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

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Одним из основных антиоксидантных ферментов клетки является супероксиддисмутаза (СОД), катализирующая реакцию дисмутации супероксида: О2-• + О2-• O2 + H2O2. Несмотря на то, что дисмутация О2-• происходит быстро и сама по себе, СОД делает реакцию практически молниеносной (k=2х109 M-1•s-1) ADDIN EN.CITE <EndNote><Cite><Author>McCord</Author><Year>1969</Year><RecNum>207</RecNum><DisplayText>[50]</DisplayText><record><rec-number>207</rec-number><foreign-keys><key app="EN" db-id="w2wfxafe6va9z5eev2l55aa8sxsa599eev2s">207</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>McCord, J. M.</author><author>Fridovich, I.</author></authors></contributors><titles><title>Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein)</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>6049-55</pages><volume>244</volume><number>22</number><edition>1969/11/25</edition><keywords><keyword>Adrenochrome</keyword><keyword>Alkanes</keyword><keyword>Animals</keyword><keyword>Blood Proteins</keyword><keyword>Cattle</keyword><keyword>Centrifugation</keyword><keyword>Copper</keyword><keyword>Cytochromes</keyword><keyword>Epinephrine</keyword><keyword>Erythrocytes/enzymology</keyword><keyword>Free Radicals</keyword><keyword>Hydrogen Peroxide</keyword><keyword>Oxidoreductases/blood/isolation &amp; purification</keyword><keyword>Oxygen</keyword><keyword>Radiochemistry</keyword><keyword>Spectrophotometry</keyword><keyword>Xanthine Oxidase</keyword></keywords><dates><year>1969</year><pub-dates><date>Nov 25</date></pub-dates></dates><isbn>0021-9258 (Print)&#xD;0021-9258 (Linking)</isbn><accession-num>5389100</accession-num><urls></urls><remote-database-provider>NLM</remote-database-provider><language>eng</language></record></Cite></EndNote>[50]. Cуществует три изоформы СОД: митохондриальная (MnСОД) ADDIN EN.CITE <EndNote><Cite><Author>McCord</Author><Year>1969</Year><RecNum>207</RecNum><DisplayText>[50]</DisplayText><record><rec-number>207</rec-number><foreign-keys><key app="EN" db-id="w2wfxafe6va9z5eev2l55aa8sxsa599eev2s">207</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>McCord, J. M.</author><author>Fridovich, I.</author></authors></contributors><titles><title>Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein)</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>6049-55</pages><volume>244</volume><number>22</number><edition>1969/11/25</edition><keywords><keyword>Adrenochrome</keyword><keyword>Alkanes</keyword><keyword>Animals</keyword><keyword>Blood Proteins</keyword><keyword>Cattle</keyword><keyword>Centrifugation</keyword><keyword>Copper</keyword><keyword>Cytochromes</keyword><keyword>Epinephrine</keyword><keyword>Erythrocytes/enzymology</keyword><keyword>Free Radicals</keyword><keyword>Hydrogen Peroxide</keyword><keyword>Oxidoreductases/blood/isolation &amp; purification</keyword><keyword>Oxygen</keyword><keyword>Radiochemistry</keyword><keyword>Spectrophotometry</keyword><keyword>Xanthine Oxidase</keyword></keywords><dates><year>1969</year><pub-dates><date>Nov 25</date></pub-dates></dates><isbn>0021-9258 (Print)&#xD;0021-9258 (Linking)</isbn><accession-num>5389100</accession-num><urls></urls><remote-database-provider>NLM</remote-database-provider><language>eng</language></record></Cite></EndNote>[50], цитоплазматическая (CuZnСОД) ADDIN EN.CITE <EndNote><Cite><Author>Fridovich</Author><Year>1989</Year><RecNum>208</RecNum><DisplayText>[51]</DisplayText><record><rec-number>208</rec-number><foreign-keys><key app="EN" db-id="w2wfxafe6va9z5eev2l55aa8sxsa599eev2s">208</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Fridovich, I.</author></authors></contributors><auth-address>Department of Biochemistry, Duke University Medical Center, Durham, North Carolina 27710.</auth-address><titles><title>Superoxide dismutases. An adaptation to a paramagnetic gas</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>7761-4</pages><volume>264</volume><number>14</number><edition>1989/05/15</edition><keywords><keyword>Catalysis</keyword><keyword>Chemical Phenomena</keyword><keyword>Chemistry</keyword><keyword>Free Radicals</keyword><keyword>Inflammation</keyword><keyword>Magnetics</keyword><keyword>Oxidation-Reduction</keyword><keyword>Oxygen/metabolism</keyword><keyword>Oxygen Consumption</keyword><keyword>Phagocytosis</keyword><keyword>Reperfusion Injury</keyword><keyword>Superoxide Dismutase/ physiology</keyword><keyword>Superoxides/metabolism</keyword></keywords><dates><year>1989</year><pub-dates><date>May 15</date></pub-dates></dates><isbn>0021-9258 (Print)&#xD;0021-9258 (Linking)</isbn><accession-num>2542241</accession-num><urls></urls><remote-database-provider>NLM</remote-database-provider><language>eng</language></record></Cite></EndNote>[51] и внеклеточная, на поверхности клеточных мембран, (ЕС(CuZn)СОД) ADDIN EN.CITE <EndNote><Cite><Author>Folz</Author><Year>1994</Year><RecNum>209</RecNum><DisplayText>[52]</DisplayText><record><rec-number>209</rec-number><foreign-keys><key app="EN" db-id="w2wfxafe6va9z5eev2l55aa8sxsa599eev2s">209</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Folz, R. J.</author><author>Crapo, J. D.</author></authors></contributors><auth-address>Department of Medicine, Duke University Medical Center, Durham, North Carolina 27710.</auth-address><titles><title>Extracellular superoxide dismutase (SOD3): tissue-specific expression, genomic characterization, and computer-assisted sequence analysis of the human EC SOD gene</title><secondary-title>Genomics</secondary-title><alt-title>Genomics</alt-title></titles><periodical><full-title>Genomics</full-title><abbr-1>Genomics</abbr-1></periodical><alt-periodical><full-title>Genomics</full-title><abbr-1>Genomics</abbr-1></alt-periodical><pages>162-71</pages><volume>22</volume><number>1</number><edition>1994/07/01</edition><keywords><keyword>Amino Acid Sequence</keyword><keyword>Base Sequence</keyword><keyword>Chromosome Mapping</keyword><keyword>DNA/genetics</keyword><keyword>DNA Primers/genetics</keyword><keyword>Exons</keyword><keyword>Extracellular Space/enzymology</keyword><keyword>Gene Expression Regulation, Enzymologic</keyword><keyword>Humans</keyword><keyword>Introns</keyword><keyword>Molecular Sequence Data</keyword><keyword>RNA, Messenger/genetics/metabolism</keyword><keyword>Repetitive Sequences, Nucleic Acid</keyword><keyword>Superoxide Dismutase/ genetics</keyword><keyword>Tissue Distribution</keyword></keywords><dates><year>1994</year><pub-dates><date>Jul 1</date></pub-dates></dates><isbn>0888-7543 (Print)&#xD;0888-7543 (Linking)</isbn><accession-num>7959763</accession-num><urls></urls><electronic-resource-num>10.1006/geno.1994.1357</electronic-resource-num><remote-database-provider>NLM</remote-database-provider><language>eng</language></record></Cite></EndNote>[52]. Поскольку митохондрии являются главным источником АФК в клетке, митохондриальная MnСОД представляется первым барьером защищающим клетку от окислительного повреждения. Несколькими независимыми лабораториями было показано, что полное ингибирование MnСОД (Sod2-/-) у новорожденных мышей приводит к гибели животных в течение 1-18 дней после рождения и сопровождается дилатационной кардиомиопатией, усилением накопления липидов в печени и метаболическим ацитодозом PEVuZE5vdGU+PENpdGU+PEF1dGhvcj5MZWJvdml0ejwvQXV0aG9yPjxZZWFyPjE5OTY8L1llYXI+

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ADDIN EN.CITE.DATA [53, 54]. Ингибирование экспрессии других изоформ СОД, каталазы или глутатионпероксидазы было совместимо с жизнью. Частичное ингибирование активности MnСОД (Sod2+/-) приводило к нарушению функционирования митохондрий и усилению их окислительного повреждения, а также увеличению риска развития опухолей PEVuZE5vdGU+PENpdGU+PEF1dGhvcj5WYW4gUmVtbWVuPC9BdXRob3I+PFllYXI+MjAwMzwvWWVh

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ADDIN EN.CITE.DATA [55-57]. Окислительное повреждение митохондрий и нарушение их функции, видимо, и являются причиной усиления образования митохондриальных АФК в опухолевых клетках. Пероксид водорода, образующийся в результате дисмутации О2-•, утилизируется в пероксисомах с помощью каталазы (H2O2 + H2O2 H2O + O2) PEVuZE5vdGU+PENpdGU+PEF1dGhvcj5Mb2V3PC9BdXRob3I+PFllYXI+MTkwMDwvWWVhcj48UmVj

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ADDIN EN.CITE.DATA [58, 59] или в цитоплазме с помощью глутатионпероксидазы (GPx) (H2O2 + 2GSH 2H2O + GSSG). Причем, GPx катализирует реакцию не только с H2O2, но и с ROOH приводя к образованию спиртов (ROH) PEVuZE5vdGU+PENpdGU+PEF1dGhvcj5NaWxsczwvQXV0aG9yPjxZZWFyPjE5NTc8L1llYXI+PFJl

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RW5kTm90ZT5=

ADDIN EN.CITE.DATA [60, 61].

Благодаря способности модулировать внутриклеточный уровень АФК антиоксиданты способны влиять на пролиферацию клеток. Как было отмечено выше (см. 1.1.1), в небольших количествах АФК индуцируют пролиферацию клеток. Снижение уровня Н2О2 за счет усиления экспрессии каталазы в эндотелиальных клетках и HER-2/Neu-трансформированных Rat-1 фибробластах приводило к ингибированию пролиферации этих клеток PEVuZE5vdGU+PENpdGU+PEF1dGhvcj5aYW5ldHRpPC9BdXRob3I+PFllYXI+MjAwMjwvWWVhcj48

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ADDIN EN.CITE.DATA [64, 65].

Исследование пролиферации эмбриональных мышиных фибробластов с различным уровнем экспрессии MnСОД выявило, что пролиферация клеток содержащих MnСОД (+/+) замедляется по мере увеличения плотности популяции (контактное торможение). Частичное подавление экспрессии MnСОД приводило к тому, что MnСОД (+/-) клетки были нечувствительны к контактному торможению и продолжали пролиферировать. Рост MnСОД (-/-) фибробластов был существенно замедлен. Усиление экспрессии MnСОД в MnСОД (+/-) клетках приводило к замедлению пролиферации. Ингибирование MnСОД в клетках экспрессирующих MnСОД (+/+), наоборот, приводило к усилению пролиферации. Интересно отметить, что обработка MnСОД (+/-) клеток с помощью Tiron, ловушки для O2-•, приводила к понижению уровня O2-• и замедлению пролиферации, указывая на важную роль O2-• в поддержании пролиферации. Замедление пролиферации также сопровождалось повышением концентрации Н2О2, продукта работы MnСОД ADDIN EN.CITE <EndNote><Cite><Author>Sarsour</Author><Year>2008</Year><RecNum>59</RecNum><DisplayText>[66]</DisplayText><record><rec-number>59</rec-number><foreign-keys><key app="EN" db-id="w2wfxafe6va9z5eev2l55aa8sxsa599eev2s">59</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Sarsour, E. H.</author><author>Venkataraman, S.</author><author>Kalen, A. L.</author><author>Oberley, L. W.</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, IA 52242, USA.</auth-address><titles><title>Manganese superoxide dismutase activity regulates transitions between quiescent and proliferative growth</title><secondary-title>Aging Cell</secondary-title><alt-title>Aging cell</alt-title></titles><periodical><full-title>Aging Cell</full-title><abbr-1>Aging cell</abbr-1></periodical><alt-periodical><full-title>Aging Cell</full-title><abbr-1>Aging cell</abbr-1></alt-periodical><pages>405-17</pages><volume>7</volume><number>3</number><edition>2008/03/12</edition><keywords><keyword>Cell Proliferation</keyword><keyword>Cells, Cultured</keyword><keyword>Cyclin B/metabolism</keyword><keyword>Cyclin B1</keyword><keyword>Cyclin D1/metabolism</keyword><keyword>Fibroblasts/cytology/metabolism</keyword><keyword>Humans</keyword><keyword>Hydrogen Peroxide/analysis</keyword><keyword>Reactive Oxygen Species/analysis/metabolism</keyword><keyword>Superoxide Dismutase/deficiency/ metabolism</keyword><keyword>Superoxides/analysis/metabolism</keyword></keywords><dates><year>2008</year><pub-dates><date>Jun</date></pub-dates></dates><isbn>1474-9726 (Electronic)&#xD;1474-9718 (Linking)</isbn><accession-num>18331617</accession-num><urls></urls><custom2>PMC2538945</custom2><custom6>Nihms59373</custom6><electronic-resource-num>10.1111/j.1474-9726.2008.00384.x</electronic-resource-num><remote-database-provider>NLM</remote-database-provider><language>eng</language></record></Cite></EndNote>[66]. Исследование посттрансляционных модификаций в молекуле MnСОД выявило различия в сайтах метилирования в пролиферирующих и покоящихся клетках. Уровень метилирования MnСОД в активно пролиферирующих клетках был ниже, чем в клетках, пролиферация которых была замедленна PEVuZE5vdGU+PENpdGU+PEF1dGhvcj5TYXJzb3VyPC9BdXRob3I+PFllYXI+MjAxMjwvWWVhcj48

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ADDIN EN.CITE.DATA [27].

Опухолевые клетки часто характеризуются смещением редокс в более окисленное состояние, что происходит в результате усиления образования АФК и ослабления работы антиоксидантных ферментов PEVuZE5vdGU+PENpdGU+PEF1dGhvcj5DaGl1PC9BdXRob3I+PFllYXI+MjAxMjwvWWVhcj48UmVj

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ADDIN EN.CITE.DATA [67-70]. В отличие от нормальных клеток, в которых уровень GSH снижался по мере увеличения количества клеток (т.н. контактное торможение), уровень GSH в опухолевых клеток был постоянно высоким PEVuZE5vdGU+PENpdGU+PEF1dGhvcj5IdXR0ZXI8L0F1dGhvcj48WWVhcj4xOTk3PC9ZZWFyPjxS

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ADDIN EN.CITE.DATA [71]. Вероятно, поэтому опухолевые клетки были невосприимчивы к действию NAC, предшественнику GSH. Обработка клеток карциномы молочной железы с помощью NAC не приводила к восстановлению редокс и формированию G1 блока PEVuZE5vdGU+PENpdGU+PEF1dGhvcj5NZW5vbjwvQXV0aG9yPjxZZWFyPjIwMDU8L1llYXI+PFJl

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