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

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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&apos;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)&#xD;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.





</author><author>Hunter, T.</author></authors></contributors><auth-address>Molecular Biology and Virology Laboratory, Salk Institute for Biological Studies, San Diego, California 92138.</auth-address><titles><title>Isolation of a human cyclin cDNA: evidence for cyclin mRNA and protein regulation in the cell cycle and for interaction with p34cdc2</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>833-46</pages><volume>58</volume><number>5</number><edition>1989/09/08</edition><keywords><keyword>Amino Acid Sequence</keyword><keyword>Base Sequence</keyword><keyword>CDC2 Protein Kinase</keyword><keyword>Cell Cycle</keyword><keyword>Cloning, Molecular</keyword><keyword>DNA/genetics</keyword><keyword>Gene Expression Regulation</keyword><keyword>HeLa Cells</keyword><keyword>Humans</keyword><keyword>Mitosis</keyword><keyword>Molecular Sequence Data</keyword><keyword>Nuclear Proteins/ genetics/immunology</keyword><keyword>Phosphoproteins/metabolism</keyword><keyword>Proliferating Cell Nuclear Antigen</keyword><keyword>Protamine Kinase/metabolism</keyword><keyword>Protein Binding</keyword></keywords><dates><year>1989</year><pub-dates><date>Sep 8</date></pub-dates></dates><isbn>0092-8674 (Print)&#xD;0092-8674 (Linking)</isbn><accession-num>2570636</accession-num><urls></urls><remote-database-provider>NLM</remote-database-provider><language>eng</language></record></Cite></EndNote>[121]. На сегодняшний день семейство циклинов В состоит из 5 белков – циклины В1, В2, В3, В4 и В5, из которых В1 является наиболее охарактеризованным ADDIN EN.CITE <EndNote><Cite><Author>Ito</Author><Year>2000</Year><RecNum>472</RecNum><DisplayText>[122]</DisplayText><record><rec-number>472</rec-number><foreign-keys><key app="EN" db-id="w2wfxafe6va9z5eev2l55aa8sxsa599eev2s">472</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Ito, M.</author></authors></contributors><auth-address>Department of Biological Sciences, Graduate School of Science, University of Tokyo, Japan.</auth-address><titles><title>Factors controlling cyclin B expression</title><secondary-title>Plant Mol Biol</secondary-title><alt-title>Plant molecular biology</alt-title></titles><periodical><full-title>Plant Mol Biol</full-title><abbr-1>Plant molecular biology</abbr-1></periodical><alt-periodical><full-title>Plant Mol Biol</full-title><abbr-1>Plant molecular biology</abbr-1></alt-periodical><pages>677-90</pages><volume>43</volume><number>5-6</number><edition>2000/11/23</edition><keywords><keyword>Animals</keyword><keyword>Base Sequence</keyword><keyword>Cell Cycle</keyword><keyword>Cyclin B/ genetics/metabolism</keyword><keyword>Cyclin-Dependent Kinases/metabolism</keyword><keyword>Gene Expression Regulation, Plant</keyword><keyword>Genes, Plant</keyword><keyword>Molecular Sequence Data</keyword><keyword>Phylogeny</keyword><keyword>Plants/ genetics/metabolism</keyword><keyword>Promoter Regions, Genetic</keyword><keyword>Sequence Alignment</keyword><keyword>Yeasts/genetics/metabolism</keyword></keywords><dates><year>2000</year><pub-dates><date>Aug</date></pub-dates></dates><isbn>0167-4412 (Print)&#xD;0167-4412 (Linking)</isbn><accession-num>11089869</accession-num><urls></urls><remote-database-provider>NLM</remote-database-provider><language>eng</language></record></Cite></EndNote>[122]. Промотор циклина В1 содержит сайты связывания для множества транскрипционных факторов, в том числе B-Myb, NF-Y, USF, p53, p21, Ap-1, Ap-2, Ets-1 и др. PEVuZE5vdGU+PENpdGU+PEF1dGhvcj5UcmVtYmxleTwvQXV0aG9yPjxZZWFyPjIwMDA8L1llYXI+

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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)&#xD;0196-4763 (Linking)</isbn><accession-num>8723902</accession-num><urls></urls><electronic-resource-num>10.1002/(sici)1097-0320(19960501)24:1&lt;49::aid-cyto6&gt;3.0.co;2-d</electronic-resource-num><remote-database-provider>NLM</remote-database-provider><language>eng</language></record></Cite></EndNote>[124]. В середине митоза уровень циклина В1 резко снижается за счет работы АРС и остается низким до поздней S фазы, когда происходит ингибирование АРС с помощью Emi1 и комплекса циклин А/CDK2 PEVuZE5vdGU+PENpdGU+PEF1dGhvcj5Ic3U8L0F1dGhvcj48WWVhcj4yMDAyPC9ZZWFyPjxSZWNO

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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]. Транслокация циклин В1/CDK1 в ядро возможна только при фосфорилировании 5 серинов в сайте удерживающем циклин В1 в цитоплазме (cytoplasmic retention site, CRS): Ser116, Ser26, Ser128, Ser133 и Ser147 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)&#xD;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 [128]. Однако комплекс остается неактивным, потому что протеинкиназы Wee1 и Myt1 фосфорилируют CDK1 по Thr14 и Tyr15, ингибируя активность CDK1. Wee1 находится в ядре, а Myt1 – на цитоплазматической стороне мембраны эндоплазматического ретикулума PEVuZE5vdGU+PENpdGU+PEF1dGhvcj5Tb2xvbW9uPC9BdXRob3I+PFllYXI+MTk5MjwvWWVhcj48

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ADDIN EN.CITE.DATA [129-131]. Интересно отметить, что активация ERK1/2 снижает активность Myt1 через активацию RSK, непосредственного субстрата ERK1/2, который фосфорилирует и ингибирует Myt1, приводя к остановке клеточного цикла в G2/M PEVuZE5vdGU+PENpdGU+PEF1dGhvcj5QYWxtZXI8L0F1dGhvcj48WWVhcj4xOTk4PC9ZZWFyPjxS

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ADDIN EN.CITE.DATA [132]. Для активации комплекса циклин В/CDK1 необходима фосфатаза Cdc25С, которая дефосфорилирует CDK1, убирая ингибирующие фосфаты PEVuZE5vdGU+PENpdGU+PEF1dGhvcj5TdHJhdXNmZWxkPC9BdXRob3I+PFllYXI+MTk5MTwvWWVh

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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 &amp; 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)&#xD;1059-1524 (Linking)</isbn><accession-num>1532335</accession-num><urls></urls><custom2>PMC275499</custom2><remote-database-provider>NLM</remote-database-provider><language>eng</language></record></Cite></EndNote>[129]. Параллельно с активацией циклин В/CDK1 происходит ингибирование Wee1 и Myt1. В течение интерфазы Cdc25C-associated protein kinase (C-TAK1) фосфорилируют Cdc25С по Ser216, что способствует его связыванию с белком 14-3-3 PEVuZE5vdGU+PENpdGU+PEF1dGhvcj5HcmF2ZXM8L0F1dGhvcj48WWVhcj4yMDAwPC9ZZWFyPjxS

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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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