<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE root>
<article 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" xmlns:ali="http://www.niso.org/schemas/ali/1.0/" article-type="review-article" dtd-version="1.2" xml:lang="en"><front><journal-meta><journal-id journal-id-type="publisher-id">Russian Journal of Physiology</journal-id><journal-title-group><journal-title xml:lang="en">Russian Journal of Physiology</journal-title><trans-title-group xml:lang="ru"><trans-title>Российский физиологический журнал им. И.М. Сеченова</trans-title></trans-title-group></journal-title-group><issn publication-format="print">0869-8139</issn><issn publication-format="electronic">2658-655X</issn><publisher><publisher-name xml:lang="en">The Russian Academy of Sciences</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="publisher-id">682327</article-id><article-id pub-id-type="doi">10.31857/S0869813924110037</article-id><article-id pub-id-type="edn">VGKLQN</article-id><article-categories><subj-group subj-group-type="toc-heading" xml:lang="en"><subject>REVIEW</subject></subj-group><subj-group subj-group-type="toc-heading" xml:lang="ru"><subject>ОБЗОРНЫЕ СТАТЬИ</subject></subj-group><subj-group subj-group-type="article-type"><subject>Review Article</subject></subj-group></article-categories><title-group><article-title xml:lang="en">Endothelium, aging and vascular diseases</article-title><trans-title-group xml:lang="ru"><trans-title>Эндотелий, старение и сосудистые заболевания</trans-title></trans-title-group></title-group><contrib-group><contrib contrib-type="author"><name-alternatives><name xml:lang="en"><surname>Goncharov</surname><given-names>N. V.</given-names></name><name xml:lang="ru"><surname>Гончаров</surname><given-names>Н. В.</given-names></name></name-alternatives><address><country country="RU">Russian Federation</country></address><email>ngoncharov@gmail.com</email><xref ref-type="aff" rid="aff1"/><xref ref-type="aff" rid="aff2"/></contrib><contrib contrib-type="author"><name-alternatives><name xml:lang="en"><surname>Popova</surname><given-names>P. I.</given-names></name><name xml:lang="ru"><surname>Попова</surname><given-names>П. И.</given-names></name></name-alternatives><address><country country="RU">Russian Federation</country></address><email>ngoncharov@gmail.com</email><xref ref-type="aff" rid="aff3"/></contrib><contrib contrib-type="author"><name-alternatives><name xml:lang="en"><surname>Nadeev</surname><given-names>А. D.</given-names></name><name xml:lang="ru"><surname>Надеев</surname><given-names>А. Д.</given-names></name></name-alternatives><address><country country="RU">Russian Federation</country></address><email>ngoncharov@gmail.com</email><xref ref-type="aff" rid="aff4"/></contrib><contrib contrib-type="author"><name-alternatives><name xml:lang="en"><surname>Belinskaia</surname><given-names>D. A.</given-names></name><name xml:lang="ru"><surname>Белинская</surname><given-names>Д. А.</given-names></name></name-alternatives><address><country country="RU">Russian Federation</country></address><email>ngoncharov@gmail.com</email><xref ref-type="aff" rid="aff2"/></contrib><contrib contrib-type="author"><name-alternatives><name xml:lang="en"><surname>Korf</surname><given-names>E. A.</given-names></name><name xml:lang="ru"><surname>Корф</surname><given-names>Е. А.</given-names></name></name-alternatives><address><country country="RU">Russian Federation</country></address><email>ngoncharov@gmail.com</email><xref ref-type="aff" rid="aff2"/></contrib><contrib contrib-type="author"><name-alternatives><name xml:lang="en"><surname>Avdonin</surname><given-names>P. V.</given-names></name><name xml:lang="ru"><surname>Авдонин</surname><given-names>П. В.</given-names></name></name-alternatives><address><country country="RU">Russian Federation</country></address><email>ngoncharov@gmail.com</email><xref ref-type="aff" rid="aff5"/></contrib></contrib-group><aff-alternatives id="aff1"><aff><institution xml:lang="en">Research Institute of Hygiene, Occupational Pathology and Human Ecology</institution></aff><aff><institution xml:lang="ru">НИИ гигиены, профпатологии и экологии человека</institution></aff></aff-alternatives><aff-alternatives id="aff2"><aff><institution xml:lang="en">Sechenov Institute of Evolutionary Physiology and Biochemistry of the Russian Academy of Sciences</institution></aff><aff><institution xml:lang="ru">Институт эволюционной физиологии и биохимии им. И.М. Сеченова РАН</institution></aff></aff-alternatives><aff-alternatives id="aff3"><aff><institution xml:lang="en">City Polyclinic No. 112</institution></aff><aff><institution xml:lang="ru">Городская поликлиника №112</institution></aff></aff-alternatives><aff-alternatives id="aff4"><aff><institution xml:lang="en">Institute of Cell Biophysics of the Russian Academy of Sciences</institution></aff><aff><institution xml:lang="ru">Институт биофизики клетки РАН</institution></aff></aff-alternatives><aff-alternatives id="aff5"><aff><institution xml:lang="en">Koltsov Institute of Development Biology, Russian Academy of Sciences</institution></aff><aff><institution xml:lang="ru">Институт биологии развития им. Н.К. Кольцова РАН</institution></aff></aff-alternatives><pub-date date-type="pub" iso-8601-date="2024-11-15" publication-format="electronic"><day>15</day><month>11</month><year>2024</year></pub-date><volume>110</volume><issue>11</issue><history><date date-type="received" iso-8601-date="2025-06-03"><day>03</day><month>06</month><year>2025</year></date></history><permissions><copyright-statement xml:lang="en">Copyright ©; 2024, Russian Academy of Sciences</copyright-statement><copyright-statement xml:lang="ru">Copyright ©; 2024, Российская академия наук</copyright-statement><copyright-year>2024</copyright-year><copyright-holder xml:lang="en">Russian Academy of Sciences</copyright-holder><copyright-holder xml:lang="ru">Российская академия наук</copyright-holder></permissions><self-uri xlink:href="https://transsyst.ru/0869-8139/article/view/682327">https://transsyst.ru/0869-8139/article/view/682327</self-uri><abstract xml:lang="en"><p>Aging of the organism is inextricably linked with endothelial dysfunction and the development of vascular diseases. However, age <italic>per se</italic> is only one of the factors of vascular aging. Reactive oxygen species (ROS) play an important role in the mechanisms of aging and death of endothelial cells (EC). Senescence of EC can be associated with endothelial reprogramming, when cells acquire an immunological phenotype or are transformed into myofibroblasts (endothelial-immune or endothelial-mesenchymal transition, respectively). Atherosclerosis is perhaps the most well-known vascular pathology that initiates other diseases. Atherosclerosis is one of the most well-known vascular diseases, which initiates other, more severe diseases. The mechanisms of atherosclerosis development are associated not only with an increased level of "bad" cholesterol, but also with the desialylation of lipoproteins and the simultaneous desialylation of EC. Many factors related to heredity, lifestyle, frequency and intensity of infectious diseases cause damage to the EC and early aging of blood vessels, which leads to secondary vascular diseases, accelerated aging of the body, cognitive impairment and the development of neurodegenerative diseases. The review highlights some of these processes, their chronological and functional relationships.</p></abstract><trans-abstract xml:lang="ru"><p>Старение организма неразрывно связано с эндотелиальной дисфункцией и развитием сосудистых заболеваний. Однако возраст как таковой является лишь одним из факторов старения сосудов. Активные формы кислорода (АФК) играют важную роль в механизмах старения и гибели эндотелиальных клеток (ЭК). Старение ЭК может быть сопряжено с эндотелиальным перепрограммированием, когда клетки приобретают иммунологический фенотип или трансформируются в миофибробласты (эндотелиально-иммунный или эндотелиально-мезенхимальный переход соответственно). Атеросклероз – одно из наиболее известных заболеваний сосудов, которое инициирует другие, более тяжелые заболевания. Механизмы развития атеросклероза связаны не только с повышенным уровнем “плохого” холестерина, но также с десиалированием липопротеидов и эндотелия. Множество факторов, связанных с наследственностью, образом жизни, частотой и интенсивностью инфекционных заболеваний, обусловливают повреждение ЭК и раннее старение сосудов, что приводит к ускоренному старению организма, нарушению когнитивных функций, развитию нейродегенеративных заболеваний. В обзоре освещены некоторые из этих процессов, их хронологическая и функциональная взаимосвязь.</p></trans-abstract><kwd-group xml:lang="en"><kwd>blood vessels</kwd><kwd>endothelium</kwd><kwd>endothelial dysfunction</kwd><kwd>nitric oxide</kwd><kwd>aging</kwd><kwd>immunosenescence</kwd><kwd>atherosclerosis</kwd><kwd>neurodegenerative diseases</kwd></kwd-group><kwd-group xml:lang="ru"><kwd>кровеносные сосуды</kwd><kwd>эндотелий</kwd><kwd>эндотелиальная дисфункция</kwd><kwd>оксид азота</kwd><kwd>старение</kwd><kwd>иммуностарение</kwd><kwd>атеросклероз</kwd><kwd>нейродегенеративные заболевания</kwd></kwd-group><funding-group><award-group><funding-source><institution-wrap><institution xml:lang="ru">Российский научный фонд</institution></institution-wrap><institution-wrap><institution xml:lang="en">Russian Science Foundation</institution></institution-wrap></funding-source><award-id>22-15-00155</award-id></award-group></funding-group></article-meta></front><body></body><back><ref-list><ref id="B1"><label>1.</label><mixed-citation>Dolgyras P, Anyfanti P, Lazaridis A, Gavriilaki E, Koletsos N, Triantafyllou A, Barbara N, Mastrogiannis K, Yiannaki E, Papakonstantinou A, Galanapoulou V, Douma S, Gkaliagkousi E (2024) Endothelial dysfunction and complement activation are independently associated with disease duration in patients with systemic vasculitis. Microvasc Res 154: 104692. https://doi.org/10.1016/j.mvr.2024.104692</mixed-citation></ref><ref id="B2"><label>2.</label><mixed-citation>Khaddaj Mallat R, Mathew John C, Kendrick DJ, Braun AP (2017) The vascular endothelium: A regulator of arterial tone and interface for the immune system. Crit Rev Clin Lab Sci 54: 458–470.https://doi.org/10.1080/10408363.2017.1394267</mixed-citation></ref><ref id="B3"><label>3.</label><mixed-citation>Goncharov NV, Nadeev AD, Jenkins RO, Avdonin PV (2017) Markers and Biomarkers of Endothelium: When Something Is Rotten in the State. Oxid Med Cell Longev 2017: 9759735. https://doi.org/10.1155/2017/9759735</mixed-citation></ref><ref id="B4"><label>4.</label><mixed-citation>Di Pietro N, Baldassarre MPA, Cichelli A, Pandolfi A, Formoso G, Pipino C (2020) Role of Polyphenols and Carotenoids in Endothelial Dysfunction: An Overview from Classic to Innovative Biomarkers. Oxid Med Cell Longev 2020: 1–19. https://doi.org/10.1155/2020/6381380</mixed-citation></ref><ref id="B5"><label>5.</label><mixed-citation>Carge MJ, Liberati DM, Diebel LN (2021) A biomimetic shock model on the effect of endothelial aging on vascular barrier properties. J Trauma Acute Care Surg 91: 849–855. https://doi.org/10.1097/TA.0000000000003207</mixed-citation></ref><ref id="B6"><label>6.</label><mixed-citation>Zhang J, Li C, Zhang Y, Wu J, Huang Z (2023) Therapeutic potential of nitric oxide in vascular aging due to the promotion of angiogenesis. Chem Biol Drug Des 102: 395–407.</mixed-citation></ref><ref id="B7"><label>7.</label><mixed-citation>https://doi.org/10.1111/cbdd.14248</mixed-citation></ref><ref id="B8"><label>8.</label><mixed-citation>Kobayashi R, Sakazaki M, Nagai Y, Okamoto T, Hashimoto Y, Sato K, Seki S, Hata U, Esaki K, Tanigawa R, Mitsuoka A, Funaki A, Niki Y, Hashiguchi T, Negoro H (2024) Habitual isomaltulose intake reduces arterial stiffness associated with postprandial hyperglycemia in middle-aged and elderly people: A randomized controlled trial. Heart Vessels 39: 123–134. https://doi.org/10.1007/s00380-023-02316-y</mixed-citation></ref><ref id="B9"><label>9.</label><mixed-citation>Shields KL, Jarrett CL, Bisconti AV, Park SH, Craig JC, Broxterman RM, Richardson RS (2023) Preserved endothelium-independent vascular function with aging in men and women: evidence from the peripheral and cerebral vasculature. J Appl Physiol 135: 559–571. https://doi.org/10.1152/japplphysiol.00571.2022</mixed-citation></ref><ref id="B10"><label>10.</label><mixed-citation>Bruno F, Abondio P, Bruno R, Ceraudo L, Paparazzo E, Citrigno L, Luiselli D, Bruni AC, Passarino G, Colao R, Maletta R, Montesanto A (2023) Alzheimer’s disease as a viral disease: Revisiting the infectious hypothesis. Ageing Res Rev 91: 102068. https://doi.org/10.1016/j.arr.2023.102068</mixed-citation></ref><ref id="B11"><label>11.</label><mixed-citation>Goncharov NV, Popova PI, Golovkin AS, Zalutskaya NM, Palchikova EI, Zanin KV, Avdonin РV (2020) Vascular endotelial dysfunction is a pathogenetic factor in the development of neurodegenerative diseases and cognitive impairment. VM Bekhterev Rev Psychiatr Med Psychol 11–26. https://doi.org/10.31363/2313-7053-2020-3-11-26</mixed-citation></ref><ref id="B12"><label>12.</label><mixed-citation>Davidson CG, Woodford SJ, Mathur S, Valle DB, Foster D, Kioutchoukova I, Mahmood A, Lucke-Wold B (2023) Investigation into the vascular contributors to dementia and the associated treatments. Explor Neurosci 224–237. https://doi.org/10.37349/en.2023.00023</mixed-citation></ref><ref id="B13"><label>13.</label><mixed-citation>Raposo N, Périole C, Planton M (2024) In-vivo diagnosis of cerebral amyloid angiopathy: An updated review. Curr Opin Neurol 37: 19–25. https://doi.org/10.1097/WCO.0000000000001236</mixed-citation></ref><ref id="B14"><label>14.</label><mixed-citation>Vara D, Pula G (2014) Reactive oxygen species: physiological roles in the regulation of vascular cells. Curr Mol Med 14: 1103–1125. https://doi.org/10.2174/1566524014666140603114010</mixed-citation></ref><ref id="B15"><label>15.</label><mixed-citation>Ткачук В, Тюрин-Кузьмин П, Белоусов В, Воротников А (2012) Пероксид водорода как новый вторичный посредник. Биол мембр 29: 21–37. [Tkachuk V, Tyurin-Kuzmin P, Belousov V, Vorotnikov A (2012) Hydrogen Peroxide as a New Second Messenger. Biol Membr 29: 21-37. (In Russ)].</mixed-citation></ref><ref id="B16"><label>16.</label><mixed-citation>Chen Q, Wang Q, Zhu J, Xiao Q, Zhang L (2018) Reactive oxygen species: Key regulators in vascular health and diseases. Br J Pharmacol 175: 1279–1292. https://doi.org/10.1111/bph.13828</mixed-citation></ref><ref id="B17"><label>17.</label><mixed-citation>Надеев АД, Зинченко ВП, Авдонин ПВ, Гончаров НВ (2014) Токсические и сигнальные эффекты активных форм кислорода. Токсикол вестн 22–27 [Nadeev A, Zinchenko V, Avdonin P, Goncharov N (2014) Toxic and signal properties of active forms of oxygen. Toksikol Vest. (In Russ)].</mixed-citation></ref><ref id="B18"><label>18.</label><mixed-citation>Goncharov NV, Avdonin PV, Nadeev AD, Zharkikh IL, Jenkins RO (2015) Reactive oxygen species in pathogenesis of atherosclerosis. Curr Pharm Des 21: 1134–1146. https://doi.org/10.2174/1381612820666141014142557</mixed-citation></ref><ref id="B19"><label>19.</label><mixed-citation>Martin-Ventura JL, Madrigal-Matute J, Martinez-Pinna R, Ramos-Mozo P, Blanco-Colio LM, Moreno JA, Tarin C, Burillo E, Fernandez-Garcia CE, Egido J, Meilhac O, Michel J-B (2012) Erythrocytes, leukocytes and platelets as a source of oxidative stress in chronic vascular diseases: Detoxifying mechanisms and potential therapeutic options. Thromb Haemost 108: 435–442. https://doi.org/10.1160/TH12-04-0248</mixed-citation></ref><ref id="B20"><label>20.</label><mixed-citation>Knock GA (2019) NADPH oxidase in the vasculature: Expression, regulation and signalling pathways; role in normal cardiovascular physiology and its dysregulation in hypertension. Free Radic Biol Med 145: 385–427. https://doi.org/10.1016/j.freeradbiomed.2019.09.029</mixed-citation></ref><ref id="B21"><label>21.</label><mixed-citation>Vieceli Dalla Sega F, Zambonin L, Fiorentini D, Rizzo B, Caliceti C, Landi L, Hrelia S, Prata C (2014) Specific aquaporins facilitate Nox-produced hydrogen peroxide transport through plasma membrane in leukaemia cells. Biochim Biophys Acta 1843: 806–814. https://doi.org/10.1016/j.bbamcr.2014.01.011</mixed-citation></ref><ref id="B22"><label>22.</label><mixed-citation>Miller EW, Dickinson BC, Chang CJ (2010) Aquaporin-3 mediates hydrogen peroxide uptake to regulate downstream intracellular signaling. Proc Natl Acad Sci U S A 107: 15681–15686. https://doi.org/10.1073/pnas.1005776107</mixed-citation></ref><ref id="B23"><label>23.</label><mixed-citation>Shappell SB, Toman C, Anderson DC, Taylor AA, Entman ML, Smith CW (1990) Mac-1 (CD11b/CD18) mediates adherence-dependent hydrogen peroxide production by human and canine neutrophils. J Immunol Baltim Md 1950 144: 2702–2711.</mixed-citation></ref><ref id="B24"><label>24.</label><mixed-citation>Jones DP (2008) Radical-free biology of oxidative stress. Am J Physiol Cell Physiol 295: C849-С868. https://doi.org/10.1152/ajpcell.00283.2008</mixed-citation></ref><ref id="B25"><label>25.</label><mixed-citation>Murdoch CE, Alom-Ruiz SP, Wang M, Zhang M, Walker S, Yu B, Brewer A, Shah AM (2011) Role of endothelial Nox2 NADPH oxidase in angiotensin II-induced hypertension and vasomotor dysfunction. Basic Res Cardiol 106: 527–538. https://doi.org/10.1007/s00395-011-0179-7</mixed-citation></ref><ref id="B26"><label>26.</label><mixed-citation>Holland JA, Meyer JW, Chang MM, O’Donnell RW, Johnson DK, Ziegler LM (1998) Thrombin stimulated reactive oxygen species production in cultured human endothelial cells. Endothelium 6: 113–121. https://doi.org/10.3109/10623329809072198</mixed-citation></ref><ref id="B27"><label>27.</label><mixed-citation>Ray R, Murdoch CE, Wang M, Santos CX, Zhang M, Alom-Ruiz S, Anilkumar N, Ouattara A, Cave AC, Walker SJ, Grieve DJ, Charles RL, Eaton P, Brewer AC, Shah AM (2011) Endothelial Nox4 NADPH oxidase enhances vasodilatation and reduces blood pressure in vivo. Arterioscler Thromb Vasc Biol 31: 1368–1376. https://doi.org/10.1161/ATVBAHA.110.219238</mixed-citation></ref><ref id="B28"><label>28.</label><mixed-citation>Tobolska A, Jabłońska AE, Suwińska A, Wawrzyniak UE, Wróblewski W, Wezynfeld NE (2024) The effect of histidine, histamine, and imidazole on electrochemical properties of Cu(II) complexes of Aβ peptides containing His-2 and His-3 motifs. Dalton Trans Camb Engl 2003 53: 15359–15371. https://doi.org/10.1039/d4dt01354a</mixed-citation></ref><ref id="B29"><label>29.</label><mixed-citation>Avdonin PV, Rybakova EYu, Avdonin PP, Trufanov SK, Mironova GYu, Tsitrina AA, Goncharov NV (2019) VAS2870 Inhibits Histamine-Induced Calcium Signaling and vWF Secretion in Human Umbilical Vein Endothelial Cells. Cells 8: 196. https://doi.org/10.3390/cells8020196</mixed-citation></ref><ref id="B30"><label>30.</label><mixed-citation>Zharkich IL, Nadeev AD, Tsitrin EB, Goncharov NV, Avdonin PV (2016) Suppression of Histamine-Induced Relaxation of Rat Aorta and Calcium Signaling in Endothelial Cells by Two-Pore Channel Blocker trans-NED19 and Hydrogen Peroxide. Izv Akad Nauk Ser Biol 430–438.</mixed-citation></ref><ref id="B31"><label>31.</label><mixed-citation>Lange S, Heger J, Euler G, Wartenberg M, Piper HM, Sauer H (2009) Platelet-derived growth factor BB stimulates vasculogenesis of embryonic stem cell-derived endothelial cells by calcium-mediated generation of reactive oxygen species. Cardiovasc Res 81: 159–168. https://doi.org/10.1093/cvr/cvn258</mixed-citation></ref><ref id="B32"><label>32.</label><mixed-citation>Thannickal VJ, Hassoun PM, White AC, Fanburg BL (1993) Enhanced rate of H2O2 release from bovine pulmonary artery endothelial cells induced by TGF-beta 1. Am J Physiol 265: L622-L626. https://doi.org/10.1152/ajplung.1993.265.6.L622</mixed-citation></ref><ref id="B33"><label>33.</label><mixed-citation>Matsubara T, Ziff M (1986) Increased superoxide anion release from human endothelial cells in response to cytokines. J Immunol Baltim Md 1950 137: 3295–3298</mixed-citation></ref><ref id="B34"><label>34.</label><mixed-citation>Knopp T, Jung R, Wild J, Bochenek ML, Efentakis P, Lehmann A, Bieler T, Garlapati V, Richter C, Molitor M, Perius K, Finger S, Lagrange J, Ghasemi I, Zifkos K, Kommoss KS, Masri J, Reißig S, Randriamboavonjy V, Wunderlich T, Hövelmeyer N, Weber ANR, Mufazalov IA, Bosmann M, Bechmann I, Fleming I, Oelze M, Daiber A, Münzel T, Schäfer K, Wenzel P, Waisman A, Karbach S (2024) Myeloid cell-derived interleukin-6 induces vascular dysfunction and vascular and systemic inflammation. Eur Heart J Open 4: oeae046. https://doi.org/10.1093/ehjopen/oeae046</mixed-citation></ref><ref id="B35"><label>35.</label><mixed-citation>Reddy SS, Chauhan P, Maurya P, Saini D, Yadav PP, Barthwal MK (2016) Coagulin-L ameliorates TLR4 induced oxidative damage and immune response by regulating mitochondria and NOX-derived ROS. Toxicol Appl Pharmacol 309: 87–100. https://doi.org/10.1016/j.taap.2016.08.022</mixed-citation></ref><ref id="B36"><label>36.</label><mixed-citation>Yan S, Sheak JR, Walker BR, Jernigan NL, Resta TC (2023) Contribution of Mitochondrial Reactive Oxygen Species to Chronic Hypoxia-Induced Pulmonary Hypertension. Antioxid Basel Switz 12: 2060. https://doi.org/10.3390/antiox12122060</mixed-citation></ref><ref id="B37"><label>37.</label><mixed-citation>Giorgi C, Agnoletto C, Baldini C, Bononi A, Bonora M, Marchi S, Missiroli S, Patergnani S, Poletti F, Rimessi A, Zavan B, Pinton P (2010) Redox control of protein kinase C: cell- and disease-specific aspects. Antioxid Redox Signal 13: 1051–1085. https://doi.org/10.1089/ars.2009.2825</mixed-citation></ref><ref id="B38"><label>38.</label><mixed-citation>Tabet F, Schiffrin EL, Callera GE, He Y, Yao G, Ostman A, Kappert K, Tonks NK, Touyz RM (2008) Redox-sensitive signaling by angiotensin II involves oxidative inactivation and blunted phosphorylation of protein tyrosine phosphatase SHP-2 in vascular smooth muscle cells from SHR. Circ Res 103: 149–158. https://doi.org/10.1161/CIRCRESAHA.108.178608</mixed-citation></ref><ref id="B39"><label>39.</label><mixed-citation>Förstermann U, Xia N, Li H (2017) Roles of Vascular Oxidative Stress and Nitric Oxide in the Pathogenesis of Atherosclerosis. Circ Res 120: 713–735. https://doi.org/10.1161/CIRCRESAHA.116.309326</mixed-citation></ref><ref id="B40"><label>40.</label><mixed-citation>Singer M, Young PJ, Laffey JG, Asfar P, Taccone FS, Skrifvars MB, Meyhoff CS, Radermacher P (2021) Dangers of hyperoxia. Crit Care 25: 440. https://doi.org/10.1186/s13054-021-03815-y</mixed-citation></ref><ref id="B41"><label>41.</label><mixed-citation>Smith KA, Schumacker PT (2019) Sensors and signals: The role of reactive oxygen species in hypoxic pulmonary vasoconstriction. J Physiol 597: 1033–1043. https://doi.org/10.1113/JP275852</mixed-citation></ref><ref id="B42"><label>42.</label><mixed-citation>Abdulmahdi W, Patel D, Rabadi MM, Azar T, Jules E, Lipphardt M, Hashemiyoon R, Ratliff BB (2017) HMGB1 redox during sepsis. Redox Biol 13: 600–607. https://doi.org/10.1016/j.redox.2017.08.001</mixed-citation></ref><ref id="B43"><label>43.</label><mixed-citation>Hou Y, Wang XF, Lang ZQ, Jin YC, Fu JR, Xv XM, Sun ST, Xin X, Zhang LS (2018) Adiponectin is protective against endoplasmic reticulum stress-induced apoptosis of endothelial cells in sepsis. Braz J Med Biol Res 51: e7747. https://doi.org/10.1590/1414-431X20187747</mixed-citation></ref><ref id="B44"><label>44.</label><mixed-citation>Lee Y-J, Kang I-J, Bünger R, Kang Y-H (2004) Enhanced survival effect of pyruvate correlates MAPK and NF-kappaB activation in hydrogen peroxide-treated human endothelial cells. J Appl Physiol (1985) 96: 793–801. https://doi.org/10.1152/japplphysiol.00797.2003</mixed-citation></ref><ref id="B45"><label>45.</label><mixed-citation>Xie C-L, Hu L-Q, Pan Y-B, Qian Y-N (2015) Propofol attenuation of hydrogen peroxide-induced injury in human umbilical vein endothelial cells involves aldose reductase. Pharm 70: 103–109.</mixed-citation></ref><ref id="B46"><label>46.</label><mixed-citation>Liu R, Liu H, Ha Y, Tilton RG, Zhang W (2014) Oxidative stress induces endothelial cell senescence via downregulation of Sirt6. Biomed Res Int 2014: 902842. https://doi.org/10.1155/2014/902842</mixed-citation></ref><ref id="B47"><label>47.</label><mixed-citation>Smedlund K, Bah M, Vazquez G (2012) On the role of endothelial TRPC3 channels in endothelial dysfunction and cardiovascular disease. Cardiovasc Hematol Agents Med Chem 10: 265–274. https://doi.org/10.2174/187152512802651051</mixed-citation></ref><ref id="B48"><label>48.</label><mixed-citation>Sun L, Yau H-Y, Wong W-Y, Li RA, Huang Y, Yao X (2012) Role of TRPM2 in H(2)O(2)-induced cell apoptosis in endothelial cells. PloS One 7: e43186. https://doi.org/10.1371/journal.pone.0043186</mixed-citation></ref><ref id="B49"><label>49.</label><mixed-citation>Sumoza-Toledo A, Penner R (2011) TRPM2: A multifunctional ion channel for calcium signalling. J Physiol 589: 1515–1525. https://doi.org/10.1113/jphysiol.2010.201855</mixed-citation></ref><ref id="B50"><label>50.</label><mixed-citation>Yamamoto S, Shimizu S (2016) Targeting TRPM2 in ROS-Coupled Diseases. Pharm Basel Switz 9: 57. https://doi.org/10.3390/ph9030057</mixed-citation></ref><ref id="B51"><label>51.</label><mixed-citation>Avdonin PV, Nadeev AD, Tsitrin EB, Tsitrina AA, Avdonin PP, Mironova GYu, Zharkikh IL, Goncharov NV (2017) Involvement of two-pore channels in hydrogen peroxide-induced increase in the level of calcium ions in the cytoplasm of human umbilical vein endothelial cells. Dokl Biochem Biophys 474: 209–212. https://doi.org/10.1134/S1607672917030152</mixed-citation></ref><ref id="B52"><label>52.</label><mixed-citation>Trufanov SK, Rybakova EYu, Avdonin PP, Tsitrina AA, Zharkikh IL, Goncharov NV, Jenkins RO, Avdonin PV (2019) The Role of Two-Pore Channels in Norepinephrine-Induced [Ca2+]i Rise in Rat Aortic Smooth Muscle Cells and Aorta Contraction. Cells 8: 1144. https://doi.org/10.3390/cells8101144</mixed-citation></ref><ref id="B53"><label>53.</label><mixed-citation>Neumann P, Gertzberg N, Vaughan E, Weisbrot J, Woodburn R, Lambert W, Johnson A (2006) Peroxynitrite mediates TNF-alpha-induced endothelial barrier dysfunction and nitration of actin. Am J Physiol Lung Cell Mol Physiol 290: L674–L684. https://doi.org/10.1152/ajplung.00391.2005</mixed-citation></ref><ref id="B54"><label>54.</label><mixed-citation>Liu G, Vogel SM, Gao X, Javaid K, Hu G, Danilov SM, Malik AB, Minshall RD (2011) Src phosphorylation of endothelial cell surface intercellular adhesion molecule-1 mediates neutrophil adhesion and contributes to the mechanism of lung inflammation. Arterioscler Thromb Vasc Biol 31: 1342–1350. https://doi.org/10.1161/ATVBAHA.110.222208</mixed-citation></ref><ref id="B55"><label>55.</label><mixed-citation>Pattillo CB, Pardue S, Shen X, Fang K, Langston W, Jourd’heuil D, Kavanagh TJ, Patel RP, Kevil CG (2010) ICAM-1 cytoplasmic tail regulates endothelial glutathione synthesis through a NOX4/PI3-kinase-dependent pathway. Free Radic Biol Med 49: 1119–1128. https://doi.org/10.1016/j.freeradbiomed.2010.06.030</mixed-citation></ref><ref id="B56"><label>56.</label><mixed-citation>Kudryavtsev IV, Garnyuk VV, Nadeev AD, Goncharov NV (2014) Hydrogen peroxide modulates expression of surface antigens by human umbilical vein endothelial cells in vitro. Biochem Mosc Suppl Ser Membr Cell Biol 8: 97–102. https://doi.org/10.1134/S1990747813050103</mixed-citation></ref><ref id="B57"><label>57.</label><mixed-citation>Терехина ИЛ, Надеев АД, Кожевникова ЛМ, Гончаров НВ, Авдонин ПВ (2012) 5НТ1В- и 5НТ2В-рецепторы вызывают увеличение концентрации ионов кальция в эндотелиальных клетках кровеносных сосудов. Патогенез 10: 70–72 [Terexina IL, Nadeev AD, Kozhevnikova LM, Goncharov NV, Avdonin PV (2012) 5HT1B and 5HT2B receptors cause an increase in the concentration of calcium ions in the endothelial cells of blood vessels. Patogenez. (In Russ)].</mixed-citation></ref><ref id="B58"><label>58.</label><mixed-citation>Profirovic J, Strekalova E, Urao N, Krbanjevic A, Andreeva AV, Varadarajan S, Fukai T, Hen R, Ushio-Fukai M, Voyno-Yasenetskaya TA (2013) A novel regulator of angiogenesis in endothelial cells: 5-hydroxytriptamine 4 receptor. Angiogenesis 16: 15–28. https://doi.org/10.1007/s10456-012-9296-7</mixed-citation></ref><ref id="B59"><label>59.</label><mixed-citation>Yang L, Froio RM, Sciuto TE, Dvorak AM, Alon R, Luscinskas FW (2005) ICAM-1 regulates neutrophil adhesion and transcellular migration of TNF-alpha-activated vascular endothelium under flow. Blood 106: 584–592. https://doi.org/10.1182/blood-2004-12-4942</mixed-citation></ref><ref id="B60"><label>60.</label><mixed-citation>Войтенко НГ, Гарнюк ВВ, Прокофьева ДС, Гончаров НВ (2015) О новом скрининговом биомаркере для оценки состояния здоровья персонала предприятия по уничтожению химического оружия. Мед труда пром экол 2015: 38–42.</mixed-citation></ref><ref id="B61"><label>61.</label><mixed-citation>Irani K (2000) Oxidant signaling in vascular cell growth, death, and survival: A review of the roles of reactive oxygen species in smooth muscle and endothelial cell mitogenic and apoptotic signaling. Circ Res 87: 179–183. https://doi.org/10.1161/01.res.87.3.179</mixed-citation></ref><ref id="B62"><label>62.</label><mixed-citation>Kang H, Yu H, Fan J, Cao G (2021) Rotigotine protects against oxidized low-density lipoprotein(ox-LDL)-induced damages in human umbilical vein endothelial cells(HUVECs). Bioengineered 12: 10568–10579. https://doi.org/10.1080/21655979.2021.2000224</mixed-citation></ref><ref id="B63"><label>63.</label><mixed-citation>Zhang L, Li Q, Chen Y, Zhu Q (2021) LncRNA OIP5-AS1 accelerates ox-LDL-treated HUVECs injury by NF-κB pathway via miR-30c-5p. Clin Hemorheol Microcirc 78: 449–460. https://doi.org/10.3233/CH-211130</mixed-citation></ref><ref id="B64"><label>64.</label><mixed-citation>Yazdanpanah B, Wiegmann K, Tchikov V, Krut O, Pongratz C, Schramm M, Kleinridders A, Wunderlich T, Kashkar H, Utermöhlen O, Brüning JC, Schütze S, Krönke M (2009) Riboflavin kinase couples TNF receptor 1 to NADPH oxidase. Nature 460: 1159–1163. https://doi.org/10.1038/nature08206</mixed-citation></ref><ref id="B65"><label>65.</label><mixed-citation>Block K, Eid A, Griendling KK, Lee D-Y, Wittrant Y, Gorin Y (2008) Nox4 NAD(P)H oxidase mediates Src-dependent tyrosine phosphorylation of PDK-1 in response to angiotensin II: Role in mesangial cell hypertrophy and fibronectin expression. J Biol Chem 283: 24061–24076. https://doi.org/10.1074/jbc.M803964200</mixed-citation></ref><ref id="B66"><label>66.</label><mixed-citation>Ushio-Fukai M, Alexander RW, Akers M, Yin Q, Fujio Y, Walsh K, Griendling KK (1999) Reactive oxygen species mediate the activation of Akt/protein kinase B by angiotensin II in vascular smooth muscle cells. J Biol Chem 274: 22699–22704. https://doi.org/10.1074/jbc.274.32.22699</mixed-citation></ref><ref id="B67"><label>67.</label><mixed-citation>Zhong X, Wang K, Wang Y, Wang L, Wang S, Huang W, Jia Z, Dai S-S, Huang Z (2024) Angiotension II directly bind P2X7 receptor to induce myocardial ferroptosis and remodeling by activating human antigen R. Redox Biol 72: 103154. https://doi.org/10.1016/j.redox.2024.103154</mixed-citation></ref><ref id="B68"><label>68.</label><mixed-citation>Patterson CE, Lum H (2001) Update on pulmonary edema: The role and regulation of endothelial barrier function. Endothelium 8: 75–105. https://doi.org/10.3109/10623320109165319</mixed-citation></ref><ref id="B69"><label>69.</label><mixed-citation>Carrim N, Arthur JF, Hamilton JR, Gardiner EE, Andrews RK, Moran N, Berndt MC, Metharom P (2015) Thrombin-induced reactive oxygen species generation in platelets: A novel role for protease-activated receptor 4 and GPIbα. Redox Biol 6: 640–647. https://doi.org/10.1016/j.redox.2015.10.009</mixed-citation></ref><ref id="B70"><label>70.</label><mixed-citation>Fang X-L, Shu G, Yu J-J, Wang L-N, Yang J, Zeng Q-J, Cheng X, Zhang Z-Q, Wang S-B, Gao P, Zhu X-T, Xi Q-Y, Zhang Y-L, Jiang Q-Y (2013) The anorexigenic effect of serotonin is mediated by the generation of NADPH oxidase-dependent ROS. PloS One 8: e53142. https://doi.org/10.1371/journal.pone.0053142</mixed-citation></ref><ref id="B71"><label>71.</label><mixed-citation>Lee SL, Wang WW, Fanburg BL (1998) Superoxide as an intermediate signal for serotonin-induced mitogenesis. Free Radic Biol Med 24: 855–858. https://doi.org/10.1016/s0891-5849(97)00359-6</mixed-citation></ref><ref id="B72"><label>72.</label><mixed-citation>Liu Y, Fanburg BL (2006) Serotonin-induced growth of pulmonary artery smooth muscle requires activation of phosphatidylinositol 3-kinase/serine-threonine protein kinase B/mammalian target of rapamycin/p70 ribosomal S6 kinase 1. Am J Respir Cell Mol Biol 34: 182–191. https://doi.org/10.1165/rcmb.2005-0163OC</mixed-citation></ref><ref id="B73"><label>73.</label><mixed-citation>Rybakova EYu, Avdonin PP, Trufanov SK, Goncharov NV, Avdonin PV (2023) Synergistic Interaction of 5-HT1B and 5-HT2B Receptors in Cytoplasmic Ca2+ Regulation in Human Umbilical Vein Endothelial Cells: Possible Involvement in Pathologies. Int J Mol Sci 24: 13833. https://doi.org/10.3390/ijms241813833</mixed-citation></ref><ref id="B74"><label>74.</label><mixed-citation>Avdonin PV, Nadeev AD, Mironova GYu, Zharkikh IL, Avdonin PP, Goncharov NV (2019) Enhancement by Hydrogen Peroxide of Calcium Signals in Endothelial Cells Induced by 5-HT1B and 5-HT2B Receptor Agonists. Oxid Med Cell Longev 2019: 1–8. https://doi.org/10.1155/2019/1701478</mixed-citation></ref><ref id="B75"><label>75.</label><mixed-citation>Alves JV, da Costa RM, Awata WMC, Bruder-Nascimento A, Singh S, Tostes RC, Bruder-Nascimento T (2024) NADPH oxidase 4-derived hydrogen peroxide counterbalances testosterone-induced endothelial dysfunction and migration. Am J Physiol Endocrinol Metab 327: E1–E12. https://doi.org/10.1152/ajpendo.00365.2023</mixed-citation></ref><ref id="B76"><label>76.</label><mixed-citation>Yu Y, Su F-F, Xu C (2024) Maximakinin reversed H2O2 induced oxidative damage in rat cardiac H9c2 cells through AMPK/Akt and AMPK/ERK1/2 signaling pathways. Biomed Pharmacother 174: 116489. https://doi.org/10.1016/j.biopha.2024.116489</mixed-citation></ref><ref id="B77"><label>77.</label><mixed-citation>Eller-Borges R, Rodrigues EG, Teodoro ACS, Moraes MS, Arruda DC, Paschoalin T, Curcio MF, da Costa PE, Do Nascimento IR, Calixto LA, Stern A, Monteiro HP, Batista WL (2023) Bradykinin promotes murine melanoma cell migration and invasion through endogenous production of superoxide and nitric oxide. Nitric Oxide Biol Chem 132: 15–26. https://doi.org/10.1016/j.niox.2023.01.006</mixed-citation></ref><ref id="B78"><label>78.</label><mixed-citation>Deng W, Baki L, Baumgarten CM (2010) Endothelin signalling regulates volume-sensitive Cl- current via NADPH oxidase and mitochondrial reactive oxygen species. Cardiovasc Res 88: 93–100. https://doi.org/10.1093/cvr/cvq125</mixed-citation></ref><ref id="B79"><label>79.</label><mixed-citation>Sensi SL, Yin HZ, Weiss JH (1999) Glutamate triggers preferential Zn2+ flux through Ca2+ permeable AMPA channels and consequent ROS production. Neuroreport 10: 1723–1727. https://doi.org/10.1097/00001756-199906030-00018</mixed-citation></ref><ref id="B80"><label>80.</label><mixed-citation>Carriedo SG, Sensi SL, Yin HZ, Weiss JH (2000) AMPA exposures induce mitochondrial Ca(2+) overload and ROS generation in spinal motor neurons in vitro. J Neurosci 20: 240–250. https://doi.org/10.1523/JNEUROSCI.20-01-00240.2000</mixed-citation></ref><ref id="B81"><label>81.</label><mixed-citation>Gasiorowska A, Wydrych M, Drapich P, Zadrozny M, Steczkowska M, Niewiadomski W, Niewiadomska G (2021) The Biology and Pathobiology of Glutamatergic, Cholinergic, and Dopaminergic Signaling in the Aging Brain. Front Aging Neurosci 13: 654931. https://doi.org/10.3389/fnagi.2021.654931</mixed-citation></ref><ref id="B82"><label>82.</label><mixed-citation>Yao Z, Tong J, Tan X, Li C, Shao Z, Kim WC, vanden Hoek TL, Becker LB, Head CA, Schumacker PT (1999) Role of reactive oxygen species in acetylcholine-induced preconditioning in cardiomyocytes. Am J Physiol 277: H2504-H2509. https://doi.org/10.1152/ajpheart.1999.277.6.H2504</mixed-citation></ref><ref id="B83"><label>83.</label><mixed-citation>Wu X, Tian Y, Wang H, Chen H, Hou H, Hu Q (2024) Dual Regulation of Nicotine on NLRP3 Inflammasome in Macrophages with the Involvement of Lysosomal Destabilization, ROS and α7nAChR. Inflammation. https://doi.org/10.1007/s10753-024-02036-z</mixed-citation></ref><ref id="B84"><label>84.</label><mixed-citation>Safronova VG, Vulfius CA, Shelukhina IV, Mal’tseva VN, Berezhnov AV, Fedotova EI, Miftahova RG, Kryukova EV, Grinevich AA, Tsetlin VI (2016) Nicotinic receptor involvement in regulation of functions of mouse neutrophils from inflammatory site. Immunobiology 221: 761–772. https://doi.org/10.1016/j.imbio.2016.01.016</mixed-citation></ref><ref id="B85"><label>85.</label><mixed-citation>Novikova IN, Manole A, Zherebtsov EA, Stavtsev DD, Vukolova MN, Dunaev AV, Angelova PR, Abramov AY (2020) Adrenaline induces calcium signal in astrocytes and vasoconstriction via activation of monoamine oxidase. Free Radic Biol Med 159: 15–22. https://doi.org/10.1016/j.freeradbiomed.2020.07.011</mixed-citation></ref><ref id="B86"><label>86.</label><mixed-citation>May JM, de Haën C (1979) Insulin-stimulated intracellular hydrogen peroxide production in rat epididymal fat cells. J Biol Chem 254: 2214–2220.</mixed-citation></ref><ref id="B87"><label>87.</label><mixed-citation>Ceolotto G, Bevilacqua M, Papparella I, Baritono E, Franco L, Corvaja C, Mazzoni M, Semplicini A, Avogaro A (2004) Insulin generates free radicals by an NAD(P)H, phosphatidylinositol 3’-kinase-dependent mechanism in human skin fibroblasts ex vivo. Diabetes 53: 1344–1351. https://doi.org/10.2337/diabetes.53.5.1344</mixed-citation></ref><ref id="B88"><label>88.</label><mixed-citation>Kang SW (2007) Two axes in platelet-derived growth factor signaling: tyrosine phosphorylation and reactive oxygen species. Cell Mol Life Sci CMLS 64: 533–541. https://doi.org/10.1007/s00018-007-6437-z</mixed-citation></ref><ref id="B89"><label>89.</label><mixed-citation>Goldman R, Zor U, Meller R, Moshonov S, Fürstenberger G, Seger R (1997) Activation of MAP kinases, cPLA2 and reactive oxygen species formation by EGF and calcium mobilizing agonists in a human keratinocyte cell line. Adv Exp Med Biol 407: 289–293. https://doi.org/10.1007/978-1-4899-1813-0_43</mixed-citation></ref><ref id="B90"><label>90.</label><mixed-citation>Thannickal VJ, Day RM, Klinz SG, Bastien MC, Larios JM, Fanburg BL (2000) Ras-dependent and -independent regulation of reactive oxygen species by mitogenic growth factors and TGF-beta1. FASEB J 14: 1741–1748. https://doi.org/10.1096/fj.99-0878com</mixed-citation></ref><ref id="B91"><label>91.</label><mixed-citation>Lo YY, Cruz TF (1995) Involvement of reactive oxygen species in cytokine and growth factor induction of c-fos expression in chondrocytes. J Biol Chem 270: 11727–11730. https://doi.org/10.1074/jbc.270.20.11727</mixed-citation></ref><ref id="B92"><label>92.</label><mixed-citation>Hennet T, Richter C, Peterhans E (1993) Tumour necrosis factor-alpha induces superoxide anion generation in mitochondria of L929 cells. Biochem J 289 (Pt 2): 587–592. https://doi.org/10.1042/bj2890587</mixed-citation></ref><ref id="B93"><label>93.</label><mixed-citation>Meier B, Radeke HH, Selle S, Younes M, Sies H, Resch K, Habermehl GG (1989) Human fibroblasts release reactive oxygen species in response to interleukin-1 or tumour necrosis factor-alpha. Biochem J 263: 539–545. https://doi.org/10.1042/bj2630539</mixed-citation></ref><ref id="B94"><label>94.</label><mixed-citation>De Keulenaer GW, Alexander RW, Ushio-Fukai M, Ishizaka N, Griendling KK (1998) Tumour necrosis factor alpha activates a p22phox-based NADH oxidase in vascular smooth muscle. Biochem J 329(Pt 3): 653–657. https://doi.org/10.1042/bj3290653</mixed-citation></ref><ref id="B95"><label>95.</label><mixed-citation>Schwabe RF, Brenner DA (2006) Mechanisms of Liver Injury. I. TNF-alpha-induced liver injury: Role of IKK, JNK, and ROS pathways. Am J Physiol Gastrointest Liver Physiol 290: G583-G589. https://doi.org/10.1152/ajpgi.00422.2005</mixed-citation></ref><ref id="B96"><label>96.</label><mixed-citation>Ismail S, Sturrock A, Wu P, Cahill B, Norman K, Huecksteadt T, Sanders K, Kennedy T, Hoidal J (2009) NOX4 mediates hypoxia-induced proliferation of human pulmonary artery smooth muscle cells: The role of autocrine production of transforming growth factor-{beta}1 and insulin-like growth factor binding protein-3. Am J Physiol Lung Cell Mol Physiol 296: L489-L499. https://doi.org/10.1152/ajplung.90488.2008</mixed-citation></ref><ref id="B97"><label>97.</label><mixed-citation>Pawate S, Shen Q, Fan F, Bhat NR (2004) Redox regulation of glial inflammatory response to lipopolysaccharide and interferongamma. J Neurosci Res 77: 540–551. https://doi.org/10.1002/jnr.20180</mixed-citation></ref><ref id="B98"><label>98.</label><mixed-citation>Franceschelli S, Pesce M, Vinciguerra I, Ferrone A, Riccioni G, Patruno A, Grilli A, Felaco M, Speranza L (2011) Licocalchone-C extracted from Glycyrrhiza glabra inhibits lipopolysaccharide-interferon-γ inflammation by improving antioxidant conditions and regulating inducible nitric oxide synthase expression. Mol Basel Switz 16: 5720–5734. https://doi.org/10.3390/molecules16075720</mixed-citation></ref><ref id="B99"><label>99.</label><mixed-citation>Spulber S, Edoff K, Hong L, Morisawa S, Shirahata S, Ceccatelli S (2012) Molecular hydrogen reduces LPS-induced neuroinflammation and promotes recovery from sickness behaviour in mice. PloS One 7: e42078. https://doi.org/10.1371/journal.pone.0042078</mixed-citation></ref><ref id="B100"><label>100.</label><mixed-citation>Muzykantov VR, Sakharov DV, Domogatsky SP, Goncharov NV, Danilov SM (1987) Directed targeting of immunoerythrocytes provides local protection of endothelial cells from damage by hydrogen peroxide. Am J Pathol 128: 276–285. i (2014) The effects of biogenic and abiogenic disulphides on endothelial cells in culture: Comparison of three methods of viability assessment. Cell Tissue Biol 8: 389–399. https://doi.org/10.1134/s1990519x1405006x</mixed-citation></ref><ref id="B101"><label>101.</label><mixed-citation>Song W, Pu J, He B (2014) Tanshinol protects human umbilical vein endothelial cells against hydrogen peroxide-induced apoptosis. Mol Med Rep 10: 2764–2770. https://doi.org/10.3892/mmr.2014.2541</mixed-citation></ref><ref id="B102"><label>102.</label><mixed-citation>Kroemer G, Galluzzi L, Vandenabeele P, Abrams J, Alnemri ES, Baehrecke EH, Blagosklonny MV, El-Deiry WS, Golstein P, Green DR, Hengartner M, Knight RA, Kumar S, Lipton SA, Malorni W, Nuñez G, Peter ME, Tschopp J, Yuan J, Piacentini M, Zhivotovsky B, Melino G, Nomenclature Committee on Cell Death 2009 (2009) Classification of cell death: Recommendations of the Nomenclature Committee on Cell Death 2009. Cell Death Differ 16: 3–11. https://doi.org/10.1038/cdd.2008.150</mixed-citation></ref><ref id="B103"><label>103.</label><mixed-citation>Galluzzi L, Vitale I, Abrams JM, Alnemri ES, Baehrecke EH, Blagosklonny MV, Dawson TM, Dawson VL, El-Deiry WS, Fulda S, Gottlieb E, Green DR, Hengartner MO, Kepp O, Knight RA, Kumar S, Lipton SA, Lu X, Madeo F, Malorni W, Mehlen P, Nuñez G, Peter ME, Piacentini M, Rubinsztein DC, Shi Y, Simon H-U, Vandenabeele P, White E, Yuan J, Zhivotovsky B, Melino G, Kroemer G (2012) Molecular definitions of cell death subroutines: recommendations of the Nomenclature Committee on Cell Death 2012. Cell Death Differ 19: 107–120. https://doi.org/10.1038/cdd.2011.96</mixed-citation></ref><ref id="B104"><label>104.</label><mixed-citation>Mutin M, Dignat‐George F, Sampol J (1997) Immunologic phenotype of cultured endothelial cells: Quantitative analysis of cell surface molecules. Tissue Antigens 50: 449–458. https://doi.org/10.1111/j.1399-0039.1997.tb02899.x</mixed-citation></ref><ref id="B105"><label>105.</label><mixed-citation>Goncharov NV, Popova PI, Avdonin PP, Kudryavtsev IV, Serebryakova MK, Korf EA, Avdonin PV (2020) Markers of Endothelial Cells in Normal and Pathological Conditions. Biochem Mosc Suppl Ser Membr Cell Biol 14: 167–183. https://doi.org/10.1134/S1990747819030140</mixed-citation></ref><ref id="B106"><label>106.</label><mixed-citation>Goncharov NV, Terpilowski MA, Nadeev AD, Kudryavtsev IV, Serebriakova MK, Zinchenko VP, Avdonin PV (2018) Cytotoxic Power of Hydrogen Peroxide Effect on Endothelial Cells in vitro. Biochem Mosc Suppl Ser Membr Cell Biol 12: 180–188. https://doi.org/10.1134/S199074781802006X</mixed-citation></ref><ref id="B107"><label>107.</label><mixed-citation>Гончаров НВ, Терпиловский МА, Соболев ВЕ, Корф ЕА, Белинская ДА (2019) Проблема безопасности применения нутрицевтиков. Успехи совр биол 139: 487–499. https://doi.org/10.1134/S0042132419050041</mixed-citation></ref><ref id="B108"><label>108.</label><mixed-citation>Erusalimsky JD (2009) Vascular endothelial senescence: From mechanisms to pathophysiology. J Appl Physiol (1985) 106: 326–332. https://doi.org/10.1152/japplphysiol.91353.2008</mixed-citation></ref><ref id="B109"><label>109.</label><mixed-citation>Kida Y, Goligorsky MS (2016) Sirtuins, Cell Senescence, and Vascular Aging. Can J Cardiol 32: 634–641. https://doi.org/10.1016/j.cjca.2015.11.022</mixed-citation></ref><ref id="B110"><label>110.</label><mixed-citation>Zhang L, Wu X, Hong L (2024) Endothelial Reprogramming in Atherosclerosis. Bioengineering 11: 325. https://doi.org/10.3390/bioengineering11040325</mixed-citation></ref><ref id="B111"><label>111.</label><mixed-citation>Chen P-Y, Qin L, Baeyens N, Li G, Afolabi T, Budatha M, Tellides G, Schwartz MA, Simons M (2015) Endothelial-to-mesenchymal transition drives atherosclerosis progression. J Clin Invest 125: 4514–4528. https://doi.org/10.1172/JCI82719</mixed-citation></ref><ref id="B112"><label>112.</label><mixed-citation>Piera-Velazquez S, Mendoza FA, Jimenez SA (2016) Endothelial to Mesenchymal Transition (EndoMT) in the Pathogenesis of Human Fibrotic Diseases. J Clin Med 5: 45. https://doi.org/10.3390/jcm5040045</mixed-citation></ref><ref id="B113"><label>113.</label><mixed-citation>Rieder F, Kessler SP, West GA, Bhilocha S, de la Motte C, Sadler TM, Gopalan B, Stylianou E, Fiocchi C (2011) Inflammation-induced endothelial-to-mesenchymal transition: a novel mechanism of intestinal fibrosis. Am J Pathol 179: 2660–2673. https://doi.org/10.1016/j.ajpath.2011.07.042</mixed-citation></ref><ref id="B114"><label>114.</label><mixed-citation>Patschan D, Schwarze K, Henze E, Patschan S, Müller GA (2016) Endothelial autophagy and Endothelial-to-Mesenchymal Transition (EndoMT) in eEPC treatment of ischemic AKI. J Nephrol 29: 637–644. https://doi.org/10.1007/s40620-015-0222-0</mixed-citation></ref><ref id="B115"><label>115.</label><mixed-citation>Wang J, Feng Y, Wang Y, Xiang D, Zhang X, Yuan F (2017) Autophagy regulates Endothelial-Mesenchymal transition by decreasing the phosphorylation level of Smad3. Biochem Biophys Res Commun 487: 740–747. https://doi.org/10.1016/j.bbrc.2017.04.130</mixed-citation></ref><ref id="B116"><label>116.</label><mixed-citation>Mendoza FA, Mansoor M, Jimenez SA (2016) Treatment of Rapidly Progressive Systemic Sclerosis: Current and Futures Perspectives. Expert Opin Orphan Drugs 4: 31–47. https://doi.org/10.1517/21678707.2016.1114454</mixed-citation></ref><ref id="B117"><label>117.</label><mixed-citation>Ubil E, Duan J, Pillai ICL, Rosa-Garrido M, Wu Y, Bargiacchi F, Lu Y, Stanbouly S, Huang J, Rojas M, Vondriska TM, Stefani E, Deb A (2014) Mesenchymal-endothelial transition contributes to cardiac neovascularization. Nature 514: 585–590. https://doi.org/10.1038/nature13839</mixed-citation></ref><ref id="B118"><label>118.</label><mixed-citation>Muller L, Di Benedetto S (2023) From aging to long COVID: exploring the convergence of immunosenescence, inflammaging, and autoimmunity. Front Immunol 14: 1298004. https://doi.org/10.3389/fimmu.2023.1298004</mixed-citation></ref><ref id="B119"><label>119.</label><mixed-citation>Sorrenti V, Benedetti F, Buriani A, Fortinguerra S, Caudullo G, Davinelli S, Zella D, Scapagnini G (2022) Immunomodulatory and Antiaging Mechanisms of Resveratrol, Rapamycin, and Metformin: Focus on mTOR and AMPK Signaling Networks. Pharmaceuticals 15: 912. https://doi.org/10.3390/ph15080912</mixed-citation></ref><ref id="B120"><label>120.</label><mixed-citation>Immanuel J, Yun S (2023) Vascular Inflammatory Diseases and Endothelial Phenotypes. Cells 12: 1640. https://doi.org/10.3390/cells12121640</mixed-citation></ref><ref id="B121"><label>121.</label><mixed-citation>Edfeldt K, Swedenborg J, Hansson GK, Yan Z (2002) Expression of toll-like receptors in human atherosclerotic lesions: a possible pathway for plaque activation. Circulation 105: 1158–1161.</mixed-citation></ref><ref id="B122"><label>122.</label><mixed-citation>Leeuwenberg JF, Van Damme J, Meager T, Jeunhomme TM, Buurman WA (1988) Effects of tumor necrosis factor on the interferon-gamma-induced major histocompatibility complex class II antigen expression by human endothelial cells. Eur J Immunol 18: 1469–1472. https://doi.org/10.1002/eji.1830180925</mixed-citation></ref><ref id="B123"><label>123.</label><mixed-citation>Bradley JR, Johnson DR, Pober JS (1993) Endothelial activation by hydrogen peroxide. Selective increases of intercellular adhesion molecule-1 and major histocompatibility complex class I. Am J Pathol 142: 1598–1609.</mixed-citation></ref><ref id="B124"><label>124.</label><mixed-citation>Mishima K, Watabe T, Saito A, Yoshimatsu Y, Imaizumi N, Masui S, Hirashima M, Morisada T, Oike Y, Araie M, Niwa H, Kubo H, Suda T, Miyazono K (2007) Prox1 induces lymphatic endothelial differentiation via integrin alpha9 and other signaling cascades. Mol Biol Cell 18: 1421–1429. https://doi.org/10.1091/mbc.e06-09-0780</mixed-citation></ref><ref id="B125"><label>125.</label><mixed-citation>Johnson NC, Dillard ME, Baluk P, McDonald DM, Harvey NL, Frase SL, Oliver G (2008) Lymphatic endothelial cell identity is reversible and its maintenance requires Prox1 activity. Genes Dev 22: 3282–3291. https://doi.org/10.1101/gad.1727208</mixed-citation></ref><ref id="B126"><label>126.</label><mixed-citation>Andueza A, Kumar S, Kim J, Kang D-W, Mumme HL, Perez JI, Villa-Roel N, Jo H (2020) Endothelial Reprogramming by Disturbed Flow Revealed by Single-Cell RNA and Chromatin Accessibility Study. Cell Rep 33: 108491. https://doi.org/10.1016/j.celrep.2020.108491</mixed-citation></ref><ref id="B127"><label>127.</label><mixed-citation>Tamargo IA, Baek KI, Kim Y, Park C, Jo H (2023) Flow-induced reprogramming of endothelial cells in atherosclerosis. Nat Rev Cardiol 20: 738–753. https://doi.org/10.1038/s41569-023-00883-1</mixed-citation></ref><ref id="B128"><label>128.</label><mixed-citation>Mai J, Virtue A, Shen J, Wang H, Yang X-F (2013) An evolving new paradigm: endothelial cells – conditional innate immune cells. J Hematol Oncol 6: 61. https://doi.org/10.1186/1756-8722-6-61</mixed-citation></ref><ref id="B129"><label>129.</label><mixed-citation>Ghibelli L, Nosseri C, Coppola S, Maresca V, Dini L (1995) The increase in H2O2-induced apoptosis by ADP-ribosylation inhibitors is related to cell blebbing. Exp Cell Res 221: 470–477. https://doi.org/10.1006/excr.1995.1398</mixed-citation></ref><ref id="B130"><label>130.</label><mixed-citation>Yamauchi S, Kawamura K, Okamoto S, Morinaga T, Jiang Y, Shingyoji M, Sekine I, Kubo S, Tada Y, Tatsumi K, Shimada H, Hiroshima K, Tagawa M (2015) Replication-competent adenoviruses with the type 35-derived fiber-knob region achieve reactive oxygen species-dependent cytotoxicity and produce greater toxicity than those with the type 5-derived region in pancreatic carcinoma. Apoptosis Int J Program Cell Death 20: 1587–1598. https://doi.org/10.1007/s10495-015-1171-8</mixed-citation></ref><ref id="B131"><label>131.</label><mixed-citation>Rengarajan M, Hayer A, Theriot JA (2016) Endothelial Cells Use a Formin-Dependent Phagocytosis-Like Process to Internalize the Bacterium Listeria monocytogenes. PLoS Pathog 12: e1005603. https://doi.org/10.1371/journal.ppat.1005603</mixed-citation></ref><ref id="B132"><label>132.</label><mixed-citation>Belcher JD, Chen C, Nguyen J, Milbauer L, Abdulla F, Alayash AI, Smith A, Nath KA, Hebbel RP, Vercellotti GM (2014) Heme triggers TLR4 signaling leading to endothelial cell activation and vaso-occlusion in murine sickle cell disease. Blood 123: 377–390. https://doi.org/10.1182/blood-2013-04-495887</mixed-citation></ref><ref id="B133"><label>133.</label><mixed-citation>Kofler S, Nickel T, Weis M (2005) Role of cytokines in cardiovascular diseases: A focus on endothelial responses to inflammation. Clin Sci Lond Engl 1979 108: 205–213. https://doi.org/10.1042/CS20040174</mixed-citation></ref><ref id="B134"><label>134.</label><mixed-citation>Raucci A, Macrì F, Castiglione S, Badi I, Vinci MC, Zuccolo E (2021) MicroRNA-34a: the bad guy in age-related vascular diseases. Cell Mol Life Sci 78: 7355–7378. https://doi.org/10.1007/s00018-021-03979-4</mixed-citation></ref><ref id="B135"><label>135.</label><mixed-citation>Roth GA, Mensah GA, Johnson CO, Addolorato G, Ammirati E, Baddour LM, Barengo NC, Beaton AZ, Benjamin EJ, Benziger CP, Bonny A, Brauer M, Brodmann M, Cahill TJ, Carapetis J, Catapano AL, Chugh SS, Cooper LT, Coresh J, Criqui M, DeCleene N, Eagle KA, Emmons-Bell S, Feigin VL, Fernández-Solà J, Fowkes G, Gakidou E, Grundy SM, He FJ, Howard G, Hu F, Inker L, Karthikeyan G, Kassebaum N, Koroshetz W, Lavie C, Lloyd-Jones D, Lu HS, Mirijello A, Temesgen AM, Mokdad A, Moran AE, Muntner P, Narula J, Neal B, Ntsekhe M, Moraes De Oliveira G, Otto C, Owolabi M, Pratt M, Rajagopalan S, Reitsma M, Ribeiro ALP, Rigotti N, Rodgers A, Sable C, Shakil S, Sliwa-Hahnle K, Stark B, Sundström J, Timpel P, Tleyjeh IM, Valgimigli M, Vos T, Whelton PK, Yacoub M, Zuhlke L, Murray C, Fuster V, Roth GA, Mensah GA, Johnson CO, Addolorato G, Ammirati E, Baddour LM, Barengo NC, Beaton A, Benjamin EJ, Benziger CP, Bonny A, Brauer M, Brodmann M, Cahill TJ, Carapetis JR, Catapano AL, Chugh S, Cooper LT, Coresh J, Criqui MH, DeCleene NK, Eagle KA, Emmons-Bell S, Feigin VL, Fernández-Sola J, Fowkes FGR, Gakidou E, Grundy SM, He FJ, Howard G, Hu F, Inker L, Karthikeyan G, Kassebaum NJ, Koroshetz WJ, Lavie C, Lloyd-Jones D, Lu HS, Mirijello A, Misganaw AT, Mokdad AH, Moran AE, Muntner P, Narula J, Neal B, Ntsekhe M, Oliveira GMM, Otto CM, Owolabi MO, Pratt M, Rajagopalan S, Reitsma MB, Ribeiro ALP, Rigotti NA, Rodgers A, Sable CA, Shakil SS, Sliwa K, Stark BA, Sundström J, Timpel P, Tleyjeh II, Valgimigli M, Vos T, Whelton PK, Yacoub M, Zuhlke LJ, Abbasi-Kangevari M, Abdi A, Abedi A, Aboyans V, Abrha WA, Abu-Gharbieh E, Abushouk AI, Acharya D, Adair T, Adebayo OM, Ademi Z, Advani SM, Afshari K, Afshin A, Agarwal G, Agasthi P, Ahmad S, Ahmadi S, Ahmed MB, Aji B, Akalu Y, Akande-Sholabi W, Aklilu A, Akunna CJ, Alahdab F, Al-Eyadhy A, Alhabib KF, Alif SM, Alipour V, Aljunid SM, Alla F, Almasi-Hashiani A, Almustanyir S, Al-Raddadi RM, Amegah AK, Amini S, Aminorroaya A, Amu H, Amugsi DA, Ancuceanu R, Anderlini D, Andrei T, Andrei CL, Ansari-Moghaddam A, Anteneh ZA, Antonazzo IC, Antony B, Anwer R, Appiah LT, Arabloo J, Ärnlöv J, Artanti KD, Ataro Z, Ausloos M, Avila-Burgos L, Awan AT, Awoke MA, Ayele HT, Ayza MA, Azari S, B DB, Baheiraei N, Baig AA, Bakhtiari A, Banach M, Banik PC, Baptista EA, Barboza MA, Barua L, Basu S, Bedi N, Béjot Y, Bennett DA, Bensenor IM, Berman AE, Bezabih YM, Bhagavathula AS, Bhaskar S, Bhattacharyya K, Bijani A, Bikbov B, Birhanu MM, Boloor A, Brant LC, Brenner H, Briko NI, Butt ZA, Caetano Dos Santos FL, Cahill LE, Cahuana-Hurtado L, Cámera LA, Campos-Nonato IR, Cantu-Brito C, Car J, Carrero JJ, Carvalho F, Castañeda-Orjuela CA, Catalá-López F, Cerin E, Charan J, Chattu VK, Chen S, Chin KL, Choi J-YJ, Chu D-T, Chung S-C, Cirillo M, Coffey S, Conti S, Costa VM, Cundiff DK, Dadras O, Dagnew B, Dai X, Damasceno AAM, Dandona L, Dandona R, Davletov K, De La Cruz-Góngora V, De La Hoz FP, De Neve J-W, Denova-Gutiérrez E, Derbew Molla M, Derseh BT, Desai R, Deuschl G, Dharmaratne SD, Dhimal M, Dhungana RR, Dianatinasab M, Diaz D, Djalalinia S, Dokova K, Douiri A, Duncan BB, Duraes AR, Eagan AW, Ebtehaj S, Eftekhari A, Eftekharzadeh S, Ekholuenetale M, El Nahas N, Elgendy IY, Elhadi M, El-Jaafary SI, Esteghamati S, Etisso AE, Eyawo O, Fadhil I, Faraon EJA, Faris PS, Farwati M, Farzadfar F, Fernandes E, Fernandez Prendes C, Ferrara P, Filip I, Fischer F, Flood D, Fukumoto T, Gad MM, Gaidhane S, Ganji M, Garg J, Gebre AK, Gebregiorgis BG, Gebregzabiher KZ, Gebremeskel GG, Getacher L, Obsa AG, Ghajar A, Ghashghaee A, Ghith N, Giampaoli S, Gilani SA, Gill PS, Gillum RF, Glushkova EV, Gnedovskaya EV, Golechha M, Gonfa KB, Goudarzian AH, Goulart AC, Guadamuz JS, Guha A, Guo Y, Gupta R, Hachinski V, Hafezi-Nejad N, Haile TG, Hamadeh RR, Hamidi S, Hankey GJ, Hargono A, Hartono RK, Hashemian M, Hashi A, Hassan S, Hassen HY, Havmoeller RJ, Hay SI, Hayat K, Heidari G, Herteliu C, Holla R, Hosseini M, Hosseinzadeh M, Hostiuc M, Hostiuc S, Househ M, Huang J, Humayun A, Iavicoli I, Ibeneme CU, Ibitoye SE, Ilesanmi OS, Ilic IM, Ilic MD, Iqbal U, Irvani SSN, Islam SMS, Islam RM, Iso H, Iwagami M, Jain V, Javaheri T, Jayapal SK, Jayaram S, Jayawardena R, Jeemon P, Jha RP, Jonas JB, Jonnagaddala J, Joukar F, Jozwiak JJ, Jürisson M, Kabir A, Kahlon T, Kalani R, Kalhor R, Kamath A, Kamel I, Kandel H, Kandel A, Karch A, Kasa AS, Katoto PDMC, Kayode GA, Khader YS, Khammarnia M, Khan MS, Khan MN, Khan M, Khan EA, Khatab K, Kibria GMA, Kim YJ, Kim GR, Kimokoti RW, Kisa S, Kisa A, Kivimäki M, Kolte D, Koolivand A, Korshunov VA, Koulmane Laxminarayana SL, Koyanagi A, Krishan K, Krishnamoorthy V, Kuate Defo B, Kucuk Bicer B, Kulkarni V, Kumar GA, Kumar N, Kurmi OP, Kusuma D, Kwan GF, La Vecchia C, Lacey B, Lallukka T, Lan Q, Lasrado S, Lassi ZS, Lauriola P, Lawrence WR, Laxmaiah A, LeGrand KE, Li M-C, Li B, Li S, Lim SS, Lim L-L, Lin H, Lin Z, Lin R-T, Liu X, Lopez AD, Lorkowski S, Lotufo PA, Lugo A, M NK, Madotto F, Mahmoudi M, Majeed A, Malekzadeh R, Malik AA, Mamun AA, Manafi N, Mansournia MA, Mantovani LG, Martini S, Mathur MR, Mazzaglia G, Mehata S, Mehndiratta MM, Meier T, Menezes RG, Meretoja A, Mestrovic T, Miazgowski B, Miazgowski T, Michalek IM, Miller TR, Mirrakhimov EM, Mirzaei H, Moazen B, Moghadaszadeh M, Mohammad Y, Mohammad DK, Mohammed S, Mohammed MA, Mokhayeri Y, Molokhia M, Montasir AA, Moradi G, Moradzadeh R, Moraga P, Morawska L, Moreno Velásquez I, Morze J, Mubarik S, Muruet W, Musa KI, Nagarajan AJ, Nalini M, Nangia V, Naqvi AA, Narasimha Swamy S, Nascimento BR, Nayak VC, Nazari J, Nazarzadeh M, Negoi RI, Neupane Kandel S, Nguyen HLT, Nixon MR, Norrving B, Noubiap JJ, Nouthe BE, Nowak C, Odukoya OO, Ogbo FA, Olagunju AT, Orru H, Ortiz A, Ostroff SM, Padubidri JR, Palladino R, Pana A, Panda-Jonas S, Parekh U, Park E-C, Parvizi M, Pashazadeh Kan F, Patel UK, Pathak M, Paudel R, Pepito VCF, Perianayagam A, Perico N, Pham HQ, Pilgrim T, Piradov MA, Pishgar F, Podder V, Polibin RV, Pourshams A, Pribadi DRA, Rabiee N, Rabiee M, Radfar A, Rafiei A, Rahim F, Rahimi-Movaghar V, Ur Rahman MH, Rahman MA, Rahmani AM, Rakovac I, Ram P, Ramalingam S, Rana J, Ranasinghe P, Rao SJ, Rathi P, Rawal L, Rawasia WF, Rawassizadeh R, Remuzzi G, Renzaho AMN, Rezapour A, Riahi SM, Roberts-Thomson RL, Roever L, Rohloff P, Romoli M, Roshandel G, Rwegerera GM, Saadatagah S, Saber-Ayad MM, Sabour S, Sacco S, Sadeghi M, Saeedi Moghaddam S, Safari S, Sahebkar A, Salehi S, Salimzadeh H, Samaei M, Samy AM, Santos IS, Santric-Milicevic MM, Sarrafzadegan N, Sarveazad A, Sathish T, Sawhney M, Saylan M, Schmidt MI, Schutte AE, Senthilkumaran S, Sepanlou SG, Sha F, Shahabi S, Shahid I, Shaikh MA, Shamali M, Shamsizadeh M, Shawon MSR, Sheikh A, Shigematsu M, Shin M-J, Shin JI, Shiri R, Shiue I, Shuval K, Siabani S, Siddiqi TJ, Silva DAS, Singh JA, Mtech AS, Skryabin VY, Skryabina AA, Soheili A, Spurlock EE, Stockfelt L, Stortecky S, Stranges S, Suliankatchi Abdulkader R, Tadbiri H, Tadesse EG, Tadesse DB, Tajdini M, Tariqujjaman M, Teklehaimanot BF, Temsah M-H, Tesema AK, Thakur B, Thankappan KR, Thapar R, Thrift AG, Timalsina B, Tonelli M, Touvier M, Tovani-Palone MR, Tripathi A, Tripathy JP, Truelsen TC, Tsegay GM, Tsegaye GW, Tsilimparis N, Tusa BS, Tyrovolas S, Umapathi KK, Unim B, Unnikrishnan B, Usman MS, Vaduganathan M, Valdez PR, Vasankari TJ, Velazquez DZ, Venketasubramanian N, Vu GT, Vujcic IS, Waheed Y, Wang Y, Wang F, Wei J, Weintraub RG, Weldemariam AH, Westerman R, Winkler AS, Wiysonge CS, Wolfe CDA, Wubishet BL, Xu G, Yadollahpour A, Yamagishi K, Yan LL, Yandrapalli S, Yano Y, Yatsuya H, Yeheyis TY, Yeshaw Y, Yilgwan CS, Yonemoto N, Yu C, Yusefzadeh H, Zachariah G, Zaman SB, Zaman MS, Zamanian M, Zand R, Zandifar A, Zarghi A, Zastrozhin MS, Zastrozhina A, Zhang Z-J, Zhang Y, Zhang W, Zhong C, Zou Z, Zuniga YMH, Murray CJL, Fuster V (2020) Global Burden of Cardiovascular Diseases and Risk Factors, 1990–2019. J Am Coll Cardiol 76: 2982–3021. https://doi.org/10.1016/j.jacc.2020.11.010</mixed-citation></ref><ref id="B136"><label>136.</label><mixed-citation>Ohlsson L (2010) Dairy products and plasma cholesterol levels. Food Nutr Res 54: 5124. https://doi.org/10.3402/fnr.v54i0.5124</mixed-citation></ref><ref id="B137"><label>137.</label><mixed-citation>Forrester JS (2010) Redefining normal low-density lipoprotein cholesterol: A strategy to unseat coronary disease as the nation’s leading killer. J Am Coll Cardiol 56: 630–636. https://doi.org/10.1016/j.jacc.2009.11.090</mixed-citation></ref><ref id="B138"><label>138.</label><mixed-citation>Packard RRS, Libby P (2008) Inflammation in atherosclerosis: From vascular biology to biomarker discovery and risk prediction. Clin Chem 54: 24–38. https://doi.org/10.1373/clinchem.2007.097360</mixed-citation></ref><ref id="B139"><label>139.</label><mixed-citation>Miller YI, Choi S-H, Fang L, Tsimikas S (2010) Lipoprotein modification and macrophage uptake: Role of pathologic cholesterol transport in atherogenesis. Subcell Biochem 51: 229–251. https://doi.org/10.1007/978-90-481-8622-8_8</mixed-citation></ref><ref id="B140"><label>140.</label><mixed-citation>Dallinga-Thie GM, Franssen R, Mooij HL, Visser ME, Hassing HC, Peelman F, Kastelein JJP, Péterfy M, Nieuwdorp M (2010) The metabolism of triglyceride-rich lipoproteins revisited: new players, new insight. Atherosclerosis 211: 1–8. https://doi.org/10.1016/j.atherosclerosis.2009.12.027</mixed-citation></ref><ref id="B141"><label>141.</label><mixed-citation>Badimón L, Vilahur G, Padró T (2009) Lipoproteins, platelets and atherothrombosis. Rev Esp Cardiol 62: 1161–1178. https://doi.org/10.1016/s1885-5857(09)73331-6</mixed-citation></ref><ref id="B142"><label>142.</label><mixed-citation>Ishigaki Y, Oka Y, Katagiri H (2009) Circulating oxidized LDL: A biomarker and a pathogenic factor. Curr Opin Lipidol 20: 363–369. https://doi.org/10.1097/MOL.0b013e32832fa58d</mixed-citation></ref><ref id="B143"><label>143.</label><mixed-citation>Twardowski L, Cheng F, Michaelsen J, Winter S, Hofmann U, Schaeffeler E, Müller S, Sonnenberg M, Steuer K, Ott G, Schwab M, Franke UFW, Torzewski M (2015) Enzymatically Modified Low‐Density Lipoprotein Is Present in All Stages of Aortic Valve Sclerosis: Implications for Pathogenesis of the Disease. J Am Heart Assoc 4: e002156. https://doi.org/10.1161/JAHA.115.002156</mixed-citation></ref><ref id="B144"><label>144.</label><mixed-citation>Orekhov AN, Melnichenko AA, Sobenin IA (2014) Approach to Reduction of Blood Atherogenicity. Oxid Med Cell Longev 2014: 1–8. https://doi.org/10.1155/2014/738679</mixed-citation></ref><ref id="B145"><label>145.</label><mixed-citation>Sukhorukov VN, Karagodin VP, Orekhov AN (2016) Atherogenic modification of low-density lipoproteins. Biomed Khim 62: 391–402. https://doi.org/10.18097/pbmc20166204391</mixed-citation></ref><ref id="B146"><label>146.</label><mixed-citation>Nikifirov NG, Zakiev ER, Elizova NV, Sukhorukov VN, Orekhov AN (2017) Multiple-modified Low-Density Lipoprotein as Atherogenic Factor of Patients’; Blood: Development of Therapeutic Approaches to Reduce Blood Atherogenicity. Curr Pharm Des 23: 932–936. https://doi.org/10.2174/1381612823666170124112918</mixed-citation></ref><ref id="B147"><label>147.</label><mixed-citation>Palinski W, Rosenfeld ME, Ylä-Herttuala S, Gurtner GC, Socher SS, Butler SW, Parthasarathy S, Carew TE, Steinberg D, Witztum JL (1989) Low density lipoprotein undergoes oxidative modification in vivo. Proc Natl Acad Sci U S A 86: 1372–1376. https://doi.org/10.1073/pnas.86.4.1372</mixed-citation></ref><ref id="B148"><label>148.</label><mixed-citation>Orekhov AN, Tertov VV, Mukhin DN, Mikhailenko IA (1989) Modification of low density lipoprotein by desialylation causes lipid accumulation in cultured cells: Discovery of desialylated lipoprotein with altered cellular metabolism in the blood of atherosclerotic patients. Biochem Biophys Res Commun 162: 206–211. https://doi.org/10.1016/0006-291x(89)91982-7</mixed-citation></ref><ref id="B149"><label>149.</label><mixed-citation>Orekhov AN, Tertov VV, Kabakov AE, Adamova IYu, Pokrovsky SN, Smirnov VN (1991) Autoantibodies against modified low density lipoprotein. Nonlipid factor of blood plasma that stimulates foam cell formation. Arterioscler Thromb 11: 316–326. https://doi.org/10.1161/01.ATV.11.2.316</mixed-citation></ref><ref id="B150"><label>150.</label><mixed-citation>Tertov VV, Kaplun VV, Sobenin IA, Orekhov AN (1998) Low-density lipoprotein modification occurring in human plasma possible mechanism of in vivo lipoprotein desialylation as a primary step of atherogenic modification. Atherosclerosis 138: 183–195. https://doi.org/10.1016/s0021-9150(98)00023-9</mixed-citation></ref><ref id="B151"><label>151.</label><mixed-citation>Orekhov A, Khotina V, Sukhorukov V, Sobenin I (2024) Non-oxidative vs Oxidative Forms of Modified Low-density Lipoprotein: What is More Important in Atherogenesis? Curr Med Chem 31: 2309–2313. https://doi.org/10.2174/0109298673294245240102105814</mixed-citation></ref><ref id="B152"><label>152.</label><mixed-citation>Schauer R (2009) Sialic acids as regulators of molecular and cellular interactions. Curr Opin Struct Biol 19: 507–514. https://doi.org/10.1016/j.sbi.2009.06.003</mixed-citation></ref><ref id="B153"><label>153.</label><mixed-citation>Iijima R, Takahashi H, Namme R, Ikegami S, Yamazaki M (2004) Novel biological function of sialic acid (N-acetylneuraminic acid) as a hydrogen peroxide scavenger. FEBS Lett 561: 163–166.https://doi.org/10.1016/S0014-5793(04)00164-4</mixed-citation></ref><ref id="B154"><label>154.</label><mixed-citation>Ogasawara Y, Namai T, Yoshino F, Lee M-C, Ishii K (2007) Sialic acid is an essential moiety of mucin as a hydroxyl radical scavenger. FEBS Lett 581: 2473–2477. https://doi.org/10.1016/j.febslet.2007.04.062</mixed-citation></ref><ref id="B155"><label>155.</label><mixed-citation>Volkhina IV, Butolin EG (2022) Clinical and Diagnostic Significance of Sialic Acids Determination in Biological Material. Biochem Mosc Suppl Ser B Biomed Chem 16: 165–174. https://doi.org/10.1134/S199075082203012X</mixed-citation></ref><ref id="B156"><label>156.</label><mixed-citation>Fujioka Y, Taniguchi T, Ishikawa Y, Yokoyama M (2000) Significance of acidic sugar chains of apolipoprotein B-100 in cellular metabolism of low-density lipoproteins. J Lab Clin Med 136: 355–362. https://doi.org/10.1067/mlc.2000.110103</mixed-citation></ref><ref id="B157"><label>157.</label><mixed-citation>Miyagi T, Wada T, Yamaguchi K, Hata K, Shiozaki K (2008) Plasma membrane-associated sialidase as a crucial regulator of transmembrane signalling. J Biochem (Tokyo) 144: 279–285. https://doi.org/10.1093/jb/mvn089</mixed-citation></ref><ref id="B158"><label>158.</label><mixed-citation>Buschiazzo A, Alzari PM (2008) Structural insights into sialic acid enzymology. Curr Opin Chem Biol 12: 565–572. https://doi.org/10.1016/j.cbpa.2008.06.017</mixed-citation></ref><ref id="B159"><label>159.</label><mixed-citation>Datta AK (2009) Comparative sequence analysis in the sialyltransferase protein family: Analysis of motifs. Curr Drug Targets 10: 483–498. https://doi.org/10.2174/138945009788488422</mixed-citation></ref><ref id="B160"><label>160.</label><mixed-citation>Juge N, Tailford L, Owen CD (2016) Sialidases from gut bacteria: A mini-review. Biochem Soc Trans 44: 166–175. https://doi.org/10.1042/BST20150226</mixed-citation></ref><ref id="B161"><label>161.</label><mixed-citation>Neres J, Bryce RA, Douglas KT (2008) Rational drug design in parasitology: Trans-sialidase as a case study for Chagas disease. Drug Discov Today 13: 110–117. https://doi.org/10.1016/j.drudis.2007.12.004</mixed-citation></ref><ref id="B162"><label>162.</label><mixed-citation>Lipničanová S, Chmelová D, Ondrejovič M, Frecer V, Miertuš S (2020) Diversity of sialidases found in the human body – A review. Int J Biol Macromol 148: 857–868. https://doi.org/10.1016/j.ijbiomac.2020.01.123</mixed-citation></ref><ref id="B163"><label>163.</label><mixed-citation>Keil JM, Rafn GR, Turan IM, Aljohani MA, Sahebjam-Atabaki R, Sun X-L (2022) Sialidase Inhibitors with Different Mechanisms. J Med Chem 65: 13574–13593. https://doi.org/10.1021/acs.jmedchem.2c01258</mixed-citation></ref><ref id="B164"><label>164.</label><mixed-citation>Eguchi H, Ikeda Y, Ookawara T, Koyota S, Fujiwara N, Honke K, Wang PG, Taniguchi N, Suzuki K (2005) Modification of oligosaccharides by reactive oxygen species decreases sialyl lewis x-mediated cell adhesion. Glycobiology 15: 1094–1101. https://doi.org/10.1093/glycob/cwj003</mixed-citation></ref><ref id="B165"><label>165.</label><mixed-citation>Sun L, Wang L, Ye KX, Wang S, Zhang R, Juan Z, Feng L, Min S (2023) Endothelial Glycocalyx in Aging and Age-related Diseases. Aging Dis 14: 1606. https://doi.org/10.14336/AD.2023.0131</mixed-citation></ref><ref id="B166"><label>166.</label><mixed-citation>Cerne D, Jürgens G, Ledinski G, Kager G, Greilberger J, Lukac-Bajalo J (2002) Relationship between the sialic acid content of low-density lipoprotein (LDL) and autoantibodies to oxidized LDL in the plasma of healthy subjects and patients with atherosclerosis. Clin Chem Lab Med 40: 15–20. https://doi.org/10.1515/CCLM.2002.004</mixed-citation></ref><ref id="B167"><label>167.</label><mixed-citation>Cheeseman J, Kuhnle G, Stafford G, Gardner RA, Spencer DI, Osborn HM (2021) Sialic acid as a potential biomarker for cardiovascular disease, diabetes and cancer. Biomark Med 15: 911–928. https://doi.org/10.2217/bmm-2020-0776</mixed-citation></ref><ref id="B168"><label>168.</label><mixed-citation>Mezentsev A, Bezsonov E, Kashirskikh D, Baig MS, Eid AH, Orekhov A (2021) Proatherogenic Sialidases and Desialylated Lipoproteins: 35 Years of Research and Current State from Bench to Bedside. Biomedicines 9: 600. https://doi.org/10.3390/biomedicines9060600</mixed-citation></ref><ref id="B169"><label>169.</label><mixed-citation>Mehr K, Withers SG (2016) Mechanisms of the sialidase and trans-sialidase activities of bacterial sialyltransferases from glycosyltransferase family 80. Glycobiology 26: 353–359. https://doi.org/10.1093/glycob/cwv105</mixed-citation></ref><ref id="B170"><label>170.</label><mixed-citation>Kuro-o M (2009) Klotho and aging. Biochim Biophys Acta BBA – Gen Subj 1790: 1049–1058. https://doi.org/10.1016/j.bbagen.2009.02.005</mixed-citation></ref><ref id="B171"><label>171.</label><mixed-citation>Cuniberti LA, Martinez V, Schachter J, Magariños G, Meckert PC, Laguens RP, Levenson J, Werba JP (2005) Sialic acid as a protective barrier against neointima development. Atherosclerosis 181: 225–231. https://doi.org/10.1016/j.atherosclerosis.2005.01.021</mixed-citation></ref><ref id="B172"><label>172.</label><mixed-citation>Görög P, Born GV (1982) Increased adhesiveness of granulocytes in rabbit ear-chamber blood vessels perfused with neuraminidase. Microvasc Res 23: 380–384. https://doi.org/10.1016/s0026-2862(82)80010-1</mixed-citation></ref><ref id="B173"><label>173.</label><mixed-citation>Betteridge KB, Arkill KP, Neal CR, Harper SJ, Foster RR, Satchell SC, Bates DO, Salmon AHJ (2017) Sialic acids regulate microvessel permeability, revealed by novel in vivo studies of endothelial glycocalyx structure and function. J Physiol 595: 5015–5035. https://doi.org/10.1113/JP274167</mixed-citation></ref><ref id="B174"><label>174.</label><mixed-citation>Psefteli P-M, Kitscha P, Vizcay G, Fleck R, Chapple SJ, Mann GE, Fowler M, Siow RC (2021) Glycocalyx sialic acids regulate Nrf2-mediated signaling by fluid shear stress in human endothelial cells. Redox Biol 38: 101816. https://doi.org/10.1016/j.redox.2020.101816</mixed-citation></ref><ref id="B175"><label>175.</label><mixed-citation>Miyagi T, Yamaguchi K (2012) Mammalian sialidases: Physiological and pathological roles in cellular functions. Glycobiology 22: 880–896. https://doi.org/10.1093/glycob/cws057</mixed-citation></ref><ref id="B176"><label>176.</label><mixed-citation>Sakarya S, Rifat S, Zhou J, Bannerman DD, Stamatos NM, Cross AS, Goldblum SE (2004) Mobilization of neutrophil sialidase activity desialylates the pulmonary vascular endothelial surface and increases resting neutrophil adhesion to and migration across the endothelium. Glycobiology 14: 481–494. https://doi.org/10.1093/glycob/cwh065</mixed-citation></ref><ref id="B177"><label>177.</label><mixed-citation>Amith SR, Jayanth P, Franchuk S, Finlay T, Seyrantepe V, Beyaert R, Pshezhetsky AV, Szewczuk MR (2010) Neu1 desialylation of sialyl alpha-2,3-linked beta-galactosyl residues of TOLL-like receptor 4 is essential for receptor activation and cellular signaling. Cell Signal 22: 314–324. https://doi.org/10.1016/j.cellsig.2009.09.038</mixed-citation></ref><ref id="B178"><label>178.</label><mixed-citation>Kawabe J, Hasebe N (2014) Role of the Vasa Vasorum and Vascular Resident Stem Cells in Atherosclerosis. Biomed Res Int 2014: 1–8. https://doi.org/10.1155/2014/701571</mixed-citation></ref><ref id="B179"><label>179.</label><mixed-citation>Sedding DG, Boyle EC, Demandt JAF, Sluimer JC, Dutzmann J, Haverich A, Bauersachs J (2018) Vasa Vasorum Angiogenesis: Key Player in the Initiation and Progression of Atherosclerosis and Potential Target for the Treatment of Cardiovascular Disease. Front Immunol 9: 706. https://doi.org/10.3389/fimmu.2018.00706</mixed-citation></ref><ref id="B180"><label>180.</label><mixed-citation>Shimizu Y (2022) Mechanism underlying vascular remodeling in relation to circulating CD34-positive cells among older Japanese men. Sci Rep 12: 21823. https://doi.org/10.1038/s41598-022-26089-y</mixed-citation></ref><ref id="B181"><label>181.</label><mixed-citation>Koueik J, Wesley UV, Dempsey RJ (2023) Pathophysiology, cellular and molecular mechanisms of large and small vessel diseases. Neurochem Int 164: 105499. https://doi.org/10.1016/j.neuint.2023.105499</mixed-citation></ref><ref id="B182"><label>182.</label><mixed-citation>Erdő F, Krajcsi P (2019) Age-Related Functional and Expressional Changes in Efflux Pathways at the Blood-Brain Barrier. Front Aging Neurosci 11: 196. https://doi.org/10.3389/fnagi.2019.00196</mixed-citation></ref><ref id="B183"><label>183.</label><mixed-citation>Sweeney MD, Zhao Z, Montagne A, Nelson AR, Zlokovic BV (2019) Blood-Brain Barrier: From Physiology to Disease and Back. Physiol Rev 99: 21–78. https://doi.org/10.1152/physrev.00050.2017</mixed-citation></ref><ref id="B184"><label>184.</label><mixed-citation>Khatri R, McKinney AM, Swenson B, Janardhan V (2012) Blood-brain barrier, reperfusion injury, and hemorrhagic transformation in acute ischemic stroke. Neurology 79. https://doi.org/10.1212/WNL.0b013e3182697e70</mixed-citation></ref><ref id="B185"><label>185.</label><mixed-citation>Lekoubou A, Ssentongo P, Maffie J, Debroy K, Kwon M, Nguyen C, Pelton M, Watt B, Ceasar J, Dinunno N, Satyasi V, Pascal Kengne A, Bonilha L, Chinchilli VM (2023) Associations of small vessel disease and acute symptomatic seizures in ischemic stroke patients. Epilepsy Behav 145: 109233. https://doi.org/10.1016/j.yebeh.2023.109233</mixed-citation></ref><ref id="B186"><label>186.</label><mixed-citation>Zhou D, Meng R, Li S, Ya J, Ding J, Shang S, Ding Y, Ji X (2018) Advances in chronic cerebral circulation insufficiency. CNS Neurosci Ther 24: 5–17. https://doi.org/10.1111/cns.12780</mixed-citation></ref><ref id="B187"><label>187.</label><mixed-citation>Safouris A, Hambye A-S, Sculier C, Papageorgiou SG, Vasdekis SN, Gazagnes M-D, Tsivgoulis G (2015) Chronic brain hypoperfusion due to multi-vessel extracranial atherosclerotic disease: A potentially reversible cause of cognitive impairment. J Alzheimers Dis 43: 23–27. https://doi.org/10.3233/JAD-141203</mixed-citation></ref><ref id="B188"><label>188.</label><mixed-citation>Wang Y, Tu D, Du J, Han X, Sun Y, Xu Q, Zhai G, Zhou Y (2019) Classification of Subcortical Vascular Cognitive Impairment Using Single MRI Sequence and Deep Learning Convolutional Neural Networks. Front Neurosci 13: 627. https://doi.org/10.3389/fnins.2019.00627</mixed-citation></ref><ref id="B189"><label>189.</label><mixed-citation>Jokinen H (2006) Cognitive profile of subcortical ischaemic vascular disease. J Neurol Neurosurg Psychiatry 77: 28–33. https://doi.org/10.1136/jnnp.2005.069120</mixed-citation></ref><ref id="B190"><label>190.</label><mixed-citation>Vilar-Bergua A, Riba-Llena I, Nafría C, Bustamante A, Llombart V, Delgado P, Montaner J (2016) Blood and CSF biomarkers in brain subcortical ischemic vascular disease: Involved pathways and clinical applicability. J Cereb Blood Flow Metab 36: 55–71. https://doi.org/10.1038/jcbfm.2015.68</mixed-citation></ref><ref id="B191"><label>191.</label><mixed-citation>Bataille S, Baralla C, Torro D, Buffat C, Berland Y, Alazia M, Loundou A, Michelet P, Vacher-Coponat H (2014) Undercorrection of hypernatremia is frequent and associated with mortality. BMC Nephrol 15: 37. https://doi.org/10.1186/1471-2369-15-37</mixed-citation></ref><ref id="B192"><label>192.</label><mixed-citation>Liamis G, Barkas F, Megapanou E, Christopoulou E, Makri A, Makaritsis K, Ntaios G, Elisaf M, Milionis H (2019) Hyponatremia in Acute Stroke Patients: Pathophysiology, Clinical Significance, and Management Options. Eur Neurol 82: 32–40. https://doi.org/10.1159/000504475</mixed-citation></ref><ref id="B193"><label>193.</label><mixed-citation>Caruso P, Signori R, Moretti R (2019) Small vessel disease to subcortical dementia: A dynamic model, which interfaces aging, cholinergic dysregulation and the neurovascular unit. Vasc Health Risk Manag 15: 259–281. https://doi.org/10.2147/VHRM.S190470</mixed-citation></ref><ref id="B194"><label>194.</label><mixed-citation>Arvanitakis Z, Capuano AW, Leurgans SE, Bennett DA, Schneider JA (2016) Relation of cerebral vessel disease to Alzheimer’s disease dementia and cognitive function in elderly people: A cross-sectional study. Lancet Neurol 15: 934–943. https://doi.org/10.1016/S1474-4422(16)30029-1</mixed-citation></ref><ref id="B195"><label>195.</label><mixed-citation>Qiu F, Huang Y, Saunders NR, Habgood MD, Dziegielewska KM (2022) Age dependent contribution of entry via the CSF to the overall brain entry of small and large hydrophilic markers. Fluids Barriers CNS 19: 90. https://doi.org/10.1186/s12987-022-00387-z</mixed-citation></ref><ref id="B196"><label>196.</label><mixed-citation>LeVine SM (2016) Albumin and multiple sclerosis. BMC Neurol 16: 47. https://doi.org/10.1186/s12883-016-0564-9</mixed-citation></ref><ref id="B197"><label>197.</label><mixed-citation>Candeloro R, Ferri C, Bellini T, Pugliatti M, Castellazzi M (2024) Breaking Barriers: Unveiling Sex-Related Differences in Cerebrospinal Fluid Analysis–A Narrative Review. Biology 13: 420. https://doi.org/10.3390/biology13060420</mixed-citation></ref><ref id="B198"><label>198.</label><mixed-citation>Toyama K, Spin JM, Mogi M, Tsao PS (2019) Therapeutic perspective on vascular cognitive impairment. Pharmacol Res 146: 104266. https://doi.org/10.1016/j.phrs.2019.104266</mixed-citation></ref><ref id="B199"><label>199.</label><mixed-citation>Shen R, Ardianto C, Celia C, Sidharta VM, Sasmita PK, Satriotomo I, Turana Y (2023) Brain-derived neurotrophic factor interplay with oxidative stress: Neuropathology approach in potential biomarker of Alzheimer’s disease. Dement Neuropsychol 17: e20230012. https://doi.org/10.1590/1980-5764-dn-2023-0012</mixed-citation></ref><ref id="B200"><label>200.</label><mixed-citation>Zinellu A, Tommasi S, Sedda S, Mangoni AA (2023) Circulating arginine metabolites in Alzheimer’s disease and vascular dementia: A systematic review and meta-analysis. Ageing Res Rev 92: 102139.https://doi.org/10.1016/j.arr.2023.102139</mixed-citation></ref><ref id="B201"><label>201.</label><mixed-citation>Goncharov NV, Popova PI, Kudryavtsev IV, Golovkin AS, Savitskaya IV, Avdonin PP, Korf EA, Voitenko NG, Belinskaia DA, Serebryakova MK, Matveeva NV, Gerlakh NO, Anikievich NE, Gubatenko MA, Dobrylko IA, Trulioff AS, Aquino AD, Jenkins RO, Avdonin PV (2024) Immunological Profile and Markers of Endothelial Dysfunction in Elderly Patients with Cognitive Impairments. Int J Mol Sci 25: 1888. https://doi.org/10.3390/ijms25031888</mixed-citation></ref><ref id="B202"><label>202.</label><mixed-citation>Asgari R, Vaisi-Raygani A, Aleagha MSE, Mohammadi P, Bakhtiari M, Arghiani N (2023) CD147 and MMPs as key factors in physiological and pathological processes. Biomed Pharmacother 157: 113983. https://doi.org/10.1016/j.biopha.2022.113983</mixed-citation></ref><ref id="B203"><label>203.</label><mixed-citation>Nisa A, Kumar R, Ramasamy S, Kolloli A, Olejnik J, Jalloh S, Gummuluru S, Subbian S, Bushkin Y (2024) Modulations of Homeostatic ACE2, CD147, GRP78 Pathways Correlate with Vascular and Endothelial Performance Markers during Pulmonary SARS-CoV-2 Infection. Cells 13: 432. https://doi.org/10.3390/cells13050432</mixed-citation></ref><ref id="B204"><label>204.</label><mixed-citation>Cunnane SC, Swerdlow RH, Inzitari M, Olaso‐Gonzalez G, Viña J (2022) Multimodal strategy to rescue the brain in mild cognitive impairment: Ketogenic oral nutrition supplementation with B vitamins and aerobic exercise. Eur J Clin Invest 52: e13806. https://doi.org/10.1111/eci.13806</mixed-citation></ref><ref id="B205"><label>205.</label><mixed-citation>Guzman-Martinez L, Calfío C, Farias GA, Vilches C, Prieto R, Maccioni RB (2021) New Frontiers in the Prevention, Diagnosis, and Treatment of Alzheimer’s Disease. J Alzheimers Dis 82: S51–S63. https://doi.org/10.3233/JAD-201059</mixed-citation></ref><ref id="B206"><label>206.</label><mixed-citation>Voss MW, Sutterer M, Weng TB, Burzynska AZ, Fanning J, Salerno E, Gothe NP, Ehlers DK, McAuley E, Kramer AF (2019) Nutritional supplementation boosts aerobic exercise effects on functional brain systems. J Appl Physiol 126: 77–87. https://doi.org/10.1152/japplphysiol.00917.2017</mixed-citation></ref><ref id="B207"><label>207.</label><mixed-citation>Königstein K, Dipla K, Zafeiridis A (2023) Training the Vessels: Molecular and Clinical Effects of Exercise on Vascular Health–A Narrative Review. Cells 12: 2544. https://doi.org/10.3390/cells12212544</mixed-citation></ref><ref id="B208"><label>208.</label><mixed-citation>Benincasa G, Coscioni E, Napoli C (2022) Cardiovascular risk factors and molecular routes underlying endothelial dysfunction: Novel opportunities for primary prevention. Biochem Pharmacol 202: 115108. https://doi.org/10.1016/j.bcp.2022.115108</mixed-citation></ref><ref id="B209"><label>209.</label><mixed-citation>Baldassarre MPA, Pipino C, Pandolfi A, Consoli A, Di Pietro N, Formoso G (2021) Old and New Biomarkers Associated with Endothelial Dysfunction in Chronic Hyperglycemia. Oxid Med Cell Longev 2021: 7887426. https://doi.org/10.1155/2021/7887426</mixed-citation></ref></ref-list></back></article>
