«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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PjM4NzwvcmVjLW51bWJlcj48Zm9yZWlnbi1rZXlzPjxrZXkgYXBwPSJFTiIgZGItaWQ9Incyd2Z4
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b3I+PGF1dGhvcj5IdSwgUy48L2F1dGhvcj48YXV0aG9yPkxpbiwgSi48L2F1dGhvcj48YXV0aG9y
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cmlidXRvcnM+PGF1dGgtYWRkcmVzcz5EZXBhcnRtZW50IG9mIE5ldXJvc3VyZ2VyeSwgU291dGh3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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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d29yZD48a2V5d29yZD5BbmltYWxzPC9rZXl3b3JkPjxrZXl3b3JkPkJhY3RlcmlhbCBQcm90ZWlu
cy9jaGVtaXN0cnkvbWV0YWJvbGlzbS9waHlzaW9sb2d5PC9rZXl3b3JkPjxrZXl3b3JkPkJpdmFs
dmlhL2dlbmV0aWNzPC9rZXl3b3JkPjxrZXl3b3JkPkNITyBDZWxscy9jaGVtaXN0cnkvcGh5c2lv
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LVJlZHVjdGlvbjwva2V5d29yZD48a2V5d29yZD5Qcm90ZWluIFN0cnVjdHVyZSwgU2Vjb25kYXJ5
L2dlbmV0aWNzL3BoeXNpb2xvZ3k8L2tleXdvcmQ+PGtleXdvcmQ+UHJvdG96b2FuIFByb3RlaW5z
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dGljczwva2V5d29yZD48a2V5d29yZD5Td2luZS9nZW5ldGljczwva2V5d29yZD48a2V5d29yZD5Y
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PC9kYXRlPjwvcHViLWRhdGVzPjwvZGF0ZXM+PGlzYm4+MTUzMS0yMjY3IChFbGVjdHJvbmljKSYj
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YWdlPmVuZzwvbGFuZ3VhZ2U+PC9yZWNvcmQ+PC9DaXRlPjwvRW5kTm90ZT5=
ADDIN EN.CITE PEVuZE5vdGU+PENpdGU+PEF1dGhvcj5Db25vdXI8L0F1dGhvcj48WWVhcj4yMDA0PC9ZZWFyPjxS
ZWNOdW0+MzU8L1JlY051bT48RGlzcGxheVRleHQ+WzE0OV08L0Rpc3BsYXlUZXh0PjxyZWNvcmQ+
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b250cmlidXRvcnM+PGF1dGhvcnM+PGF1dGhvcj5Db25vdXIsIEouIEUuPC9hdXRob3I+PGF1dGhv
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aHlzaW9sIEdlbm9taWNzPC9mdWxsLXRpdGxlPjxhYmJyLTE+UGh5c2lvbG9naWNhbCBnZW5vbWlj
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d29yZD48a2V5d29yZD5BbmltYWxzPC9rZXl3b3JkPjxrZXl3b3JkPkJhY3RlcmlhbCBQcm90ZWlu
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bG9neTwva2V5d29yZD48a2V5d29yZD5Ib3JzZXMvZ2VuZXRpY3M8L2tleXdvcmQ+PGtleXdvcmQ+
SHVtYW5zPC9rZXl3b3JkPjxrZXl3b3JkPk1pY2U8L2tleXdvcmQ+PGtleXdvcmQ+T3hpZGF0aW9u
LVJlZHVjdGlvbjwva2V5d29yZD48a2V5d29yZD5Qcm90ZWluIFN0cnVjdHVyZSwgU2Vjb25kYXJ5
L2dlbmV0aWNzL3BoeXNpb2xvZ3k8L2tleXdvcmQ+PGtleXdvcmQ+UHJvdG96b2FuIFByb3RlaW5z
L2NoZW1pc3RyeS9tZXRhYm9saXNtL3BoeXNpb2xvZ3k8L2tleXdvcmQ+PGtleXdvcmQ+UmF0czwv
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ZW5vcHVzIFByb3RlaW5zL2NoZW1pc3RyeS9tZXRhYm9saXNtL3BoeXNpb2xvZ3k8L2tleXdvcmQ+
PC9rZXl3b3Jkcz48ZGF0ZXM+PHllYXI+MjAwNDwveWVhcj48cHViLWRhdGVzPjxkYXRlPkp1bCA4
PC9kYXRlPjwvcHViLWRhdGVzPjwvZGF0ZXM+PGlzYm4+MTUzMS0yMjY3IChFbGVjdHJvbmljKSYj
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dGUtZGF0YWJhc2UtcHJvdmlkZXI+TkxNPC9yZW1vdGUtZGF0YWJhc2UtcHJvdmlkZXI+PGxhbmd1
YWdlPmVuZzwvbGFuZ3VhZ2U+PC9yZWNvcmQ+PC9DaXRlPjwvRW5kTm90ZT5=
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 & medicine</alt-title></titles><periodical><full-title>Free Radic Biol Med</full-title><abbr-1>Free radical biology & medicine</abbr-1></periodical><alt-periodical><full-title>Free Radic Biol Med</full-title><abbr-1>Free radical biology & 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)
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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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 & redox signaling</alt-title></titles><periodical><full-title>Antioxid Redox Signal</full-title><abbr-1>Antioxidants & redox signaling</abbr-1></periodical><alt-periodical><full-title>Antioxid Redox Signal</full-title><abbr-1>Antioxidants & 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)
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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 & redox signaling</alt-title></titles><periodical><full-title>Antioxid Redox Signal</full-title><abbr-1>Antioxidants & redox signaling</abbr-1></periodical><alt-periodical><full-title>Antioxid Redox Signal</full-title><abbr-1>Antioxidants & 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)
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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ADDIN EN.CITE.DATA [63, 171, 172]. Обработка Her1 фибробластов с помощью Н2О2, наоборот, повышала уровень циклина D1, что предположительно было результатом ингибирования деградации циклина D1 PEVuZE5vdGU+PENpdGU+PEF1dGhvcj5NYXJ0aW5leiBNdW5vejwvQXV0aG9yPjxZZWFyPjIwMDE8
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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)
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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