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

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ADDIN EN.CITE.DATA [138, 177]. В независимом исследовании было показано, что обработка клеток Н2О2 приводит к инактивации Cdc25C, в то время как белок мутантный по Cys377 и Cys330 был нечувствителен к действию Н2О2. PEVuZE5vdGU+PENpdGU+PEF1dGhvcj5Tb2huPC9BdXRob3I+PFllYXI+MjAwMzwvWWVhcj48UmVj

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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 [181].

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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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RW5kTm90ZT4A

ADDIN EN.CITE.DATA [3-6], которая катализирует образование пептидной связи между -аланином и L-гистидином, используя энергию АТФ и ионы Mg2+:

-аланин + L-гистидин + АТФ = карнозин + Pi + АДФ PEVuZE5vdGU+PENpdGU+PEF1dGhvcj5Ecm96YWs8L0F1dGhvcj48WWVhcj4yMDEwPC9ZZWFyPjxS

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ADDIN EN.CITE.DATA [7]Карнозин-синтетаза относится к семейству ATP-grasp ферментов, катализирующих АТФ-зависимое присоединение карбоксила одной молекулы к амино- или тиоловой группе другой с образованием АДФ и органического фосфата (Pi) ADDIN EN.CITE <EndNote><Cite><Author>Galperin</Author><Year>1997</Year><RecNum>328</RecNum><DisplayText>[185]</DisplayText><record><rec-number>328</rec-number><foreign-keys><key app="EN" db-id="w2wfxafe6va9z5eev2l55aa8sxsa599eev2s">328</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Galperin, M. Y.</author><author>Koonin, E. V.</author></authors></contributors><auth-address>National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, Maryland 20894, USA. galperin@ncbi.nlm.nih.gov</auth-address><titles><title>A diverse superfamily of enzymes with ATP-dependent carboxylate-amine/thiol ligase activity</title><secondary-title>Protein Sci</secondary-title><alt-title>Protein science : a publication of the Protein Society</alt-title></titles><periodical><full-title>Protein Sci</full-title><abbr-1>Protein science : a publication of the Protein Society</abbr-1></periodical><alt-periodical><full-title>Protein Sci</full-title><abbr-1>Protein science : a publication of the Protein Society</abbr-1></alt-periodical><pages>2639-43</pages><volume>6</volume><number>12</number><edition>1998/01/07</edition><keywords><keyword>Adenosine Triphosphate/metabolism/ pharmacology</keyword><keyword>Amino Acid Sequence</keyword><keyword>Binding Sites</keyword><keyword>Carbon-Nitrogen Ligases/ chemistry/ metabolism</keyword><keyword>Conserved Sequence</keyword><keyword>Molecular Sequence Data</keyword><keyword>Sequence Alignment</keyword><keyword>Sequence Analysis</keyword><keyword>Structure-Activity Relationship</keyword></keywords><dates><year>1997</year><pub-dates><date>Dec</date></pub-dates></dates><isbn>0961-8368 (Print)&#xD;0961-8368 (Linking)</isbn><accession-num>9416615</accession-num><urls></urls><custom2>PMC2143612</custom2><electronic-resource-num>10.1002/pro.5560061218</electronic-resource-num><remote-database-provider>NLM</remote-database-provider><language>eng</language></record></Cite></EndNote>[185]. Ген карнозин-синтетазы располагается в 11q13 хромосоме человека и экспрессируется главным образом в мозге и мышцах PEVuZE5vdGU+PENpdGU+PEF1dGhvcj5Ecm96YWs8L0F1dGhvcj48WWVhcj4yMDEwPC9ZZWFyPjxS

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ADDIN EN.CITE.DATA [7]. Bauer et al. показали, что карнозин и его производные синтезируется в основном клетками глии. Интересно, что опухолевые клетки, глиомы С6, тоже активно синтезировали карнозин и родственные соединения ADDIN EN.CITE <EndNote><Cite><Author>Bauer</Author><Year>1979</Year><RecNum>343</RecNum><DisplayText>[186]</DisplayText><record><rec-number>343</rec-number><foreign-keys><key app="EN" db-id="w2wfxafe6va9z5eev2l55aa8sxsa599eev2s">343</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Bauer, K.</author><author>Salnikow, J.</author><author>de Vitry, F.</author><author>Tixier-Vidal, A.</author><author>Kleinkauf, H.</author></authors></contributors><titles><title>Characterization and biosynthesis of omega-aminoacyl amino acids from rat brain and the C-6 glioma cell line</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>6402-7</pages><volume>254</volume><number>14</number><edition>1979/07/25</edition><keywords><keyword>Alanine/metabolism</keyword><keyword>Aminobutyrates/metabolism</keyword><keyword>Animals</keyword><keyword>Brain/ metabolism</keyword><keyword>Carnosine/biosynthesis</keyword><keyword>Cell Line</keyword><keyword>Dipeptides/ biosynthesis</keyword><keyword>Glioma/ metabolism</keyword><keyword>Ornithine/metabolism</keyword><keyword>Peptide Biosynthesis</keyword><keyword>Rats</keyword></keywords><dates><year>1979</year><pub-dates><date>Jul 25</date></pub-dates></dates><isbn>0021-9258 (Print)&#xD;0021-9258 (Linking)</isbn><accession-num>447723</accession-num><urls></urls><remote-database-provider>NLM</remote-database-provider><language>eng</language></record></Cite></EndNote>[186]. Синтез карнозина в нейронах обнаружен не был, однако нейроны были способны поглощать карнозин из среды и метаболизировать его PEVuZE5vdGU+PENpdGU+PEF1dGhvcj5CYXVlcjwvQXV0aG9yPjxZZWFyPjE5ODI8L1llYXI+PFJl

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ADDIN EN.CITE.DATA [187-190]. Интересно отметить, что усиление синтеза карнозина сопровождалось дифференцировкой глиальных клеток, что оценивалось по усилению иммуноокрашивания антителами к маркерам дифференциации ADDIN EN.CITE <EndNote><Cite><Author>Hoffmann</Author><Year>1996</Year><RecNum>335</RecNum><DisplayText>[189]</DisplayText><record><rec-number>335</rec-number><foreign-keys><key app="EN" db-id="w2wfxafe6va9z5eev2l55aa8sxsa599eev2s">335</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Hoffmann, A. M.</author><author>Bakardjiev, A.</author><author>Bauer, K.</author></authors></contributors><auth-address>Max-Planck-Institut fur experimentelle Endokrinologie, Hannover, Germany.</auth-address><titles><title>Carnosine-synthesis in cultures of rat glial cells is restricted to oligodendrocytes and carnosine uptake to astrocytes</title><secondary-title>Neurosci Lett</secondary-title><alt-title>Neuroscience letters</alt-title></titles><periodical><full-title>Neurosci Lett</full-title><abbr-1>Neuroscience letters</abbr-1></periodical><alt-periodical><full-title>Neurosci Lett</full-title><abbr-1>Neuroscience letters</abbr-1></alt-periodical><pages>29-32</pages><volume>215</volume><number>1</number><edition>1996/08/30</edition><keywords><keyword>Animals</keyword><keyword>Astrocytes/ metabolism</keyword><keyword>Carnosine/ metabolism</keyword><keyword>Cells, Cultured/metabolism</keyword><keyword>Neuroglia/ metabolism</keyword><keyword>Oligodendroglia/ metabolism</keyword><keyword>Rats</keyword><keyword>Rats, Sprague-Dawley</keyword></keywords><dates><year>1996</year><pub-dates><date>Aug 30</date></pub-dates></dates><isbn>0304-3940 (Print)&#xD;0304-3940 (Linking)</isbn><accession-num>8880746</accession-num><urls></urls><remote-database-provider>NLM</remote-database-provider><language>eng</language></record></Cite></EndNote>[189]. Сходный эффект наблюдали при обработке скелетных мышц новорожденных цыплят. Усиление синтеза карнозина замедляло скорость деления клеток и способствовало превращению миобластов в миотубулы PEVuZE5vdGU+PENpdGU+PEF1dGhvcj5CYWthcmRqaWV2PC9BdXRob3I+PFllYXI+MTk5NDwvWWVh

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ADDIN EN.CITE.DATA [191, 192].

В организме человека существует два фермента, способных расщеплять карнозин на составные аминокислоты: сывороточная (CN1) ADDIN EN.CITE <EndNote><Cite><Author>Perry</Author><Year>1968</Year><RecNum>262</RecNum><DisplayText>[193]</DisplayText><record><rec-number>262</rec-number><foreign-keys><key app="EN" db-id="w2wfxafe6va9z5eev2l55aa8sxsa599eev2s">262</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Perry, T. L.</author><author>Hansen, S.</author><author>Love, D. L.</author></authors></contributors><titles><title>Serum-carnosinase deficiency in carnosinaemia</title><secondary-title>Lancet</secondary-title><alt-title>Lancet</alt-title></titles><periodical><full-title>Lancet</full-title><abbr-1>Lancet</abbr-1></periodical><alt-periodical><full-title>Lancet</full-title><abbr-1>Lancet</abbr-1></alt-periodical><pages>1229-30</pages><volume>1</volume><number>7554</number><edition>1968/06/08</edition><keywords><keyword>Adult</keyword><keyword>Child, Preschool</keyword><keyword>Diet</keyword><keyword>Dipeptidases/ blood</keyword><keyword>Dipeptides/ blood</keyword><keyword>Female</keyword><keyword>Humans</keyword><keyword>Infant</keyword><keyword>Intellectual Disability/blood/complications</keyword><keyword>Male</keyword><keyword>Metabolism, Inborn Errors/ blood</keyword><keyword>Nervous System Diseases/blood/complications</keyword></keywords><dates><year>1968</year><pub-dates><date>Jun 8</date></pub-dates></dates><isbn>0140-6736 (Print)&#xD;0140-6736 (Linking)</isbn><accession-num>4172777</accession-num><urls></urls><remote-database-provider>NLM</remote-database-provider><language>eng</language></record></Cite></EndNote>[193] и тканевая/цитозольная (CN2) карнозиназы PEVuZE5vdGU+PENpdGU+PEF1dGhvcj5MZW5uZXk8L0F1dGhvcj48WWVhcj4xOTg1PC9ZZWFyPjxS

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