«Антипролиферативное действие карнозина и его производных на опухолевые клетки нейрального происхождения ...»
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ADDIN EN.CITE.DATA [116]. Как только клетки входят в S фазу циклин Е деградирует и CDK2 соединяется с циклином А PEVuZE5vdGU+PENpdGU+PEF1dGhvcj5TaGVycjwvQXV0aG9yPjxZZWFyPjE5OTM8L1llYXI+PFJl
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AG==
ADDIN EN.CITE.DATA [81, 110]. Циклин А не накапливается в клетке вплоть до поздней G1 фазы из-за убиквитинирования под действием АРС. Циклины D и Е нечувствительны к действию АРС. Перед входом в S фазу Emi1, экспрессия которого запускается с помощью E2F, ингибирует АРС, способствуя стабилизации циклина А и активации СDK2. PEVuZE5vdGU+PENpdGU+PEF1dGhvcj5Ic3U8L0F1dGhvcj48WWVhcj4yMDAyPC9ZZWFyPjxSZWNO
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ADDIN EN.CITE.DATA [117].
S фаза. Основным событием S фазы является удвоение ДНК (репликация) и хроматина. Репликация может начинаться только в определенных местах – точках начала репликации (origins of replication, OR), которые разбросаны по всей ДНК. Подготовка к репликации начинает еще в конце митоза – начале G1 фазы, когда в точках начала репликации собираются т.н. пререпликационные комплексы (pre-RC), состоящие из большого количества белков необходимых для инициации репликации. Эта стадия часто называется лицензированием (licensing) точек начала репликации, т.к. синтез ДНК может происходить только в OR содержащих pre-RC. В S фазе активный комплекс циклин А/CDK2 запускает сборку преинициирующих комплексов вокруг компонентов pre-RC. Преинициирующие комплексы раскручивают спираль ДНК подготавливая место посадки ДНК, полимеразы и других ферментов репликации. Сразу после репликации OR комплекс pre-RC разбирается под действием циклин А/CDK2. Сборка новых pre-RC в S фазе невозможна из-за присутствия активных СDK, что препятствует множественной репликации PEVuZE5vdGU+PENpdGU+PEF1dGhvcj5CZWxsPC9BdXRob3I+PFllYXI+MjAwMjwvWWVhcj48UmVj
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ADDIN EN.CITE.DATA [118, 119]. Репликация хромосом состоит из репликации ДНК и репликации хроматина. Основную массу хроматина составляют белки гистоны. Циклин А/CDK2 индуцирует синтез гистонов, поставляя материал для упаковки новосинтезированной ДНК. К концу S фазы каждая хромосома состоит из двух пар идентичных сестринских хроматид. Каждая пара сестринских хроматид связана между собой комплексами белков, когезинами, которые регулируют процесс разделения сестринских хроматид при митозе ADDIN EN.CITE <EndNote><Cite><Author>Groth</Author><Year>2007</Year><RecNum>415</RecNum><DisplayText>[120]</DisplayText><record><rec-number>415</rec-number><foreign-keys><key app="EN" db-id="w2wfxafe6va9z5eev2l55aa8sxsa599eev2s">415</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Groth, A.</author><author>Rocha, W.</author><author>Verreault, A.</author><author>Almouzni, G.</author></authors></contributors><auth-address>Laboratory of Nuclear Dynamics and Genome Plasticity, UMR 218 CNRS/Institut Curie, 26 rue d'Ulm, 75248 Paris, Cedex 5, France.</auth-address><titles><title>Chromatin challenges during DNA replication and repair</title><secondary-title>Cell</secondary-title><alt-title>Cell</alt-title></titles><periodical><full-title>Cell</full-title><abbr-1>Cell</abbr-1></periodical><alt-periodical><full-title>Cell</full-title><abbr-1>Cell</abbr-1></alt-periodical><pages>721-33</pages><volume>128</volume><number>4</number><edition>2007/02/27</edition><keywords><keyword>Animals</keyword><keyword>Chromatin/ genetics</keyword><keyword>DNA Repair/ genetics</keyword><keyword>DNA Replication/ genetics</keyword><keyword>Epigenesis, Genetic/ genetics</keyword><keyword>Histones/genetics/metabolism</keyword><keyword>Humans</keyword><keyword>Nucleosomes/genetics</keyword><keyword>Protein Processing, Post-Translational/genetics</keyword><keyword>Transcription Factors/metabolism</keyword></keywords><dates><year>2007</year><pub-dates><date>Feb 23</date></pub-dates></dates><isbn>0092-8674 (Print)
0092-8674 (Linking)</isbn><accession-num>17320509</accession-num><urls></urls><electronic-resource-num>10.1016/j.cell.2007.01.030</electronic-resource-num><remote-database-provider>NLM</remote-database-provider><language>eng</language></record></Cite></EndNote>[120].
G2 фаза. Прохождение клетки через G2 фазу и вход в митоз регулируется комплексом циклина В/CDK1 ADDIN EN.CITE <EndNote><Cite><Author>Pines</Author><Year>1989</Year><RecNum>225</RecNum><DisplayText>[121]</DisplayText><record><rec-number>225</rec-number><foreign-keys><key app="EN" db-id="w2wfxafe6va9z5eev2l55aa8sxsa599eev2s">225</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Pines, J.
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ADDIN EN.CITE.DATA [123]. Экспрессия гена циклина В1 наблюдается на протяжении всего клеточного цикла, однако в G2 уровень циклина В1 в 50 раз больше, чем в G1. Наивысшего уровня циклин В1 достигает в конце G2 фазы – начале митоза ADDIN EN.CITE <EndNote><Cite><Author>Kakino</Author><Year>1996</Year><RecNum>470</RecNum><DisplayText>[124]</DisplayText><record><rec-number>470</rec-number><foreign-keys><key app="EN" db-id="w2wfxafe6va9z5eev2l55aa8sxsa599eev2s">470</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Kakino, S.</author><author>Sasaki, K.</author><author>Kurose, A.</author><author>Ito, H.</author></authors></contributors><auth-address>Department of Neurosurgery, Yamaguchi University School of Medicine, Japan.</auth-address><titles><title>Intracellular localization of cyclin B1 during the cell cycle in glioma cells</title><secondary-title>Cytometry</secondary-title><alt-title>Cytometry</alt-title></titles><periodical><full-title>Cytometry</full-title><abbr-1>Cytometry</abbr-1></periodical><alt-periodical><full-title>Cytometry</full-title><abbr-1>Cytometry</abbr-1></alt-periodical><pages>49-54</pages><volume>24</volume><number>1</number><edition>1996/05/01</edition><keywords><keyword>Cell Cycle</keyword><keyword>Cyclin B</keyword><keyword>Cyclin B1</keyword><keyword>Cyclins/ analysis</keyword><keyword>Cytophotometry/ methods</keyword><keyword>Flow Cytometry/ methods</keyword><keyword>Glioblastoma</keyword><keyword>Humans</keyword><keyword>Neuroglia/ chemistry</keyword><keyword>Tumor Cells, Cultured</keyword></keywords><dates><year>1996</year><pub-dates><date>May 1</date></pub-dates></dates><isbn>0196-4763 (Print)
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ADDIN EN.CITE.DATA [117, 125]. Усиление экспрессии циклина В1 приводит к его накоплению в цитоплазме, достигнув определенной концентрации циклин В связывается с CDK1. Образовавшийся комплекс циклин В1/CDK1 перемещается в ядро PEVuZE5vdGU+PENpdGU+PEF1dGhvcj5MaTwvQXV0aG9yPjxZZWFyPjE5OTc8L1llYXI+PFJlY051
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ADDIN EN.CITE.DATA [126]. Показано, что ингибирование ERK1/2 препятствует фосфорилированию CRS, что приводит к удерживанию комплекса циклин В1/CDK1 в цитозоле ADDIN EN.CITE <EndNote><Cite><Author>Walsh</Author><Year>2003</Year><RecNum>490</RecNum><DisplayText>[127]</DisplayText><record><rec-number>490</rec-number><foreign-keys><key app="EN" db-id="w2wfxafe6va9z5eev2l55aa8sxsa599eev2s">490</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Walsh, S.</author><author>Margolis, S. S.</author><author>Kornbluth, S.</author></authors></contributors><auth-address>Duke University Medical Center, Durham, NC 27710, USA.</auth-address><titles><title>Phosphorylation of the cyclin b1 cytoplasmic retention sequence by mitogen-activated protein kinase and Plx</title><secondary-title>Mol Cancer Res</secondary-title><alt-title>Molecular cancer research : MCR</alt-title></titles><periodical><full-title>Mol Cancer Res</full-title><abbr-1>Molecular cancer research : MCR</abbr-1></periodical><alt-periodical><full-title>Mol Cancer Res</full-title><abbr-1>Molecular cancer research : MCR</abbr-1></alt-periodical><pages>280-9</pages><volume>1</volume><number>4</number><edition>2003/03/04</edition><keywords><keyword>Amino Acid Sequence</keyword><keyword>Animals</keyword><keyword>Cell Cycle Proteins</keyword><keyword>Cell Extracts</keyword><keyword>Cyclin B/ chemistry/ metabolism</keyword><keyword>Cyclin B1</keyword><keyword>MAP Kinase Signaling System</keyword><keyword>Mitogen-Activated Protein Kinases/ metabolism</keyword><keyword>Molecular Sequence Data</keyword><keyword>Oocytes/metabolism</keyword><keyword>Phosphorylation</keyword><keyword>Protein-Serine-Threonine Kinases/ metabolism</keyword><keyword>Serine/metabolism</keyword><keyword>Xenopus Proteins/metabolism</keyword><keyword>Xenopus laevis/metabolism</keyword></keywords><dates><year>2003</year><pub-dates><date>Feb</date></pub-dates></dates><isbn>1541-7786 (Print)
1541-7786 (Linking)</isbn><accession-num>12612056</accession-num><urls></urls><remote-database-provider>NLM</remote-database-provider><language>eng</language></record></Cite></EndNote>[127]. Yang et al. предполагают, что CRS циклина В1 является частью последовательности для экспорта белка в ядро (nuclear export sequences, NES), с помощью которой циклин В1 взаимодействует с экспортирующим ядерным рецептором (chromosome region maintenance 1, CRM1) PEVuZE5vdGU+PENpdGU+PEF1dGhvcj5ZYW5nPC9BdXRob3I+PFllYXI+MTk5ODwvWWVhcj48UmVj
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ADDIN EN.CITE.DATA [133, 134]. Активированный циклин В/CDK1 запускает события раннего митоза ADDIN EN.CITE <EndNote><Cite><Author>Solomon</Author><Year>1992</Year><RecNum>255</RecNum><DisplayText>[129]</DisplayText><record><rec-number>255</rec-number><foreign-keys><key app="EN" db-id="w2wfxafe6va9z5eev2l55aa8sxsa599eev2s">255</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Solomon, M. J.</author><author>Lee, T.</author><author>Kirschner, M. W.</author></authors></contributors><auth-address>Department of Biochemistry and Biophysics, University of California, San Francisco 94143-0448.</auth-address><titles><title>Role of phosphorylation in p34cdc2 activation: identification of an activating kinase</title><secondary-title>Mol Biol Cell</secondary-title><alt-title>Molecular biology of the cell</alt-title></titles><periodical><full-title>Mol Biol Cell</full-title><abbr-1>Molecular biology of the cell</abbr-1></periodical><alt-periodical><full-title>Mol Biol Cell</full-title><abbr-1>Molecular biology of the cell</abbr-1></alt-periodical><pages>13-27</pages><volume>3</volume><number>1</number><edition>1992/01/01</edition><keywords><keyword>Adenosine Triphosphate/metabolism</keyword><keyword>Animals</keyword><keyword>Antibodies, Monoclonal/immunology</keyword><keyword>Base Sequence</keyword><keyword>Binding Sites</keyword><keyword>CDC2 Protein Kinase/isolation & purification/ metabolism</keyword><keyword>Cyclins/metabolism</keyword><keyword>Enzyme Activation</keyword><keyword>Immunoblotting</keyword><keyword>Mitosis/drug effects</keyword><keyword>Molecular Sequence Data</keyword><keyword>Phosphorylation</keyword><keyword>Vanadates/pharmacology</keyword><keyword>Xenopus laevis</keyword></keywords><dates><year>1992</year><pub-dates><date>Jan</date></pub-dates></dates><isbn>1059-1524 (Print)
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ADDIN EN.CITE.DATA [138, 139]. Активирующаяся в ответ на повреждение ДНК Chk1 киназа тоже способна фосфорилировать Cdc25С, приводя к ингибированию фосфатазы и остановке прогрессии клеточного цикла PEVuZE5vdGU+PENpdGU+PEF1dGhvcj5QZW5nPC9BdXRob3I+PFllYXI+MTk5NzwvWWVhcj48UmVj
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