<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE article PUBLIC "-//NLM//DTD JATS (Z39.96) Journal Publishing DTD v1.3 20210610//EN" "JATS-journalpublishing1-3.dtd">
<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">ophthalmology</journal-id><journal-title-group><journal-title xml:lang="ru">Офтальмология</journal-title><trans-title-group xml:lang="en"><trans-title>Ophthalmology in Russia</trans-title></trans-title-group></journal-title-group><issn pub-type="ppub">1816-5095</issn><issn pub-type="epub">2500-0845</issn><publisher><publisher-name>Ophthalmology</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="doi">10.18008/1816-5095-2020-3-330-335</article-id><article-id custom-type="elpub" pub-id-type="custom">ophthalmology-1271</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>REVIEWS</subject></subj-group></article-categories><title-group><article-title>Сиртуины и их роль в старении органа зрения. Обзор литературы</article-title><trans-title-group xml:lang="en"><trans-title>Sirtuins and Their Role in the Aging Eye (Review)</trans-title></trans-title-group></title-group><contrib-group><contrib contrib-type="author" corresp="yes"><contrib-id contrib-id-type="orcid">https://orcid.org/0000-0002-5899-2714</contrib-id><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Мошетова</surname><given-names>Л. К.</given-names></name><name name-style="western" xml:lang="en"><surname>Moshetova</surname><given-names>L. K.</given-names></name></name-alternatives><bio xml:lang="ru"><p>доктор медицинских наук, профессор, академик РАН, заведующий кафедрой офтальмологии,</p><p>ул. Баррикадная, 2/1, Москва, 125993</p></bio><bio xml:lang="en"><p>MD, Professor, Academician of the Russian Academy of Sciences, Head of Department of Eye Diseases,</p><p>Barrikadnaja str., 2/1, Moscow 123995</p></bio><xref ref-type="aff" rid="aff-1"/></contrib><contrib contrib-type="author" corresp="yes"><contrib-id contrib-id-type="orcid">https://orcid.org/0000-0002-6156-6126</contrib-id><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Абрамова</surname><given-names>О. И.</given-names></name><name name-style="western" xml:lang="en"><surname>Abramova</surname><given-names>O. I.</given-names></name></name-alternatives><bio xml:lang="ru"><p>аспирант кафедры офтальмологии,</p><p>ул. Баррикадная, 2/1, Москва, 125993</p></bio><bio xml:lang="en"><p>postgraduate of Department of Eye Diseases,</p><p>Barrikadnaja str., 2/1, Moscow 123995</p></bio><email xlink:type="simple">abramovao2019@mail.ru</email><xref ref-type="aff" rid="aff-1"/></contrib><contrib contrib-type="author" corresp="yes"><contrib-id contrib-id-type="orcid">https://orcid.org/0000-0002-4989-7467</contrib-id><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Туркина</surname><given-names>К. И.</given-names></name><name name-style="western" xml:lang="en"><surname>Turkina</surname><given-names>K. I.</given-names></name></name-alternatives><bio xml:lang="ru"><p>кандидат медицинских наук, доцент кафедры офтальмологии,</p><p>ул. Баррикадная, 2/1, Москва, 125993</p></bio><bio xml:lang="en"><p>PhD, Assistant Professor of Department of Eye Diseases,</p><p>Barrikadnaja str., 2/1, Moscow 123995</p></bio><xref ref-type="aff" rid="aff-1"/></contrib><contrib contrib-type="author" corresp="yes"><contrib-id contrib-id-type="orcid">https://orcid.org/0000-0002-9383-8026</contrib-id><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Нурбеков</surname><given-names>М. К.</given-names></name><name name-style="western" xml:lang="en"><surname>Nurbekov</surname><given-names>M. K.</given-names></name></name-alternatives><bio xml:lang="ru"><p>кандидат биологических наук, ведущий научный сотрудник,</p><p>ул. Балтийская, 8, Москва, 125315</p></bio><bio xml:lang="en"><p>Candidate of Biological Sciences, Senior Research Officer,</p><p>Baltiyskaya str., 8, Moscow, 125315</p></bio><xref ref-type="aff" rid="aff-2"/></contrib><contrib contrib-type="author" corresp="yes"><contrib-id contrib-id-type="orcid">https://orcid.org/0000-0002-2067-0971</contrib-id><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Дмитренко</surname><given-names>О. П.</given-names></name><name name-style="western" xml:lang="en"><surname>Dmitrenko</surname><given-names>O. P.</given-names></name></name-alternatives><bio xml:lang="ru"><p>младший научный сотрудник,</p><p>ул. Балтийская, 8, Москва, 125315</p></bio><bio xml:lang="en"><p>Research Assistant,</p><p>Baltiyskaya str., 8, Moscow, 125315</p></bio><xref ref-type="aff" rid="aff-2"/></contrib><contrib contrib-type="author" corresp="yes"><contrib-id contrib-id-type="orcid">https://orcid.org/0000-0003-2014-2535</contrib-id><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Сабурина</surname><given-names>И. Н.</given-names></name><name name-style="western" xml:lang="en"><surname>Saburina</surname><given-names>I. N.</given-names></name></name-alternatives><bio xml:lang="ru"><p>доктор биологических наук, профессор,</p><p>2-й Боткинский проезд, 7, корп. 2, Москва, 125284;</p><p>ул. Балтийская, 8, Москва, 125315</p></bio><bio xml:lang="en"><p>Dr. of Biological Sciences, Professor,</p><p>2nd Botkinsky passage, 7/2, Moscow 125284;</p><p>Baltiyskaya str., 8, Moscow, 125315</p></bio><xref ref-type="aff" rid="aff-3"/></contrib><contrib contrib-type="author" corresp="yes"><contrib-id contrib-id-type="orcid">https://orcid.org/0000-0002-8913-822X</contrib-id><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Кочергин</surname><given-names>С. А.</given-names></name><name name-style="western" xml:lang="en"><surname>Kochergin</surname><given-names>S. A.</given-names></name></name-alternatives><bio xml:lang="ru"><p>доктор медицинских наук, профессор кафедры офтальмологии,</p><p>ул. Баррикадная, 2/1, Москва, 125993</p></bio><bio xml:lang="en"><p>MD, Professor of Department of Eye Diseases,</p><p>Barrikadnaja str., 2/1, Moscow 123995</p></bio><xref ref-type="aff" rid="aff-1"/></contrib></contrib-group><aff-alternatives id="aff-1"><aff xml:lang="ru"><institution>ФГБОУ ДПО «Российская медицинская академия непрерывного профессионального образования»&#13;
Министерства здравоохранения Российской Федерации</institution><country>Россия</country></aff><aff xml:lang="en"><institution>Russian Medical Academy of Continuous Professional Education</institution><country>Russian Federation</country></aff></aff-alternatives><aff-alternatives id="aff-2"><aff xml:lang="ru"><institution>ФГБОУ «Научно-исследовательский институт общей патологии и патофизиологии»</institution><country>Россия</country></aff><aff xml:lang="en"><institution>The Institute of General Pathology and Pathophysiology</institution><country>Russian Federation</country></aff></aff-alternatives><aff-alternatives id="aff-3"><aff xml:lang="ru"><institution>Научно-исследовательский институт молекулярной и персонализированной медицины&#13;
ФГБОУ ДПО «Российская медицинская академия непрерывного профессионального образования» Министерства здравоохранения Российской Федерации;&#13;
ФГБОУ «Научно-исследовательский институт общей патологии и патофизиологии»</institution><country>Россия</country></aff><aff xml:lang="en"><institution>ar and Personalized Medicine of Russian Medical Academy of Continuous Professional Education;&#13;
The Institute of General Pathology and Pathophysiology</institution><country>Russian Federation</country></aff></aff-alternatives><pub-date pub-type="collection"><year>2020</year></pub-date><pub-date pub-type="epub"><day>22</day><month>09</month><year>2020</year></pub-date><volume>17</volume><issue>3</issue><fpage>330</fpage><lpage>335</lpage><permissions><copyright-statement>Copyright &amp;#x00A9; Мошетова Л.К., Абрамова О.И., Туркина К.И., Нурбеков М.К., Дмитренко О.П., Сабурина И.Н., Кочергин С.А., 2020</copyright-statement><copyright-year>2020</copyright-year><copyright-holder xml:lang="ru">Мошетова Л.К., Абрамова О.И., Туркина К.И., Нурбеков М.К., Дмитренко О.П., Сабурина И.Н., Кочергин С.А.</copyright-holder><copyright-holder xml:lang="en">Moshetova L.K., Abramova O.I., Turkina K.I., Nurbekov M.K., Dmitrenko O.P., Saburina I.N., Kochergin S.A.</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.ophthalmojournal.com/opht/article/view/1271">https://www.ophthalmojournal.com/opht/article/view/1271</self-uri><abstract><p>Нарушение зрения у пожилых людей — это серьезная проблема, которая существенно влияет на качество жизни миллионов людей во всем мире. Масштабы этой проблемы становятся все более очевидными по мере старения населения и увеличения числа пожилых людей. Возрастная дегенерация желтого пятна (ВМД) является третьей по значимости причиной слепоты во всем мире и основной причиной потери зрения у лиц старше 60 лет. Ожидается, что к 2040 году ВМД затронет около 288 миллионов человек. ВМД является многофакторным заболеванием, имеющим прогрессирующий характер течения. Возникающие дистрофические изменения сетчатки не может обратить вспять ни один из ныне существующих методов лечения. Много исследований и усилий уже было приложено для выявления различных биомаркеров прогнозирования заболеваемости, лиц, подверженных риску, патогенетических механизмов данного заболевания, а также для поиска действенных способов лечения и профилактики. Основой патогенетических изменений, которые возникают при ВМД, является старение. Биомаркеры старения — это измеряемые показатели жизнедеятельности, которые качественно и количественно изменяются в зависимости от возраста организма. Метилирование ДНК — молекулярный механизм, являющийся потенциальным биомаркером старения. Сиртуины опосредованно участвуют в данном процессе, регулируя активность фермента DNMT1. В статье рассматриваются современные знания о механизмах, лежащих в основе действия сиртуинов (Sirtuins/SIRT), с акцентом на SIRT1. Анализ влияния на звенья патофизиологической цепочки действия сиртуинов может сказаться на предотвращении и лечении патологических изменений глаза, связанных с ВМД. В статье приведены источники литературы, содержащие результаты исследований по влиянию SIRT1 как маркера старения тканей организма. Учитывая эти данные, можно сказать, что SIRT1 служит привлекательным кандидатом для разработки терапевтических стратегий по предотвращению раннего старения тканей глаза, в частности такого возраст-ассоциированного заболевания, как возрастная макулярная дегенерация. Воздействие на генетические механизмы возникновения данного заболевания является перспективным направлением в его лечении.</p></abstract><trans-abstract xml:lang="en"><p>Visual impairment in elderly people is a serious problem that significantly affects the quality of life of millions people around the world. The magnitude of this problem is becoming increasingly apparent as the population ages and the number of older people increases. Age-related macular degeneration (AMD) is the third leading cause of blindness worldwide and the main cause of vision loss in people over 60 years. It is expected that AMD will affect about 288 million people by 2040. AMD is a multifactorial disease with a progressive course. The arised dystrophic changes in the retina cannot be reversed by any of the known treatment methods. A lot of research and effort has already been invested in identifying various biomarkers for predicting the incidence rate, identifying people at risk, finding out the pathogenetic mechanisms of this disease, and finding effective methods of treatment and prevention.</p><p>Aging is the basis of pathological changes that occur during AMD. Aging biomarkers are measurable vital signs that qualitatively and quantitatively change with the age of the body. DNA methylation is a molecular mechanism that is a potential biomarker of aging. Sirtuins indirectly participate in this process, regulating the activity of the DNMT1 enzyme. The article discusses current knowledge of the mechanisms underlying the action of sirtuins (Sirtuins / SIRT), with an emphasis on SIRT1. Analysis of the pathophysiological action of sirtuins can affect the prevention and treatment of pathological eye changes associated with AMD. The article provides literature sources containing the results of studies of the effect of SIRT1 as a marker of aging in body tissues. SIRT1 is an attractive candidate for developing therapeutic strategies preventing early eye aging, in particular, age-associated diseases such as AMD The impact on the genetic mechanisms of this disease is a promising direction in treatment.</p></trans-abstract><kwd-group xml:lang="ru"><kwd>сиртуины</kwd><kwd>гены старения</kwd><kwd>возрастная макулярная дегенерация</kwd><kwd>SIRT1</kwd><kwd>возраст-ассоциированные заболевания</kwd></kwd-group><kwd-group xml:lang="en"><kwd>sirtuins</kwd><kwd>aging genes</kwd><kwd>age-related macular degeneration</kwd><kwd>SIRT1</kwd><kwd>age associated diseases</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">Al-Zamil W.M., Yassin S.A. Recent developments in age-related macular degeneration: a review. Clin Interv Aging. 2017;12:1313–1330. DOI: 10.2147/CIA.S143508</mixed-citation><mixed-citation xml:lang="en">Al-Zamil W.M., Yassin S.A. Recent developments in age-related macular degeneration: a review. Clin Interv Aging. 2017;12:1313–1330. DOI: 10.2147/CIA.S143508</mixed-citation></citation-alternatives></ref><ref id="cit2"><label>2</label><citation-alternatives><mixed-citation xml:lang="ru">De Jong P.T.V.M. Elusive drusen and changing terminology of amd. Eye. 2018;32:904–914. DOI: 10.1038/eye.2017.298</mixed-citation><mixed-citation xml:lang="en">De Jong P.T.V.M. Elusive drusen and changing terminology of amd. Eye. 2018;32:904–914. DOI: 10.1038/eye.2017.298</mixed-citation></citation-alternatives></ref><ref id="cit3"><label>3</label><citation-alternatives><mixed-citation xml:lang="ru">Peng L., Yuan Z., Ling H., Fukasawa K., Robertson K., Olashaw N., Koomen J., Chen J., Lane W.S., Seto E. SIRT1 deacetylates the DNA methyltransferase 1 (DNMT1) protein and alters its activities. Mol. Cell. Biol. 2011;31:4720–4734. DOI: 10.1128/MCB.06147-11</mixed-citation><mixed-citation xml:lang="en">Peng L., Yuan Z., Ling H., Fukasawa K., Robertson K., Olashaw N., Koomen J., Chen  J., Lane W.S., Seto E. SIRT1 deacetylates the DNA methyltransferase 1 (DNMT1) protein and alters its activities. Mol. Cell. Biol. 2011;31:4720–4734. DOI: 10.1128/MCB.06147-11</mixed-citation></citation-alternatives></ref><ref id="cit4"><label>4</label><citation-alternatives><mixed-citation xml:lang="ru">Kang H., Oka S., Lee D.Y., Park J., Aponte A.M., Jung Y.S., Bitterman J., Zhai P., He Y., Kooshapur H Sirt1 carboxyl-domain is an ATP-repressible domain that is transferrable to other proteins. Nat. Commun. 2017;8:15560. DOI: 10.1038/ncomms15560</mixed-citation><mixed-citation xml:lang="en">Kang H., Oka S., Lee D.Y., Park J., Aponte A.M., Jung Y.S., Bitterman J., Zhai P., He Y., Kooshapur H Sirt1 carboxyl-domain is an ATP-repressible domain that is transferrable to other proteins. Nat. Commun. 2017;8:15560. DOI: 10.1038/ncomms15560</mixed-citation></citation-alternatives></ref><ref id="cit5"><label>5</label><citation-alternatives><mixed-citation xml:lang="ru">Morigi M., Perico L., Benigni A. Sirtuins in Renal Health and Disease. J Am Soc Nephrol. 2018;29(7):1799–1809. DOI: 10.1681/ASN.2017111218</mixed-citation><mixed-citation xml:lang="en">Morigi M., Perico L., Benigni A. Sirtuins in Renal Health and Disease. J Am Soc Nephrol. 2018;29(7):1799–1809. DOI: 10.1681/ASN.2017111218</mixed-citation></citation-alternatives></ref><ref id="cit6"><label>6</label><citation-alternatives><mixed-citation xml:lang="ru">Grabowska W., Sikora E., Bielak-Zmijewska A. Sirtuins, a promising target in slowing down the ageing process. Biogerontology. 2017;18(4):447–476. DOI: 10.1007/s10522-017-9685-9</mixed-citation><mixed-citation xml:lang="en">Grabowska W., Sikora E., Bielak-Zmijewska A. Sirtuins, a promising target in slowing down the ageing process. Biogerontology. 2017;18(4):447–476. DOI: 10.1007/s10522-017-9685-9</mixed-citation></citation-alternatives></ref><ref id="cit7"><label>7</label><citation-alternatives><mixed-citation xml:lang="ru">Frye R.A. Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins. Biochem Biophys Res Commun. 2000;273(2):793–798. DOI: 10.1006/bbrc.2000.3000</mixed-citation><mixed-citation xml:lang="en">Frye R.A. Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins.  Biochem Biophys Res Commun. 2000;273(2):793–798. DOI: 10.1006/bbrc.2000.3000</mixed-citation></citation-alternatives></ref><ref id="cit8"><label>8</label><citation-alternatives><mixed-citation xml:lang="ru">Houtkooper R.H., Pirinen E., Auwerx J. Sirtuins as regulators of metabolism and healthspan. Nat Rev Mol Cell Biol. 2012;13(4):225–238. DOI: 10.1038/nrm3293</mixed-citation><mixed-citation xml:lang="en">Houtkooper R.H., Pirinen E., Auwerx J. Sirtuins as regulators of metabolism and healthspan. Nat Rev Mol Cell Biol. 2012;13(4):225–238. DOI: 10.1038/nrm3293</mixed-citation></citation-alternatives></ref><ref id="cit9"><label>9</label><citation-alternatives><mixed-citation xml:lang="ru">Huang J.Y., Hirschey M.D., Shimazu T., Ho L., Verdin E. Mitochondrial sirtuins. Biochim Biophys Acta. 2010;1804(8):1645–1651B. DOI: 10.1016/j.bbapap.2009.12.021</mixed-citation><mixed-citation xml:lang="en">Huang J.Y., Hirschey M.D., Shimazu T., Ho L., Verdin E. Mitochondrial sirtuins. Biochim Biophys Acta. 2010;1804(8):1645–1651B. DOI: 10.1016/j.bbapap.2009.12.021</mixed-citation></citation-alternatives></ref><ref id="cit10"><label>10</label><citation-alternatives><mixed-citation xml:lang="ru">Kaeberlein M., McVey M., Guarente L. The SIR2/3/4 complex and SIR2 alone promote longevity in Saccharomyces cerevisiae by two different mechanisms. Genes Dev. 1999;13(19):2570–2580. DOI: 10.1101/gad.13.19.2570</mixed-citation><mixed-citation xml:lang="en">Kaeberlein M., McVey M., Guarente L. The SIR2/3/4 complex and SIR2 alone promote longevity in Saccharomyces cerevisiae by two different mechanisms. Genes Dev. 1999;13(19):2570–2580. DOI: 10.1101/gad.13.19.2570</mixed-citation></citation-alternatives></ref><ref id="cit11"><label>11</label><citation-alternatives><mixed-citation xml:lang="ru">Kanfi Y., Naiman S., Amir G. The sirtuin SIRT6 regulates lifespan in male mice. Nature. 2012;483(7388):218–221. DOI: 10.1038/nature10815</mixed-citation><mixed-citation xml:lang="en">Kanfi Y., Naiman S., Amir G. The sirtuin SIRT6 regulates lifespan in male mice. Nature. 2012;483(7388):218–221. DOI: 10.1038/nature10815</mixed-citation></citation-alternatives></ref><ref id="cit12"><label>12</label><citation-alternatives><mixed-citation xml:lang="ru">O’Callaghan C., Vassilopoulos A. Sirtuins at the crossroads of stemness, aging, and cancer. Aging Cell. 2017;16(6):1208–1218. DOI: 10.1111/acel.12685</mixed-citation><mixed-citation xml:lang="en">O’Callaghan C., Vassilopoulos A. Sirtuins at the crossroads of stemness, aging, and cancer. Aging Cell. 2017;16(6):1208–1218. DOI: 10.1111/acel.12685</mixed-citation></citation-alternatives></ref><ref id="cit13"><label>13</label><citation-alternatives><mixed-citation xml:lang="ru">Lee S.H., Lee J.H., Lee H.Y., Min K.J. Sirtuin signaling in cellular senescence and aging. BMB Rep. 2019;52(1):24–34. DOI: 10.5483/BMBRep.2019.52.1.290</mixed-citation><mixed-citation xml:lang="en">Lee S.H., Lee J.H., Lee H.Y., Min K.J. Sirtuin signaling in cellular senescence and aging. BMB Rep. 2019;52(1):24–34. DOI: 10.5483/BMBRep.2019.52.1.290</mixed-citation></citation-alternatives></ref><ref id="cit14"><label>14</label><citation-alternatives><mixed-citation xml:lang="ru">Ford E., Voit R., Liszt G., Magin C., Grummt I., Guarente L. Mammalian Sir2 homolog SIRT7 is an activator of RNA polymerase I transcription. Genes Dev. 2006;20(9):1075–1080. DOI: 10.1101/gad.1399706</mixed-citation><mixed-citation xml:lang="en">Ford E., Voit R., Liszt G., Magin C., Grummt I., Guarente L. Mammalian Sir2 homolog SIRT7 is an activator of RNA polymerase I transcription. Genes Dev. 2006;20(9):1075–1080. DOI: 10.1101/gad.1399706</mixed-citation></citation-alternatives></ref><ref id="cit15"><label>15</label><citation-alternatives><mixed-citation xml:lang="ru">Dryden S.C., Nahhas F.A., Nowak J.E., Goustin A.S., Tainsky M.A. Role for human SIRT2 NAD-dependent deacetylase activity in control of mitotic exit in the cell cycle. Mol Cell Biol. 2003;23(9):3173–3185. DOI: 10.1128/mcb.23.9.3173-3185.2003</mixed-citation><mixed-citation xml:lang="en">Dryden S.C., Nahhas F.A., Nowak J.E., Goustin A.S., Tainsky M.A. Role for human SIRT2 NAD-dependent deacetylase activity in control of mitotic exit in the cell cycle. Mol Cell Biol. 2003;23(9):3173–3185. DOI: 10.1128/mcb.23.9.3173-3185.2003</mixed-citation></citation-alternatives></ref><ref id="cit16"><label>16</label><citation-alternatives><mixed-citation xml:lang="ru">Scher M.B., Vaquero A., Reinberg D. SirT3 is a nuclear NAD+-dependent histone deacetylase that translocates to the mitochondria upon cellular stress. Genes Dev. 2007;21(8):920–928. DOI: 10.1101/gad.1527307</mixed-citation><mixed-citation xml:lang="en">Scher M.B., Vaquero A., Reinberg D. SirT3 is a nuclear NAD+-dependent histone deacetylase that translocates to the mitochondria upon cellular stress. Genes Dev. 2007;21(8):920–928. DOI: 10.1101/gad.1527307</mixed-citation></citation-alternatives></ref><ref id="cit17"><label>17</label><citation-alternatives><mixed-citation xml:lang="ru">Ban N., Ozawa Y., Inaba T. Light-dark condition regulates sirtuin mRNA levels in the retina. Experimental Gerontology. 2013;48(11):1212–1217. DOI: 10.1016/j.exger.2013.04.010</mixed-citation><mixed-citation xml:lang="en">Ban N., Ozawa Y., Inaba T. Light-dark condition regulates sirtuin mRNA levels in the retina. Experimental Gerontology. 2013;48(11):1212–1217. DOI: 10.1016/j.exger.2013.04.010</mixed-citation></citation-alternatives></ref><ref id="cit18"><label>18</label><citation-alternatives><mixed-citation xml:lang="ru">Balaiya S., Abu-Amero K.K., Kondkar A.A., Chalam K.V. Sirtuins Expression and Their Role in Retinal Diseases. Oxid Med Cell Longev. 2017;2017:3187594. DOI: 10.1155/2017/3187594</mixed-citation><mixed-citation xml:lang="en">Balaiya S., Abu-Amero K.K., Kondkar A.A., Chalam K.V. Sirtuins Expression and Their Role in Retinal Diseases. Oxid Med Cell Longev. 2017;2017:3187594. DOI: 10.1155/2017/3187594</mixed-citation></citation-alternatives></ref><ref id="cit19"><label>19</label><citation-alternatives><mixed-citation xml:lang="ru">Lee Michan S., Sinclair D. Sirtuins in mammals: insights into their biological function. Biochem J. 2007;404:1–13. DOI: 10.1042/BJ20070140</mixed-citation><mixed-citation xml:lang="en">Lee Michan S., Sinclair D. Sirtuins in mammals: insights into their biological function. Biochem J. 2007;404:1–13. DOI: 10.1042/BJ20070140</mixed-citation></citation-alternatives></ref><ref id="cit20"><label>20</label><citation-alternatives><mixed-citation xml:lang="ru">Xu Z., Zhang L., Fei X., Yi X., Li W., Wang Q. The miR-29b-Sirt1 axis regulates selfrenewal of mouse embryonic stem cells in response to reactive oxygen species. Cell Signal. 2014;26:1500–1505. DOI: 10.1016/j.cellsig.2014.03.010</mixed-citation><mixed-citation xml:lang="en">Xu Z., Zhang L., Fei X., Yi X., Li W., Wang Q. The miR-29b-Sirt1 axis regulates selfrenewal of mouse embryonic stem cells in response to reactive oxygen species. Cell Signal. 2014;26:1500–1505. DOI: 10.1016/j.cellsig.2014.03.010</mixed-citation></citation-alternatives></ref><ref id="cit21"><label>21</label><citation-alternatives><mixed-citation xml:lang="ru">Han M.K., Song E.K., Guo Y., Ou X., Mantel C., Broxmeyer H.E. SIRT1 regulates apoptosis and Nanog expression in mouse embryonic stem cells by controlling p53 subcellular localization. Cell Stem Cell. 2008;2(3):241–251. DOI: 10.1016/j.stem.2008.01.002</mixed-citation><mixed-citation xml:lang="en">Han M.K., Song E.K., Guo Y., Ou X., Mantel C., Broxmeyer H.E. SIRT1 regulates apoptosis and Nanog expression in mouse embryonic stem cells by controlling p53 subcellular localization. Cell Stem Cell. 2008;2(3):241–251. DOI: 10.1016/j.stem.2008.01.002</mixed-citation></citation-alternatives></ref><ref id="cit22"><label>22</label><citation-alternatives><mixed-citation xml:lang="ru">Calvanese V., Lara E., Suárez-Alvarez B. Sirtuin 1 regulation of developmental genes during differentiation of stem cells. Proc Natl Acad Sci USA. 2010;107(31):13736– 13741. DOI: 10.1073/pnas.1001399107</mixed-citation><mixed-citation xml:lang="en">Calvanese V., Lara E., Suárez-Alvarez B. Sirtuin 1 regulation of developmental genes during differentiation of stem cells. Proc Natl Acad Sci USA. 2010;107(31):13736– 13741. DOI: 10.1073/pnas.1001399107</mixed-citation></citation-alternatives></ref><ref id="cit23"><label>23</label><citation-alternatives><mixed-citation xml:lang="ru">Toh T.B., Lim J.J., Chow E.K. Epigenetics in cancer stem cells. Mol Cancer. 2017;16(1):29. DOI: 10.1186/s12943-017-0596-9</mixed-citation><mixed-citation xml:lang="en">Toh T.B., Lim J.J., Chow E.K. Epigenetics in cancer stem cells.  Mol Cancer. 2017;16(1):29. DOI: 10.1186/s12943-017-0596-9</mixed-citation></citation-alternatives></ref><ref id="cit24"><label>24</label><citation-alternatives><mixed-citation xml:lang="ru">Fulco M., Schiltz R.L., Iezzi S. Sir2 regulates skeletal muscle differentiation as a potential sensor of the redox state. Mol Cell. 2003;12(1):51–62. DOI: 10.1016/s10972765(03)00226-0</mixed-citation><mixed-citation xml:lang="en">Fulco M., Schiltz R.L., Iezzi S. Sir2 regulates skeletal muscle differentiation as a potential sensor of the redox state. Mol Cell. 2003;12(1):51–62. DOI: 10.1016/s10972765(03)00226-0</mixed-citation></citation-alternatives></ref><ref id="cit25"><label>25</label><citation-alternatives><mixed-citation xml:lang="ru">Prozorovski T., Schulze-Topphoff U., Glumm R.. Sirt1 contributes critically to the redox-dependent fate of neural progenitors. Nat Cell Biol. 2008;10(4):385–394. DOI: 10.1038/ncb1700</mixed-citation><mixed-citation xml:lang="en">Prozorovski T., Schulze-Topphoff U., Glumm R.. Sirt1 contributes critically to the redox-dependent fate of neural progenitors. Nat Cell Biol. 2008;10(4):385–394. DOI: 10.1038/ncb1700</mixed-citation></citation-alternatives></ref><ref id="cit26"><label>26</label><citation-alternatives><mixed-citation xml:lang="ru">Быков А.Т., Дюжиков А.А., Маляренко Т.Н. Современные представления о роли диеты и мышечных нагрузок в торможении старения и развития возрастно-зависимых кардиоваскулярных заболеваний. Медицинский журнал. 2015;3:7–12.</mixed-citation><mixed-citation xml:lang="en">Bykov A.T., Dyuzhikov A.A., Malyarenko T.N. Current views on age-related and dependent cardiovascular diseases. Medical Journal = Medicinskij zhurnal. 2015;3:7–12 (In Russ.).</mixed-citation></citation-alternatives></ref><ref id="cit27"><label>27</label><citation-alternatives><mixed-citation xml:lang="ru">Hu B., Guo Y., Chen C.. Repression of SIRT1 promotes the differentiation of mouse induced pluripotent stem cells into neural stem cells. Cell Mol Neurobiol. 2014;34(6):905–912. DOI: 10.1007/s10571-014-0071-8</mixed-citation><mixed-citation xml:lang="en">Hu B., Guo Y., Chen C.. Repression of SIRT1 promotes the differentiation of mouse induced pluripotent stem cells into neural stem cells. Cell Mol Neurobiol. 2014;34(6):905–912. DOI: 10.1007/s10571-014-0071-8</mixed-citation></citation-alternatives></ref><ref id="cit28"><label>28</label><citation-alternatives><mixed-citation xml:lang="ru">Zeng Y., Yang K. Sirtuin 1 participates in the process of age-related retinal degeneration. Biochem Biophys Res Commun. 2015;468(1–2):167–172. DOI: 10.1016/j.bbrc.2015.10.139</mixed-citation><mixed-citation xml:lang="en">Zeng Y., Yang K. Sirtuin 1 participates in the process of age-related retinal degeneration. Biochem Biophys Res Commun. 2015;468(1–2):167–172. DOI: 10.1016/j.bbrc.2015.10.139</mixed-citation></citation-alternatives></ref><ref id="cit29"><label>29</label><citation-alternatives><mixed-citation xml:lang="ru">Maugeri A., Mazzone M.G., Giuliano F., Vinciguerra M., Basile G., Barchitta M., Agodi A. Curcumin modulates DNA methyltransferases functions in a cellular model of diabetic retinopathy. Oxid. Med. Cell. Longev. 2018;2018:5407482. DOI: 10.1155/2018/5407482</mixed-citation><mixed-citation xml:lang="en">Maugeri A., Mazzone M.G., Giuliano F., Vinciguerra M., Basile G., Barchitta M., Agodi A. Curcumin modulates DNA methyltransferases functions in a cellular model of diabetic retinopathy. Oxid. Med. Cell. Longev. 2018;2018:5407482. DOI: 10.1155/2018/5407482</mixed-citation></citation-alternatives></ref><ref id="cit30"><label>30</label><citation-alternatives><mixed-citation xml:lang="ru">Maugeri A., Barchitta M., Mazzone M.G., Giuliano F., Basile G., Agodi A. Resveratrol modulates SIRT1 and DNMT functions and restores LINE-1 methylation levels in ARPE-19 cells under oxidative stress and inflammation. Int. J. Mol. Sci. 2018;19:2118 DOI: 10.3390/ijms19072118</mixed-citation><mixed-citation xml:lang="en">Maugeri A., Barchitta M., Mazzone M.G., Giuliano F., Basile G., Agodi A. Resveratrol modulates SIRT1 and DNMT functions and restores LINE-1 methylation levels in ARPE-19 cells under oxidative stress and inflammation. Int. J. Mol. Sci. 2018;19:2118 DOI: 10.3390/ijms19072118</mixed-citation></citation-alternatives></ref><ref id="cit31"><label>31</label><citation-alternatives><mixed-citation xml:lang="ru">Maugeri A., Barchitta M., Fallico M., Castellino N., Reibaldi M., Agodi A. Characterization of SIRT1/DNMTs Functions and LINE-1 Methylation in Patients with Age-Related Macular Degeneration. J Clin Med. 2019;8(2):159. DOI: 10.3390/jcm8020159</mixed-citation><mixed-citation xml:lang="en">Maugeri A., Barchitta M., Fallico M., Castellino N., Reibaldi M., Agodi A. Characterization of SIRT1/DNMTs Functions and LINE-1 Methylation in Patients with Age-Related Macular Degeneration. J Clin Med. 2019;8(2):159. DOI: 10.3390/jcm8020159</mixed-citation></citation-alternatives></ref><ref id="cit32"><label>32</label><citation-alternatives><mixed-citation xml:lang="ru">Maloney S.C., Antecka E., Granner T., Fernandes B., Lim L.A., Orellana M.E., Burnier M.N. Jr. Expression of SIRT1 in choroidal neovascular membranes. Retina. 2013. 33:862–866. DOI: 10.1097/IAE.0b013e31826af556</mixed-citation><mixed-citation xml:lang="en">Maloney S.C., Antecka E., Granner T., Fernandes B., Lim L.A., Orellana M.E., Burnier M.N. Jr. Expression of SIRT1 in choroidal neovascular membranes. Retina. 2013. 33:862–866. DOI: 10.1097/IAE.0b013e31826af556</mixed-citation></citation-alternatives></ref><ref id="cit33"><label>33</label><citation-alternatives><mixed-citation xml:lang="ru">Cabral T., Mello LGM., Lima L.H. Retinal and choroidal angiogenesis: a review of new targets. Int J Retina Vitreous. 2017;3:31. DOI: 10.1186/s40942-017-0084-9</mixed-citation><mixed-citation xml:lang="en">Cabral T., Mello LGM., Lima L.H. Retinal and choroidal angiogenesis: a review of new targets. Int J Retina Vitreous. 2017;3:31. DOI: 10.1186/s40942-017-0084-9</mixed-citation></citation-alternatives></ref><ref id="cit34"><label>34</label><citation-alternatives><mixed-citation xml:lang="ru">Golestaneh N., Chu Y., Cheng S.K., Cao H., Poliakov E., Berinstein D.M. Repressed SIRT1/PGC-1α pathway and mitochondrial disintegration in iPSC-derived RPE disease model of age-related macular degeneration. J Transl Med. 2016;14(1):344. DOI: 10.1186/s12967-016-1101-8</mixed-citation><mixed-citation xml:lang="en">Golestaneh N., Chu Y., Cheng S.K., Cao H., Poliakov E., Berinstein D.M. Repressed SIRT1/PGC-1α pathway and mitochondrial disintegration in iPSC-derived RPE disease model of age-related macular degeneration. J Transl Med. 2016;14(1):344. DOI: 10.1186/s12967-016-1101-8</mixed-citation></citation-alternatives></ref><ref id="cit35"><label>35</label><citation-alternatives><mixed-citation xml:lang="ru">Chen Z., Zhai Y., Zhang W., Teng Y., Yao K. Single Nucleotide Polymorphisms of the Sirtuin 1 (SIRT1) Gene are Associated with age-Related Macular Degeneration in Chinese Han Individuals: A Case-Control Pilot Study. Medicine (Baltimore). 2015;94(49):e2238. DOI: 10.1097/MD.0000000000002238</mixed-citation><mixed-citation xml:lang="en">Chen Z., Zhai Y., Zhang W., Teng Y., Yao K. Single Nucleotide Polymorphisms of the Sirtuin 1 (SIRT1) Gene are Associated with age-Related Macular Degeneration in Chinese Han Individuals: A Case-Control Pilot Study. Medicine (Baltimore). 2015;94(49):e2238. DOI: 10.1097/MD.0000000000002238</mixed-citation></citation-alternatives></ref><ref id="cit36"><label>36</label><citation-alternatives><mixed-citation xml:lang="ru">Kubota S., Kurihara T., Ebinuma M. Resveratrol prevents light-induced retinal degeneration via suppressing activator protein-1 activation. Am J Pathol. 2010;177(4):1725–1731. DOI: 10.2353/ajpath.2010.100098</mixed-citation><mixed-citation xml:lang="en">Kubota S., Kurihara T., Ebinuma M. Resveratrol prevents light-induced retinal degeneration via suppressing activator protein-1 activation. Am J Pathol. 2010;177(4):1725–1731. DOI: 10.2353/ajpath.2010.100098</mixed-citation></citation-alternatives></ref><ref id="cit37"><label>37</label><citation-alternatives><mixed-citation xml:lang="ru">Zhang H., He S., Spee C., Ishikawa K., Hinton D.R. SIRT1 mediated inhibition of VEGF/VEGFR2 signaling by Resveratrol and its relevance to choroidal neovascularization. Cytokine. 2015;76(2):549–552. DOI: 10.1016/j.cyto.2015.06.019</mixed-citation><mixed-citation xml:lang="en">Zhang H., He S., Spee C., Ishikawa K., Hinton D.R. SIRT1 mediated inhibition of VEGF/VEGFR2 signaling by Resveratrol and its relevance to choroidal neovascularization. Cytokine. 2015;76(2):549–552. DOI: 10.1016/j.cyto.2015.06.019</mixed-citation></citation-alternatives></ref><ref id="cit38"><label>38</label><citation-alternatives><mixed-citation xml:lang="ru">Kang J.H., Choung S.Y. Protective effects of resveratrol and its analogs on age-related macular degeneration in vitro. Arch Pharm Res. 2016;39(12):1703–1715. DOI: 10.1007/s12272-016-0839-0</mixed-citation><mixed-citation xml:lang="en">Kang J.H., Choung S.Y. Protective effects of resveratrol and its analogs on age-related macular degeneration in vitro. Arch Pharm Res. 2016;39(12):1703–1715. DOI: 10.1007/s12272-016-0839-0</mixed-citation></citation-alternatives></ref><ref id="cit39"><label>39</label><citation-alternatives><mixed-citation xml:lang="ru">Richer S., Patel S., Sockanathan S., Ulanski L.J., Miller L., Podella C. Resveratrol based oral nutritional supplement produces long-term beneficial effects on structure and visual function in human patients. Nutrients. 2014;6(10):4404–4420. DOI: 10.3390/nu6104404</mixed-citation><mixed-citation xml:lang="en">Richer S., Patel S., Sockanathan S., Ulanski L.J., Miller L., Podella C. Resveratrol based oral nutritional supplement produces long-term beneficial effects on structure and visual function in human patients. Nutrients. 2014;6(10):4404–4420. DOI: 10.3390/nu6104404</mixed-citation></citation-alternatives></ref><ref id="cit40"><label>40</label><citation-alternatives><mixed-citation xml:lang="ru">Zhou M., Luo J., Zhang H. Role of Sirtuin 1 in the pathogenesis of ocular disease (Review). Int J Mol Med. 2018;42(1):13–20. DOI: 10.3892/ijmm.2018.3623</mixed-citation><mixed-citation xml:lang="en">Zhou M., Luo J., Zhang H. Role of Sirtuin 1 in the pathogenesis of ocular disease (Review). Int J Mol Med. 2018;42(1):13–20. DOI: 10.3892/ijmm.2018.3623</mixed-citation></citation-alternatives></ref><ref id="cit41"><label>41</label><citation-alternatives><mixed-citation xml:lang="ru">Kondo A., Goto M., Mimura T., Matsubara M. Silent information regulator T1 in aqueous humor of patients with cataract. Clin Ophthalmol. 2016;10:307–312. DOI: 10.2147/OPTH.S100213</mixed-citation><mixed-citation xml:lang="en">Kondo A., Goto M., Mimura T., Matsubara M. Silent information regulator T1 in aqueous humor of patients with cataract. Clin Ophthalmol. 2016;10:307–312. DOI: 10.2147/OPTH.S100213</mixed-citation></citation-alternatives></ref><ref id="cit42"><label>42</label><citation-alternatives><mixed-citation xml:lang="ru">Zhang Y., Li H., Cao Y., Zhang M., Wei S. Sirtuin 1 regulates lipid metabolism associated with optic nerve regeneration. Mol Med Rep. 2015;12(5):6962–6968. DOI: 10.3892/mmr.2015.4286</mixed-citation><mixed-citation xml:lang="en">Zhang Y., Li H., Cao Y., Zhang M., Wei S. Sirtuin 1 regulates lipid metabolism associated with optic nerve regeneration. Mol Med Rep. 2015;12(5):6962–6968. DOI: 10.3892/mmr.2015.4286</mixed-citation></citation-alternatives></ref><ref id="cit43"><label>43</label><citation-alternatives><mixed-citation xml:lang="ru">Liu S., Lin Y.U., Liu X. Protective effects of SIRT1 in patients with proliferative diabetic retinopathy via the inhibition of IL-17 expression. Exp Ther Med. 2016;11(1):257–262. DOI: 10.3892/etm.2015.2877</mixed-citation><mixed-citation xml:lang="en">Liu S., Lin Y.U., Liu X. Protective effects of SIRT1 in patients with proliferative diabetic retinopathy via the inhibition of IL-17 expression. Exp Ther Med. 2016;11(1):257–262. DOI: 10.3892/etm.2015.2877</mixed-citation></citation-alternatives></ref><ref id="cit44"><label>44</label><citation-alternatives><mixed-citation xml:lang="ru">Zuo L., Khan R.S., Lee V., Dine K., Wu W., Shindler K.S. SIRT1 promotes RGC survival and delays loss of function following optic nerve crush. Invest Ophthalmol Vis Sci. 2013;54(7):5097–5102. DOI: 10.1167/iovs.13-12157</mixed-citation><mixed-citation xml:lang="en">Zuo L., Khan R.S., Lee V., Dine K., Wu W., Shindler K.S. SIRT1 promotes RGC survival and delays loss of function following optic nerve crush. Invest Ophthalmol Vis Sci. 2013;54(7):5097–5102. DOI: 10.1167/iovs.13-12157</mixed-citation></citation-alternatives></ref><ref id="cit45"><label>45</label><citation-alternatives><mixed-citation xml:lang="ru">Isas J.M., Luibl V., Johnson L.V. Soluble and mature amyloid fibrils in drusen deposits. Invest Ophthalmol Vis Sci. 2010;51(3):1304–1310. DOI: 10.1167/iovs.09-4207</mixed-citation><mixed-citation xml:lang="en">Isas J.M., Luibl V., Johnson L.V. Soluble and mature amyloid fibrils in drusen deposits. Invest Ophthalmol Vis Sci. 2010;51(3):1304–1310. DOI: 10.1167/iovs.09-4207</mixed-citation></citation-alternatives></ref><ref id="cit46"><label>46</label><citation-alternatives><mixed-citation xml:lang="ru">Cao L., Liu C., Wang F., Wang H. SIRT1 negatively regulates amyloid-beta-induced inflammation via the NF-κB pathway. Braz J Med Biol Res. 2013;46(8):659–669. DOI: 10.1590/1414-431X20132903</mixed-citation><mixed-citation xml:lang="en">Cao L., Liu C., Wang F., Wang H. SIRT1 negatively regulates amyloid-beta-induced inflammation via the NF-κB pathway. Braz J Med Biol Res. 2013;46(8):659–669. DOI: 10.1590/1414-431X20132903</mixed-citation></citation-alternatives></ref><ref id="cit47"><label>47</label><citation-alternatives><mixed-citation xml:lang="ru">Li F., Gong Q., Dong H., Shi J. Resveratrol, a neuroprotective supplement for Alzheimer’s disease. Curr Pharm Des. 2012;18:27–33. DOI: 10.2174/138161212798919075</mixed-citation><mixed-citation xml:lang="en">Li F., Gong Q., Dong H., Shi J. Resveratrol, a neuroprotective supplement for Alzheimer’s disease. Curr Pharm Des. 2012;18:27–33. DOI: 10.2174/138161212798919075</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>
