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<article article-type="research-article" dtd-version="1.3" xmlns:mml="http://www.w3.org/1998/Math/MathML" xmlns:xlink="http://www.w3.org/1999/xlink" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xml:lang="ru"><front><journal-meta><journal-id journal-id-type="publisher-id">ssmu</journal-id><journal-title-group><journal-title xml:lang="ru">Бюллетень сибирской медицины</journal-title><trans-title-group xml:lang="en"><trans-title>Bulletin of Siberian Medicine</trans-title></trans-title-group></journal-title-group><issn pub-type="ppub">1682-0363</issn><issn pub-type="epub">1819-3684</issn><publisher><publisher-name>Siberian State Medical University, the Ministry of Healthcare of the Russian Federation</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="doi">10.20538/1682-0363-2025-4-184-193</article-id><article-id custom-type="elpub" pub-id-type="custom">ssmu-6281</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 И ЛЕКЦИИ</subject></subj-group><subj-group subj-group-type="section-heading" xml:lang="en"><subject>REVIEW AND LECTURES</subject></subj-group></article-categories><title-group><article-title>Галектин-1 и -3: внутриклеточные пути сигнальной трансдукции в канцерогенезе (лекция)</article-title><trans-title-group xml:lang="en"><trans-title>Galectin-1 and -3: intracellular pathways of signal transduction in carcinogenesis (lecture)</trans-title></trans-title-group></title-group><contrib-group><contrib contrib-type="author" corresp="yes"><contrib-id contrib-id-type="orcid">https://orcid.org/0000-0001-7078-4988</contrib-id><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Серебрякова</surname><given-names>В. A.</given-names></name><name name-style="western" xml:lang="en"><surname>Serebryakova</surname><given-names>V. A.</given-names></name></name-alternatives><bio xml:lang="ru"><p>Серебрякова Валентина Александровна – д-р мед. наук, доцент, профессор кафедры фармакологии</p><p>634050, г. Томск, Московский тракт, 2</p></bio><bio xml:lang="en"><p>2 Moscovsky trakt, 634050 Tomsk</p></bio><email xlink:type="simple">serebryakova-val@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/0000-0001-6132-9617</contrib-id><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Головина</surname><given-names>Е. Л.</given-names></name><name name-style="western" xml:lang="en"><surname>Golovina</surname><given-names>E. L.</given-names></name></name-alternatives><bio xml:lang="ru"><p>Головина Евгения Леонидовна – канд. мед. наук, доцент кафедры фармакологии</p><p>634050, г. Томск, Московский тракт, 2</p></bio><bio xml:lang="en"><p>2 Moscovsky trakt, 634050 Tomsk</p></bio><email xlink:type="simple">golovina.el@ssmu.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/0000-0001-8405-5655</contrib-id><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Мелешко</surname><given-names>М. В.</given-names></name><name name-style="western" xml:lang="en"><surname>Meleshko</surname><given-names>M. V.</given-names></name></name-alternatives><bio xml:lang="ru"><p>Мелешко Марина Владимировна – канд. биол. наук, доцент кафедры фармакологии</p><p>634050, г. Томск, Московский тракт, 2</p></bio><bio xml:lang="en"><p>2 Moscovsky trakt, 634050 Tomsk</p></bio><email xlink:type="simple">meleshko.mv@ssmu.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/0000-0003-4083-976X</contrib-id><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Ваизова</surname><given-names>О. Е.</given-names></name><name name-style="western" xml:lang="en"><surname>Vaizova</surname><given-names>O. E.</given-names></name></name-alternatives><bio xml:lang="ru"><p>Ваизова Ольга Евгеньевна – д-р мед. наук, профессор, профессор кафедры фармакологии</p><p>634050, г. Томск, Московский тракт, 2</p></bio><bio xml:lang="en"><p>2 Moscovsky trakt, 634050 Tomsk</p></bio><email xlink:type="simple">vaizova@mail.ru</email><xref ref-type="aff" rid="aff-1"/></contrib></contrib-group><aff-alternatives id="aff-1"><aff xml:lang="ru"><institution>Сибирский государственный медицинский университет (СибГМУ)</institution><country>Россия</country></aff><aff xml:lang="en"><institution>Siberian State Medical University (SibSMU)</institution><country>Russian Federation</country></aff></aff-alternatives><pub-date pub-type="collection"><year>2025</year></pub-date><pub-date pub-type="epub"><day>14</day><month>01</month><year>2026</year></pub-date><volume>24</volume><issue>4</issue><fpage>184</fpage><lpage>193</lpage><permissions><copyright-statement>Copyright &amp;#x00A9; Серебрякова В.A., Головина Е.Л., Мелешко М.В., Ваизова О.Е., 2025</copyright-statement><copyright-year>2025</copyright-year><copyright-holder xml:lang="ru">Серебрякова В.A., Головина Е.Л., Мелешко М.В., Ваизова О.Е.</copyright-holder><copyright-holder xml:lang="en">Serebryakova V.A., Golovina E.L., Meleshko M.V., Vaizova O.E.</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://bulletin.ssmu.ru/jour/article/view/6281">https://bulletin.ssmu.ru/jour/article/view/6281</self-uri><abstract><p>Лекция разработана на основе анализа данных экспериментальных работ и обзорных статей, представленных в базе данных PubMed. Лекция состоит из пяти частей, обобщающих данные литературы о галектине-1 и -3 с позиции их модулирующего действия в процессах сигнальной трансдукции. Рассмотрены возможные механизмы участия галектина-1 и -3 в пролиферации, апоптозе, ангиогенезе, миграции и адгезии опухолевых клеток. Данные, представленные в лекции, позволяют обозначить внутриклеточные молекулы-посредники, качественные или количественные изменения которых способны доказать действие соединений-кандидатов ингибиторов галектинов-1 и -3 как потенциальных противоопухолевых средств.</p></abstract><trans-abstract xml:lang="en"><p>The lecture was created following the analysis of experimental data and review articles presented in the PubMed database. The lecture consists of five parts summarizing the literature data on galectin-1 and -3 in terms of their modulating effect in signal transduction processes. Possible mechanisms of galectin-1 and -3 involvement in proliferation, apoptosis, angiogenesis, migration, and adhesion of tumor cells are considered. The lecture data make it possible to identify intracellular signaling molecules, whose qualitative or quantitative changes can prove the effect of candidate compounds of galectin-1 and -3 inhibitors as potential antitumor agents.</p></trans-abstract><kwd-group xml:lang="ru"><kwd>галектин-1</kwd><kwd>галектин-3</kwd><kwd>пролиферация</kwd><kwd>апоптоз</kwd><kwd>ангиогенез</kwd><kwd>миграция</kwd><kwd>адгезия</kwd><kwd>канцерогенез</kwd></kwd-group><kwd-group xml:lang="en"><kwd>galectin-1</kwd><kwd>galectin-3</kwd><kwd>proliferation</kwd><kwd>apoptosis</kwd><kwd>angiogenesis</kwd><kwd>migration</kwd><kwd>adhesion</kwd><kwd>carcinogenesis</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">Guda M.R., Tsung A.J., Asuthkar S., Velpula K.K. Galectin-1 activates carbonic anhydrase IX and modulates glioma metabolism. Cell Death Dis. 2022;13(6):574. DOI: 10.1038/s41419-022-05024-z.</mixed-citation><mixed-citation xml:lang="en">Guda M.R., Tsung A.J., Asuthkar S., Velpula K.K. Galectin-1 activates carbonic anhydrase IX and modulates glioma metabolism. Cell Death Dis. 2022;13(6):574. DOI: 10.1038/s41419-022-05024-z.</mixed-citation></citation-alternatives></ref><ref id="cit2"><label>2</label><citation-alternatives><mixed-citation xml:lang="ru">Radziejewska I. Galectin-3 and epithelial MUC1 mucin-interactions supporting cancer development. Cancers (Basel). 2023;15(10):2680. DOI: 10.3390/cancers15102680.</mixed-citation><mixed-citation xml:lang="en">Radziejewska I. Galectin-3 and epithelial MUC1 mucin-interactions supporting cancer development. Cancers (Basel). 2023;15(10):2680. DOI: 10.3390/cancers15102680.</mixed-citation></citation-alternatives></ref><ref id="cit3"><label>3</label><citation-alternatives><mixed-citation xml:lang="ru">Yaylim I., Aru M., Farooqi A.A., Hakan M.T., Buttari B., Arese M. et al. Regulation of Nrf2/Keap1 signaling pathway in cancer drug resistance by galectin-1: cellular and molecular implications. Cancer Drug Resist. 2024;7:8. DOI: 10.20517/cdr.2023.79.</mixed-citation><mixed-citation xml:lang="en">Yaylim I., Aru M., Farooqi A.A., Hakan M.T., Buttari B., Arese M. et al. Regulation of Nrf2/Keap1 signaling pathway in cancer drug resistance by galectin-1: cellular and molecular implications. Cancer Drug Resist. 2024;7:8. DOI: 10.20517/cdr.2023.79.</mixed-citation></citation-alternatives></ref><ref id="cit4"><label>4</label><citation-alternatives><mixed-citation xml:lang="ru">Girotti M.R., Salatino M., Dalotto-Moreno T., Rabinovich G.A. Sweetening the hallmarks of cancer: galectins as multifunctional mediators of tumor progression. J. Exp. Med. 2020;217(2):e20182041. DOI: 10.1084/jem.20182041.</mixed-citation><mixed-citation xml:lang="en">Girotti M.R., Salatino M., Dalotto-Moreno T., Rabinovich G.A. Sweetening the hallmarks of cancer: galectins as multifunctional mediators of tumor progression. J. Exp. Med. 2020;217(2):e20182041. DOI: 10.1084/jem.20182041.</mixed-citation></citation-alternatives></ref><ref id="cit5"><label>5</label><citation-alternatives><mixed-citation xml:lang="ru">Ko F.C.F., Yan S., Lee K.W., Lam S.K., Ho J.C.M. Chimera and tandem-repeat type galectins: the new targets for cancer immunotherapy. Biomolecules. 2023;13(6):902. DOI: 10.3390/biom13060902.</mixed-citation><mixed-citation xml:lang="en">Ko F.C.F., Yan S., Lee K.W., Lam S.K., Ho J.C.M. Chimera and tandem-repeat type galectins: the new targets for cancer immunotherapy. Biomolecules. 2023;13(6):902. DOI: 10.3390/biom13060902.</mixed-citation></citation-alternatives></ref><ref id="cit6"><label>6</label><citation-alternatives><mixed-citation xml:lang="ru">Kapetanakis N.I., Busson P. Galectins as pivotal components in oncogenesis and immune exclusion in human malignancies. Front. Immunol. 2023;14:1145268. DOI: 10.3389/fimmu.2023.1145268.</mixed-citation><mixed-citation xml:lang="en">Kapetanakis N.I., Busson P. Galectins as pivotal components in oncogenesis and immune exclusion in human malignancies. Front. Immunol. 2023;14:1145268. DOI: 10.3389/fimmu.2023.1145268.</mixed-citation></citation-alternatives></ref><ref id="cit7"><label>7</label><citation-alternatives><mixed-citation xml:lang="ru">Bogut A., Stojanovic B., Jovanovic M., Dimitrijevic Stojanovic M., Gajovic N., Stojanovic B.S. et al. Galectin-1 in pancreatic ductal adenocarcinoma: bridging tumor biology, immune evasion, and therapeutic opportunities. Int. J. Mol. Sci. 2023;24(21):15500. DOI: 10.3390/ijms242115500.</mixed-citation><mixed-citation xml:lang="en">Bogut A., Stojanovic B., Jovanovic M., Dimitrijevic Stojanovic M., Gajovic N., Stojanovic B.S. et al. Galectin-1 in pancreatic ductal adenocarcinoma: bridging tumor biology, immune evasion, and therapeutic opportunities. Int. J. Mol. Sci. 2023;24(21):15500. DOI: 10.3390/ijms242115500.</mixed-citation></citation-alternatives></ref><ref id="cit8"><label>8</label><citation-alternatives><mixed-citation xml:lang="ru">Le Mercier M., Fortin S., Mathieu V., Kiss R., Lefranc F. Galectins and gliomas. Brain Pathol. 2010;20(1):17–27. DOI: 10.1111/j.1750-3639.2009.00270.x.</mixed-citation><mixed-citation xml:lang="en">Le Mercier M., Fortin S., Mathieu V., Kiss R., Lefranc F. Galectins and gliomas. Brain Pathol. 2010;20(1):17–27. DOI: 10.1111/j.1750-3639.2009.00270.x.</mixed-citation></citation-alternatives></ref><ref id="cit9"><label>9</label><citation-alternatives><mixed-citation xml:lang="ru">Nehmé R., St-Pierre Y. Targeting intracellular galectins for cancer treatment. Front. Immunol. 2023;14:1269391. DOI: 10.3389/fimmu.2023.1269391.</mixed-citation><mixed-citation xml:lang="en">Nehmé R., St-Pierre Y. Targeting intracellular galectins for cancer treatment. Front. Immunol. 2023;14:1269391. DOI: 10.3389/fimmu.2023.1269391.</mixed-citation></citation-alternatives></ref><ref id="cit10"><label>10</label><citation-alternatives><mixed-citation xml:lang="ru">Stanley P. Galectin-1 pulls the strings on VEGFR2. Cell. 2014;156(4):625–626. DOI: 10.1016/j.cell.2014.01.059.</mixed-citation><mixed-citation xml:lang="en">Stanley P. Galectin-1 pulls the strings on VEGFR2. Cell. 2014;156(4):625–626. DOI: 10.1016/j.cell.2014.01.059.</mixed-citation></citation-alternatives></ref><ref id="cit11"><label>11</label><citation-alternatives><mixed-citation xml:lang="ru">Storti P., Marchica V., Giuliani N. Role of galectins in multiple myeloma. Int. J. Mol. Sci. 2017;18(12):2740. DOI: 10.3390/ijms18122740.</mixed-citation><mixed-citation xml:lang="en">Storti P., Marchica V., Giuliani N. Role of galectins in multiple myeloma. Int. J. Mol. Sci. 2017;18(12):2740. DOI: 10.3390/ijms18122740.</mixed-citation></citation-alternatives></ref><ref id="cit12"><label>12</label><citation-alternatives><mixed-citation xml:lang="ru">Lin Y., Lubman D.M. The role of N-glycosylation in cancer. Acta Pharm. Sin. B. 2024;14(3):1098–1110. DOI: 10.1016/j.apsb.2023.10.014.</mixed-citation><mixed-citation xml:lang="en">Lin Y., Lubman D.M. The role of N-glycosylation in cancer. Acta Pharm. Sin. B. 2024;14(3):1098–1110. DOI: 10.1016/j.apsb.2023.10.014.</mixed-citation></citation-alternatives></ref><ref id="cit13"><label>13</label><citation-alternatives><mixed-citation xml:lang="ru">Croci D.O., Cerliani J.P., Dalotto-Moreno T., Méndez-Huergo S.P., Mascanfroni I.D., Dergan-Dylon S. et al. Glycosylation-dependent lectin-receptor interactions preserve angiogenesis in anti-VEGF refractory tumors. Cell. 2014;156:744–758. DOI: 10.1016/j.cell.2014.01.043.</mixed-citation><mixed-citation xml:lang="en">Croci D.O., Cerliani J.P., Dalotto-Moreno T., Méndez-Huergo S.P., Mascanfroni I.D., Dergan-Dylon S. et al. Glycosylation-dependent lectin-receptor interactions preserve angiogenesis in anti-VEGF refractory tumors. Cell. 2014;156:744–758. DOI: 10.1016/j.cell.2014.01.043.</mixed-citation></citation-alternatives></ref><ref id="cit14"><label>14</label><citation-alternatives><mixed-citation xml:lang="ru">Cardoso A.C., Andrade L.N., Bustos S.O., Chammas R. Galectin-3 determines tumor cell adaptive strategies in stressed tumor microenvironments. Front. Oncol. 2016;6:127. DOI: 10.3389/fonc.2016.00127.</mixed-citation><mixed-citation xml:lang="en">Cardoso A.C., Andrade L.N., Bustos S.O., Chammas R. Galectin-3 determines tumor cell adaptive strategies in stressed tumor microenvironments. Front. Oncol. 2016;6:127. DOI: 10.3389/fonc.2016.00127.</mixed-citation></citation-alternatives></ref><ref id="cit15"><label>15</label><citation-alternatives><mixed-citation xml:lang="ru">Hassinen A., Khoder-Agha F., Khosrowabadi E., Mennerich D., Harrus D., Noel M. et al. A Golgi-associated redox switch regulates catalytic activation and cooperative functioning of ST6Gal-I with B4GalT-I. Redox Biol. 2019;24:101182. DOI: 10.1016/j.redox.2019.101182.</mixed-citation><mixed-citation xml:lang="en">Hassinen A., Khoder-Agha F., Khosrowabadi E., Mennerich D., Harrus D., Noel M. et al. A Golgi-associated redox switch regulates catalytic activation and cooperative functioning of ST6Gal-I with B4GalT-I. Redox Biol. 2019;24:101182. DOI: 10.1016/j.redox.2019.101182.</mixed-citation></citation-alternatives></ref><ref id="cit16"><label>16</label><citation-alternatives><mixed-citation xml:lang="ru">Marhuenda E., Fabre C., Zhang C., Martin-Fernandez M., Iskratsch T., Saleh A. et al. Glioma stem cells invasive phenotype at optimal stiffness is driven by MGAT5 dependent mechanosensing. J. Exp. Clin. Cancer Res. 2021;40(1):139. DOI: 10.1186/s13046-021-01925-7.</mixed-citation><mixed-citation xml:lang="en">Marhuenda E., Fabre C., Zhang C., Martin-Fernandez M., Iskratsch T., Saleh A. et al. Glioma stem cells invasive phenotype at optimal stiffness is driven by MGAT5 dependent mechanosensing. J. Exp. Clin. Cancer Res. 2021;40(1):139. DOI: 10.1186/s13046-021-01925-7.</mixed-citation></citation-alternatives></ref><ref id="cit17"><label>17</label><citation-alternatives><mixed-citation xml:lang="ru">Lin Y., Lubman D.M. The role of N-glycosylation in cancer. Acta Pharm. Sin. B. 2024;14(3):1098–1110. DOI: 10.1016/j.apsb.2023.10.014.</mixed-citation><mixed-citation xml:lang="en">Lin Y., Lubman D.M. The role of N-glycosylation in cancer. Acta Pharm. Sin. B. 2024;14(3):1098–1110. DOI: 10.1016/j.apsb.2023.10.014.</mixed-citation></citation-alternatives></ref><ref id="cit18"><label>18</label><citation-alternatives><mixed-citation xml:lang="ru">De-Souza-Ferreira M., Ferreira É.E., de-Freitas-Junior J.C.M. Aberrant N-glycosylation in cancer: MGAT5 and β1,6-GlcNAc branched N-glycans as critical regulators of tumor development and progression. Cell. Oncol. (Dordr.). 2023;46(3):481–501. DOI: 10.1007/s13402-023-00770-4.</mixed-citation><mixed-citation xml:lang="en">De-Souza-Ferreira M., Ferreira É.E., de-Freitas-Junior J.C.M. Aberrant N-glycosylation in cancer: MGAT5 and β1,6-GlcNAc branched N-glycans as critical regulators of tumor development and progression. Cell. Oncol. (Dordr.). 2023;46(3):481–501. DOI: 10.1007/s13402-023-00770-4.</mixed-citation></citation-alternatives></ref><ref id="cit19"><label>19</label><citation-alternatives><mixed-citation xml:lang="ru">Liu Y., Bineva-Todd G., Meek R.W., Mazo L., Piniello B., Moroz O. A bioorthogonal precision tool for human N-acetylglucosaminyltransferase V. J. Am. Chem. Soc. 2024;146(39):26707–26718. DOI: 10.1021/jacs.4c05955.</mixed-citation><mixed-citation xml:lang="en">Liu Y., Bineva-Todd G., Meek R.W., Mazo L., Piniello B., Moroz O. A bioorthogonal precision tool for human N-acetylglucosaminyltransferase V. J. Am. Chem. Soc. 2024;146(39):26707–26718. DOI: 10.1021/jacs.4c05955.</mixed-citation></citation-alternatives></ref><ref id="cit20"><label>20</label><citation-alternatives><mixed-citation xml:lang="ru">Funasaka T., Raz A., Nangia-Makker P. Galectin-3 in angiogenesis and metastasis. Glycobiology. 2014;24(10):886–891. DOI: 10.1093/glycob/cwu086.</mixed-citation><mixed-citation xml:lang="en">Funasaka T., Raz A., Nangia-Makker P. Galectin-3 in angiogenesis and metastasis. Glycobiology. 2014;24(10):886–891. DOI: 10.1093/glycob/cwu086.</mixed-citation></citation-alternatives></ref><ref id="cit21"><label>21</label><citation-alternatives><mixed-citation xml:lang="ru">Carabias P., Espelt M.V., Bacigalupo M.L., Rojas P., Sarrias L., Rubin A. et al. Galectin-1 confers resistance to doxorubicin in hepatocellular carcinoma cells through modulation of P-glycoprotein expression. Cell Death Dis. 2022;13(1):79. DOI: 10.1038/s41419-022-04520-6.</mixed-citation><mixed-citation xml:lang="en">Carabias P., Espelt M.V., Bacigalupo M.L., Rojas P., Sarrias L., Rubin A. et al. Galectin-1 confers resistance to doxorubicin in hepatocellular carcinoma cells through modulation of P-glycoprotein expression. Cell Death Dis. 2022;13(1):79. DOI: 10.1038/s41419-022-04520-6.</mixed-citation></citation-alternatives></ref><ref id="cit22"><label>22</label><citation-alternatives><mixed-citation xml:lang="ru">Elad-Sfadia G., Haklai R., Ballan E., Gabius H.J., Kloog Y. Galectin-1 augments Ras activation and diverts Ras signals to Raf-1 at the expense of phosphoinositide 3-kinase. J. Biol. Chem. 2002;277(40):37169–37175. DOI: 10.1074/jbc.M205698200.</mixed-citation><mixed-citation xml:lang="en">Elad-Sfadia G., Haklai R., Ballan E., Gabius H.J., Kloog Y. Galectin-1 augments Ras activation and diverts Ras signals to Raf-1 at the expense of phosphoinositide 3-kinase. J. Biol. Chem. 2002;277(40):37169–37175. DOI: 10.1074/jbc.M205698200.</mixed-citation></citation-alternatives></ref><ref id="cit23"><label>23</label><citation-alternatives><mixed-citation xml:lang="ru">Shalom-Feuerstein R., Cooks T., Raz A., Kloog Y. Galectin-3 regulates a molecular switch from N-Ras to K-Ras usage in human breast carcinoma cells. Cancer Res. 2005;65(16):7292– 7300. DOI: 10.1158/0008-5472.CAN-05-0775.</mixed-citation><mixed-citation xml:lang="en">Shalom-Feuerstein R., Cooks T., Raz A., Kloog Y. Galectin-3 regulates a molecular switch from N-Ras to K-Ras usage in human breast carcinoma cells. Cancer Res. 2005;65(16):7292– 7300. DOI: 10.1158/0008-5472.CAN-05-0775.</mixed-citation></citation-alternatives></ref><ref id="cit24"><label>24</label><citation-alternatives><mixed-citation xml:lang="ru">Elad-Sfadia G., Haklai R., Balan E., Kloog Y. Galectin-3 augments K-Ras activation and triggers a Ras signal that attenuates ERK but not phosphoinositide 3-kinase activity. J. Biol. Chem. 2004;279(33):34922–34930. DOI: 10.1074/jbc.M312697200.</mixed-citation><mixed-citation xml:lang="en">Elad-Sfadia G., Haklai R., Balan E., Kloog Y. Galectin-3 augments K-Ras activation and triggers a Ras signal that attenuates ERK but not phosphoinositide 3-kinase activity. J. Biol. Chem. 2004;279(33):34922–34930. DOI: 10.1074/jbc.M312697200.</mixed-citation></citation-alternatives></ref><ref id="cit25"><label>25</label><citation-alternatives><mixed-citation xml:lang="ru">Wang H.C., Xia R., Chang W.H., Hsu S.W., Wu C.T., Chen C.H. et al. Improving cancer immunotherapy in prostate cancer by modulating T cell function through targeting the galectin-1. Front. Immunol. 2024;15:1372956. DOI: 10.3389/fimmu.2024.1372956.</mixed-citation><mixed-citation xml:lang="en">Wang H.C., Xia R., Chang W.H., Hsu S.W., Wu C.T., Chen C.H. et al. Improving cancer immunotherapy in prostate cancer by modulating T cell function through targeting the galectin-1. Front. Immunol. 2024;15:1372956. DOI: 10.3389/fimmu.2024.1372956.</mixed-citation></citation-alternatives></ref><ref id="cit26"><label>26</label><citation-alternatives><mixed-citation xml:lang="ru">Fischer C., Sanchez-Ruderisch H., Welzel M., Wiedenmann B., Sakai T., André S. et al. Galectin-1 interacts with the {alpha}5{beta}1 fibronectin receptor to restrict carcinoma cell growth via induction of p21 and p27. J. Biol. Chem. 2005;280(44):37266–37277. DOI: 10.1074/jbc.M411580200.</mixed-citation><mixed-citation xml:lang="en">Fischer C., Sanchez-Ruderisch H., Welzel M., Wiedenmann B., Sakai T., André S. et al. Galectin-1 interacts with the {alpha}5{beta}1 fibronectin receptor to restrict carcinoma cell growth via induction of p21 and p27. J. Biol. Chem. 2005;280(44):37266–37277. DOI: 10.1074/jbc.M411580200.</mixed-citation></citation-alternatives></ref><ref id="cit27"><label>27</label><citation-alternatives><mixed-citation xml:lang="ru">Wang Y., Nangia-Makker P., Tait L., Balan V., Hogan V., Pienta K.J. et al. Regulation of prostate cancer progression by galectin-3. Am. J. Pathol. 2009;174(4):1515–1523. DOI: 10.2353/ajpath.2009.080816.</mixed-citation><mixed-citation xml:lang="en">Wang Y., Nangia-Makker P., Tait L., Balan V., Hogan V., Pienta K.J. et al. Regulation of prostate cancer progression by galectin-3. Am. J. Pathol. 2009;174(4):1515–1523. DOI: 10.2353/ajpath.2009.080816.</mixed-citation></citation-alternatives></ref><ref id="cit28"><label>28</label><citation-alternatives><mixed-citation xml:lang="ru">Yu F., Yu C., Li F., Zuo Y., Wang Y., Yao L. et al. Wnt/β-catenin signaling in cancers and targeted therapies. Signal Transduct. Target. Ther. 2021;6(1):307. DOI: 10.1038/s41392-021-00701-5.</mixed-citation><mixed-citation xml:lang="en">Yu F., Yu C., Li F., Zuo Y., Wang Y., Yao L. et al. Wnt/β-catenin signaling in cancers and targeted therapies. Signal Transduct. Target. Ther. 2021;6(1):307. DOI: 10.1038/s41392-021-00701-5.</mixed-citation></citation-alternatives></ref><ref id="cit29"><label>29</label><citation-alternatives><mixed-citation xml:lang="ru">Liu J., Xiao Q., Xiao J., Niu C., Li Y., Zhang X. et al. Wnt/β-catenin signalling: function, biological mechanisms, and therapeutic opportunities. Signal Transduct. Target. Ther. 2022;7(1):1–23. DOI: 10.1038/s41392-021-00762-6.</mixed-citation><mixed-citation xml:lang="en">Liu J., Xiao Q., Xiao J., Niu C., Li Y., Zhang X. et al. Wnt/β-catenin signalling: function, biological mechanisms, and therapeutic opportunities. Signal Transduct. Target. Ther. 2022;7(1):1–23. DOI: 10.1038/s41392-021-00762-6.</mixed-citation></citation-alternatives></ref><ref id="cit30"><label>30</label><citation-alternatives><mixed-citation xml:lang="ru">Song M., Pan Q., Yang J., He J., Zeng J., Cheng S. et al. Galectin-3 favours tumour metastasis via the activation of β-catenin signalling in hepatocellular carcinoma. Br. J. Cancer. 2020;123(10):1521–1534. DOI: 10.1038/s41416-020-1022-4.</mixed-citation><mixed-citation xml:lang="en">Song M., Pan Q., Yang J., He J., Zeng J., Cheng S. et al. Galectin-3 favours tumour metastasis via the activation of β-catenin signalling in hepatocellular carcinoma. Br. J. Cancer. 2020;123(10):1521–1534. DOI: 10.1038/s41416-020-1022-4.</mixed-citation></citation-alternatives></ref><ref id="cit31"><label>31</label><citation-alternatives><mixed-citation xml:lang="ru">Liu Y., Xie L., Wang D., Li D., Xu G., Wang L. et al. Galectin-3 and β-catenin are associated with a poor prognosis in serous epithelial ovarian cancer. Cancer Manag. Res. 2018;10:3963–3971. DOI: 10.2147/CMAR.S171146.</mixed-citation><mixed-citation xml:lang="en">Liu Y., Xie L., Wang D., Li D., Xu G., Wang L. et al. Galectin-3 and β-catenin are associated with a poor prognosis in serous epithelial ovarian cancer. Cancer Manag. Res. 2018;10:3963–3971. DOI: 10.2147/CMAR.S171146.</mixed-citation></citation-alternatives></ref><ref id="cit32"><label>32</label><citation-alternatives><mixed-citation xml:lang="ru">Merlin J., Stechly L., de Beaucé S., Monte D., Leteurtre E., Van Seuningen I. et al. Galectin-3 regulates MUC1 and EGFR cellular distribution and EGFR downstream pathways in pancreatic cancer cells. Oncogene. 2011;30:2514–2525. DOI:10.1038/onc.2010.631.</mixed-citation><mixed-citation xml:lang="en">Merlin J., Stechly L., de Beaucé S., Monte D., Leteurtre E., Van Seuningen I. et al. Galectin-3 regulates MUC1 and EGFR cellular distribution and EGFR downstream pathways in pancreatic cancer cells. Oncogene. 2011;30:2514–2525. DOI:10.1038/onc.2010.631.</mixed-citation></citation-alternatives></ref><ref id="cit33"><label>33</label><citation-alternatives><mixed-citation xml:lang="ru">Wu M.H., Ying N.W., Hong T.M., Chiang W.F., Lin Y.T., Chen Y.L. Galectin-1 increases vascular permeability through the neuropilin-1/vascular endothelial growth factor receptor-1 complex. Angiogenesis. 2014;17:839–849. DOI: 10.1007/s10456-014-9431-8.28.</mixed-citation><mixed-citation xml:lang="en">Wu M.H., Ying N.W., Hong T.M., Chiang W.F., Lin Y.T., Chen Y.L. Galectin-1 increases vascular permeability through the neuropilin-1/vascular endothelial growth factor receptor-1 complex. Angiogenesis. 2014;17:839–849. DOI: 10.1007/s10456-014-9431-8.28.</mixed-citation></citation-alternatives></ref><ref id="cit34"><label>34</label><citation-alternatives><mixed-citation xml:lang="ru">Pan Z., Xu G., Zhang Y., Wu M., Yu J., He X. et al. Galectin-1 promotes gastric carcinoma progression and cisplatin resistance through the NRP-1/c-JUN/Wee1 pathway. J. Gastric Cancer. 2024;24(3):300–315. DOI: 10.5230/jgc.2024.24.e25.</mixed-citation><mixed-citation xml:lang="en">Pan Z., Xu G., Zhang Y., Wu M., Yu J., He X. et al. Galectin-1 promotes gastric carcinoma progression and cisplatin resistance through the NRP-1/c-JUN/Wee1 pathway. J. Gastric Cancer. 2024;24(3):300–315. DOI: 10.5230/jgc.2024.24.e25.</mixed-citation></citation-alternatives></ref><ref id="cit35"><label>35</label><citation-alternatives><mixed-citation xml:lang="ru">Mori Y., Yashiro M., Sawada T., Hirakawa K., Murata T., Nakada H. Binding of galectin-3, a β-galactoside-binding lectin, to MUC1 protein enhances phosphorylation of extracellular signal-regulated Kinase ½ (ERK1/2) and Akt, promoting tumor cell malignancy. J. Biol. Chem. 2015;290:26125–26140. DOI: 10.1074/jbc.M115.651489.</mixed-citation><mixed-citation xml:lang="en">Mori Y., Yashiro M., Sawada T., Hirakawa K., Murata T., Nakada H. Binding of galectin-3, a β-galactoside-binding lectin, to MUC1 protein enhances phosphorylation of extracellular signal-regulated Kinase ½ (ERK1/2) and Akt, promoting tumor cell malignancy. J. Biol. Chem. 2015;290:26125–26140. DOI: 10.1074/jbc.M115.651489.</mixed-citation></citation-alternatives></ref><ref id="cit36"><label>36</label><citation-alternatives><mixed-citation xml:lang="ru">Колобовникова Ю.В., Дмитриева А.И., Янкович К.И., Васильева О.А., Пурлик И.Л., Новицкий В.В. и др. Галектин-1-опосредованная экспрессия белков-регуляторов клеточного цикла и ростовых факторов при раке желудка. Бюллетень сибирской медицины. 2017;16(4):165–172. DOI: 10.20538/1682-0363-2017-4-165-172.</mixed-citation><mixed-citation xml:lang="en">Колобовникова Ю.В., Дмитриева А.И., Янкович К.И., Васильева О.А., Пурлик И.Л., Новицкий В.В. и др. Галектин-1-опосредованная экспрессия белков-регуляторов клеточного цикла и ростовых факторов при раке желудка. Бюллетень сибирской медицины. 2017;16(4):165–172. DOI: 10.20538/1682-0363-2017-4-165-172.</mixed-citation></citation-alternatives></ref><ref id="cit37"><label>37</label><citation-alternatives><mixed-citation xml:lang="ru">Mazurek N., Sun Y.J., Liu K.F., Gilcrease M.Z., Schober W., Nangia-Makker P. et al. Phosphorylated galectin-3 mediates tumor necrosis factor-related apoptosis-inducing ligand signaling by regulating phosphatase and tensin homologue deleted on chromosome 10 in human breast carcinoma cells. J. Biol. Chem. 2007;282(29):21337–21348. DOI: 10.1074/jbc.M608810200.</mixed-citation><mixed-citation xml:lang="en">Mazurek N., Sun Y.J., Liu K.F., Gilcrease M.Z., Schober W., Nangia-Makker P. et al. Phosphorylated galectin-3 mediates tumor necrosis factor-related apoptosis-inducing ligand signaling by regulating phosphatase and tensin homologue deleted on chromosome 10 in human breast carcinoma cells. J. Biol. Chem. 2007;282(29):21337–21348. DOI: 10.1074/jbc.M608810200.</mixed-citation></citation-alternatives></ref><ref id="cit38"><label>38</label><citation-alternatives><mixed-citation xml:lang="ru">Woś J., Szymańska A., Lehman N., Chocholska S., Zarobkiewicz M., Pożarowski P. et al. Can galectin-3 be a novel biomarker in chronic lymphocytic leukemia? Cells. 2023;13(1):30. DOI: 10.3390/cells13010030.</mixed-citation><mixed-citation xml:lang="en">Woś J., Szymańska A., Lehman N., Chocholska S., Zarobkiewicz M., Pożarowski P. et al. Can galectin-3 be a novel biomarker in chronic lymphocytic leukemia? Cells. 2023;13(1):30. DOI: 10.3390/cells13010030.</mixed-citation></citation-alternatives></ref><ref id="cit39"><label>39</label><citation-alternatives><mixed-citation xml:lang="ru">Oka N., Nakahara S., Takenaka Y., Fukumori T., Hogan V., Kanayama H.O. Galectin-3 inhibits tumor necrosis factor-related apoptosis-inducing ligand-induced apoptosis by activating Akt in human bladder carcinoma cells. Cancer Res. 2005;65(17):7546–7553. DOI: 10.1158/0008-5472.CAN-05-1197.</mixed-citation><mixed-citation xml:lang="en">Oka N., Nakahara S., Takenaka Y., Fukumori T., Hogan V., Kanayama H.O. Galectin-3 inhibits tumor necrosis factor-related apoptosis-inducing ligand-induced apoptosis by activating Akt in human bladder carcinoma cells. Cancer Res. 2005;65(17):7546–7553. DOI: 10.1158/0008-5472.CAN-05-1197.</mixed-citation></citation-alternatives></ref><ref id="cit40"><label>40</label><citation-alternatives><mixed-citation xml:lang="ru">Fang Z., Qiu F., Zhao J.F., Sun Q., Qiao B. et al. Role and mechanism of Galectin-3 gene in proliferation, invasion, and apoptosis of oral squamous cell carcinoma. West China J. Stomat. 2018;36(4):404409. DOI: 10.7518/hxkq.2018.04.011.</mixed-citation><mixed-citation xml:lang="en">Fang Z., Qiu F., Zhao J.F., Sun Q., Qiao B. et al. Role and mechanism of Galectin-3 gene in proliferation, invasion, and apoptosis of oral squamous cell carcinoma. West China J. Stomat. 2018;36(4):404409. DOI: 10.7518/hxkq.2018.04.011.</mixed-citation></citation-alternatives></ref><ref id="cit41"><label>41</label><citation-alternatives><mixed-citation xml:lang="ru">Zhao Z., Wang M., Miller M.C., He Z., Xu X., Zhou Y. et al. Isomerization of proline-46 in the N-terminal tail of galectin-3 enhances T cell apoptosis via the ROS-ERK pathway. Int. J. Biol. Macromol. 2024;256(Pt 1):128304. DOI: 10.1016/j.ijbiomac.2023.128304.</mixed-citation><mixed-citation xml:lang="en">Zhao Z., Wang M., Miller M.C., He Z., Xu X., Zhou Y. et al. Isomerization of proline-46 in the N-terminal tail of galectin-3 enhances T cell apoptosis via the ROS-ERK pathway. Int. J. Biol. Macromol. 2024;256(Pt 1):128304. DOI: 10.1016/j.ijbiomac.2023.128304.</mixed-citation></citation-alternatives></ref><ref id="cit42"><label>42</label><citation-alternatives><mixed-citation xml:lang="ru">Yu X., Qian J., Ding L., Yin S., Zhou L., Zheng S. Galectin-1: a traditionally immunosuppressive protein displays context-dependent capacities. Int. J. Mol. Sci. 2023;24(7):6501. DOI: 10.3390/ijms24076501.</mixed-citation><mixed-citation xml:lang="en">Yu X., Qian J., Ding L., Yin S., Zhou L., Zheng S. Galectin-1: a traditionally immunosuppressive protein displays context-dependent capacities. Int. J. Mol. Sci. 2023;24(7):6501. DOI: 10.3390/ijms24076501.</mixed-citation></citation-alternatives></ref><ref id="cit43"><label>43</label><citation-alternatives><mixed-citation xml:lang="ru">Brandt B., Abou-Eladab E.F., Tiedge M., Walzel H. Role of the JNK/c-Jun/AP-1 signaling pathway in galectin-1-induced T-cell death. Cell Death Dis. 2010;1(2):e23. DOI: 10.1038/cddis.2010.1.</mixed-citation><mixed-citation xml:lang="en">Brandt B., Abou-Eladab E.F., Tiedge M., Walzel H. Role of the JNK/c-Jun/AP-1 signaling pathway in galectin-1-induced T-cell death. Cell Death Dis. 2010;1(2):e23. DOI: 10.1038/cddis.2010.1.</mixed-citation></citation-alternatives></ref><ref id="cit44"><label>44</label><citation-alternatives><mixed-citation xml:lang="ru">Zetterberg F.R., Peterson K., Nilsson U.J., Andréasson Dahlgren K., Diehl C., Holyer I. et al. Discovery of the selective and orally available galectin-1 inhibitor GB1908 as a potential treatment for lung cancer. J. Med. Chem. 2024;67(11):9374– 9388. DOI: 10.1021/acs.jmedchem.4c00485.</mixed-citation><mixed-citation xml:lang="en">Zetterberg F.R., Peterson K., Nilsson U.J., Andréasson Dahlgren K., Diehl C., Holyer I. et al. Discovery of the selective and orally available galectin-1 inhibitor GB1908 as a potential treatment for lung cancer. J. Med. Chem. 2024;67(11):9374– 9388. DOI: 10.1021/acs.jmedchem.4c00485.</mixed-citation></citation-alternatives></ref><ref id="cit45"><label>45</label><citation-alternatives><mixed-citation xml:lang="ru">Hahn H.P., Pang M., He J., Hernandez J.D., Yang R.Y., Li L.Y. et al. Galectin-1 induces nuclear translocation of endonuclease G in caspase- and cytochrome c-independent T cell death. Cell Death Differ. 2004;11(12):1277–1286. DOI: 10.1038/sj.cdd.4401485.</mixed-citation><mixed-citation xml:lang="en">Hahn H.P., Pang M., He J., Hernandez J.D., Yang R.Y., Li L.Y. et al. Galectin-1 induces nuclear translocation of endonuclease G in caspase- and cytochrome c-independent T cell death. Cell Death Differ. 2004;11(12):1277–1286. DOI: 10.1038/sj.cdd.4401485.</mixed-citation></citation-alternatives></ref><ref id="cit46"><label>46</label><citation-alternatives><mixed-citation xml:lang="ru">Васильева О.А., Новицкий В.В. Апоптоз опухолевых клеток линии Jurkat под действием галектина-3. Российский иммунологический журнал. 2015;91(2-2(18)):202–204.</mixed-citation><mixed-citation xml:lang="en">Васильева О.А., Новицкий В.В. Апоптоз опухолевых клеток линии Jurkat под действием галектина-3. Российский иммунологический журнал. 2015;91(2-2(18)):202–204.</mixed-citation></citation-alternatives></ref><ref id="cit47"><label>47</label><citation-alternatives><mixed-citation xml:lang="ru">Васильева О.А., Исаева А.В., Рязанцева Н.В. Влияние галектина-3 на апоптоз активированных in vitro CD4+ - лимфоцитов. Вестник науки Сибири. 2015;(15):347–351.</mixed-citation><mixed-citation xml:lang="en">Васильева О.А., Исаева А.В., Рязанцева Н.В. Влияние галектина-3 на апоптоз активированных in vitro CD4+ - лимфоцитов. Вестник науки Сибири. 2015;(15):347–351.</mixed-citation></citation-alternatives></ref><ref id="cit48"><label>48</label><citation-alternatives><mixed-citation xml:lang="ru">Thijssen V.L., Barkan B., Shoji H., Aries I.M., Mathieu V., Deltour L. et al. Tumor cells secrete galectin-1 to enhance endothelial cell activity. Cancer Res. 2010;70(15):6216–6224. DOI: 10.1158/0008-5472.CAN-09-4150.</mixed-citation><mixed-citation xml:lang="en">Thijssen V.L., Barkan B., Shoji H., Aries I.M., Mathieu V., Deltour L. et al. Tumor cells secrete galectin-1 to enhance endothelial cell activity. Cancer Res. 2010;70(15):6216–6224. DOI: 10.1158/0008-5472.CAN-09-4150.</mixed-citation></citation-alternatives></ref><ref id="cit49"><label>49</label><citation-alternatives><mixed-citation xml:lang="ru">Курносенко А.В., Рейнгардт Г.В., Полетика В.С., Колобовникова Ю.В., Уразова О.И. Связь галектинов-1 и -3 с проангиогенными факторами и дисфункцией эндотелия при раке толстой кишки. Казанский медицинский журнал. 2024;(4):551–559. DOI: 10.17816/KMJ623114.</mixed-citation><mixed-citation xml:lang="en">Курносенко А.В., Рейнгардт Г.В., Полетика В.С., Колобовникова Ю.В., Уразова О.И. Связь галектинов-1 и -3 с проангиогенными факторами и дисфункцией эндотелия при раке толстой кишки. Казанский медицинский журнал. 2024;(4):551–559. DOI: 10.17816/KMJ623114.</mixed-citation></citation-alternatives></ref><ref id="cit50"><label>50</label><citation-alternatives><mixed-citation xml:lang="ru">Ozawa K., Kondo T., Hori O., Kitao Y., Stern D.M., Eisenmenger W. et al. Expression of the oxygen-regulated protein ORP150 accelerates wound healing by modulating intracellular VEGF transport. J. Clin. Invest. 2001;108(1):41–50. DOI: 10.1172/JCI11772.</mixed-citation><mixed-citation xml:lang="en">Ozawa K., Kondo T., Hori O., Kitao Y., Stern D.M., Eisenmenger W. et al. Expression of the oxygen-regulated protein ORP150 accelerates wound healing by modulating intracellular VEGF transport. J. Clin. Invest. 2001;108(1):41–50. DOI: 10.1172/JCI11772.</mixed-citation></citation-alternatives></ref><ref id="cit51"><label>51</label><citation-alternatives><mixed-citation xml:lang="ru">Markowska A.I., Liu F.T., Panjwani N. Galectin-3 is an important mediator of VEGF- and bFGF-mediated angiogenic response. J. Exp. Med. 2010;207(9):1981–1993. DOI: 10.1084/jem.20090121.</mixed-citation><mixed-citation xml:lang="en">Markowska A.I., Liu F.T., Panjwani N. Galectin-3 is an important mediator of VEGF- and bFGF-mediated angiogenic response. J. Exp. Med. 2010;207(9):1981–1993. DOI: 10.1084/jem.20090121.</mixed-citation></citation-alternatives></ref><ref id="cit52"><label>52</label><citation-alternatives><mixed-citation xml:lang="ru">Lagana A., Goetz J.G., Cheung P., Raz A., Dennis J.W., Nabi I.R. Galectin binding to Mgat5-modified N-glycans regulates fibronectin matrix remodeling in tumor cells. Mol. Cell Biol. 2006;26(8):3181–3193. DOI: 10.1128/MCB.26.8.3181-3193.2006.</mixed-citation><mixed-citation xml:lang="en">Lagana A., Goetz J.G., Cheung P., Raz A., Dennis J.W., Nabi I.R. Galectin binding to Mgat5-modified N-glycans regulates fibronectin matrix remodeling in tumor cells. Mol. Cell Biol. 2006;26(8):3181–3193. DOI: 10.1128/MCB.26.8.3181-3193.2006.</mixed-citation></citation-alternatives></ref><ref id="cit53"><label>53</label><citation-alternatives><mixed-citation xml:lang="ru">Jung T.Y., Jung S., Ryu H.H., Jeong Y.I., Jin Y.H., Jin S.G. et al. Role of galectin-1 in migration and invasion of human glioblastoma multiforme cell lines. J. Neurosurg. 2008;109(2):273–284. DOI: 10.3171/JNS/2008/109/8/0273.</mixed-citation><mixed-citation xml:lang="en">Jung T.Y., Jung S., Ryu H.H., Jeong Y.I., Jin Y.H., Jin S.G. et al. Role of galectin-1 in migration and invasion of human glioblastoma multiforme cell lines. J. Neurosurg. 2008;109(2):273–284. DOI: 10.3171/JNS/2008/109/8/0273.</mixed-citation></citation-alternatives></ref><ref id="cit54"><label>54</label><citation-alternatives><mixed-citation xml:lang="ru">Huang Y., Wang H.C., Zhao J., Wu M.H., Shih T.C. Immunosuppressive roles of galectin-1 in the tumor microenvironment. Biomolecules. 2021;11(10):1398. DOI: 10.3390/biom11101398.</mixed-citation><mixed-citation xml:lang="en">Huang Y., Wang H.C., Zhao J., Wu M.H., Shih T.C. Immunosuppressive roles of galectin-1 in the tumor microenvironment. Biomolecules. 2021;11(10):1398. DOI: 10.3390/biom11101398.</mixed-citation></citation-alternatives></ref><ref id="cit55"><label>55</label><citation-alternatives><mixed-citation xml:lang="ru">Fortin S., Le Mercier M., Camby I., Spiegl-Kreinecker S., Berger W., Lefranc F. et al. Galectin-1 is implicated in the protein kinase C epsilon/vimentin-controlled trafficking of integrin-beta1 in glioblastoma cells. Brain Pathol. 2010;20(1):39– 49. DOI: 10.1111/j.1750-3639.2008.00227.x.</mixed-citation><mixed-citation xml:lang="en">Fortin S., Le Mercier M., Camby I., Spiegl-Kreinecker S., Berger W., Lefranc F. et al. Galectin-1 is implicated in the protein kinase C epsilon/vimentin-controlled trafficking of integrin-beta1 in glioblastoma cells. Brain Pathol. 2010;20(1):39– 49. DOI: 10.1111/j.1750-3639.2008.00227.x.</mixed-citation></citation-alternatives></ref><ref id="cit56"><label>56</label><citation-alternatives><mixed-citation xml:lang="ru">Camby I., Belot N., Lefranc F., Sadeghi N., de Launoit Y., Kaltner H. et al. Galectin-1 modulates human glioblastoma cell migration into the brain through modifications to the actin cytoskeleton and levels of expression of small GTPases. J. Neuropathol. Exp. Neurol. 2002;61(7):585–596. DOI: 10.1093/jnen/61.7.585.</mixed-citation><mixed-citation xml:lang="en">Camby I., Belot N., Lefranc F., Sadeghi N., de Launoit Y., Kaltner H. et al. Galectin-1 modulates human glioblastoma cell migration into the brain through modifications to the actin cytoskeleton and levels of expression of small GTPases. J. Neuropathol. Exp. Neurol. 2002;61(7):585–596. DOI: 10.1093/jnen/61.7.585.</mixed-citation></citation-alternatives></ref><ref id="cit57"><label>57</label><citation-alternatives><mixed-citation xml:lang="ru">Al-Koussa H., Atat O.E., Jaafar L., Tashjian H., El-Sibai M. The Role of Rho GTPases in motility and invasion of glioblastoma cells. Anal. Cell. Pathol. (Amst.). 2020;2020:9274016. DOI: 10.1155/2020/9274016.</mixed-citation><mixed-citation xml:lang="en">Al-Koussa H., Atat O.E., Jaafar L., Tashjian H., El-Sibai M. The Role of Rho GTPases in motility and invasion of glioblastoma cells. Anal. Cell. Pathol. (Amst.). 2020;2020:9274016. DOI: 10.1155/2020/9274016.</mixed-citation></citation-alternatives></ref><ref id="cit58"><label>58</label><citation-alternatives><mixed-citation xml:lang="ru">Chen C., Duckworth C.A., Zhao Q., Pritchard D.M., Rhodes J.M., Yu L.G. Increased circulation of galectin-3 in cancer induces secretion of metastasis-promoting cytokines from blood vascular endothelium. Clin. Cancer Res. 2013;19(7):1693– 704. DOI: 10.1158/1078-0432.CCR-12-2940.</mixed-citation><mixed-citation xml:lang="en">Chen C., Duckworth C.A., Zhao Q., Pritchard D.M., Rhodes J.M., Yu L.G. Increased circulation of galectin-3 in cancer induces secretion of metastasis-promoting cytokines from blood vascular endothelium. Clin. Cancer Res. 2013;19(7):1693– 704. DOI: 10.1158/1078-0432.CCR-12-2940.</mixed-citation></citation-alternatives></ref><ref id="cit59"><label>59</label><citation-alternatives><mixed-citation xml:lang="ru">Macke A.J., Pachikov A.N., Divita T.E., Morris M.E., LaGrange C.A., Holzapfel M.S. et al. Targeting the ATF6-mediated ER stress response and autophagy blocks integrin-driven prostate cancer progression. Mol. Cancer Res. 2023;21(9):958–974. DOI: 10.1158/1541-7786.MCR-23-0108.</mixed-citation><mixed-citation xml:lang="en">Macke A.J., Pachikov A.N., Divita T.E., Morris M.E., LaGrange C.A., Holzapfel M.S. et al. Targeting the ATF6-mediated ER stress response and autophagy blocks integrin-driven prostate cancer progression. Mol. Cancer Res. 2023;21(9):958–974. DOI: 10.1158/1541-7786.MCR-23-0108.</mixed-citation></citation-alternatives></ref><ref id="cit60"><label>60</label><citation-alternatives><mixed-citation xml:lang="ru">Marhuenda E., Fabre C., Zhang C., Martin-Fernandez M., Iskratsch T., Saleh A. et al. Glioma stem cells invasive phenotype at optimal stiffness is driven by MGAT5 dependent mechanosensing. J. Exp. Clin. Cancer Res. 2021;40(1):139. DOI: 10.1186/s13046-021-01925-7.</mixed-citation><mixed-citation xml:lang="en">Marhuenda E., Fabre C., Zhang C., Martin-Fernandez M., Iskratsch T., Saleh A. et al. Glioma stem cells invasive phenotype at optimal stiffness is driven by MGAT5 dependent mechanosensing. J. Exp. Clin. Cancer Res. 2021;40(1):139. DOI: 10.1186/s13046-021-01925-7.</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>
