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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">diaendo</journal-id><journal-title-group><journal-title xml:lang="ru">Сахарный диабет</journal-title><trans-title-group xml:lang="en"><trans-title>Diabetes mellitus</trans-title></trans-title-group></journal-title-group><issn pub-type="ppub">2072-0351</issn><issn pub-type="epub">2072-0378</issn><publisher><publisher-name>Endocrinology research centre</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="doi">10.14341/DM10195</article-id><article-id custom-type="elpub" pub-id-type="custom">diaendo-10195</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>Обзоры</subject></subj-group><subj-group subj-group-type="section-heading" xml:lang="en"><subject>Review</subject></subj-group></article-categories><title-group><article-title>Потенциальная роль галанина в терапии сахарного диабета 2 типа</article-title><trans-title-group xml:lang="en"><trans-title>Potential role of galanine in the treatment of type 2 diabetes mellitus</trans-title></trans-title-group></title-group><contrib-group><contrib contrib-type="author" corresp="yes"><contrib-id contrib-id-type="orcid">https://orcid.org/0000-0001-8831-4781</contrib-id><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Доброхотов</surname><given-names>Игорь Владимирович</given-names></name><name name-style="western" xml:lang="en"><surname>Dobrokhotov</surname><given-names>Igor Vladimirovich</given-names></name></name-alternatives><bio xml:lang="ru"><p>Кандидат медицинских наук, научный сотрудник, eLibrary SPIN: 3465-7904.</p><p>121552 Москва, ул. 3-я Черепковская, д. 15a</p></bio><bio xml:lang="en"><p>MD, PhD, research associate, eLibrary SPIN: 3465-7904.</p><p>15a, Tretya Cherepkovskayast., 121552 Moscow</p></bio><email xlink:type="simple">hum.d@narod.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>Веселова</surname><given-names>Оксана Михайловна</given-names></name><name name-style="western" xml:lang="en"><surname>Veselova</surname><given-names>Oksana M.</given-names></name></name-alternatives><bio xml:lang="ru"><p>Кандидат биологических наукб, старшийн аучный сотрудник, eLibrary SPIN: 6366-4603.</p><p>Москва</p></bio><bio xml:lang="en"><p>PhD in Biology, senior research associate, eLibrary SPIN: 6366-4603.</p><p>Moscow</p></bio><email xlink:type="simple">hum.d@narod.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>Любимов</surname><given-names>Роман Олегович</given-names></name><name name-style="western" xml:lang="en"><surname>Lyubimov</surname><given-names>Roman O.</given-names></name></name-alternatives><bio xml:lang="ru"><p>Лаборант-исследователь, eLibrary SPIN: 6542-2600.</p><p>Москва</p></bio><bio xml:lang="en"><p>Research assistant, eLibrary SPIN: 6542-2600.</p><p>Moscow</p></bio><email xlink:type="simple">lubimov@onet.ru</email><xref ref-type="aff" rid="aff-1"/></contrib></contrib-group><aff-alternatives id="aff-1"><aff xml:lang="ru"><institution>Национальный медицинский исследовательский центр кардиологии</institution><country>Россия</country></aff><aff xml:lang="en"><institution>National Medical Research Center of Cardiology</institution><country>Russian Federation</country></aff></aff-alternatives><pub-date pub-type="collection"><year>2020</year></pub-date><pub-date pub-type="epub"><day>02</day><month>12</month><year>2020</year></pub-date><volume>23</volume><issue>4</issue><fpage>368</fpage><lpage>373</lpage><permissions><copyright-statement>Copyright &amp;#x00A9; Доброхотов И.В., Веселова О.М., Любимов Р.О., 2020</copyright-statement><copyright-year>2020</copyright-year><copyright-holder xml:lang="ru">Доброхотов И.В., Веселова О.М., Любимов Р.О.</copyright-holder><copyright-holder xml:lang="en">Dobrokhotov I.V., Veselova O.M., Lyubimov R.O.</copyright-holder><license xml:lang="ru" license-type="creative-commons-attribution" xlink:href="https://creativecommons.org/licenses/by/4.0/" xlink:type="simple"><license-p>Данная работа распространяется под лицензией Creative Commons Attribution 4.0.</license-p></license><license xml:lang="en" 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://www.dia-endojournals.ru/jour/article/view/10195">https://www.dia-endojournals.ru/jour/article/view/10195</self-uri><abstract><p>Растущая распространенность сахарного диабета требует оптимизации имеющихся и поиска новых подходов к лечению данного заболевания. Помимо инсулинорезистентности, вызванной дефектами в молекулярных механизмах реализации действия инсулина, необходимо изучать особенности работы других регуляторов, играющих заметную роль в процессе усвоения клетками глюкозы. Галанин, нейропептид из 29 (30 у человека) аминокислот, участвует в большом количестве различных жизненно важных функций, в том числе регуляции энергетического обмена в клетке. Галанин действует посредством взаимодействия с тремя рецепторами, связанными с G-белком, GAL1, GAL2 и GAL3, и передачи сигналов через несколько путей трансдукции, включая ингибирование циклического аденозинмонофосфата (цАМФ)/РКА (GAL1, GAL3) и стимуляцию фосфолипазы C (GAL2). Агонисты и антагонисты подтипов рецепторов галанина GalR1-3 могут использоваться в качестве предполагаемых терапевтических мишеней для лечения различных заболеваний человека. Накапливается все больше данных, доказывающих важную роль пептидного регулятора галанина в этиологии нарушения поглощения глюкозы инсулинозависимыми тканями. В обзоре рассматриваются такие эффекты галанина, как ингибирование синтеза инсулина, активация экспрессии и транслокации к плазматической клеточной мембране переносчика глюкозы GLUT4, увеличение уровня PPAR-g и уменьшение гиперконтрактивности двенадцатиперстной кишки. Приведенные данные подтверждают важность исследований, направленных на поиск эффективного антидиабетического препарата среди синтезированных аналогов галанина.</p></abstract><trans-abstract xml:lang="en"><p>The growing incidence of diabetes mellitus requires the optimizing of existing approaches and searching for new ones to treat this disease. It is necessary to study the features of other regulators that play a significant role in the process of glucose uptake by cells, along with the insulin resistance caused by defects in the molecular mechanisms of insulin action. Galanine, a neuropeptide of 29 (30 in humans) amino acids, is involved in a large number of different vital functions, including regulating energy metabolism in the cell. Galanine interacts with three G protein-coupled receptors, GAL1, GAL2, and GAL3, and transmitting signals through several transduction pathways, including cAMP/PKA inhibition (GAL1, GAL3) and phospholipase C (GAL2) stimulation. Agonists and antagonists of galanine receptor subtype GalR1-3 can be used as intended therapeutic targets to treat various human diseases. We accumulated more data that prove the importance of the galanine peptide regulator in the etiology of impaired glucose uptake by insulin-dependent tissues. The review considers such effects of galanine, as inhibition of insulin synthesis, activation of expression and translocation to the plasma cell membrane of the glucose transporter GLUT4, increase of PPAR-g level, and decrease in duodenal hyper-contractility. These data confirm the importance of research to find an effective antidiabetic drug among the synthesized analogs of galanine.</p></trans-abstract><kwd-group xml:lang="ru"><kwd>галанин</kwd><kwd>диабет</kwd><kwd>GLUT4</kwd><kwd>PPAR-g</kwd><kwd>гиперконтрактивность двенадцатиперстной кишки</kwd><kwd>синтез инсулина</kwd></kwd-group><kwd-group xml:lang="en"><kwd>galanine</kwd><kwd>diabetes</kwd><kwd>GLUT4</kwd><kwd>PPAR-g</kwd><kwd>duodenal hyper-contractility</kwd><kwd>insulin synthesis</kwd></kwd-group><funding-group><funding-statement xml:lang="ru">Поисково-аналитическая работа и подготовка статьи осуществлены на личные средства авторского коллектива</funding-statement></funding-group></article-meta></front><back><ref-list><title>References</title><ref id="cit1"><label>1</label><citation-alternatives><mixed-citation xml:lang="ru">Whiting DR, Guariguata L, Weil C, Shaw J. IDF diabetes atlas: global estimates of the prevalence of diabetes for 2011 and 2030. Diabetes Res Clin Pract. 2011;94(3):311-321. doi: https://doi.org/10.1016Zj.diabres.2011.10.029</mixed-citation><mixed-citation xml:lang="en">Whiting DR, Guariguata L, Weil C, Shaw J. IDF diabetes atlas: global estimates of the prevalence of diabetes for 2011 and 2030. Diabetes Res Clin Pract. 2011;94(3):311-321. doi: https://doi.org/10.1016Zj.diabres.2011.10.029</mixed-citation></citation-alternatives></ref><ref id="cit2"><label>2</label><citation-alternatives><mixed-citation xml:lang="ru">Taylor R. Insulin resistance and type 2 diabetes. Diabetes. 2012;61(4):778-779. doi: https://doi.org/10.2337/db12-0073</mixed-citation><mixed-citation xml:lang="en">Taylor R. Insulin resistance and type 2 diabetes. Diabetes. 2012;61(4):778-779. doi: https://doi.org/10.2337/db12-0073</mixed-citation></citation-alternatives></ref><ref id="cit3"><label>3</label><citation-alternatives><mixed-citation xml:lang="ru">Evans H, Baumgartner M, Shine J, Herzog H. Genomic organization and localization of the gene encoding human preprogalanin. Genomics. 1993;18(3):473-477. doi: https://doi.org/10.1016/s0888-7543(11)80002-9</mixed-citation><mixed-citation xml:lang="en">Evans H, Baumgartner M, Shine J, Herzog H. Genomic organization and localization of the gene encoding human preprogalanin. Genomics. 1993;18(3):473-477. doi: https://doi.org/10.1016/s0888-7543(11)80002-9</mixed-citation></citation-alternatives></ref><ref id="cit4"><label>4</label><citation-alternatives><mixed-citation xml:lang="ru">Lang R, Gundlach AL, Holmes FE, et al. Physiology, signaling, and pharmacology of galanin peptides and receptors: three decades of emerging diversity. Pharmacol Rev. 2015;67(1):118-175. doi: https://doi.org/10.1124/pr.112.006536</mixed-citation><mixed-citation xml:lang="en">Lang R, Gundlach AL, Holmes FE, et al. Physiology, signaling, and pharmacology of galanin peptides and receptors: three decades of emerging diversity. Pharmacol Rev. 2015;67(1):118-175. doi: https://doi.org/10.1124/pr.112.006536</mixed-citation></citation-alternatives></ref><ref id="cit5"><label>5</label><citation-alternatives><mixed-citation xml:lang="ru">Mutt V. Discovery of Galanin. In: Hokfelt T, Bartfai T, Jacobowitz D, Ottoson D. Galanin: A new multifunctional peptide in the neuro-endocrine system. Palgrave, London; 1991. Р, 3-40. https://doi.org/10.1007/978-1-349-12664-4</mixed-citation><mixed-citation xml:lang="en">Mutt V. Discovery of Galanin. In: Hokfelt T, Bartfai T, Jacobowitz D, Ottoson D. Galanin: A new multifunctional peptide in the neuro-endocrine system. Palgrave, London; 1991. Р, 3-40. https://doi.org/10.1007/978-1-349-12664-4</mixed-citation></citation-alternatives></ref><ref id="cit6"><label>6</label><citation-alternatives><mixed-citation xml:lang="ru">Jacobowitz DM, Kresse A, Skofitsch G. Galanin in the brain: chemoarchitectonics and brain cartography-a historical review. Peptides. 2004;25(3):433-464. doi: https://doi.org/10.1016/j.peptides.2004.02.015</mixed-citation><mixed-citation xml:lang="en">Jacobowitz DM, Kresse A, Skofitsch G. Galanin in the brain: chemoarchitectonics and brain cartography-a historical review. Peptides. 2004;25(3):433-464. doi: https://doi.org/10.1016/j.peptides.2004.02.015</mixed-citation></citation-alternatives></ref><ref id="cit7"><label>7</label><citation-alternatives><mixed-citation xml:lang="ru">Dataset: GeneAtlas U133A, gcrma. Available from: http://biogps.org/#goto=genereport&amp;id=51083</mixed-citation><mixed-citation xml:lang="en">Dataset: GeneAtlas U133A, gcrma. Available from: http://biogps.org/#goto=genereport&amp;id=51083</mixed-citation></citation-alternatives></ref><ref id="cit8"><label>8</label><citation-alternatives><mixed-citation xml:lang="ru">Carlton SM, Coggeshall RE. Stereological analysis of galanin and CGRP synapses in the dorsal horn of neuropathic primates. Brain Res. 1996;711(1-2):16-25. doi: https://doi.org/10.1016/0006-8993(95)01303-2</mixed-citation><mixed-citation xml:lang="en">Carlton SM, Coggeshall RE. Stereological analysis of galanin and CGRP synapses in the dorsal horn of neuropathic primates. Brain Res. 1996;711(1-2):16-25. doi: https://doi.org/10.1016/0006-8993(95)01303-2</mixed-citation></citation-alternatives></ref><ref id="cit9"><label>9</label><citation-alternatives><mixed-citation xml:lang="ru">Zhang X, Dagerlind A, Bao L, et al. Increased expression of galanin in the rat superior cervical ganglion after pre- and postganglionic nerve lesions. Exp Neurol. 1994;127(1):9-22. doi: https://doi.org/10.1006/exnr.1994.1075</mixed-citation><mixed-citation xml:lang="en">Zhang X, Dagerlind A, Bao L, et al. Increased expression of galanin in the rat superior cervical ganglion after pre- and postganglionic nerve lesions. Exp Neurol. 1994;127(1):9-22. doi: https://doi.org/10.1006/exnr.1994.1075</mixed-citation></citation-alternatives></ref><ref id="cit10"><label>10</label><citation-alternatives><mixed-citation xml:lang="ru">Webling KE, Runesson J, Bartfai T, Langel U. Galanin receptors and ligands. Front Endocrinol (Lausanne). 2012;3:146. doi: https://doi.org/10.3389/fendo.2012.00146</mixed-citation><mixed-citation xml:lang="en">Webling KE, Runesson J, Bartfai T, Langel U. Galanin receptors and ligands. Front Endocrinol (Lausanne). 2012;3:146. doi: https://doi.org/10.3389/fendo.2012.00146</mixed-citation></citation-alternatives></ref><ref id="cit11"><label>11</label><citation-alternatives><mixed-citation xml:lang="ru">Fuxe K, Borroto-Escuela DO, Romero-Fernandez W, et al. On the existence and function of galanin receptor heteromers in the central nervous system. Front Endocrinol (Lausanne). 2012;3:127. doi: https://doi.org/10.3389/fendo.2012.00127</mixed-citation><mixed-citation xml:lang="en">Fuxe K, Borroto-Escuela DO, Romero-Fernandez W, et al. On the existence and function of galanin receptor heteromers in the central nervous system. Front Endocrinol (Lausanne). 2012;3:127. doi: https://doi.org/10.3389/fendo.2012.00127</mixed-citation></citation-alternatives></ref><ref id="cit12"><label>12</label><citation-alternatives><mixed-citation xml:lang="ru">Díaz Cabiale Z, Parrado C, Fuxe K, et al. Receptor-receptor interactions in central cardiovascular regulation. Focus on neuropeptide/alpha(2)-adrenoreceptor interactions in the nucleus tractussolitarius. J Neural Transm. 2007;114(1):115-125. doi: https://doi.org/10.1007/s00702-006-0559-6</mixed-citation><mixed-citation xml:lang="en">Díaz Cabiale Z, Parrado C, Fuxe K, et al. Receptor-receptor interactions in central cardiovascular regulation. Focus on neuropeptide/alpha(2)-adrenoreceptor interactions in the nucleus tractussolitarius. J Neural Transm. 2007;114(1):115-125. doi: https://doi.org/10.1007/s00702-006-0559-6</mixed-citation></citation-alternatives></ref><ref id="cit13"><label>13</label><citation-alternatives><mixed-citation xml:lang="ru">Lindskog S, Ahren B, Dunning BE, Sundler F. Galanin-immunoreactive nerves in the mouse and rat pancreas. Cell Tissue Res. 1991;264(2):363-368. doi: https://doi.org/10.1007/BF00313975</mixed-citation><mixed-citation xml:lang="en">Lindskog S, Ahren B, Dunning BE, Sundler F. Galanin-immunoreactive nerves in the mouse and rat pancreas. Cell Tissue Res. 1991;264(2):363-368. doi: https://doi.org/10.1007/BF00313975</mixed-citation></citation-alternatives></ref><ref id="cit14"><label>14</label><citation-alternatives><mixed-citation xml:lang="ru">Adeghate E, Ponery AS. Large reduction in the number of galanin-immunoreactive cells in pancreatic islets of diabetic rats. J Neuroendocrinal. 2001;13(8):706-710. doi: https://doi.org/10.1046/j.1365-2826.2001.00682.x</mixed-citation><mixed-citation xml:lang="en">Adeghate E, Ponery AS. Large reduction in the number of galanin-immunoreactive cells in pancreatic islets of diabetic rats. J Neuroendocrinal. 2001;13(8):706-710. doi: https://doi.org/10.1046/j.1365-2826.2001.00682.x</mixed-citation></citation-alternatives></ref><ref id="cit15"><label>15</label><citation-alternatives><mixed-citation xml:lang="ru">Shimosegawa T, Moriizumi S, Koizumi M, et al. Immunohistochemical demonstration of galaninlike immunoreactive nerves in the human pancreas. Gastroenterology. 1992;102(1):263-271. doi: https://doi.org/10.1016/0016-5085(92)91809-i</mixed-citation><mixed-citation xml:lang="en">Shimosegawa T, Moriizumi S, Koizumi M, et al. Immunohistochemical demonstration of galaninlike immunoreactive nerves in the human pancreas. Gastroenterology. 1992;102(1):263-271. doi: https://doi.org/10.1016/0016-5085(92)91809-i</mixed-citation></citation-alternatives></ref><ref id="cit16"><label>16</label><citation-alternatives><mixed-citation xml:lang="ru">Flynn SP White HS. Regulation of glucose and insulin release following acute and repeated treatment with the synthetic galanin analog NAX-5055. Neuropeptides. 2015;50:35-42. doi: https://doi.org/10.1016Zj.npep.2015.01.001</mixed-citation><mixed-citation xml:lang="en">Flynn SP White HS. Regulation of glucose and insulin release following acute and repeated treatment with the synthetic galanin analog NAX-5055. Neuropeptides. 2015;50:35-42. doi: https://doi.org/10.1016Zj.npep.2015.01.001</mixed-citation></citation-alternatives></ref><ref id="cit17"><label>17</label><citation-alternatives><mixed-citation xml:lang="ru">Manabe T, Okada Y, Sawai H, et al. Effect of galanin on plasma glucose, insulin and pancreatic glucagon in dogs. J Int Med Res. 2003;31(2):126-132. doi: https://doi.org/10.1177/147323000303100209</mixed-citation><mixed-citation xml:lang="en">Manabe T, Okada Y, Sawai H, et al. Effect of galanin on plasma glucose, insulin and pancreatic glucagon in dogs. J Int Med Res. 2003;31(2):126-132. doi: https://doi.org/10.1177/147323000303100209</mixed-citation></citation-alternatives></ref><ref id="cit18"><label>18</label><citation-alternatives><mixed-citation xml:lang="ru">Bauer FE, Zintel A, Kenny MJ, et al. Inhibitory effect of galanin on postprandial gastrointestinal motility and gut hormone release in humans. Gastroenterology. 1989;97(2):260-264. doi: https://doi.org/10.1016/0016-5085(89)90059-0</mixed-citation><mixed-citation xml:lang="en">Bauer FE, Zintel A, Kenny MJ, et al. Inhibitory effect of galanin on postprandial gastrointestinal motility and gut hormone release in humans. Gastroenterology. 1989;97(2):260-264. doi: https://doi.org/10.1016/0016-5085(89)90059-0</mixed-citation></citation-alternatives></ref><ref id="cit19"><label>19</label><citation-alternatives><mixed-citation xml:lang="ru">Gilbey SG, Stephenson J, O’Halloran DJ, et al. High-dose porcine galanin infusion and effect on intravenous glucose tolerance in humans. Diabetes. 1989;38(9):1114-1116. doi: https://doi.org/10.2337/diab.38.9.1114</mixed-citation><mixed-citation xml:lang="en">Gilbey SG, Stephenson J, O’Halloran DJ, et al. High-dose porcine galanin infusion and effect on intravenous glucose tolerance in humans. Diabetes. 1989;38(9):1114-1116. doi: https://doi.org/10.2337/diab.38.9.1114</mixed-citation></citation-alternatives></ref><ref id="cit20"><label>20</label><citation-alternatives><mixed-citation xml:lang="ru">Ahren B. Effects of galanin and calcitonin gene-related peptide on insulin and glucagon secretion in man. Acta Endocrinol (Copenh). 1990;123:591-597.</mixed-citation><mixed-citation xml:lang="en">Ahren B. Effects of galanin and calcitonin gene-related peptide on insulin and glucagon secretion in man. Acta Endocrinol (Copenh). 1990;123:591-597.</mixed-citation></citation-alternatives></ref><ref id="cit21"><label>21</label><citation-alternatives><mixed-citation xml:lang="ru">Smith KE, Walker MW, Artymyshyn R, et al. Cloned human and rat galanin GALR3 receptors. Pharmacology and activation of G-protein inwardly rectifying K+ channels. J Biol Chem. 1998;273(36):23321-23326. doi: https://doi.org/10.1074/jbc.273.36.23321</mixed-citation><mixed-citation xml:lang="en">Smith KE, Walker MW, Artymyshyn R, et al. Cloned human and rat galanin GALR3 receptors. Pharmacology and activation of G-protein inwardly rectifying K+ channels. J Biol Chem. 1998;273(36):23321-23326. doi: https://doi.org/10.1074/jbc.273.36.23321</mixed-citation></citation-alternatives></ref><ref id="cit22"><label>22</label><citation-alternatives><mixed-citation xml:lang="ru">Wang Y, Park S, Bajpayee NS, et al. Augmented glucose-induced insulin release in mice lacking G(o2), but not G(o1) or G(i) proteins. Proc Natl Acad Sci U S A. 2011;108(4):1693-1698. doi: https://doi.org/10.1073/pnas.1018903108</mixed-citation><mixed-citation xml:lang="en">Wang Y, Park S, Bajpayee NS, et al. Augmented glucose-induced insulin release in mice lacking G(o2), but not G(o1) or G(i) proteins. Proc Natl Acad Sci U S A. 2011;108(4):1693-1698. doi: https://doi.org/10.1073/pnas.1018903108</mixed-citation></citation-alternatives></ref><ref id="cit23"><label>23</label><citation-alternatives><mixed-citation xml:lang="ru">Tang G, Wang Y, Park S, et al. Go2 G protein mediates galanin inhibitory effects on insulin release from pancreatic в cells. Proc Natl Acad Sci U S A. 2012;14;109(7):2636-2641. doi: https://doi.org/10.1073/pnas.1200100109</mixed-citation><mixed-citation xml:lang="en">Tang G, Wang Y, Park S, et al. Go2 G protein mediates galanin inhibitory effects on insulin release from pancreatic в cells. Proc Natl Acad Sci U S A. 2012;14;109(7):2636-2641. doi: https://doi.org/10.1073/pnas.1200100109</mixed-citation></citation-alternatives></ref><ref id="cit24"><label>24</label><citation-alternatives><mixed-citation xml:lang="ru">Jaldin-Fincati JR, Pavarotti M, Frendo-Cumbo S, et al. Update on GLUT4 vesicle traffic: a cornerstone of insulin action. Trends Endocrinol Metab. 2017;28(8):597-611. doi: https://doi.org/10.1016/j.tem.2017.05.002</mixed-citation><mixed-citation xml:lang="en">Jaldin-Fincati JR, Pavarotti M, Frendo-Cumbo S, et al. Update on GLUT4 vesicle traffic: a cornerstone of insulin action. Trends Endocrinol Metab. 2017;28(8):597-611. doi: https://doi.org/10.1016/j.tem.2017.05.002</mixed-citation></citation-alternatives></ref><ref id="cit25"><label>25</label><citation-alternatives><mixed-citation xml:lang="ru">Alam F, Islam MA, Khalil MI, Gan SH. Metabolic control of type 2 diabetes by targeting the glut4 glucose transporter: intervention approaches. Curr Pharm Des. 2016;22(20):3034-3049. doi: https://doi.org/10.2174/1381612822666160307145801</mixed-citation><mixed-citation xml:lang="en">Alam F, Islam MA, Khalil MI, Gan SH. Metabolic control of type 2 diabetes by targeting the glut4 glucose transporter: intervention approaches. Curr Pharm Des. 2016;22(20):3034-3049. doi: https://doi.org/10.2174/1381612822666160307145801</mixed-citation></citation-alternatives></ref><ref id="cit26"><label>26</label><citation-alternatives><mixed-citation xml:lang="ru">Leto D, Saltiel AR. Regulation of glucose transport by insulin: traffic control of GLUT4. Nat Rev Mol Cell Biol. 2012;13(6):383-396. doi: https://doi.org/10.1038/nrm3351</mixed-citation><mixed-citation xml:lang="en">Leto D, Saltiel AR. Regulation of glucose transport by insulin: traffic control of GLUT4. Nat Rev Mol Cell Biol. 2012;13(6):383-396. doi: https://doi.org/10.1038/nrm3351</mixed-citation></citation-alternatives></ref><ref id="cit27"><label>27</label><citation-alternatives><mixed-citation xml:lang="ru">Fang P Shi M, Guo L, et al. Effect of endogenous galanin on glucose transporter 4 expression in cardiac muscle of type 2 diabetic rats. Peptides. 2014;62:159-163. doi: https://doi.org/10.1016/j.peptides.2014.10.001</mixed-citation><mixed-citation xml:lang="en">Fang P Shi M, Guo L, et al. Effect of endogenous galanin on glucose transporter 4 expression in cardiac muscle of type 2 diabetic rats. Peptides. 2014;62:159-163. doi: https://doi.org/10.1016/j.peptides.2014.10.001</mixed-citation></citation-alternatives></ref><ref id="cit28"><label>28</label><citation-alternatives><mixed-citation xml:lang="ru">Fang P Shi M, Zhu Y, et al. Central injection of GalR1 agonist M617 facilitates GLUT4 expression in cardiac muscle of type 2 diabetic rats. Exp Gerontol. 2015;65:85-89.</mixed-citation><mixed-citation xml:lang="en">Fang P Shi M, Zhu Y, et al. Central injection of GalR1 agonist M617 facilitates GLUT4 expression in cardiac muscle of type 2 diabetic rats. Exp Gerontol. 2015;65:85-89.</mixed-citation></citation-alternatives></ref><ref id="cit29"><label>29</label><citation-alternatives><mixed-citation xml:lang="ru">Fang P Zhang L, Yu M, et al. Activiatedgalanin receptor 2 attenuates insulin resistance in skeletal muscle of obese mice. Peptides. 2018;99:92-98. doi: https://doi.org/10.1016/j.peptides.2017.11.018</mixed-citation><mixed-citation xml:lang="en">Fang P Zhang L, Yu M, et al. Activiatedgalanin receptor 2 attenuates insulin resistance in skeletal muscle of obese mice. Peptides. 2018;99:92-98. doi: https://doi.org/10.1016/j.peptides.2017.11.018</mixed-citation></citation-alternatives></ref><ref id="cit30"><label>30</label><citation-alternatives><mixed-citation xml:lang="ru">Yun R, Dourmashkin JT, Hill J, et al. PVN galanin increases fat storage and promotes obesity by causing muscle to utilize carbohydrate more than fat. Peptides. 2005;26(1 1):2265-2273. doi: https://doi.org/10.1016/j.peptides.2005.04.005</mixed-citation><mixed-citation xml:lang="en">Yun R, Dourmashkin JT, Hill J, et al. PVN galanin increases fat storage and promotes obesity by causing muscle to utilize carbohydrate more than fat. Peptides. 2005;26(1 1):2265-2273. doi: https://doi.org/10.1016/j.peptides.2005.04.005</mixed-citation></citation-alternatives></ref><ref id="cit31"><label>31</label><citation-alternatives><mixed-citation xml:lang="ru">Fang P He B, Yu M, et al. Central galanin receptor 2 mediates galanin action to promote systemic glucose metabolism of type 2 diabetic rats. Biochem Pharmacol. 2018;156:241-247. doi: https://doi.org/10.1016/jbcp.2018.08.036</mixed-citation><mixed-citation xml:lang="en">Fang P He B, Yu M, et al. Central galanin receptor 2 mediates galanin action to promote systemic glucose metabolism of type 2 diabetic rats. Biochem Pharmacol. 2018;156:241-247. doi: https://doi.org/10.1016/jbcp.2018.08.036</mixed-citation></citation-alternatives></ref><ref id="cit32"><label>32</label><citation-alternatives><mixed-citation xml:lang="ru">Abot A, Lucas A, Bautzova T, et al. Galanin enhances systemic glucose metabolism through enteric Nitric Oxide Synthase-expressed neurons. Mol Metab. 2018;10:100-108. doi: https://doi.org/10.1016/j.molmet.2018.01.020</mixed-citation><mixed-citation xml:lang="en">Abot A, Lucas A, Bautzova T, et al. Galanin enhances systemic glucose metabolism through enteric Nitric Oxide Synthase-expressed neurons. Mol Metab. 2018;10:100-108. doi: https://doi.org/10.1016/j.molmet.2018.01.020</mixed-citation></citation-alternatives></ref><ref id="cit33"><label>33</label><citation-alternatives><mixed-citation xml:lang="ru">Khan AH, Pessin JE. Insulin regulation of glucose uptake: a complex interplay of intracellular signalling pathways. Diabetologia. 2002;45(11):1475-1483. doi: https://doi.org/10.1007/s00125-002-0974-7</mixed-citation><mixed-citation xml:lang="en">Khan AH, Pessin JE. Insulin regulation of glucose uptake: a complex interplay of intracellular signalling pathways. Diabetologia. 2002;45(11):1475-1483. doi: https://doi.org/10.1007/s00125-002-0974-7</mixed-citation></citation-alternatives></ref><ref id="cit34"><label>34</label><citation-alternatives><mixed-citation xml:lang="ru">Denley A, Carroll JM, Brierley GV, et al. Differential activation of insulin receptor substrates 1 and 2 by insulin-likegrowth factor-activated insulin receptors. Jr Mol Cell Biol. 2007;27(10):3569-3577. doi: https://doi.org/10.1128/MCB.01447-06</mixed-citation><mixed-citation xml:lang="en">Denley A, Carroll JM, Brierley GV, et al. Differential activation of insulin receptor substrates 1 and 2 by insulin-likegrowth factor-activated insulin receptors. Jr Mol Cell Biol. 2007;27(10):3569-3577. doi: https://doi.org/10.1128/MCB.01447-06</mixed-citation></citation-alternatives></ref><ref id="cit35"><label>35</label><citation-alternatives><mixed-citation xml:lang="ru">Tonks KT, Ng Y, Miller S, et al. Impaired Akt phosphorylation in insulin-resistant human muscle is accompanied by selective and heterogeneous downstream defects. Diabetologia. 2013;56(4):875-885. doi: https://doi.org/10.1007/s00125-012-2811-y</mixed-citation><mixed-citation xml:lang="en">Tonks KT, Ng Y, Miller S, et al. Impaired Akt phosphorylation in insulin-resistant human muscle is accompanied by selective and heterogeneous downstream defects. Diabetologia. 2013;56(4):875-885. doi: https://doi.org/10.1007/s00125-012-2811-y</mixed-citation></citation-alternatives></ref><ref id="cit36"><label>36</label><citation-alternatives><mixed-citation xml:lang="ru">Thong FS, Bilan PJ, Klip A. The Rab GTPase-activating protein AS160integrates Akt, protein kinase C, and AMP-activated protein kinase signals regulatingGLUT4 traffic. Diabetes. 2007;56(2): 414-423. doi: https://doi.org/10.2337/db06-0900</mixed-citation><mixed-citation xml:lang="en">Thong FS, Bilan PJ, Klip A. The Rab GTPase-activating protein AS160integrates Akt, protein kinase C, and AMP-activated protein kinase signals regulatingGLUT4 traffic. Diabetes. 2007;56(2): 414-423. doi: https://doi.org/10.2337/db06-0900</mixed-citation></citation-alternatives></ref><ref id="cit37"><label>37</label><citation-alternatives><mixed-citation xml:lang="ru">Rashid AJ, O’Dowd BF, Verma V, George SR. Neuronal Gq/11-coupled dopamine receptors: an uncharted role for dopamine. Trends PharmacolSci. 2007;28(1 1):551-555. doi: https://doi.org/10.1016/jtips.2007.10.001</mixed-citation><mixed-citation xml:lang="en">Rashid AJ, O’Dowd BF, Verma V, George SR. Neuronal Gq/11-coupled dopamine receptors: an uncharted role for dopamine. Trends PharmacolSci. 2007;28(1 1):551-555. doi: https://doi.org/10.1016/jtips.2007.10.001</mixed-citation></citation-alternatives></ref><ref id="cit38"><label>38</label><citation-alternatives><mixed-citation xml:lang="ru">Fang P, Yu M, He B, et al. Central injection of GALR1 agonist M617 attenuates diabetic rat skeletal muscle insulin resistance through the Akt/AS160/GLUT4 pathway. Mech Ageing Dev. 2017;162:122-128. doi: https://doi.org/10.1016/j.mad.2016.03.013</mixed-citation><mixed-citation xml:lang="en">Fang P, Yu M, He B, et al. Central injection of GALR1 agonist M617 attenuates diabetic rat skeletal muscle insulin resistance through the Akt/AS160/GLUT4 pathway. Mech Ageing Dev. 2017;162:122-128. doi: https://doi.org/10.1016/j.mad.2016.03.013</mixed-citation></citation-alternatives></ref><ref id="cit39"><label>39</label><citation-alternatives><mixed-citation xml:lang="ru">Bu L, Yao Q, Liu Z, et al. Combined galanin with insulin improves insulin sensitivity of diabetic rat muscles. J Endocrinol. 2014;221(1):157-165. doi: https://doi.org/10.1530/JOE-13-0444</mixed-citation><mixed-citation xml:lang="en">Bu L, Yao Q, Liu Z, et al. Combined galanin with insulin improves insulin sensitivity of diabetic rat muscles. J Endocrinol. 2014;221(1):157-165. doi: https://doi.org/10.1530/JOE-13-0444</mixed-citation></citation-alternatives></ref><ref id="cit40"><label>40</label><citation-alternatives><mixed-citation xml:lang="ru">Mirza AZ, Althagafi II, Shamshad H. Role of PPAR receptor in different diseases and their ligands: Physiological importance and clinical implications. Eur J Med Chem. 2019;15:166:502-513. doi: https://doi.org/10.1016/j.ejmech.2019.01.067</mixed-citation><mixed-citation xml:lang="en">Mirza AZ, Althagafi II, Shamshad H. Role of PPAR receptor in different diseases and their ligands: Physiological importance and clinical implications. Eur J Med Chem. 2019;15:166:502-513. doi: https://doi.org/10.1016/j.ejmech.2019.01.067</mixed-citation></citation-alternatives></ref><ref id="cit41"><label>41</label><citation-alternatives><mixed-citation xml:lang="ru">Kersten S, Desvergne B, Wahli W, Roles of PPARs in health and disease. Nature. 2000;25;405(6785):421-424. doi: https://doi.org/10.1038/35013000</mixed-citation><mixed-citation xml:lang="en">Kersten S, Desvergne B, Wahli W, Roles of PPARs in health and disease. Nature. 2000;25;405(6785):421-424. doi: https://doi.org/10.1038/35013000</mixed-citation></citation-alternatives></ref><ref id="cit42"><label>42</label><citation-alternatives><mixed-citation xml:lang="ru">Hsueh WA, Law R. The central role of fat and effect of peroxisome proliferator-activated receptorgamma on progression of insulin resistance and cardiovascular disease. Am J Cardiol. 2003;92(4A):3J-9J. doi: https://doi.org/10.1016/s0002-9149(03)00610-6</mixed-citation><mixed-citation xml:lang="en">Hsueh WA, Law R. The central role of fat and effect of peroxisome proliferator-activated receptorgamma on progression of insulin resistance and cardiovascular disease. Am J Cardiol. 2003;92(4A):3J-9J. doi: https://doi.org/10.1016/s0002-9149(03)00610-6</mixed-citation></citation-alternatives></ref><ref id="cit43"><label>43</label><citation-alternatives><mixed-citation xml:lang="ru">Kim A, Park T. Diet-induced obesity regulates the galanin-mediated signaling cascade in the adipose tissue of mice. Mol Nutr Food Res. 2010;54(9):1361-1370. doi: https://doi.org/10.1002/mnfr.200900317</mixed-citation><mixed-citation xml:lang="en">Kim A, Park T. Diet-induced obesity regulates the galanin-mediated signaling cascade in the adipose tissue of mice. Mol Nutr Food Res. 2010;54(9):1361-1370. doi: https://doi.org/10.1002/mnfr.200900317</mixed-citation></citation-alternatives></ref><ref id="cit44"><label>44</label><citation-alternatives><mixed-citation xml:lang="ru">Celi F, Bini V, Papi F, et al. Circulating acylated and total ghrelin and galanin inchildren with insulin-treated type 1 diabetes: relationship to insulin therapy, metaboliccontrol and pubertal development. Clin Endocrinol (Oxf). 2005;63(2):139-145. doi: https://doi.org/10.1111/j.1365-2265.2005.02313.x</mixed-citation><mixed-citation xml:lang="en">Celi F, Bini V, Papi F, et al. Circulating acylated and total ghrelin and galanin inchildren with insulin-treated type 1 diabetes: relationship to insulin therapy, metaboliccontrol and pubertal development. Clin Endocrinol (Oxf). 2005;63(2):139-145. doi: https://doi.org/10.1111/j.1365-2265.2005.02313.x</mixed-citation></citation-alternatives></ref><ref id="cit45"><label>45</label><citation-alternatives><mixed-citation xml:lang="ru">Alotibi MN, Alnoury AM, Alhozali AM. Serum nesfatin-1 and galanin concentrations in the adult with metabolic syndrome. Relationships to insulin resistance and obesity. Saudi Med J. 2019;40(1):19-25. doi: https://doi.org/10.15537/smj.2019.L22825</mixed-citation><mixed-citation xml:lang="en">Alotibi MN, Alnoury AM, Alhozali AM. Serum nesfatin-1 and galanin concentrations in the adult with metabolic syndrome. Relationships to insulin resistance and obesity. Saudi Med J. 2019;40(1):19-25. doi: https://doi.org/10.15537/smj.2019.L22825</mixed-citation></citation-alternatives></ref><ref id="cit46"><label>46</label><citation-alternatives><mixed-citation xml:lang="ru">Acar S, Paketji A, Kume T, et al. Positive correlation of galanin with insulin resistance and triglyceride levels in obese children. Turk J Med Sci. 2018;48(3):560-568. doi: https://doi.org/10.3906/sag-1710-68</mixed-citation><mixed-citation xml:lang="en">Acar S, Paketji A, Kume T, et al. Positive correlation of galanin with insulin resistance and triglyceride levels in obese children. Turk J Med Sci. 2018;48(3):560-568. doi: https://doi.org/10.3906/sag-1710-68</mixed-citation></citation-alternatives></ref><ref id="cit47"><label>47</label><citation-alternatives><mixed-citation xml:lang="ru">Fang P, Shi M, Zhu Y, et al. Type 2 diabetes mellitus as a disorder of galanin resistance. Exp Gerontol. 2016;73:72-77. doi: https://doi.org/10.1016/j.exger.2015.11.007</mixed-citation><mixed-citation xml:lang="en">Fang P, Shi M, Zhu Y, et al. Type 2 diabetes mellitus as a disorder of galanin resistance. Exp Gerontol. 2016;73:72-77. doi: https://doi.org/10.1016/j.exger.2015.11.007</mixed-citation></citation-alternatives></ref><ref id="cit48"><label>48</label><citation-alternatives><mixed-citation xml:lang="ru">Weber C. Neurogastroenterology: improving glucose tolerance via the gut-brain axis. Nat Rev Gastroenterol Hepatol. 2016;13(1):4. doi: https://doi.org/10.1038/nrgastro.2015.204</mixed-citation><mixed-citation xml:lang="en">Weber C. Neurogastroenterology: improving glucose tolerance via the gut-brain axis. Nat Rev Gastroenterol Hepatol. 2016;13(1):4. doi: https://doi.org/10.1038/nrgastro.2015.204</mixed-citation></citation-alternatives></ref><ref id="cit49"><label>49</label><citation-alternatives><mixed-citation xml:lang="ru">Fournel A, Drougard A, Duparc T, et al. Apelin targets gut contraction to control glucose metabolism via the brain. Gut. 2017;66(2):258-269. doi: https://doi.org/10.1136/gutjnl-2015-310230</mixed-citation><mixed-citation xml:lang="en">Fournel A, Drougard A, Duparc T, et al. Apelin targets gut contraction to control glucose metabolism via the brain. Gut. 2017;66(2):258-269. doi: https://doi.org/10.1136/gutjnl-2015-310230</mixed-citation></citation-alternatives></ref><ref id="cit50"><label>50</label><citation-alternatives><mixed-citation xml:lang="ru">Fournel A, Marlin A, Abot A, et al. Glucosensing in the gastrointestinal tract: impact on glucose metabolism. Am J Physiol Gastrointest Liver Physiol. 2016;310(9):G645-G658. doi: https://doi.org/10.1152/ajpgi.00015.2016</mixed-citation><mixed-citation xml:lang="en">Fournel A, Marlin A, Abot A, et al. Glucosensing in the gastrointestinal tract: impact on glucose metabolism. Am J Physiol Gastrointest Liver Physiol. 2016;310(9):G645-G658. doi: https://doi.org/10.1152/ajpgi.00015.2016</mixed-citation></citation-alternatives></ref><ref id="cit51"><label>51</label><citation-alternatives><mixed-citation xml:lang="ru">Chandrasekharan B, Srinivasan S. Diabetes and the enteric nervous system. Neurogastroenterol Motil. 2007;19(12):951-960. doi: https://doi.org/10.1111/j.1365-2982.2007.01023.x</mixed-citation><mixed-citation xml:lang="en">Chandrasekharan B, Srinivasan S. Diabetes and the enteric nervous system. Neurogastroenterol Motil. 2007;19(12):951-960. doi: https://doi.org/10.1111/j.1365-2982.2007.01023.x</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>
