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<article article-type="research-article" dtd-version="1.3" xmlns:mml="http://www.w3.org/1998/Math/MathML" xmlns:xlink="http://www.w3.org/1999/xlink" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xml:lang="ru"><front><journal-meta><journal-id journal-id-type="publisher-id">vavilov</journal-id><journal-title-group><journal-title xml:lang="ru">Вавиловский журнал генетики и селекции</journal-title><trans-title-group xml:lang="en"><trans-title>Vavilov Journal of Genetics and Breeding</trans-title></trans-title-group></journal-title-group><issn pub-type="epub">2500-3259</issn><publisher><publisher-name>Institute of Cytology and Genetics of Siberian Branch of the RAS</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="doi">10.18699/VJ16.156</article-id><article-id custom-type="elpub" pub-id-type="custom">vavilov-588</article-id><article-categories><subj-group subj-group-type="heading"><subject>Research Article</subject></subj-group><subj-group subj-group-type="section-heading" xml:lang="ru"><subject>Экспрессия ключевых генов физиологических функций. ОБЗОР</subject></subj-group><subj-group subj-group-type="section-heading" xml:lang="en"><subject>Expression of genes crucial for physiological functions. REVIEW</subject></subj-group></article-categories><title-group><article-title>Тирозингидроксилаза мозга и ее регуляция глюкокортикоидами</article-title><trans-title-group xml:lang="en"><trans-title>Tyrosine hydroxylase of the brain and it’s regulation by glucocorticoids</trans-title></trans-title-group></title-group><contrib-group><contrib contrib-type="author" corresp="yes"><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Сухарева</surname><given-names>Е. В.</given-names></name><name name-style="western" xml:lang="en"><surname>Sukhareva</surname><given-names>E. V.</given-names></name></name-alternatives><email xlink:type="simple">evsukhareva@mail.ru</email><xref ref-type="aff" rid="aff-1"/></contrib><contrib contrib-type="author" corresp="yes"><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Калинина</surname><given-names>Т. С.</given-names></name><name name-style="western" xml:lang="en"><surname>Kalinina</surname><given-names>T. S.</given-names></name></name-alternatives><xref ref-type="aff" rid="aff-2"/></contrib><contrib contrib-type="author" corresp="yes"><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Булыгина</surname><given-names>В. В.</given-names></name><name name-style="western" xml:lang="en"><surname>Bulygina</surname><given-names>V. V.</given-names></name></name-alternatives><xref ref-type="aff" rid="aff-1"/></contrib><contrib contrib-type="author" corresp="yes"><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Дыгало</surname><given-names>Н. Н.</given-names></name><name name-style="western" xml:lang="en"><surname>Dygalo</surname><given-names>N. N.</given-names></name></name-alternatives><xref ref-type="aff" rid="aff-3"/></contrib></contrib-group><aff-alternatives id="aff-1"><aff xml:lang="ru">Федеральное государственное бюджетное научное учреждение «Федеральный исследовательский центр Институт цитологии и генетики&#13;
Сибирского отделения Российской академии наук», Новосибирск, Россия<country>Россия</country></aff><aff xml:lang="en">Institute of Cytology and Genetics SB RAS, Novosibirsk, Russia<country>Russian Federation</country></aff></aff-alternatives><aff-alternatives id="aff-2"><aff xml:lang="ru">Федеральное государственное бюджетное научное учреждение «Федеральный исследовательский центр Институт цитологии и генетики&#13;
Сибирского отделения Российской академии наук», Новосибирск, Россия&#13;
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Федеральное государственное автономное образовательное учреждение высшего образования «Новосибирский национальный исследовательский государственный университет», Новосибирск, Россия<country>Россия</country></aff><aff xml:lang="en">Institute of Cytology and Genetics SB RAS, Novosibirsk, Russia&#13;
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Novosibirsk State University, Novosibirsk, Russia<country>Russian Federation</country></aff></aff-alternatives><aff-alternatives id="aff-3"><aff xml:lang="ru">Федеральное государственное бюджетное научное учреждение «Федеральный исследовательский центр Институт цитологии и генетики Сибирского отделения Российской академии наук», Новосибирск, Россия&#13;
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Федеральное государственное автономное образовательное учреждение высшего образования «Новосибирский национальный исследовательский государственный университет», Новосибирск, Россия<country>Россия</country></aff><aff xml:lang="en">Institute of Cytology and Genetics SB RAS, Novosibirsk, Russia&#13;
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Novosibirsk State University, Novosibirsk, Russia<country>Russian Federation</country></aff></aff-alternatives><pub-date pub-type="collection"><year>2016</year></pub-date><pub-date pub-type="epub"><day>18</day><month>05</month><year>2016</year></pub-date><volume>20</volume><issue>2</issue><fpage>212</fpage><lpage>219</lpage><permissions><copyright-statement>Copyright &amp;#x00A9; Сухарева Е.В., Калинина Т.С., Булыгина В.В., Дыгало Н.Н., 2016</copyright-statement><copyright-year>2016</copyright-year><copyright-holder xml:lang="ru">Сухарева Е.В., Калинина Т.С., Булыгина В.В., Дыгало Н.Н.</copyright-holder><copyright-holder xml:lang="en">Sukhareva E.V., Kalinina T.S., Bulygina V.V., Dygalo N.N.</copyright-holder><license license-type="creative-commons-attribution" xlink:href="https://creativecommons.org/licenses/by/4.0/" xlink:type="simple"><license-p>This work is licensed under a Creative Commons Attribution 4.0 License.</license-p></license></permissions><self-uri xlink:href="https://vavilov.elpub.ru/jour/article/view/588">https://vavilov.elpub.ru/jour/article/view/588</self-uri><abstract><p>В основе долговременных изменений нейрохимических систем мозга и регулируемых ими физиологических функций и поведения под действием неблагоприятных факторов раннего онтогенеза находится изменение экспрессии важных для функционирования нейрохимической системы генов. Ключевой фермент биосинтеза катехоламинов, тирозингидроксилаза (ТГ), определяет активность нейрохимической системы и индуцируется гормонами стресса, глюкокортикоидами, in vitro и in vivo. Анализ собственных и литературных данных по влиянию гормонов стресса – глюкокортикоидов – в критические периоды перинатального онтогенеза на экспрессию гена ТГ, уровень его белка и активность фермента в процессе развития, а также рассмотрение возможных механизмов такого влияния послужило задачей обзора. Введение дексаметазона или гидрокортизона повышает через 6 ч уровень мРНК ТГ в стволе мозга 20-суточных плодов и трехдневных крысят, что сопровождается увеличением активности фермента и иммуногистохимически выявляемого белка ТГ в стволе мозга. Изменение экспрессии гена ТГ в критический период раннего развития приводит к повышению уровня мРНК ТГ в стволе мозга 25- и 70-дневных крысят и активности фермента в стволе и коре мозга взрослых животных. Период чувствительности ТГ к уровню глюкокортикоидов зависит от возраста. Введение гормонов на восьмой день жизни не сопровождается изменениями в уровне мРНК и активности фермента. Промотор гена ТГ не имеет классического функционально активного гормонозависимого элемента. Механизм гормональной индукции экспрессии ТГ может быть основан на неканоническом пути действия глюкокортикоидов в результате известного белок-белкового взаимодействия глюкокортикоидного рецептора с другими транскрипционными факторами, такими как белки АР-1 комплекса. Именно этот механизм регуляции экспрессии ТГ дексаметазоном установлен для культуры феохромацитомы. Доказательство существования подобного механизма для глюкокортикоидной регуляции ТГ in vivo необходимо для понимания многообразия уровней регуляции экспрессии нейрогенов факторами внешней среды.</p></abstract><trans-abstract xml:lang="en"><p>Early life stress events can produce long-lasting changes in neurochemistry and behaviors related to monoamine systems, with increased risks of cardiovascular, metabolic, neuroendocrine, psychiatric disorders, generalized anxiety and depression in adulthood. Tyrosine hydroxylase (TH), the key enzyme for catecholamine synthesis, also plays an important role in the activity of the noradrenergic system and may be a target for glucocorticoids during the perinatal programming of physiological functions and behavior. Administration of hydrocortisone or dexamethasone to female rats on day 20 of pregnancy and to 3-day-old neonatal pups significantly increased TH mRNA levels (real-time PCR) and enzyme activity as well as protein levels determined by ICH in the locus coeruleus. Moreover, our treatment led to increase in TH mRNA levels in 25- and 70-day-old animals, as well as an increase in enzyme activity in the brainstem and cerebral cortex of adult rats. The long-term changes in TH expression are limited by the perinatal period of development. Administration of hormones on day 8 of life was not accompanied by changes in TH mRNA levels or enzyme activity. Glucocorticoids use several mechanisms to bring about transactivation or transrepression of genes. The main mechanism includes direct binding of the hormone-activated GRs to glucocorticoid responsive elements (GREs) in the promoter region of genes. However, despite optimistic claims made the classical GRE was not found in the TH gene promoter. Protein – protein interactions between hormone-activated GR and other transcription factors, for example, AP-1, provide an additional mechanism for the effects of glucocorticoids on gene expression. An important feature of this mechanism is its dependence on the composition of proteins formed by AP-1. Hormone-activated GRs are able to enhance gene expression when AP-1 consists of the Jun / Jun homodimer, but do not do that when AP-1 appears as the Jun / Fos heterodimer. Furthermore, as has been shown recently, the GRE / AP-1 composite site is the major site of interaction of glucocorticoids with  the TH gene in the pheochromocytoma cell line. Ontogenetic variation in the expression of Fos and Jun family proteins, which affects their ratio, can be one of the reasons for the TH gene regulation by glucocorticoids at near-term fetuses and neonates. However, to date this hypothesis has been supported only by in vitro data, and the existence of this mechanism in in vivo conditions needs to be explored in further studies.</p></trans-abstract><kwd-group xml:lang="ru"><kwd>тирозингидроксилаза</kwd><kwd>глюкокортикоиды</kwd><kwd>онтогенетическое программирование</kwd><kwd>экспрессия генов</kwd><kwd>головной мозг.</kwd></kwd-group><kwd-group xml:lang="en"><kwd>tyrosine hydroxylase</kwd><kwd>glucocorticoids</kwd><kwd>ontogenetic programming</kwd><kwd>gene expression</kwd><kwd>brain</kwd></kwd-group></article-meta></front><back><ref-list><title>References</title><ref id="cit1"><label>1</label><citation-alternatives><mixed-citation xml:lang="ru">Дыгало Н.Н., Калинина Т.С. Эффекты взаимодействия генотипа и глюкокортикоидов на активность тирозингидроксилазы мозга плодов крыс. Генетика. 1993;29(9):1453-1459.</mixed-citation><mixed-citation xml:lang="en">Altmann C.R., Brivanlou A.H. Neural patterning in the vertebrate embryo. Int. Rev. Cytol. 2001;203:447482.</mixed-citation></citation-alternatives></ref><ref id="cit2"><label>2</label><citation-alternatives><mixed-citation xml:lang="ru">Калинина Т.С., Дыгало Н.Н. Развитие норадренергической системы мозга крыс после пренатального воздействия кортикостероном. Изв. РАН. Сер. биол. 2013;4:447-452.</mixed-citation><mixed-citation xml:lang="en">Bademci G., Vance J.M., Wang L. Tyrosine hydroxylase gene: another piece of the  genetic puzzle of Parkinson’s disease. CNS Neurol. Disord. Drug Targets. 2012;11(4):469-481.</mixed-citation></citation-alternatives></ref><ref id="cit3"><label>3</label><citation-alternatives><mixed-citation xml:lang="ru">Сухарева Е.В., Дыгало Н.Н., Калинина Т.С. Влияние дексаметазона на экспрессию генов раннего ответа c-fos и c-jun в различных отделах неонатального мозга. Молекуляр. биология. 2016; 50(2):266-271.</mixed-citation><mixed-citation xml:lang="en">Barker D.J. Fetal origins of coronary heart disease. BMJ. 1995; 311(6998):171-174.</mixed-citation></citation-alternatives></ref><ref id="cit4"><label>4</label><citation-alternatives><mixed-citation xml:lang="ru">Сухарева Е.В., Калинина Т.С., Ланшаков Д.А., Булыгина В.В., Дыгало Н.Н. Белки AP-1 комплекса в индукции глюкокортикоидами тирозингидроскилазы мозга в раннем онтогенезе. Матер. Седьм. Всерос. науч.-практ. конф. «Фундаментальные аспекты компенсаторно-приспособительных процессов» и Молодежн. симп. «Молекулярно-клеточные и медико-экологические проблемы компенсации и приспособления». 2015;271-272.</mixed-citation><mixed-citation xml:lang="en">Barth K.A., Kishimoto Y., Rohr K.B., Seydler C., Schulte-Merker S., Wilson S.W. Bmp  activity establishes a gradient of positional information throughout the entire  neural plate. Development. 1999; 126(22):4977-4987.</mixed-citation></citation-alternatives></ref><ref id="cit5"><label>5</label><citation-alternatives><mixed-citation xml:lang="ru">Altmann C.R., Brivanlou A.H. Neural patterning in the vertebrate embryo. Int. Rev. Cytol. 2001;203:447-482.</mixed-citation><mixed-citation xml:lang="en">Beck I.M., Vanden Berghe W., Vermeulen L., Yamamoto K.R., Haegeman G., De Bosscher  K. Crosstalk in inflammation: the interplay of glucocorticoid receptor-based  mechanisms and kinases and phosphatases. Endocr. Rev. 2009;30(7):830-882. DOI 10.1210/er.2009-0013</mixed-citation></citation-alternatives></ref><ref id="cit6"><label>6</label><citation-alternatives><mixed-citation xml:lang="ru">Bademci G., Vance J.M., Wang L. Tyrosine hydroxylase gene: another piece of the genetic puzzle of Parkinson’s disease. CNS Neurol. Disord. Drug Targets. 2012;11(4):469-481.</mixed-citation><mixed-citation xml:lang="en">Bingham B.C., Sheela Rani C.S., Frazer A., Strong R., Morilak D.A. Exogenous  prenatal corticosterone exposure mimics the effects of prenatal stress on adult  brain stress response systems and fear extinction behavior.  Psychoneuroendocrinology. 2013;38(11):2746-2757. DOI 10.1016/j.psyneuen.2013.07.003</mixed-citation></citation-alternatives></ref><ref id="cit7"><label>7</label><citation-alternatives><mixed-citation xml:lang="ru">Barker D.J. Fetal origins of coronary heart disease. BMJ. 1995; 311(6998):171-174.</mixed-citation><mixed-citation xml:lang="en">Bonnin A., de Miguel R., Rodriguez-Manzaneque J.C., Fernandez-Ruiz J.J., Santos A.,  Ramos J.A. Changes in tyrosine hydroxylase gene expression in mesencephalic  catecholaminergic neurons of immature and adult male rats perinatally exposed to  cannabinoids. Brain Res. Develop. Brain Res. 1994;81(1):147-150.</mixed-citation></citation-alternatives></ref><ref id="cit8"><label>8</label><citation-alternatives><mixed-citation xml:lang="ru">Barth K.A., Kishimoto Y., Rohr K.B., Seydler C., Schulte-Merker S., Wilson S.W. Bmp activity establishes a gradient of positional information throughout the entire neural plate. Development. 1999; 126(22):4977-4987.</mixed-citation><mixed-citation xml:lang="en">Bornstein S.R., Tian H., Haidan A., Böttner A., Hiroi N., Eisenhofer G., McCann  S.M., Chrousos G.P., Roffler-Tarlov S. Deletion of tyrosine hydroxylase gene reveals   functional interdependence of adrenocortical and chromaffin cell system in vivo.  Proc. Natl Acad. Sci. USA. 2000;97(26):14742-14747. DOI 10.1073/pnas.97.26.14742</mixed-citation></citation-alternatives></ref><ref id="cit9"><label>9</label><citation-alternatives><mixed-citation xml:lang="ru">Beck I.M., Vanden Berghe W., Vermeulen L., Yamamoto K.R., Haegeman G., De Bosscher K. Crosstalk in inflammation: the interplay of glucocorticoid receptor-based mechanisms and kinases and phosphatases. Endocr. Rev. 2009;30(7):830-882. DOI 10.1210/er.2009- 0013</mixed-citation><mixed-citation xml:lang="en">Boschi N.M., Takeuchi K., Sterling C., Tank A.W. Differential expression of  polycytosine-binding protein isoforms in adrenal gland, locus coeruleus and midbrain. Neuroscience. 2015;286:1-12. DOI 10.1016/j.neuroscience.2014.11.038</mixed-citation></citation-alternatives></ref><ref id="cit10"><label>10</label><citation-alternatives><mixed-citation xml:lang="ru">Bingham B.C., Sheela Rani C.S., Frazer A., Strong R., Morilak D.A. Exogenous prenatal corticosterone exposure mimics the effects of prenatal stress on adult brain stress response systems and fear extinction behavior. Psychoneuroendocrinology. 2013;38(11):2746-2757. DOI 10.1016/j.psyneuen.2013.07.003</mixed-citation><mixed-citation xml:lang="en">Candy J., Collet C. Two tyrosine hydroxylase genes in teleosts. Biochim. Biophys. Acta. 2005;1727(1):35-44.</mixed-citation></citation-alternatives></ref><ref id="cit11"><label>11</label><citation-alternatives><mixed-citation xml:lang="ru">Bonnin A., de Miguel R., Rodriguez-Manzaneque J.C., Fernandez-Ruiz J.J., Santos A., Ramos J.A. Changes in tyrosine hydroxylase gene expression in mesencephalic catecholaminergic neurons of immature and adult male rats perinatally exposed to cannabinoids. Brain Res. Develop. Brain Res. 1994;81(1):147-150.</mixed-citation><mixed-citation xml:lang="en">Carson R.P., Robertson D. Genetic manipulation of noradrenergic neurons. J. Pharmacol. Exp. Ther. 2002;301(2):410-417.</mixed-citation></citation-alternatives></ref><ref id="cit12"><label>12</label><citation-alternatives><mixed-citation xml:lang="ru">Bornstein S.R., Tian H., Haidan A., Böttner A., Hiroi N., Eisenhofer G., McCann S.M., Chrousos G.P., Roffler-Tarlov S. Deletion of tyrosine hydroxylase gene reveals functional interdependence of adrenocortical and chromaffin cell system in vivo. Proc. Natl Acad. Sci. USA. 2000;97(26):14742-14747. DOI 10.1073/pnas.97.26.14742</mixed-citation><mixed-citation xml:lang="en">Champagne D.L., de Kloet E.R., Joels M. Fundamental aspects of the impact of  glucocorticoids on the (immature) brain. Semin. Fetal Neonatal Med. 2009;14(3):136-142. DOI 10.1016/j.siny.2008.11.006</mixed-citation></citation-alternatives></ref><ref id="cit13"><label>13</label><citation-alternatives><mixed-citation xml:lang="ru">Boschi N.M., Takeuchi K., Sterling C., Tank A.W. Differential expression of polycytosine-binding protein isoforms in adrenal gland, locus coeruleus and midbrain. Neuroscience. 2015;286:1-12. DOI 10.1016/j.neuroscience.2014.11.038</mixed-citation><mixed-citation xml:lang="en">Craig S.P., Buckle V.J., Lamouroux A., Mallet J., Craig I. Localization of the human  tyrosine hydroxylase gene to 11p15: gene duplication and evolution of metabolic  pathways. Cytogenet. Cell Genet. 1986;42(1/2):29-32.</mixed-citation></citation-alternatives></ref><ref id="cit14"><label>14</label><citation-alternatives><mixed-citation xml:lang="ru">Candy J., Collet C. Two tyrosine hydroxylase genes in teleosts. Biochim. Biophys. Acta. 2005;1727(1):35-44.</mixed-citation><mixed-citation xml:lang="en">Dent G.W., Smith M.A., Levine S. Stress-induced alterations in locus coeruleus gene  expression during ontogeny. Brain Res. Develop. Brain Res. 2001;127(1):23-30.</mixed-citation></citation-alternatives></ref><ref id="cit15"><label>15</label><citation-alternatives><mixed-citation xml:lang="ru">Carson R.P., Robertson D. Genetic manipulation of noradrenergic neurons. J. Pharmacol. Exp. Ther. 2002;301(2):410-417.</mixed-citation><mixed-citation xml:lang="en">Diamond M.I., Miner J.N., Yoshinaga S.K., Yamamoto K.R. Transcription factor  interactions: selectors of positive or negative regulation from a single DNA  element. Science. 1990;249(4974):1266-1272.</mixed-citation></citation-alternatives></ref><ref id="cit16"><label>16</label><citation-alternatives><mixed-citation xml:lang="ru">Champagne D.L., de Kloet E.R., Joels M. Fundamental aspects of the impact of glucocorticoids on the (immature) brain. Semin. Fetal Neonatal Med. 2009;14(3):136-142. DOI 10.1016/j.siny.2008.11.006</mixed-citation><mixed-citation xml:lang="en">Dunkley P.R., Bobrovskaya L., Graham M.E., von Nagy-Felsobuki E.I., Dickson P.W.  Tyrosine hydroxylase phosphorylation: regulation and consequences. J. Neurochem. 2004;91(5):1025-1043.</mixed-citation></citation-alternatives></ref><ref id="cit17"><label>17</label><citation-alternatives><mixed-citation xml:lang="ru">Craig S.P., Buckle V.J., Lamouroux A., Mallet J., Craig I. Localization of the human tyrosine hydroxylase gene to 11p15: gene duplication and evolution of metabolic pathways. Cytogenet. Cell Genet. 1986;42(1/2):29-32.</mixed-citation><mixed-citation xml:lang="en">Dygalo N.N., Kalinina T.S. Effects of genotype-glucocorticoid interaction on the  tyrosine hydroxylase activity in the brain of rat fetuses. Genetika = Genetics (Moscow). 1993;29(9):1453-1459.</mixed-citation></citation-alternatives></ref><ref id="cit18"><label>18</label><citation-alternatives><mixed-citation xml:lang="ru">Dent G.W., Smith M.A., Levine S. Stress-induced alterations in locus coeruleus gene expression during ontogeny. Brain Res. Develop. Brain Res. 2001;127(1):23-30.</mixed-citation><mixed-citation xml:lang="en">Dygalo N.N., Kalinina T.S., Shishkina G.T. Neonatal programming of rat behavior by  downregulation of alpha2A-adrenoreceptor gene expression in the brain. Ann. N.Y.  Acad. Sci. 2008;1148:409-414. DOI 10.1196/annals.1410.063</mixed-citation></citation-alternatives></ref><ref id="cit19"><label>19</label><citation-alternatives><mixed-citation xml:lang="ru">Diamond M.I., Miner J.N., Yoshinaga S.K., Yamamoto K.R. Transcription factor interactions: selectors of positive or negative regulation from a single DNA element. Science. 1990;249(4974):1266-1272.</mixed-citation><mixed-citation xml:lang="en">Fossom L.H., Sterling C.R., Tank A.W. Regulation of tyrosine hydroxylase gene  transcription rate and tyrosine hydroxylase mRNA stability by cyclic AMP and  glucocorticoid. Mol. Pharmacol. 1992; 42(5):898-908.</mixed-citation></citation-alternatives></ref><ref id="cit20"><label>20</label><citation-alternatives><mixed-citation xml:lang="ru">Dunkley P.R., Bobrovskaya L., Graham M.E., von Nagy-Felsobuki E.I., Dickson P.W. Tyrosine hydroxylase phosphorylation: regulation and consequences. J. Neurochem. 2004;91(5):1025-1043.</mixed-citation><mixed-citation xml:lang="en">Friggi-Grelin F., Coulom H., Meller M., Gomez D., Hirsh J., Birman S. Targeted gene  expression in Drosophila dopaminergic cells using regulatory sequences from tyrosine  hydroxylase. J. Neurobiol. 2003; 54(4):618-627. DOI 10.1002/neu.10185</mixed-citation></citation-alternatives></ref><ref id="cit21"><label>21</label><citation-alternatives><mixed-citation xml:lang="ru">Dygalo N.N., Kalinina T.S., Shishkina G.T. Neonatal programming of rat behavior by downregulation of alpha2A-adrenoreceptor gene expression in the brain. Ann. N.Y. Acad. Sci. 2008;1148:409-414. DOI 10.1196/annals.1410.063</mixed-citation><mixed-citation xml:lang="en">Fujinaga M., Scott J.C. Gene expression of catecholamine synthesizing enzymes and  beta adrenoceptor subtypes during rat embryogenesis. Neurosci. Lett. 1997;231(2):108-112.</mixed-citation></citation-alternatives></ref><ref id="cit22"><label>22</label><citation-alternatives><mixed-citation xml:lang="ru">Fossom L.H., Sterling C.R., Tank A.W. Regulation of tyrosine hydroxylase gene transcription rate and tyrosine hydroxylase mRNA stability by cyclic AMP and glucocorticoid. Mol. Pharmacol. 1992; 42(5):898-908.</mixed-citation><mixed-citation xml:lang="en">Fung B.P., Yoon S.O., Chikaraishi D.M. Sequences that direct rat tyrosine- hydroxylase gene-expression. J. Neurochem. 1992;58(6): 2044-2052.</mixed-citation></citation-alternatives></ref><ref id="cit23"><label>23</label><citation-alternatives><mixed-citation xml:lang="ru">Friggi-Grelin F., Coulom H., Meller M., Gomez D., Hirsh J., Birman S. Targeted gene expression in Drosophila dopaminergic cells using regulatory sequences from tyrosine hydroxylase. J. Neurobiol. 2003; 54(4):618-627. DOI 10.1002/neu.10185</mixed-citation><mixed-citation xml:lang="en">Gallo L.A., Tran M., Moritz K.M., Wlodek M.E. Developmental programming: Variations  in early growth and adult disease. Clin. Exp. Pharmacol. Physiol. 2013;40(11):795-802. DOI 10.1111/1440-1681.12092</mixed-citation></citation-alternatives></ref><ref id="cit24"><label>24</label><citation-alternatives><mixed-citation xml:lang="ru">Fujinaga M., Scott J.C. Gene expression of catecholamine synthesizing enzymes and beta adrenoceptor subtypes during rat embryogenesis. Neurosci. Lett. 1997;231(2):108-112.</mixed-citation><mixed-citation xml:lang="en">Goridis C., Rohrer H. Specification of catecholaminergic and serotonergic neurons.  Nat. Rev. Neurosci. 2002;3(7):531-541. DOI 10.1038/nrn871</mixed-citation></citation-alternatives></ref><ref id="cit25"><label>25</label><citation-alternatives><mixed-citation xml:lang="ru">Fung B.P., Yoon S.O., Chikaraishi D.M. Sequences that direct rat tyrosine-hydroxylase gene-expression. J. Neurochem. 1992;58(6): 2044-2052.</mixed-citation><mixed-citation xml:lang="en">Groeneweg F.L., Karst H., de Kloet E.R., Joels M. Mineralocorticoid and  glucocorticoid receptors at the neuronal membrane, regulators of nongenomic  corticosteroid signalling. Mol. Cell. Endocrinol. 2012;350(2):299-309. DOI 10.1016/j.mce.2011.06.020</mixed-citation></citation-alternatives></ref><ref id="cit26"><label>26</label><citation-alternatives><mixed-citation xml:lang="ru">Gallo L.A., Tran M., Moritz K.M., Wlodek M.E. Developmental programming: Variations in early growth and adult disease. Clin. Exp. Pharmacol. Physiol. 2013;40(11):795-802. DOI 10.1111/1440-1681.12092</mixed-citation><mixed-citation xml:lang="en">Guo S., Brush J., Teraoka H., Goddard A., Wilson S.W., Mullins M.C., Rosenthal A.  Development of noradrenergic neurons in the zebrafish hindbrain requires BMP, FGF8,  and the homeodomain protein Soulless/ Phox2a. Neuron. 1999;24(3):555-566.</mixed-citation></citation-alternatives></ref><ref id="cit27"><label>27</label><citation-alternatives><mixed-citation xml:lang="ru">Goridis C., Rohrer H. Specification of catecholaminergic and serotonergic neurons. Nat. Rev. Neurosci. 2002;3(7):531-541. DOI 10.1038/nrn871</mixed-citation><mixed-citation xml:lang="en">Hagerty T., Morgan W.W., Elango N., Strong R. Identification of a glucocorticoid-responsive element in the promoter region of the mouse tyrosine hydroxylase gene. J. Neurochem. 2001;76(3):825-834.</mixed-citation></citation-alternatives></ref><ref id="cit28"><label>28</label><citation-alternatives><mixed-citation xml:lang="ru">Groeneweg F.L., Karst H., de Kloet E.R., Joels M. Mineralocorticoid and glucocorticoid receptors at the neuronal membrane, regulators of nongenomic corticosteroid signalling. Mol. Cell. Endocrinol. 2012;350(2):299-309. DOI 10.1016/j.mce.2011.06.020</mixed-citation><mixed-citation xml:lang="en">Harris A., Seckl J. Glucocorticoids, prenatal stress and the programming of disease.  Horm. Behav. 2011;59(3):279-289. DOI 10.1016/j.yhbeh.2010.06.007</mixed-citation></citation-alternatives></ref><ref id="cit29"><label>29</label><citation-alternatives><mixed-citation xml:lang="ru">Guo S., Brush J., Teraoka H., Goddard A., Wilson S.W., Mullins M.C., Rosenthal A. Development of noradrenergic neurons in the zebrafish hindbrain requires BMP, FGF8, and the homeodomain protein Soulless/Phox2a. Neuron. 1999;24(3):555-566.</mixed-citation><mixed-citation xml:lang="en">Haycock J.W. Species differences in the expression of multiple tyrosine hydroxylase protein isoforms. J. Neurochem. 2002;81(5):947-953.</mixed-citation></citation-alternatives></ref><ref id="cit30"><label>30</label><citation-alternatives><mixed-citation xml:lang="ru">Hagerty T., Morgan W.W., Elango N., Strong R. Identification of a glucocorticoid-responsive element in the promoter region of the mouse tyrosine hydroxylase gene. J. Neurochem. 2001;76(3):825-834.</mixed-citation><mixed-citation xml:lang="en">Hebert M.A., Serova L.I., Sabban E.L. Single and repeated immobilization stress  differentially trigger induction and phosphorylation of several transcription  factors and mitogen-activated protein kinases in the rat locus coeruleus. J. Neurochem. 2005;95(2):484-498.</mixed-citation></citation-alternatives></ref><ref id="cit31"><label>31</label><citation-alternatives><mixed-citation xml:lang="ru">Harris A., Seckl J. Glucocorticoids, prenatal stress and the programming of disease. Horm. Behav. 2011;59(3):279-289. DOI 10.1016/j. yhbeh.2010.06.007</mixed-citation><mixed-citation xml:lang="en">Herlenius E., Lagercrantz H. Development of neurotransmitter systems during critical  periods. Exp. Neurol. 2004;190:8-21. DOI 10.1016/j.expneurol.2004.03.027</mixed-citation></citation-alternatives></ref><ref id="cit32"><label>32</label><citation-alternatives><mixed-citation xml:lang="ru">Haycock J.W. Species differences in the expression of multiple tyrosine hydroxylase protein isoforms. J. Neurochem. 2002;81(5):947-953.</mixed-citation><mixed-citation xml:lang="en">Hernandez-Sanchez C., Bartulos O., Valenciano A.I., Mansilla A., de Pablo F. The  regulated expression of chimeric tyrosine hydroxylaseinsulin transcripts during  early development. Nucl. Acids. 2006; 34(12):3455-3464.</mixed-citation></citation-alternatives></ref><ref id="cit33"><label>33</label><citation-alternatives><mixed-citation xml:lang="ru">Hebert M.A., Serova L.I., Sabban E.L. Single and repeated immobilization stress differentially trigger induction and phosphorylation of several transcription factors and mitogen-activated protein kinases in the rat locus coeruleus. J. Neurochem. 2005;95(2):484-498.</mixed-citation><mixed-citation xml:lang="en">Hippenmeyer S., Kramer I., Arber S. Control of neuronal phenotype: what targets tell  the cell bodies. Trends Neurosci. 2004;27(8):482- 488. DOI 10.1016/j.tins.2004.05.012</mixed-citation></citation-alternatives></ref><ref id="cit34"><label>34</label><citation-alternatives><mixed-citation xml:lang="ru">Herlenius E., Lagercrantz H. Development of neurotransmitter systems during critical periods. Exp. Neurol. 2004;190:8-21. DOI 10.1016/j. expneurol.2004.03.027</mixed-citation><mixed-citation xml:lang="en">Hirsch M.R., Tiveron M.C., Guillemot F., Brunet J.F., Goridis C. Control of  noradrenergic differentiation and Phox2a expression by MASH1 in the central and  peripheral nervous system. Development. 1998;125(4):599-608.</mixed-citation></citation-alternatives></ref><ref id="cit35"><label>35</label><citation-alternatives><mixed-citation xml:lang="ru">Hernandez-Sanchez C., Bartulos O., Valenciano A.I., Mansilla A., de Pablo F. The regulated expression of chimeric tyrosine hydroxylaseinsulin transcripts during early development. Nucl. Acids. 2006; 34(12):3455-3464.</mixed-citation><mixed-citation xml:lang="en">Holm P.C., Rodriguez F.J., Kele J., Castelo-Branco G., Kitajewski J., Arenas E.  BMPs, FGF8 and Wnts regulate the differentiation of locus coeruleus noradrenergic  neuronal precursors. J. Neurochem. 2006;99(1):343-352. DOI 10.1111/j.1471-4159.2006.04039.x</mixed-citation></citation-alternatives></ref><ref id="cit36"><label>36</label><citation-alternatives><mixed-citation xml:lang="ru">Hippenmeyer S., Kramer I., Arber S. Control of neuronal phenotype: what targets tell the cell bodies. Trends Neurosci. 2004;27(8):482-488. DOI 10.1016/j.tins.2004.05.012</mixed-citation><mixed-citation xml:lang="en">Kalinina T.S., Dygalo N.N. Development of the noradrenergic system of the rat brain  after prenatal exposure to corticosterone. Izvestiya Rossiiskoi Akademii Nauk –  Seriya Biologicheskaya = Biology Bulletin of the Russian Academy of Science.  2013;4:447-452. DOI 10.7868/S0002332913040048</mixed-citation></citation-alternatives></ref><ref id="cit37"><label>37</label><citation-alternatives><mixed-citation xml:lang="ru">Hirsch M.R., Tiveron M.C., Guillemot F., Brunet J.F., Goridis C. Control of noradrenergic differentiation and Phox2a expression by MASH1 in the central and peripheral nervous system. Development. 1998;125(4):599-608.</mixed-citation><mixed-citation xml:lang="en">Kalinina T.S., Shishkina G.T., Dygalo N.N. Induction of tyrosine hydroxylase gene  expression by glucocorticoids in the perinatal rat brain is age-dependent.  Neurochem. Res. 2012;37(4):811-818.</mixed-citation></citation-alternatives></ref><ref id="cit38"><label>38</label><citation-alternatives><mixed-citation xml:lang="ru">Holm P.C., Rodriguez F.J., Kele J., Castelo-Branco G., Kitajewski J., Arenas E. BMPs, FGF8 and Wnts regulate the differentiation of locus coeruleus noradrenergic neuronal precursors. J. Neurochem. 2006;99(1):343-352. DOI 10.1111/j.1471-4159.2006.04039.x</mixed-citation><mixed-citation xml:lang="en">Kapoor A., Petropoulos S., Matthews S.G. Fetal programming of hypothalamic-pituitary-adrenal (HPA) axis function and behavior by synthetic glucocorticoids.  Brain Res. Rev. 2008;57(2):586-595. DOI 10.1016/j.brainresrev.2007.06.013</mixed-citation></citation-alternatives></ref><ref id="cit39"><label>39</label><citation-alternatives><mixed-citation xml:lang="ru">Kalinina T.S., Shishkina G.T., Dygalo N.N. Induction of tyrosine hydroxylase gene expression by glucocorticoids in the perinatal rat brain is age-dependent. Neurochem. Res. 2012;37(4):811-818.</mixed-citation><mixed-citation xml:lang="en">Kassel O., Herrlich P. Crosstalk between the glucocorticoid receptor and other  transcription factors: molecular aspects. Mol. Cell. Endocrinol. 2007;275(1/2):13- 29.</mixed-citation></citation-alternatives></ref><ref id="cit40"><label>40</label><citation-alternatives><mixed-citation xml:lang="ru">Kapoor A., Petropoulos S., Matthews S.G. Fetal programming of hypothalamic-pituitary-adrenal (HPA) axis function and behavior by synthetic glucocorticoids. Brain Res. Rev. 2008;57(2):586-595. DOI 10.1016/j.brainresrev.2007.06.013</mixed-citation><mixed-citation xml:lang="en">Kobayashi K., Morita S., Sawada H., Mizuguchi T., Yamada K., Nagatsu I., Hata T.,  Watanabe Y., Fujita K., Nagatsu T. Targeted disruption of the tyrosine-hydroxylase  locus results in severe catecholamine depletion and perinatal lethality in mice. J.  Biol. Chem. 1995; 270(45):27235-27243.</mixed-citation></citation-alternatives></ref><ref id="cit41"><label>41</label><citation-alternatives><mixed-citation xml:lang="ru">Kassel O., Herrlich P. Crosstalk between the glucocorticoid receptor and other transcription factors: molecular aspects. Mol. Cell. Endocrinol. 2007;275(1/2):13-29.</mixed-citation><mixed-citation xml:lang="en">Kreider M.L., Tate C.A., Cousins M.M., Oliver C.A., Seidler F.J., Slotkin T.A.  Lasting effects of developmental dexamethasone treatment on neural cell number and  size, synaptic activity, and cell signaling: critical periods of vulnerability,  dose-effect relationships, regional targets, and sex selectivity.  Neuropsychopharmacology. 2006;31(1): 12-35. DOI 10.1038/sj.npp.1300783</mixed-citation></citation-alternatives></ref><ref id="cit42"><label>42</label><citation-alternatives><mixed-citation xml:lang="ru">Kobayashi K., Morita S., Sawada H., Mizuguchi T., Yamada K., Nagatsu I., Hata T., Watanabe Y., Fujita K., Nagatsu T. Targeted disruption of the tyrosine-hydroxylase locus results in severe catecholamine depletion and perinatal lethality in mice. J. Biol. Chem. 1995; 270(45):27235-27243.</mixed-citation><mixed-citation xml:lang="en">Kumer S.C., Vrana K.E. Intricate regulation of tyrosine hydroxylase activity and gene expression. J. Neurochem. 1996;67(2):443-462.</mixed-citation></citation-alternatives></ref><ref id="cit43"><label>43</label><citation-alternatives><mixed-citation xml:lang="ru">Kreider M.L., Tate C.A., Cousins M.M., Oliver C.A., Seidler F.J., Slotkin T.A. Lasting effects of developmental dexamethasone treatment on neural cell number and size, synaptic activity, and cell signaling: critical periods of vulnerability, dose-effect relationships, regional targets, and sex selectivity. Neuropsychopharmacology. 2006;31(1): 12-35. DOI 10.1038/sj.npp.1300783</mixed-citation><mixed-citation xml:lang="en">Kvetnansky R., Sabban E.L., Palkovits M. Catecholaminergic systems in stress:  structural and molecular genetic approaches. Physiol. Rev. 2009;89(2):535-606.</mixed-citation></citation-alternatives></ref><ref id="cit44"><label>44</label><citation-alternatives><mixed-citation xml:lang="ru">Kumer S.C., Vrana K.E. Intricate regulation of tyrosine hydroxylase activity and gene expression. J. Neurochem. 1996;67(2):443-462.</mixed-citation><mixed-citation xml:lang="en">Langlais D., Couture C., Balsalobre A., Drouin J. The Stat3/GR interaction code:  predictive value of direct/indirect DNA recruitment for transcription outcome. Mol.  Cell. 2012;47(1):38-49. DOI 10.1016/j.molcel.2012.04.021</mixed-citation></citation-alternatives></ref><ref id="cit45"><label>45</label><citation-alternatives><mixed-citation xml:lang="ru">Kvetnansky R., Sabban E.L., Palkovits M. Catecholaminergic systems in stress: structural and molecular genetic approaches. Physiol. Rev. 2009;89(2):535-606.</mixed-citation><mixed-citation xml:lang="en">Lenartowski R., Goc A. Epigenetic, transcriptional and posttranscriptional regulation of the tyrosine hydroxylase gene. Int. J. Dev. Neurosci.  2011;29(8):873- 883.</mixed-citation></citation-alternatives></ref><ref id="cit46"><label>46</label><citation-alternatives><mixed-citation xml:lang="ru">Langlais D., Couture C., Balsalobre A., Drouin J. The Stat3/GR interaction code: predictive value of direct/indirect DNA recruitment for transcription outcome. Mol. Cell. 2012;47(1):38-49. DOI 10.1016/j. molcel.2012.04.021</mixed-citation><mixed-citation xml:lang="en">Lewis E.J., Tank A.W., Weiner N., Chikaraishi D.M. Regulation of tyrosine hydroxylase mRNA by glucocorticoid and cyclic AMP in a rat pheochromocytoma cell  line. Isolation of a cDNA clone for tyrosine hydroxylase mRNA. J. Biol. Chem. 1983;258(23):14632-14637.</mixed-citation></citation-alternatives></ref><ref id="cit47"><label>47</label><citation-alternatives><mixed-citation xml:lang="ru">Lenartowski R., Goc A. Epigenetic, transcriptional and posttranscriptional regulation of the tyrosine hydroxylase gene. Int. J. Dev. Neurosci. 2011;29(8):873-883.</mixed-citation><mixed-citation xml:lang="en">Liberman A.C., Refojo D., Druker J., Toscano M., Rein T., Holsboer F., Arzt E. The  activated glucocorticoid receptor inhibits the transcription factor T-bet by direct  protein-protein interaction. FASEB J. 2007;21(4):1177-1188. DOI 10.1096/fj.06- 7452com</mixed-citation></citation-alternatives></ref><ref id="cit48"><label>48</label><citation-alternatives><mixed-citation xml:lang="ru">Lewis E.J., Tank A.W., Weiner N., Chikaraishi D.M. Regulation of tyrosine hydroxylase mRNA by glucocorticoid and cyclic AMP in a rat pheochromocytoma cell line. Isolation of a cDNA clone for tyrosine hydroxylase mRNA. J. Biol. Chem. 1983;258(23):14632-14637.</mixed-citation><mixed-citation xml:lang="en">Lopez-Sanchez C., Bartulos O., Martinez-Campos E., Ganan C., Valenciano A.I.,  Garcia-Martinez V., De Pablo F., Hernandez-Sanchez C. Tyrosine hydroxylase is  expressed during early heart development and is required for cardiac chamber  formation. Cardiovasc. Res. 2010;88(1):111-120.</mixed-citation></citation-alternatives></ref><ref id="cit49"><label>49</label><citation-alternatives><mixed-citation xml:lang="ru">Liberman A.C., Refojo D., Druker J., Toscano M., Rein T., Holsboer F., Arzt E. The activated glucocorticoid receptor inhibits the transcription factor T-bet by direct protein-protein interaction. FASEB J. 2007;21(4):1177-1188. DOI 10.1096/fj.06-7452com</mixed-citation><mixed-citation xml:lang="en">Makino S., Smith M.A., Gold P.W. Regulatory role of glucocorticoids and  glucocorticoid receptor mRNA levels on tyrosine hydroxylase gene expression in the  locus coeruleus during repeated immobilization stress. Brain Res. 2002;943(2):216- 223.</mixed-citation></citation-alternatives></ref><ref id="cit50"><label>50</label><citation-alternatives><mixed-citation xml:lang="ru">Lopez-Sanchez C., Bartulos O., Martinez-Campos E., Ganan C., Valenciano A.I., Garcia-Martinez V., De Pablo F., Hernandez-Sanchez C. Tyrosine hydroxylase is expressed during early heart development and is required for cardiac chamber formation. Cardiovasc. Res. 2010;88(1):111-120.</mixed-citation><mixed-citation xml:lang="en">Markey K.A., Towle A.C., Sze P.Y. Glucocorticoid influence on tyrosine hydroxylase  activity in mouse locus coeruleus during postnatal development. Endocrinology.  1982;111(5):1519-1523. DOI 10.1210/endo-111-5-1519</mixed-citation></citation-alternatives></ref><ref id="cit51"><label>51</label><citation-alternatives><mixed-citation xml:lang="ru">Makino S., Smith M.A., Gold P.W. Regulatory role of glucocorticoids and glucocorticoid receptor mRNA levels on tyrosine hydroxylase gene expression in the locus coeruleus during repeated immobilization stress. Brain Res. 2002;943(2):216-223.</mixed-citation><mixed-citation xml:lang="en">Markham J.A., Koenig J.I. Prenatal stress: role in psychotic and depressive diseases. Psychopharmacology. 2011;214(1):89-106. DOI  10.1007/s00213-010-2035-0</mixed-citation></citation-alternatives></ref><ref id="cit52"><label>52</label><citation-alternatives><mixed-citation xml:lang="ru">Markey K.A., Towle A.C., Sze P.Y. Glucocorticoid influence on tyrosine hydroxylase activity in mouse locus coeruleus during postnatal development. Endocrinology. 1982;111(5):1519-1523. DOI 10.1210/endo-111-5-1519</mixed-citation><mixed-citation xml:lang="en">Matthews K., Dalley J.W., Matthews C., Tsai T.H., Robbins T.W. Periodic maternal  separation of neonatal rats produces region- and gender-specific effects on biogenic  amine content in postmortem adult brain. Synapse. 2001;40(1):1-10. DOI 10.1002/10982396 (200104)40:1&lt;1::AID-SYN1020&gt;3.0.CO;2-E</mixed-citation></citation-alternatives></ref><ref id="cit53"><label>53</label><citation-alternatives><mixed-citation xml:lang="ru">Markham J.A., Koenig J.I. Prenatal stress: role in psychotic and depressive diseases. Psychopharmacology. 2011;214(1):89-106. DOI 10.1007/s00213-010-2035-0</mixed-citation><mixed-citation xml:lang="en">McArthur S., McHale E., Gillies G.E. The size and distribution of midbrain dopaminergic populations are permanently altered by perinatal  glucocorticoid  exposure in a sex- region- and time-specific manner.Neuropsychopharmacology.  2007;32(7):1462-1476. DOI 10.1038/sj.npp.1301277</mixed-citation></citation-alternatives></ref><ref id="cit54"><label>54</label><citation-alternatives><mixed-citation xml:lang="ru">Matthews K., Dalley J.W., Matthews C., Tsai T.H., Robbins T.W. Periodic maternal separation of neonatal rats produces region- and gender-specific effects on biogenic amine content in postmortem adult brain. Synapse. 2001;40(1):1-10. DOI 10.1002/1098-2396 (200104)40:1&lt;1::AID-SYN1020&gt;3.0.CO;2-E</mixed-citation><mixed-citation xml:lang="en">Morin X., Cremer H., Hirsch M.R., Kapur R.P., Goridis C., Brunet J.F. Defects in  sensory and autonomic ganglia and absence of locus coeruleus in mice deficient for  the homeobox gene Phox2a. Neuron. 1997;18(3):411-423.</mixed-citation></citation-alternatives></ref><ref id="cit55"><label>55</label><citation-alternatives><mixed-citation xml:lang="ru">McArthur S., McHale E., Gillies G.E. The size and distribution of midbrain dopaminergic populations are permanently altered by perinatal glucocorticoid exposure in a sex- region- and time-specific manner. Neuropsychopharmacology. 2007;32(7):1462-1476. DOI 10.1038/ sj.npp.1301277</mixed-citation><mixed-citation xml:lang="en">Nagamoto-Combs K., Piech K.M., Best J.A., Sun B., Tank A.W. Tyrosine hydroxylase  gene promoter activity is regulated by both cyclic AMP-responsive element and AP1  sites following calcium influx. Evidence for cyclic amp-responsive element binding  protein-independent regulation. J. Biol. Chem. 1997;272(9):6051-6058.</mixed-citation></citation-alternatives></ref><ref id="cit56"><label>56</label><citation-alternatives><mixed-citation xml:lang="ru">Morin X., Cremer H., Hirsch M.R., Kapur R.P., Goridis C., Brunet J.F. Defects in sensory and autonomic ganglia and absence of locus coeruleus in mice deficient for the homeobox gene Phox2a. Neuron. 1997;18(3):411-423.</mixed-citation><mixed-citation xml:lang="en">Nagatsu T., Levitt M., Udenfriend S. Tyrosine hydroxylase. The initial step in norepinephrine biosynthesis. J. Biol. Chem. 1964;2910-2917.</mixed-citation></citation-alternatives></ref><ref id="cit57"><label>57</label><citation-alternatives><mixed-citation xml:lang="ru">Nagamoto-Combs K., Piech K.M., Best J.A., Sun B., Tank A.W. Tyrosine hydroxylase gene promoter activity is regulated by both cyclic AMP-responsive element and AP1 sites following calcium influx. Evidence for cyclic amp-responsive element binding protein-independent regulation. J. Biol. Chem. 1997;272(9):6051-6058.</mixed-citation><mixed-citation xml:lang="en">Naumenko E.V., Dygalo N.N. Noradrenergic brain mechanisms and emotional stress in  adult rats after prenatal hydrocortisone treatment. Biogenic Amines in Development.  Amsterdam: Elsevier/North Holland Biomedical Press, 1980;373-388.</mixed-citation></citation-alternatives></ref><ref id="cit58"><label>58</label><citation-alternatives><mixed-citation xml:lang="ru">Nagatsu T., Levitt M., Udenfriend S. Tyrosine hydroxylase. The initial step in norepinephrine biosynthesis. J. Biol. Chem. 1964;2910-2917.</mixed-citation><mixed-citation xml:lang="en">Newton R., Holden N.S. Separating transrepression and transactivation: a distressing  divorce for the glucocorticoid receptor? Mol. Pharmacol. 2007;72(4):799-809.</mixed-citation></citation-alternatives></ref><ref id="cit59"><label>59</label><citation-alternatives><mixed-citation xml:lang="ru">Naumenko E.V., Dygalo N.N. Noradrenergic brain mechanisms and emotional stress in adult rats after prenatal hydrocortisone treatment. Biogenic Amines in Development. Amsterdam: Elsevier/North Holland Biomedical Press, 1980;373-388.</mixed-citation><mixed-citation xml:lang="en">Oakley R.H., Cidlowski J.A. The biology of the glucocorticoid receptor: new  signaling mechanisms in health and disease. J. Allergy Clin. Immun. 2013;132(5):1033-1044. DOI 10.1016/j.jaci.2013.09.007</mixed-citation></citation-alternatives></ref><ref id="cit60"><label>60</label><citation-alternatives><mixed-citation xml:lang="ru">Newton R., Holden N.S. Separating transrepression and transactivation: a distressing divorce for the glucocorticoid receptor? Mol. Pharmacol. 2007;72(4):799-809.</mixed-citation><mixed-citation xml:lang="en">Okada Y., Saika S., Shirai K., Ohnishi Y., Senba E. Expression of AP-1 (c-fos/c-jun)  in developing mouse corneal epithelium. Graefe’s archive for clinical and  experimental ophthalmology = Albrecht von Graefes Archiv fur klinische und  experimentelle Ophthalmologie. 2003;241(4):330-333.</mixed-citation></citation-alternatives></ref><ref id="cit61"><label>61</label><citation-alternatives><mixed-citation xml:lang="ru">Oakley R.H., Cidlowski J.A. The biology of the glucocorticoid receptor: new signaling mechanisms in health and disease. J. Allergy Clin. Immun. 2013;132(5):1033-1044. DOI 10.1016/j.jaci.2013.09.007</mixed-citation><mixed-citation xml:lang="en">Qian Y., Fritzsch B., Shirasawa S., Chen C.L., Choi Y., Ma Q. Formation of brainstem  (nor)adrenergic centers and first-order relay visceral sensory neurons is dependent  on homeodomain protein Rnx/ Tlx3. Genes Dev. 2001;15(19):2533-2545.</mixed-citation></citation-alternatives></ref><ref id="cit62"><label>62</label><citation-alternatives><mixed-citation xml:lang="ru">Okada Y., Saika S., Shirai K., Ohnishi Y., Senba E. Expression of AP-1 (c-fos/c-jun) in developing mouse corneal epithelium. Graefe’s archive for clinical and experimental ophthalmology = Albrecht von Graefes Archiv fur klinische und experimentelle Ophthalmologie. 2003;241(4):330-333.</mixed-citation><mixed-citation xml:lang="en">Pattyn A., Goridis C., Brunet J.F. Specification of the central noradrenergic phenotype by the homeobox gene Phox2b. Mol. Cell. Neurosci.  2000;15(3):235-243. DOI 10.1006/mcne.1999.0826</mixed-citation></citation-alternatives></ref><ref id="cit63"><label>63</label><citation-alternatives><mixed-citation xml:lang="ru">Qian Y., Fritzsch B., Shirasawa S., Chen C.L., Choi Y., Ma Q. Formation of brainstem (nor)adrenergic centers and first-order relay visceral sensory neurons is dependent on homeodomain protein Rnx/Tlx3. Genes Dev. 2001;15(19):2533-2545.</mixed-citation><mixed-citation xml:lang="en">Paulding W.R., Schnell P.O., Bauer A.L., Striet J.B., Nash J.A.,  Kuznetsova A.V.,  Czyzyk-Krzeska M.F. Regulation of gene expression for neurotransmitters during  adaptation to hypoxia in oxygensensitive neuroendocrine cells. Microsc. Res.  Techniq. 2002;59(3): 178-187. DOI 10.1002/jemt.10192</mixed-citation></citation-alternatives></ref><ref id="cit64"><label>64</label><citation-alternatives><mixed-citation xml:lang="ru">Pattyn A., Goridis C., Brunet J.F. Specification of the central noradrenergic phenotype by the homeobox gene Phox2b. Mol. Cell. Neurosci. 2000;15(3):235-243. DOI 10.1006/mcne.1999.0826</mixed-citation><mixed-citation xml:lang="en">Pennypacker K.R. AP-1 transcription factor complexes in CNS disorders and development. J. Florida Med. Assoc. 1995;82(8):551-554.</mixed-citation></citation-alternatives></ref><ref id="cit65"><label>65</label><citation-alternatives><mixed-citation xml:lang="ru">Paulding W.R., Schnell P.O., Bauer A.L., Striet J.B., Nash J.A., Kuznetsova A.V., Czyzyk-Krzeska M.F. Regulation of gene expression for neurotransmitters during adaptation to hypoxia in oxygensensitive neuroendocrine cells. Microsc. Res. Techniq. 2002;59(3): 178-187. DOI 10.1002/jemt.10192</mixed-citation><mixed-citation xml:lang="en">Pfahl M. Nuclear receptor/AP-1 interaction. Endocr. Rev. 1993;14(5): 651-658.</mixed-citation></citation-alternatives></ref><ref id="cit66"><label>66</label><citation-alternatives><mixed-citation xml:lang="ru">Pennypacker K.R. AP-1 transcription factor complexes in CNS disorders and development. J. Florida Med. Assoc. 1995;82(8):551-554.</mixed-citation><mixed-citation xml:lang="en">Puymirat J., Faivre-Bauman A., Bizzini B., Tixier-Vidal A. Prenatal and postnatal  ontogenesis of neurotransmitter-synthetizing enzymes and [125I]tetanus toxin binding  capacity in the mouse hypothalamus. Brain Res. 1982;255(2):199-206.</mixed-citation></citation-alternatives></ref><ref id="cit67"><label>67</label><citation-alternatives><mixed-citation xml:lang="ru">Pfahl M. Nuclear receptor/AP-1 interaction. Endocr. Rev. 1993;14(5): 651-658.</mixed-citation><mixed-citation xml:lang="en">Radcliffe P.M., Sterling C.R., Tank A.W. Induction of tyrosine hydroxylase mRNA by  nicotine in rat midbrain is inhibited by mifepristone. J. Neurochem.   2009;109(5):1272-1284. DOI 10.1111/j.1471-4159. 2009.06056.x</mixed-citation></citation-alternatives></ref><ref id="cit68"><label>68</label><citation-alternatives><mixed-citation xml:lang="ru">Puymirat J., Faivre-Bauman A., Bizzini B., Tixier-Vidal A. Prenatal and postnatal ontogenesis of neurotransmitter-synthetizing enzymes and [125I]tetanus toxin binding capacity in the mouse hypothalamus. Brain Res. 1982;255(2):199-206.</mixed-citation><mixed-citation xml:lang="en">Raivich G., Behrens A. Role of the AP-1 transcription factor c-Jun in developing, adult and injured brain. Progr. Neurobiol. 2006;78(6):347-363.</mixed-citation></citation-alternatives></ref><ref id="cit69"><label>69</label><citation-alternatives><mixed-citation xml:lang="ru">Radcliffe P.M., Sterling C.R., Tank A.W. Induction of tyrosine hydroxylase mRNA by nicotine in rat midbrain is inhibited by mifepristone. J. Neurochem. 2009;109(5):1272-1284. DOI 10.1111/j.1471-4159. 2009.06056.x</mixed-citation><mixed-citation xml:lang="en">Rani C.S., Elango N., Wang S.S., Kobayashi K., Strong R. Identification of an  activator protein-1-like sequence as the glucocorticoid response element in the rat  tyrosine hydroxylase gene. Mol. Pharmacol. 2009;75(3):589-598.</mixed-citation></citation-alternatives></ref><ref id="cit70"><label>70</label><citation-alternatives><mixed-citation xml:lang="ru">Raivich G., Behrens A. Role of the AP-1 transcription factor c-Jun in developing, adult and injured brain. Progr. Neurobiol. 2006;78(6): 347-363.</mixed-citation><mixed-citation xml:lang="en">Rani C.S.S., Soto-Pina A., Iacovitti L., Strong R. Evolutionary conservation of an  atypical glucocorticoid-responsive element in the human tyrosine hydroxylase gene.  J. Neurochem. 2013;126(1):19-28. DOI 10.1111/jnc.12294</mixed-citation></citation-alternatives></ref><ref id="cit71"><label>71</label><citation-alternatives><mixed-citation xml:lang="ru">Rani C.S., Elango N., Wang S.S., Kobayashi K., Strong R. Identification of an activator protein-1-like sequence as the glucocorticoid response element in the rat tyrosine hydroxylase gene. Mol. Pharmacol. 2009;75(3):589-598.</mixed-citation><mixed-citation xml:lang="en">Reynolds R.M. Programming effects of glucocorticoids. Clin. Obstet. Gynecol. 2013;56(3):602-609. DOI 10.1097/GRF.0b013e31829939f7</mixed-citation></citation-alternatives></ref><ref id="cit72"><label>72</label><citation-alternatives><mixed-citation xml:lang="ru">Rani C.S.S., Soto-Pina A., Iacovitti L., Strong R. Evolutionary conservation of an atypical glucocorticoid-responsive element in the human tyrosine hydroxylase gene. J. Neurochem. 2013;126(1):19-28. DOI 10.1111/jnc.12294</mixed-citation><mixed-citation xml:lang="en">Rios M., Habecker B., Sasaoka T., Eisenhofer G., Tian H., Landis S., Chikaraishi D.,  Roffler-Tarlov S. Catecholamine synthesis is mediated by tyrosinase in the absence  of tyrosine hydroxylase. J. Neurosci. 1999;19(9):3519-3526.</mixed-citation></citation-alternatives></ref><ref id="cit73"><label>73</label><citation-alternatives><mixed-citation xml:lang="ru">Reynolds R.M. Programming effects of glucocorticoids. Clin. Obstet. Gynecol. 2013;56(3):602-609. DOI 10.1097/GRF.0b013e31829939f7</mixed-citation><mixed-citation xml:lang="en">Romano G., Suon S., Jin H., Donaldson A.E., Iacovitti L. Characterization of five  evolutionary conserved regions of the human tyrosine hydroxylase (TH) promoter:  implications for the engineering of a human TH minimal promoter assembled in a self- inactivating lentiviral vector system. J. Cell. Physiol. 2005;204(2):666-677.</mixed-citation></citation-alternatives></ref><ref id="cit74"><label>74</label><citation-alternatives><mixed-citation xml:lang="ru">Rios M., Habecker B., Sasaoka T., Eisenhofer G., Tian H., Landis S., Chikaraishi D., Roffler-Tarlov S. Catecholamine synthesis is mediated by tyrosinase in the absence of tyrosine hydroxylase. J. Neurosci. 1999;19(9):3519-3526.</mixed-citation><mixed-citation xml:lang="en">Sabban E.L., Hebert M.A., Liu X., Nankova B., Serova L. Differential effects of  stress on gene transcription factors in catecholaminergic systems. Ann. N.Y. Acad.  Sci. 2004;1032:130-140.</mixed-citation></citation-alternatives></ref><ref id="cit75"><label>75</label><citation-alternatives><mixed-citation xml:lang="ru">Romano G., Suon S., Jin H., Donaldson A.E., Iacovitti L. Characterization of five evolutionary conserved regions of the human tyrosine hydroxylase (TH) promoter: implications for the engineering of a human TH minimal promoter assembled in a self-inactivating lentiviral vector system. J. Cell. Physiol. 2005;204(2):666-677.</mixed-citation><mixed-citation xml:lang="en">Sabban E.L., Kvetnansky R. Stress-triggered activation of gene expression in  catecholaminergic systems: dynamics of transcriptional events. Trends Neurosci. 2001;24(2):91-98.</mixed-citation></citation-alternatives></ref><ref id="cit76"><label>76</label><citation-alternatives><mixed-citation xml:lang="ru">Sabban E.L., Hebert M.A., Liu X., Nankova B., Serova L. Differential effects of stress on gene transcription factors in catecholaminergic systems. Ann. N.Y. Acad. Sci. 2004;1032:130-140.</mixed-citation><mixed-citation xml:lang="en">Sapolsky R.M., Romero L.M., Munck A.U. How do glucocorticoids influence stress  responses? Integrating permissive, suppressive, stimulatory, and preparative actions. Endocr. Rev. 2000;21(1):55-89.</mixed-citation></citation-alternatives></ref><ref id="cit77"><label>77</label><citation-alternatives><mixed-citation xml:lang="ru">Sabban E.L., Kvetnansky R. Stress-triggered activation of gene expression in catecholaminergic systems: dynamics of transcriptional events. Trends Neurosci. 2001;24(2):91-98.</mixed-citation><mixed-citation xml:lang="en">Shishkina G.T., Kalinina T.S., Dygalo N.N. Attenuation of alpha2Aadrenergic receptor  expression in neonatal rat brain by RNA interference or antisense oligonucleotide  reduced anxiety in adulthood. Neuroscience. 2004a;129(3):521-528. DOI  10.1016/j.neuroscience.2004.08.015</mixed-citation></citation-alternatives></ref><ref id="cit78"><label>78</label><citation-alternatives><mixed-citation xml:lang="ru">Sapolsky R.M., Romero L.M., Munck A.U. How do glucocorticoids influence stress responses? Integrating permissive, suppressive, stimulatory, and preparative actions. Endocr. Rev. 2000;21(1):55-89.</mixed-citation><mixed-citation xml:lang="en">Shishkina G.T., Kalinina T.S., Popova N.K., Dygalo N.N. Influence of neonatal short- term reduction in brainstem alpha2A-adrenergic receptors on receptor ontogenesis,  acoustic startle reflex, and prepulse inhibition in rats. Behav. Neurosci.  2004b;118(6):1285-1292. DOI 10.1037/0735-7044.118.6.1285</mixed-citation></citation-alternatives></ref><ref id="cit79"><label>79</label><citation-alternatives><mixed-citation xml:lang="ru">Shishkina G.T., Kalinina T.S., Dygalo N.N. Attenuation of alpha2Aadrenergic receptor expression in neonatal rat brain by RNA interference or antisense oligonucleotide reduced anxiety in adulthood. Neuroscience. 2004a;129(3):521-528. DOI 10.1016/j.neuroscience. 2004.08.015</mixed-citation><mixed-citation xml:lang="en">Simon H.H., Scholz C., O’Leary D.D. Engrailed genes control developmental fate of  serotonergic and noradrenergic neurons in mid- and hindbrain in a gene dose- dependent manner. Mol. Cell. Neurosci. 2005;28(1):96-105. DOI 10.1016/j.mcn.2004.08.016</mixed-citation></citation-alternatives></ref><ref id="cit80"><label>80</label><citation-alternatives><mixed-citation xml:lang="ru">Shishkina G.T., Kalinina T.S., Popova N.K., Dygalo N.N. Influence of neonatal short-term reduction in brainstem alpha2A-adrenergic receptors on receptor ontogenesis, acoustic startle reflex, and prepulse inhibition in rats. Behav. Neurosci. 2004b;118(6):1285-1292. DOI 10.1037/0735-7044.118.6.1285</mixed-citation><mixed-citation xml:lang="en">Slotkin T.A., Kreider M.L., Tate C.A., Seidler F.J. Critical prenatal and postnatal  periods for persistent effects of dexamethasone on serotonergic and dopaminergic  systems. Neuropsychopharmacology. 2006;31(5):904-911. DOI 10.1038/sj.npp.1300892</mixed-citation></citation-alternatives></ref><ref id="cit81"><label>81</label><citation-alternatives><mixed-citation xml:lang="ru">Simon H.H., Scholz C., O’Leary D.D. Engrailed genes control developmental fate of serotonergic and noradrenergic neurons in mid- and hindbrain in a gene dose-dependent manner. Mol. Cell. Neurosci. 2005;28(1):96-105. DOI 10.1016/j.mcn.2004.08.016</mixed-citation><mixed-citation xml:lang="en">Sukhareva E.V., Dygalo N.N., Kalinina T.S. Influence of dexamethasone on the  expression of immediate-early c-fos and c-jun genes in different regions of the  neonatal brain. Molekulyarnaya biologiya = Molecular Biology. 2016;50(2):266-271.</mixed-citation></citation-alternatives></ref><ref id="cit82"><label>82</label><citation-alternatives><mixed-citation xml:lang="ru">Slotkin T.A., Kreider M.L., Tate C.A., Seidler F.J. Critical prenatal and postnatal periods for persistent effects of dexamethasone on serotonergic and dopaminergic systems. Neuropsychopharmacology. 2006;31(5):904-911. DOI 10.1038/sj.npp.1300892</mixed-citation><mixed-citation xml:lang="en">Sukhareva E.V., Kalinina T.S., Lanshakov D.A., Bulygina V.V., Dygalo N.N. Proteins  of the AP1 complex in glucocorticoid induction of brain tyrosine hydroxylase in  early ontogenesis. Materialy sedmoy Vserossiyskoy nauchno-prakticheskoy konferentsii  «Fundamentalnye aspekty kompensatorno-prisposobitel’ykh protsessov» i Molodezhnogo  simpoziuma «Molekulyarno-kletochnye i medikoekologicheskie problemy kompensatsii i  prisposobleniya» [Proc. 7th All-Russian Scientific-Practical Conf. “The fundamental  aspects of compensatory and adaptive processes” and the Youth Symp. “Molecular and  medicoenvironmental problems of compensation and adaptation”]. Novosibirsk,  2015;271-272.</mixed-citation></citation-alternatives></ref><ref id="cit83"><label>83</label><citation-alternatives><mixed-citation xml:lang="ru">Sun B., Chen X., Xu L., Sterling C., Tank A.W. Chronic nicotine treatment leads to induction of tyrosine hydroxylase in locus ceruleus neurons: the role of transcriptional activation. Mol. Pharmacol. 2004;66(4):1011-1021.</mixed-citation><mixed-citation xml:lang="en">Sun B., Chen X., Xu L., Sterling C., Tank A.W. Chronic nicotine  treatment leads to  induction of tyrosine hydroxylase in locus ceruleus neurons: the role of  transcriptional activation. Mol. Pharmacol. 2004;66(4):1011-1021.</mixed-citation></citation-alternatives></ref><ref id="cit84"><label>84</label><citation-alternatives><mixed-citation xml:lang="ru">Tank A.W., Curella P., Ham L. Induction of mRNA for tyrosine hydroxylase by cyclic AMP and glucocorticoids in a rat pheochromocytoma cell line: evidence for the regulation of tyrosine hydroxylase synthesis by multiple mechanisms in cells exposed to elevated levels of both inducing agents. Mol. Pharmacol. 1986;30(5):497-503.</mixed-citation><mixed-citation xml:lang="en">Tank A.W., Curella P., Ham L. Induction of mRNA for tyrosine hydroxylase by cyclic  AMP and glucocorticoids in a rat pheochromocytoma cell line: evidence for the  regulation of tyrosine hydroxylase synthesis by multiple mechanisms in cells exposed  to elevated levels of both inducing agents. Mol. Pharmacol. 1986;30(5):497-503.</mixed-citation></citation-alternatives></ref><ref id="cit85"><label>85</label><citation-alternatives><mixed-citation xml:lang="ru">Tank A.W., Xu L., Chen X., Radcliffe P., Sterling C.R. Post-transcriptional regulation of tyrosine hydroxylase expression in adrenal medulla and brain. Ann. N.Y. Acad. Sci. 2008;1148:238-248.</mixed-citation><mixed-citation xml:lang="en">Tank A.W., Xu L., Chen X., Radcliffe P., Sterling C.R. Post-transcriptional regulation of tyrosine hydroxylase expression in adrenal medulla and brain. Ann.  N.Y. Acad. Sci. 2008;1148:238-248.</mixed-citation></citation-alternatives></ref><ref id="cit86"><label>86</label><citation-alternatives><mixed-citation xml:lang="ru">Tekin I., Roskoski R. Jr., Carkaci-Salli N., Vrana K.E. Complex molecular regulation of tyrosine hydroxylase. J. Neur. Transm. (Vienna). 2014;121(12):1451-1481. DOI 10.1007/s00702-014-1238-7</mixed-citation><mixed-citation xml:lang="en">Tekin I., Roskoski R. Jr., Carkaci-Salli N., Vrana K.E. Complex molecular regulation  of tyrosine hydroxylase. J. Neur. Transm. (Vienna). 2014;121(12):1451-1481. DOI 10.1007/s00702-014-1238-7</mixed-citation></citation-alternatives></ref><ref id="cit87"><label>87</label><citation-alternatives><mixed-citation xml:lang="ru">Teurich S., Angel P. The glucocorticoid receptor synergizes with Jun homodimers to activate AP-1-regulated promoters lacking GR binding sites. Chem. Sens. 1995;20(2):251-255.</mixed-citation><mixed-citation xml:lang="en">Teurich S., Angel P. The glucocorticoid receptor synergizes with Jun homodimers to  activate AP-1-regulated promoters lacking GR binding sites. Chem. Sens. 1995;20(2):251-255.</mixed-citation></citation-alternatives></ref><ref id="cit88"><label>88</label><citation-alternatives><mixed-citation xml:lang="ru">Thomas S.A., Matsumoto A.M., Palmiter R.D. Noradrenaline is essential for mouse fetal development. Nature. 1995;374(6523):643-646.</mixed-citation><mixed-citation xml:lang="en">Thomas S.A., Matsumoto A.M., Palmiter R.D. Noradrenaline is essential for mouse fetal development. Nature. 1995;374(6523):643-646.</mixed-citation></citation-alternatives></ref><ref id="cit89"><label>89</label><citation-alternatives><mixed-citation xml:lang="ru">Vogel-Höpker A., Rohrer H. The specification of noradrenergic locus coeruleus (LC) neurones depends on bone morphogenetic proteins (BMPs). Development. 2002;129(4):983-991.</mixed-citation><mixed-citation xml:lang="en">Vogel-Höpker A., Rohrer H. The specification of noradrenergic locus coeruleus (LC)  neurones depends on bone morphogenetic proteins (BMPs). Development. 2002;129(4):983-991.</mixed-citation></citation-alternatives></ref><ref id="cit90"><label>90</label><citation-alternatives><mixed-citation xml:lang="ru">Wurst W., Bally-Cuif L. Neural plate patterning: upstream and downstream of the isthmic organizer. Nat. Rev. Neurosci. 2001;2(2):99-108. DOI 10.1038/35053516</mixed-citation><mixed-citation xml:lang="en">Wurst W., Bally-Cuif L. Neural plate patterning: upstream and downstream of the  isthmic organizer. Nat. Rev. Neurosci. 2001;2(2):99-108. DOI 10.1038/35053516</mixed-citation></citation-alternatives></ref><ref id="cit91"><label>91</label><citation-alternatives><mixed-citation xml:lang="ru">Yamamoto K., Ruuskanen J.O., Wullimann M.F., Vernier P. Two tyrosine hydroxylase genes in vertebrates New dopaminergic territories revealed in the zebrafish brain. Mol. Cell. Neurosci. 2010;43(4): 394-402.</mixed-citation><mixed-citation xml:lang="en">Yamamoto K., Ruuskanen J.O., Wullimann M.F., Vernier P. Two tyrosine hydroxylase  genes in vertebrates New dopaminergic territories revealed in the zebrafish brain. Mol. Cell. Neurosci. 2010;43(4):394-402.</mixed-citation></citation-alternatives></ref><ref id="cit92"><label>92</label><citation-alternatives><mixed-citation xml:lang="ru">Zhong S., Quealy J.A., Bode A.M., Nomura M., Kaji A., Ma W.Y., Dong Z. Organ-specific activation of activator protein-1 in transgenic mice by 12-o-tetradecanoylphorbol-13-acetate with different administration methods. Cancer Res. 2001;61(10):4084-4091.</mixed-citation><mixed-citation xml:lang="en">Zhong S., Quealy J.A., Bode A.M., Nomura M., Kaji A., Ma W.Y., Dong Z. Organ- specific activation of activator protein-1 in transgenic mice by 12-o- tetradecanoylphorbol-13-acetate with different administration methods. Cancer Res. 2001;61(10):4084-4091.</mixed-citation></citation-alternatives></ref><ref id="cit93"><label>93</label><citation-alternatives><mixed-citation xml:lang="ru">Zhou Q.Y., Quaife C.J., Palmiter R.D. Targeted disruption of the tyrosine hydroxylase gene reveals that catecholamines are required for mouse fetal development. Nature. 1995;374(6523):640-643.</mixed-citation><mixed-citation xml:lang="en">Zhou Q.Y., Quaife C.J., Palmiter R.D. Targeted disruption of the tyrosine hydroxylase gene reveals that catecholamines are required for  mouse fetal  development. Nature. 1995;374(6523):640-643.</mixed-citation></citation-alternatives></ref></ref-list><fn-group><fn fn-type="conflict"><p>The authors declare that there are no conflicts of interest present.</p></fn></fn-group></back></article>
