О2, приводило к снижению внутриклеточного уровня Н2О2 и остановке клеточного цикла в G1 фазе PEVuZE5vdGU+PENpdGU+PEF1dGhvcj5PbnVtYWg8L0F1dGhvcj48WWVhcj4yMDA5PC9ZZWFyPjxS

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