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

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ADDIN EN.CITE.DATA [9]. В отличие от CN1, CN2 экспрессируется повсеместно в тканях человека и является цитозольным ферментом. Больше всего этого фермента содержится в почках и печени, в меньшем количестве обнаружен в мозге, селезенке и поджелудочной железе, следовые количества – в легких, семенниках и яичниках, отсутствует в сердце PEVuZE5vdGU+PENpdGU+PEF1dGhvcj5UZXVmZWw8L0F1dGhvcj48WWVhcj4yMDAzPC9ZZWFyPjxS

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ADDIN EN.CITE.DATA [9]. Ферменты характеризуются разными рН-оптимумами работы. CN1 демонстрирует наибольшую активность при рН 7,5 – 8,5, CN2 характеризуется более узким оптимумом работы рН с максимумом около рН 9,5. Таким образом, при физиологических pH карнозин гидролизуется преимущественно с помощью CN1 PEVuZE5vdGU+PENpdGU+PEF1dGhvcj5UZXVmZWw8L0F1dGhvcj48WWVhcj4yMDAzPC9ZZWFyPjxS

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ADDIN EN.CITE.DATA [9]. Интересно отметить, что экспрессия CN1 отсутствует в пренатальном периоде и у новорожденных, что указывает на усиление экспрессии CN1 с возрастом PEVuZE5vdGU+PENpdGU+PEF1dGhvcj5UZXVmZWw8L0F1dGhvcj48WWVhcj4yMDAzPC9ZZWFyPjxS

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ADDIN EN.CITE.DATA [9, 196]. Кроме того, у пожилых людей обнаружен более низкий уровень гомокарнозина в сыворотке крови по сравнению с молодым поколением ADDIN EN.CITE <EndNote><Cite><Author>Perry</Author><Year>1968</Year><RecNum>331</RecNum><DisplayText>[197]</DisplayText><record><rec-number>331</rec-number><foreign-keys><key app="EN" db-id="w2wfxafe6va9z5eev2l55aa8sxsa599eev2s">331</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Perry, T.

L.</author><author>Hansen, S.</author><author>Stedman, D.</author><author>Love, D.</author></authors></contributors><titles><title>Homocarnosine in human cerebrospinal fluid: an age-dependent phenomenon</title><secondary-title>J Neurochem</secondary-title><alt-title>Journal of neurochemistry</alt-title></titles><periodical><full-title>J Neurochem</full-title><abbr-1>Journal of neurochemistry</abbr-1></periodical><alt-periodical><full-title>J Neurochem</full-title><abbr-1>Journal of neurochemistry</abbr-1></alt-periodical><pages>1203-6</pages><volume>15</volume><number>10</number><edition>1968/10/01</edition><keywords><keyword>Adolescent</keyword><keyword>Adult</keyword><keyword>Age Factors</keyword><keyword>Aged</keyword><keyword>Amides/ cerebrospinal fluid</keyword><keyword>Amino Acids/cerebrospinal fluid</keyword><keyword>Aminobutyrates/ cerebrospinal fluid</keyword><keyword>Centrifugation</keyword><keyword>Child</keyword><keyword>Child, Preschool</keyword><keyword>Chromatography, Ion Exchange</keyword><keyword>Electrophoresis</keyword><keyword>Humans</keyword><keyword>Imidazoles/ cerebrospinal fluid</keyword><keyword>Infant</keyword><keyword>Intellectual Disability/cerebrospinal fluid</keyword><keyword>Male</keyword><keyword>Middle Aged</keyword><keyword>Nervous System Diseases/cerebrospinal fluid</keyword><keyword>Propionates/ cerebrospinal fluid</keyword></keywords><dates><year>1968</year><pub-dates><date>Oct</date></pub-dates></dates><isbn>0022-3042 (Print)&#xD;0022-3042 (Linking)</isbn><accession-num>5711132</accession-num><urls></urls><remote-database-provider>NLM</remote-database-provider><language>eng</language></record></Cite></EndNote>[197].У карнозина существует несколько природных производных, в том числе: N-ацетил-карнозин (N-ацетил--аланил-L-гистидин), анзерин (-аланил-1-метил-L-гистидин) и гомокарнозин (у-амино-бутирил-L-гистидин) (см. Рис. 1.5). Считается, что -аланил-содержащие дипептиды преимущественно располагаются в скелетных мышцах, в то время как дипептиды содержащие -амино-масленную кислоту (ГАМК) типичны для центральной нервной системы PEVuZE5vdGU+PENpdGU+PEF1dGhvcj5Ecm96YWs8L0F1dGhvcj48WWVhcj4yMDEwPC9ZZWFyPjxS

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ADDIN EN.CITE.DATA [7]. Ацетилированная форма карнозина присутствует в сердечной мышце и в мозге ADDIN EN.CITE <EndNote><Cite><Author>Sobue</Author><Year>1975</Year><RecNum>158</RecNum><DisplayText>[198]</DisplayText><record><rec-number>158</rec-number><foreign-keys><key app="EN" db-id="w2wfxafe6va9z5eev2l55aa8sxsa599eev2s">158</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Sobue, K.</author><author>Konishi, H.</author><author>Nakajima, T.</author></authors></contributors><titles><title>Isolation and identification of N-acetylhomocarnosine and N-acetylcarnosine from brain and muscle</title><secondary-title>J Neurochem</secondary-title><alt-title>Journal of neurochemistry</alt-title></titles><periodical><full-title>J Neurochem</full-title><abbr-1>Journal of neurochemistry</abbr-1></periodical><alt-periodical><full-title>J Neurochem</full-title><abbr-1>Journal of neurochemistry</abbr-1></alt-periodical><pages>1261-2</pages><volume>24</volume><number>6</number><edition>1975/06/01</edition><keywords><keyword>Acetamides/isolation &amp; purification</keyword><keyword>Animals</keyword><keyword>Brain Chemistry</keyword><keyword>Carnosine/ analogs &amp; derivatives</keyword><keyword>Cattle</keyword><keyword>Chromatography, Ion Exchange</keyword><keyword>Chromatography, Paper</keyword><keyword>Dipeptides/ analogs &amp; derivatives</keyword><keyword>Kidney/analysis</keyword><keyword>Liver/analysis</keyword><keyword>Muscles/ analysis</keyword><keyword>Myocardium/analysis</keyword><keyword>Organ Specificity</keyword><keyword>Rabbits</keyword></keywords><dates><year>1975</year><pub-dates><date>Jun</date></pub-dates></dates><isbn>0022-3042 (Print)&#xD;0022-3042 (Linking)</isbn><accession-num>1127438</accession-num><urls></urls><remote-database-provider>NLM</remote-database-provider><language>eng</language></record></Cite></EndNote>[198]. Предполагается, что образование ацетилкарнозина происходит за счет ацетилирования карнозина, однако информация о ферментах, катализирующих данную реакцию пока отсутствует. Гомокарнозин (0,3-1,5 мМ ADDIN EN.CITE <EndNote><Cite><Author>Kish</Author><Year>1979</Year><RecNum>156</RecNum><DisplayText>[199]</DisplayText><record><rec-number>156</rec-number><foreign-keys><key app="EN" db-id="w2wfxafe6va9z5eev2l55aa8sxsa599eev2s">156</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Kish, S. J.</author><author>Perry, T. L.</author><author>Hansen, S.</author></authors></contributors><titles><title>Regional distribution of homocarnosine, homocarnosine-carnosine synthetase and homocarnosinase in human brain</title><secondary-title>J Neurochem</secondary-title><alt-title>Journal of neurochemistry</alt-title></titles><periodical><full-title>J Neurochem</full-title><abbr-1>Journal of neurochemistry</abbr-1></periodical><alt-periodical><full-title>J Neurochem</full-title><abbr-1>Journal of neurochemistry</abbr-1></alt-periodical><pages>1629-36</pages><volume>32</volume><number>6</number><edition>1979/06/01</edition><keywords><keyword>Adult</keyword><keyword>Alanine</keyword><keyword>Brain/ enzymology</keyword><keyword>Brain Chemistry</keyword><keyword>Carnosine/analogs &amp; derivatives/ analysis/biosynthesis</keyword><keyword>Dipeptidases/ analysis</keyword><keyword>Dipeptides/ analysis</keyword><keyword>Humans</keyword><keyword>Kinetics</keyword><keyword>Peptide Synthases/ analysis</keyword><keyword>Substrate Specificity</keyword><keyword>Tissue Distribution</keyword><keyword>gamma-Aminobutyric Acid</keyword></keywords><dates><year>1979</year><pub-dates><date>Jun</date></pub-dates></dates><isbn>0022-3042 (Print)&#xD;0022-3042 (Linking)</isbn><accession-num>448355</accession-num><urls></urls><remote-database-provider>NLM</remote-database-provider><language>eng</language></record></Cite></EndNote>[199]) синтезируется в мозге из ГАМК и L-гистидина с помощью карнозин-синтетазы. Однако скорость синтеза гомокарнозина при прочих равных условиях гораздо медленнее, чем для карнозина PEVuZE5vdGU+PENpdGU+PEF1dGhvcj5Ecm96YWs8L0F1dGhvcj48WWVhcj4yMDEwPC9ZZWFyPjxS

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ADDIN EN.CITE.DATA [5, 7]. Синтез анзерина (до 40 мМ в мышцах птиц ADDIN EN.CITE <EndNote><Cite><Author>Crush</Author><Year>1970</Year><RecNum>265</RecNum><DisplayText>[200]</DisplayText><record><rec-number>265</rec-number><foreign-keys><key app="EN" db-id="w2wfxafe6va9z5eev2l55aa8sxsa599eev2s">265</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Crush, K. G.</author></authors></contributors><titles><title>Carnosine and related substances in animal tissues</title><secondary-title>Comp Biochem Physiol</secondary-title><alt-title>Comparative biochemistry and physiology</alt-title></titles><periodical><full-title>Comp Biochem Physiol</full-title><abbr-1>Comparative biochemistry and physiology</abbr-1></periodical><alt-periodical><full-title>Comp Biochem Physiol</full-title><abbr-1>Comparative biochemistry and physiology</abbr-1></alt-periodical><pages>3-30</pages><volume>34</volume><number>1</number><edition>1970/05/01</edition><keywords><keyword>Alanine/analysis</keyword><keyword>Aminobutyrates/analysis</keyword><keyword>Amphibians</keyword><keyword>Animals</keyword><keyword>Birds</keyword><keyword>Cats</keyword><keyword>Cattle</keyword><keyword>Chromatography, Paper</keyword><keyword>Dipeptides/ analysis</keyword><keyword>Dogs</keyword><keyword>Haplorhini</keyword><keyword>Histidine/analysis</keyword><keyword>Mammals</keyword><keyword>Muscles/analysis</keyword><keyword>Postmortem Changes</keyword><keyword>Rabbits</keyword><keyword>Reptiles</keyword><keyword>Skin/analysis</keyword><keyword>Tissue Extracts/analysis</keyword></keywords><dates><year>1970</year><pub-dates><date>May 1</date></pub-dates></dates><isbn>0010-406X (Print)&#xD;0010-406X (Linking)</isbn><accession-num>4988625</accession-num><urls></urls><remote-database-provider>NLM</remote-database-provider><language>eng</language></record></Cite></EndNote>[200]) происходит в мышцах позвоночных животных путем метилирования карнозина с помощью метилтрансферазы ADDIN EN.CITE <EndNote><Cite><Author>I.R.</Author><Year>1962</Year><RecNum>157</RecNum><DisplayText>[201]</DisplayText><record><rec-number>157</rec-number><foreign-keys><key app="EN" db-id="w2wfxafe6va9z5eev2l55aa8sxsa599eev2s">157</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author> I.R., McManus</author></authors></contributors><titles><title>Enzymatic synthesis of anserine in skeletal muscle by N-methylation of carnosine</title><secondary-title>The Journal of Biological Chemistry </secondary-title></titles><periodical><full-title>J Biol Chem</full-title><abbr-1>The Journal of biological chemistry</abbr-1></periodical><pages>1207-1211</pages><volume>237</volume><section>1207</section><dates><year>1962</year></dates><urls></urls></record></Cite></EndNote>[201]. Анзерин не обнаружен в организме человека. Расщепление производных карнозина осуществляет сывороточная карнозиназа (CN1), при этом скорость гидролиза гомокарнозина составляет 11% от скорости гидролиза карнозина или анзерина PEVuZE5vdGU+PENpdGU+PEF1dGhvcj5KYWNrc29uPC9BdXRob3I+PFllYXI+MTk5MTwvWWVhcj48

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ADDIN EN.CITE.DATA [202].

Рисунок 1.5.

Структура карнозина и его производных. Из ADDIN EN.CITE <EndNote><Cite><RecNum>344</RecNum><DisplayText>[203]</DisplayText><record><rec-number>344</rec-number><foreign-keys><key app="EN" db-id="w2wfxafe6va9z5eev2l55aa8sxsa599eev2s">344</key></foreign-keys><ref-type name="Electronic Article">43</ref-type><contributors></contributors><titles><title>ChemSpider Free chemical structure database, www.chemspider.com&#xD;</title></titles><dates></dates><urls></urls></record></Cite></EndNote>[203] изменениями.

В организме человека карнозин выполняет множество функций, среди которых: pH-буфер в мышцах ADDIN EN.CITE <EndNote><Cite><Author>Северин С. Е.</Author><Year>1953</Year><RecNum>200</RecNum><DisplayText>[10]</DisplayText><record><rec-number>200</rec-number><foreign-keys><key app="EN" db-id="w2wfxafe6va9z5eev2l55aa8sxsa599eev2s">200</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author><style face="normal" font="default" charset="204" size="100%">Северин С. Е., Кирзон, М.В., Кафтанова, Т.М.</style></author></authors></contributors><titles><title><style face="normal" font="default" charset="204" size="100%">Влияние карнозина и ансерина на работу изолированной мышцы лягушки.</style></title><secondary-title><style face="normal" font="default" charset="204" size="100%">Доклад. АН СССР</style></secondary-title></titles><periodical><full-title>Доклад. АН СССР</full-title></periodical><pages><style face="normal" font="default" charset="204" size="100%">691-694</style></pages><volume><style face="normal" font="default" charset="204" size="100%">91</style></volume><dates><year><style face="normal" font="default" charset="204" size="100%">1953</style></year></dates><urls></urls></record></Cite></EndNote>[10], хелатор металлов переменной валентности (Fe, Cu, Zn, Co) PEVuZE5vdGU+PENpdGU+PEF1dGhvcj5Ccm93bjwvQXV0aG9yPjxZZWFyPjE5Nzk8L1llYXI+PFJl

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ADDIN EN.CITE.DATA [20, 21, 23, 208-210]. 1.3.2. Антиоксидантные свойства карнозина и его производныхКарнозин эффективно препятствовал окислению 2,5-бис(гидроксиметил)фурана (BHMF) и N,N-диметил-4-нитрозоанилин (RNO) под действием света в растворе, содержащем фотосенсибилизатор PEVuZE5vdGU+PENpdGU+PEF1dGhvcj5EYWhsPC9BdXRob3I+PFllYXI+MTk4ODwvWWVhcj48UmVj

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