<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE article PUBLIC "-//NLM//DTD JATS (Z39.96) Journal Publishing DTD v1.3 20210610//EN" "JATS-journalpublishing1-3.dtd">
<article article-type="research-article" dtd-version="1.3" xmlns:mml="http://www.w3.org/1998/Math/MathML" xmlns:xlink="http://www.w3.org/1999/xlink" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xml:lang="ru"><front><journal-meta><journal-id journal-id-type="publisher-id">actabiomedica</journal-id><journal-title-group><journal-title xml:lang="ru">Acta Biomedica Scientifica</journal-title><trans-title-group xml:lang="en"><trans-title>Acta Biomedica Scientifica</trans-title></trans-title-group></journal-title-group><issn pub-type="ppub">2541-9420</issn><issn pub-type="epub">2587-9596</issn><publisher><publisher-name>Scientific Centre for Family Health and Human Reproduction Problems</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="doi">10.29413/ABS.2020-5.6.9</article-id><article-id custom-type="elpub" pub-id-type="custom">actabiomedica-2499</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>ЛЕКЦИИ</subject></subj-group><subj-group subj-group-type="section-heading" xml:lang="en"><subject>LECTURES</subject></subj-group></article-categories><title-group><article-title>Роль лизосом в онкогенезе: акцент на деградацию внеклеточного матрикса</article-title><trans-title-group xml:lang="en"><trans-title>The Role of Lysosomes in the Cancer Progression: Focus on the Extracellular Matrix Degradation</trans-title></trans-title-group></title-group><contrib-group><contrib contrib-type="author" corresp="yes"><contrib-id contrib-id-type="orcid">https://orcid.org/0000-0002-0270-404X</contrib-id><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Трухан</surname><given-names>И. С.</given-names></name><name name-style="western" xml:lang="en"><surname>Trukhan</surname><given-names>I. S.</given-names></name></name-alternatives><bio xml:lang="ru"><p>кандидат биологических наук, старший научный сотрудник</p><p>664003, г. Иркутск, ул. Борцов Революции, 1, Россия </p></bio><bio xml:lang="en"/><email xlink:type="simple">PREDEL4@yandex.ru</email><xref ref-type="aff" rid="aff-1"/></contrib><contrib contrib-type="author" corresp="yes"><contrib-id contrib-id-type="orcid">https://orcid.org/0000-0002-2540-4525</contrib-id><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Дремина</surname><given-names>Н. Н.</given-names></name><name name-style="western" xml:lang="en"><surname>Dremina</surname><given-names>N. N.</given-names></name></name-alternatives><bio xml:lang="ru"><p>кандидат биологических наук, старший научный сотрудник</p><p>664003, г. Иркутск, ул. Борцов Революции, 1, Россия </p></bio><bio xml:lang="en"><p>Bortsov Revolyutsii str. 1, Irkutsk 664003, Russian Federation </p></bio><email xlink:type="simple">drema76@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/0000-0003-3980-050X</contrib-id><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Шурыгина</surname><given-names>И. А.</given-names></name><name name-style="western" xml:lang="en"><surname>Shurygina</surname><given-names>I. A.</given-names></name></name-alternatives><bio xml:lang="ru"><p>доктор медицинских наук, профессор РАН, заместитель директора по научной работе</p><p>664003, г. Иркутск, ул. Борцов Революции, 1, Россия </p></bio><bio xml:lang="en"><p>Bortsov Revolyutsii str. 1, Irkutsk 664003, Russian Federation </p></bio><email xlink:type="simple">irinashurygina@gmail.com</email><xref ref-type="aff" rid="aff-1"/></contrib></contrib-group><aff-alternatives id="aff-1"><aff xml:lang="ru"><institution>ФГБНУ «Иркутский научный центр хирургии и травматологии»</institution><country>Россия</country></aff><aff xml:lang="en"><institution>Irkutsk Scientific Centre of Surgery and Traumatology</institution><country>Russian Federation</country></aff></aff-alternatives><pub-date pub-type="collection"><year>2020</year></pub-date><pub-date pub-type="epub"><day>14</day><month>01</month><year>2021</year></pub-date><volume>5</volume><issue>6</issue><fpage>77</fpage><lpage>87</lpage><permissions><copyright-statement>Copyright &amp;#x00A9; Трухан И.С., Дремина Н.Н., Шурыгина И.А., 2021</copyright-statement><copyright-year>2021</copyright-year><copyright-holder xml:lang="ru">Трухан И.С., Дремина Н.Н., Шурыгина И.А.</copyright-holder><copyright-holder xml:lang="en">Trukhan I.S., Dremina N.N., Shurygina I.A.</copyright-holder><license xml:lang="ru" license-type="creative-commons-attribution" xlink:href="https://creativecommons.org/licenses/by/4.0/" xlink:type="simple"><license-p>Данная работа распространяется под лицензией Creative Commons Attribution 4.0.</license-p></license><license xml:lang="en" license-type="creative-commons-attribution" xlink:href="https://creativecommons.org/licenses/by/4.0/" xlink:type="simple"><license-p>This work is licensed under a Creative Commons Attribution 4.0 License.</license-p></license></permissions><self-uri xlink:href="https://www.actabiomedica.ru/jour/article/view/2499">https://www.actabiomedica.ru/jour/article/view/2499</self-uri><abstract/><trans-abstract xml:lang="en"/><kwd-group xml:lang="ru"><kwd>лизосомы</kwd><kwd>инвадоподии</kwd><kwd>внеклеточный матрикс</kwd><kwd>катепсины</kwd><kwd>метастазирование</kwd></kwd-group><kwd-group xml:lang="en"><kwd>lysosomes</kwd><kwd>invadopodia</kwd><kwd>extracellular matrix</kwd><kwd>cathepsins</kwd><kwd>metastasis</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">Ballabio A, Bonifacino JS. Lysosomes as dynamic regulators of cell and organismal homeostasis. Nat Rev Mol Cell Biol. 2020; 21: 101-118. doi: 10.1038/s41580-019-0185-4</mixed-citation><mixed-citation xml:lang="en">Ballabio A, Bonifacino JS. Lysosomes as dynamic regulators of cell and organismal homeostasis. Nat Rev Mol Cell Biol. 2020; 21: 101-118. doi: 10.1038/s41580-019-0185-4</mixed-citation></citation-alternatives></ref><ref id="cit2"><label>2</label><citation-alternatives><mixed-citation xml:lang="ru">Lawrence RE, Zoncu R. The lysosome as a cellular centre for signalling, metabolism and quality control. Nat Cell Biol. 2019; 21(2): 133-142. doi: 10.1038/s41556-018-0244-7</mixed-citation><mixed-citation xml:lang="en">Lawrence RE, Zoncu R. The lysosome as a cellular centre for signalling, metabolism and quality control. Nat Cell Biol. 2019; 21(2): 133-142. doi: 10.1038/s41556-018-0244-7</mixed-citation></citation-alternatives></ref><ref id="cit3"><label>3</label><citation-alternatives><mixed-citation xml:lang="ru">Hanahan D, Weinberg RA. Hallmarks of cancer: The next generation. Cell. 2011; 144(5): 646-674. doi: 10.1016/j.cell.2011.02.013</mixed-citation><mixed-citation xml:lang="en">Hanahan D, Weinberg RA. Hallmarks of cancer: The next generation. Cell. 2011; 144(5): 646-674. doi: 10.1016/j.cell.2011.02.013</mixed-citation></citation-alternatives></ref><ref id="cit4"><label>4</label><citation-alternatives><mixed-citation xml:lang="ru">Ji K, Mayernik L, Moin K, Sloane BF. Acidosis and proteolysis in the tumor microenvironment. Cancer Metastasis Rev. 2019; 38(1-2): 103-112. doi: 10.1007/s10555-019-09796-3</mixed-citation><mixed-citation xml:lang="en">Ji K, Mayernik L, Moin K, Sloane BF. Acidosis and proteolysis in the tumor microenvironment. Cancer Metastasis Rev. 2019; 38(1-2): 103-112. doi: 10.1007/s10555-019-09796-3</mixed-citation></citation-alternatives></ref><ref id="cit5"><label>5</label><citation-alternatives><mixed-citation xml:lang="ru">Pavlova NN, Thompson CB. The emerging hallmarks of cancer metabolism. Cell Metab. 2016; 23(1): 27-47. doi: 10.1016/j.cmet.2015.12.006</mixed-citation><mixed-citation xml:lang="en">Pavlova NN, Thompson CB. The emerging hallmarks of cancer metabolism. Cell Metab. 2016; 23(1): 27-47. doi: 10.1016/j.cmet.2015.12.006</mixed-citation></citation-alternatives></ref><ref id="cit6"><label>6</label><citation-alternatives><mixed-citation xml:lang="ru">Warburg O. The metabolism of carcinoma cells. Cancer Research. 1925; 9(1), 148-163. doi: 10.1158/jcr.1925.148</mixed-citation><mixed-citation xml:lang="en">Warburg O. The metabolism of carcinoma cells. Cancer Research. 1925; 9(1), 148-163. doi: 10.1158/jcr.1925.148</mixed-citation></citation-alternatives></ref><ref id="cit7"><label>7</label><citation-alternatives><mixed-citation xml:lang="ru">Pascale RM, Calvisi DF, Simile MM, Feo CF, Feo F. The Warburg effect 97 years after its discovery. Cancers (Basel). 2020; 12(10): 2819. doi: 10.3390/cancers12102819</mixed-citation><mixed-citation xml:lang="en">Pascale RM, Calvisi DF, Simile MM, Feo CF, Feo F. The Warburg effect 97 years after its discovery. Cancers (Basel). 2020; 12(10): 2819. doi: 10.3390/cancers12102819</mixed-citation></citation-alternatives></ref><ref id="cit8"><label>8</label><citation-alternatives><mixed-citation xml:lang="ru">Boedtkjer E, Pedersen SF. The acidic tumor microenvironment as a driver of cancer. Annu Rev Physiol. 2020; 82: 103-126. doi: 10.1146/annurev-physiol-021119-034627</mixed-citation><mixed-citation xml:lang="en">Boedtkjer E, Pedersen SF. The acidic tumor microenvironment as a driver of cancer. Annu Rev Physiol. 2020; 82: 103-126. doi: 10.1146/annurev-physiol-021119-034627</mixed-citation></citation-alternatives></ref><ref id="cit9"><label>9</label><citation-alternatives><mixed-citation xml:lang="ru">Parks SK, Mueller-Klieser W, Pouysségur J. Lactate and acidity in the cancer microenvironment. Annu Rev Cancer Biol. 2020; 4: 141-158. doi: 10.1146/annurev-cancerbio-030419-033556</mixed-citation><mixed-citation xml:lang="en">Parks SK, Mueller-Klieser W, Pouysségur J. Lactate and acidity in the cancer microenvironment. Annu Rev Cancer Biol. 2020; 4: 141-158. doi: 10.1146/annurev-cancerbio-030419-033556</mixed-citation></citation-alternatives></ref><ref id="cit10"><label>10</label><citation-alternatives><mixed-citation xml:lang="ru">Ko M, Quiñones-Hinojosa A, Rao R. Emerging links between endosomal pH and cancer. Cancer Metastasis Rev. 2020; 39(2): 519-534. doi: 10.1007/s10555-020-09870-1</mixed-citation><mixed-citation xml:lang="en">Ko M, Quiñones-Hinojosa A, Rao R. Emerging links between endosomal pH and cancer. Cancer Metastasis Rev. 2020; 39(2): 519-534. doi: 10.1007/s10555-020-09870-1</mixed-citation></citation-alternatives></ref><ref id="cit11"><label>11</label><citation-alternatives><mixed-citation xml:lang="ru">White KA, Grillo-Hill BK, Barber DL. Cancer cell behaviors mediated by dysregulated pH dynamics at a glance. J Cell Sci. 2017; 130(4): 663-669. doi: 10.1242/jcs.195297</mixed-citation><mixed-citation xml:lang="en">White KA, Grillo-Hill BK, Barber DL. Cancer cell behaviors mediated by dysregulated pH dynamics at a glance. J Cell Sci. 2017; 130(4): 663-669. doi: 10.1242/jcs.195297</mixed-citation></citation-alternatives></ref><ref id="cit12"><label>12</label><citation-alternatives><mixed-citation xml:lang="ru">Heuser J. Changes in lysosome shape and distribution correlated with changes in cytoplasmic pH. J Cell Biol. 1989; 108(3): 855-864. doi: 10.1083/jcb.108.3.855</mixed-citation><mixed-citation xml:lang="en">Heuser J. Changes in lysosome shape and distribution correlated with changes in cytoplasmic pH. J Cell Biol. 1989; 108(3): 855-864. doi: 10.1083/jcb.108.3.855</mixed-citation></citation-alternatives></ref><ref id="cit13"><label>13</label><citation-alternatives><mixed-citation xml:lang="ru">Settembre C, Fraldi A, Medina DL, Ballabio A. Signals from the lysosome: a control centre for cellular clearance and energy metabolism. Nat Rev Mol Cell Biol. 2013; 14(5): 283-296. doi: 10.1038/nrm3565</mixed-citation><mixed-citation xml:lang="en">Settembre C, Fraldi A, Medina DL, Ballabio A. Signals from the lysosome: a control centre for cellular clearance and energy metabolism. Nat Rev Mol Cell Biol. 2013; 14(5): 283-296. doi: 10.1038/nrm3565</mixed-citation></citation-alternatives></ref><ref id="cit14"><label>14</label><citation-alternatives><mixed-citation xml:lang="ru">Rozhin J, Sameni M, Ziegler G, Sloane BF. Pericellular pH affects distribution and secretion of cathepsin B in malignant cells. Cancer Res. 1994; 54(24): 6517-6525.</mixed-citation><mixed-citation xml:lang="en">Rozhin J, Sameni M, Ziegler G, Sloane BF. Pericellular pH affects distribution and secretion of cathepsin B in malignant cells. Cancer Res. 1994; 54(24): 6517-6525.</mixed-citation></citation-alternatives></ref><ref id="cit15"><label>15</label><citation-alternatives><mixed-citation xml:lang="ru">Hazen LG, Bleeker FE, Lauritzen B, Bahns S, Song J, Jonker A, et al. Comparative localization of cathepsin B protein and activity in colorectal cancer. J Histochem Cytochem. 2000; 48(10): 1421-1430. doi: 10.1177/002215540004801012</mixed-citation><mixed-citation xml:lang="en">Hazen LG, Bleeker FE, Lauritzen B, Bahns S, Song J, Jonker A, et al. Comparative localization of cathepsin B protein and activity in colorectal cancer. J Histochem Cytochem. 2000; 48(10): 1421-1430. doi: 10.1177/002215540004801012</mixed-citation></citation-alternatives></ref><ref id="cit16"><label>16</label><citation-alternatives><mixed-citation xml:lang="ru">Dykes SS, Steffan JJ, Cardelli JA. Lysosome trafficking is necessary for EGF-driven invasion and is regulated by p38 MAPK and Na+/H+ exchangers. BMC Cancer. 2017; 17(1): 672. doi: 10.1186/s12885-017-3660-3</mixed-citation><mixed-citation xml:lang="en">Dykes SS, Steffan JJ, Cardelli JA. Lysosome trafficking is necessary for EGF-driven invasion and is regulated by p38 MAPK and Na+/H+ exchangers. BMC Cancer. 2017; 17(1): 672. doi: 10.1186/s12885-017-3660-3</mixed-citation></citation-alternatives></ref><ref id="cit17"><label>17</label><citation-alternatives><mixed-citation xml:lang="ru">Steffan JJ, Williams BC, Welbourne T, Cardelli JA. HGFinduced invasion by prostate tumor cells requires anterograde lysosome trafficking and activity of Na+–H+ exchangers. J Cell Sci. 2010; 123(Pt 7): 1151-1159. doi: 10.1242/jcs.063644</mixed-citation><mixed-citation xml:lang="en">Steffan JJ, Williams BC, Welbourne T, Cardelli JA. HGFinduced invasion by prostate tumor cells requires anterograde lysosome trafficking and activity of Na+–H+ exchangers. J Cell Sci. 2010; 123(Pt 7): 1151-1159. doi: 10.1242/jcs.063644</mixed-citation></citation-alternatives></ref><ref id="cit18"><label>18</label><citation-alternatives><mixed-citation xml:lang="ru">Glunde K, Guggino SE, Solaiyappan M, Pathak AP, Ichikawa Y, Bhujwalla ZM. Extracellular acidification alters lysosomal trafficking in human breast cancer cells. Neoplasia. 2003; 5(6): 533-545. doi: 10.1016/s1476-5586(03)80037-4</mixed-citation><mixed-citation xml:lang="en">Glunde K, Guggino SE, Solaiyappan M, Pathak AP, Ichikawa Y, Bhujwalla ZM. Extracellular acidification alters lysosomal trafficking in human breast cancer cells. Neoplasia. 2003; 5(6): 533-545. doi: 10.1016/s1476-5586(03)80037-4</mixed-citation></citation-alternatives></ref><ref id="cit19"><label>19</label><citation-alternatives><mixed-citation xml:lang="ru">Damaghi M, Tafreshi NK, Lloyd MC, Sprung R, Estrella V, Wojtkowiak JW, et al. Chronic acidosis in the tumour microenvironment selects for overexpression of LAMP2 in the plasma membrane. Nat Commun. 2015; 6: 8752. doi: 10.1038/ncomms9752</mixed-citation><mixed-citation xml:lang="en">Damaghi M, Tafreshi NK, Lloyd MC, Sprung R, Estrella V, Wojtkowiak JW, et al. Chronic acidosis in the tumour microenvironment selects for overexpression of LAMP2 in the plasma membrane. Nat Commun. 2015; 6: 8752. doi: 10.1038/ncomms9752</mixed-citation></citation-alternatives></ref><ref id="cit20"><label>20</label><citation-alternatives><mixed-citation xml:lang="ru">Castro-Gomes T, Corrotte M, Tam C, Andrews NW. Plasma membrane repair is regulated extracellularly by proteases released from lysosomes. PLoS One. 2016; 11(3): e0152583. doi: 10.1371/journal.pone.0152583</mixed-citation><mixed-citation xml:lang="en">Castro-Gomes T, Corrotte M, Tam C, Andrews NW. Plasma membrane repair is regulated extracellularly by proteases released from lysosomes. PLoS One. 2016; 11(3): e0152583. doi: 10.1371/journal.pone.0152583</mixed-citation></citation-alternatives></ref><ref id="cit21"><label>21</label><citation-alternatives><mixed-citation xml:lang="ru">Sameni M, Elliott E, Ziegler G, Fortgens PH, Dennison C, Sloane BF. Cathepsin B and D are localized at the surface of human breast cancer cells. Pathol Oncol Res. 1995; 1(1): 43-53. doi: 10.1007/BF02893583</mixed-citation><mixed-citation xml:lang="en">Sameni M, Elliott E, Ziegler G, Fortgens PH, Dennison C, Sloane BF. Cathepsin B and D are localized at the surface of human breast cancer cells. Pathol Oncol Res. 1995; 1(1): 43-53. doi: 10.1007/BF02893583</mixed-citation></citation-alternatives></ref><ref id="cit22"><label>22</label><citation-alternatives><mixed-citation xml:lang="ru">Paterson EK, Courtneidge SA. Invadosomes are coming: new insights into function and disease relevance. FEBS J. 2018; 285(1): 8-27. doi: 10.1111/febs.14123</mixed-citation><mixed-citation xml:lang="en">Paterson EK, Courtneidge SA. Invadosomes are coming: new insights into function and disease relevance. FEBS J. 2018; 285(1): 8-27. doi: 10.1111/febs.14123</mixed-citation></citation-alternatives></ref><ref id="cit23"><label>23</label><citation-alternatives><mixed-citation xml:lang="ru">Brisson L, Reshkin SJ, Goré J, Roger S. pH regulators in invadosomal functioning: Proton delivery for matrix tasting. Eur J Cell Biol. 2012; 91(11-12): 847-860. doi: 10.1016/j.ejcb.2012.04.004</mixed-citation><mixed-citation xml:lang="en">Brisson L, Reshkin SJ, Goré J, Roger S. pH regulators in invadosomal functioning: Proton delivery for matrix tasting. Eur J Cell Biol. 2012; 91(11-12): 847-860. doi: 10.1016/j.ejcb.2012.04.004</mixed-citation></citation-alternatives></ref><ref id="cit24"><label>24</label><citation-alternatives><mixed-citation xml:lang="ru">Tu C, Ortega-Cava CF, Chen G, Fernandes ND, CavalloMedved D, Sloane BF, et al. Lysosomal cathepsin B participates in the podosome-mediated extracellular matrix degradation and invasion via secreted lysosomes in v-Src fibroblasts. Cancer Res. 2008; 68(22): 9147-9156. doi: 10.1158/0008-5472.CAN-07-5127</mixed-citation><mixed-citation xml:lang="en">Tu C, Ortega-Cava CF, Chen G, Fernandes ND, CavalloMedved D, Sloane BF, et al. Lysosomal cathepsin B participates in the podosome-mediated extracellular matrix degradation and invasion via secreted lysosomes in v-Src fibroblasts. Cancer Res. 2008; 68(22): 9147-9156. doi: 10.1158/0008-5472.CAN-07-5127</mixed-citation></citation-alternatives></ref><ref id="cit25"><label>25</label><citation-alternatives><mixed-citation xml:lang="ru">Kryczka J, Papiewska-Pajak I, Kowalska MA, Boncela J. Cathepsin B is upregulated and mediates ECM degradation in colon adenocarcinoma HT29 cells overexpressing snail. Cells. 2019; 8(3): 203. doi: 10.3390/cells8030203</mixed-citation><mixed-citation xml:lang="en">Kryczka J, Papiewska-Pajak I, Kowalska MA, Boncela J. Cathepsin B is upregulated and mediates ECM degradation in colon adenocarcinoma HT29 cells overexpressing snail. Cells. 2019; 8(3): 203. doi: 10.3390/cells8030203</mixed-citation></citation-alternatives></ref><ref id="cit26"><label>26</label><citation-alternatives><mixed-citation xml:lang="ru">Linder S, Wiesner C, Himmel M. Degrading devices: Invadosomes in proteolytic cell invasion. Annu Rev Cell Dev Biol. 2011; 27: 185-211. doi: 10.1146/annurev-cellbio-092910-154216</mixed-citation><mixed-citation xml:lang="en">Linder S, Wiesner C, Himmel M. Degrading devices: Invadosomes in proteolytic cell invasion. Annu Rev Cell Dev Biol. 2011; 27: 185-211. doi: 10.1146/annurev-cellbio-092910-154216</mixed-citation></citation-alternatives></ref><ref id="cit27"><label>27</label><citation-alternatives><mixed-citation xml:lang="ru">Vasiljeva O, Hostetter DR, Moore SJ, Winter MB. The multifaceted roles of tumor-associated proteases and harnessing their activity for prodrug activation. Biol Chem. 2019; 400(8): 965-977. doi: 10.1515/hsz-2018-0451</mixed-citation><mixed-citation xml:lang="en">Vasiljeva O, Hostetter DR, Moore SJ, Winter MB. The multifaceted roles of tumor-associated proteases and harnessing their activity for prodrug activation. Biol Chem. 2019; 400(8): 965-977. doi: 10.1515/hsz-2018-0451</mixed-citation></citation-alternatives></ref><ref id="cit28"><label>28</label><citation-alternatives><mixed-citation xml:lang="ru">Kramer L, Turk D, Turk B. The future of cysteine cathepsins in disease management. Trends Pharmacol Sci. 2017; 38(10): 873-898. doi: 10.1016/j.tips.2017.06.003</mixed-citation><mixed-citation xml:lang="en">Kramer L, Turk D, Turk B. The future of cysteine cathepsins in disease management. Trends Pharmacol Sci. 2017; 38(10): 873-898. doi: 10.1016/j.tips.2017.06.003</mixed-citation></citation-alternatives></ref><ref id="cit29"><label>29</label><citation-alternatives><mixed-citation xml:lang="ru">Vizovišek M, Fonović M, Turk B. Cysteine cathepsins in extracellular matrix remodeling: Extracellular matrix degradation and beyond. Matrix Biol. 2019; 75-76: 141- 159. doi: 10.1016/j.matbio.2018.01.024</mixed-citation><mixed-citation xml:lang="en">Vizovišek M, Fonović M, Turk B. Cysteine cathepsins in extracellular matrix remodeling: Extracellular matrix degradation and beyond. Matrix Biol. 2019; 75-76: 141- 159. doi: 10.1016/j.matbio.2018.01.024</mixed-citation></citation-alternatives></ref><ref id="cit30"><label>30</label><citation-alternatives><mixed-citation xml:lang="ru">Vidak E, Javoršek U, Vizovišek M, Turk B. Cysteine cathepsins and their extracellular roles: Shaping the microenvironment. Cells. 2019; 8(3): 264. doi: 10.3390/cells8030264</mixed-citation><mixed-citation xml:lang="en">Vidak E, Javoršek U, Vizovišek M, Turk B. Cysteine cathepsins and their extracellular roles: Shaping the microenvironment. Cells. 2019; 8(3): 264. doi: 10.3390/cells8030264</mixed-citation></citation-alternatives></ref><ref id="cit31"><label>31</label><citation-alternatives><mixed-citation xml:lang="ru">Yadati T, Houben T, Bitorina A, Shiri-Sverdlov R. The ins and outs of cathepsins: Physiological function and role in disease management. Cells. 2020; 9(7): 1679. doi: 10.3390/cells9071679</mixed-citation><mixed-citation xml:lang="en">Yadati T, Houben T, Bitorina A, Shiri-Sverdlov R. The ins and outs of cathepsins: Physiological function and role in disease management. Cells. 2020; 9(7): 1679. doi: 10.3390/cells9071679</mixed-citation></citation-alternatives></ref><ref id="cit32"><label>32</label><citation-alternatives><mixed-citation xml:lang="ru">Verbovšek U, Van Noorden CJ, Lah TT. Complexity of cancer protease biology: Cathepsin K expression and function in cancer progression. Semin Cancer Biol. 2015; 35: 71-84. doi: 10.1016/j.semcancer.2015.08.010</mixed-citation><mixed-citation xml:lang="en">Verbovšek U, Van Noorden CJ, Lah TT. Complexity of cancer protease biology: Cathepsin K expression and function in cancer progression. Semin Cancer Biol. 2015; 35: 71-84. doi: 10.1016/j.semcancer.2015.08.010</mixed-citation></citation-alternatives></ref><ref id="cit33"><label>33</label><citation-alternatives><mixed-citation xml:lang="ru">Lah TT, Cercek M, Blejec A, Kos J, Gorodetsky E, Somers R, et al. Cathepsin B, a prognostic indicator in lymph node-negative breast carcinoma patients: comparison with cathepsin D, cathepsin L, and other clinical indicators. Clin Cancer Res. 2000; 6(2): 578-584.</mixed-citation><mixed-citation xml:lang="en">Lah TT, Cercek M, Blejec A, Kos J, Gorodetsky E, Somers R, et al. Cathepsin B, a prognostic indicator in lymph node-negative breast carcinoma patients: comparison with cathepsin D, cathepsin L, and other clinical indicators. Clin Cancer Res. 2000; 6(2): 578-584.</mixed-citation></citation-alternatives></ref><ref id="cit34"><label>34</label><citation-alternatives><mixed-citation xml:lang="ru">Gocheva V, Wang HW, Gadea BB, Shree T, Hunter KE, Garfall AL, et al. IL-4 induces cathepsin protease activity in tumorassociated macrophages to promote cancer growth and invasion. Genes Dev. 2010; 24(3): 241-255. doi: 10.1101/gad.1874010</mixed-citation><mixed-citation xml:lang="en">Gocheva V, Wang HW, Gadea BB, Shree T, Hunter KE, Garfall AL, et al. IL-4 induces cathepsin protease activity in tumorassociated macrophages to promote cancer growth and invasion. Genes Dev. 2010; 24(3): 241-255. doi: 10.1101/gad.1874010</mixed-citation></citation-alternatives></ref><ref id="cit35"><label>35</label><citation-alternatives><mixed-citation xml:lang="ru">Tripathi R, Fiore LS, Richards DL, Yang Y, Liu J, Wang C, et al. Abl and Arg mediate cysteine cathepsin secretion to facilitate melanoma invasion and metastasis. Sci Signal. 2018; 11(518): eaao0422. doi: 10.1126/scisignal.aao0422</mixed-citation><mixed-citation xml:lang="en">Tripathi R, Fiore LS, Richards DL, Yang Y, Liu J, Wang C, et al. Abl and Arg mediate cysteine cathepsin secretion to facilitate melanoma invasion and metastasis. Sci Signal. 2018; 11(518): eaao0422. doi: 10.1126/scisignal.aao0422</mixed-citation></citation-alternatives></ref><ref id="cit36"><label>36</label><citation-alternatives><mixed-citation xml:lang="ru">Chen S, Dong H, Yang S, Guo H. Cathepsins in digestive cancers. Oncotarget. 2017; 8(25): 41690-41700. doi: 10.18632/oncotarget.16677</mixed-citation><mixed-citation xml:lang="en">Chen S, Dong H, Yang S, Guo H. Cathepsins in digestive cancers. Oncotarget. 2017; 8(25): 41690-41700. doi: 10.18632/oncotarget.16677</mixed-citation></citation-alternatives></ref><ref id="cit37"><label>37</label><citation-alternatives><mixed-citation xml:lang="ru">da Costa AC, Santa-Cruz F, Mattos LAR, Rêgo Aquino MA, Martins CR, Bandeira Ferraz ÁA, et al. Cathepsin S as a target in gastric cancer. Mol Clin Oncol. 2020; 12(2): 99-103. doi: 10.3892/mco.2019.1958</mixed-citation><mixed-citation xml:lang="en">da Costa AC, Santa-Cruz F, Mattos LAR, Rêgo Aquino MA, Martins CR, Bandeira Ferraz ÁA, et al. Cathepsin S as a target in gastric cancer. Mol Clin Oncol. 2020; 12(2): 99-103. doi: 10.3892/mco.2019.1958</mixed-citation></citation-alternatives></ref><ref id="cit38"><label>38</label><citation-alternatives><mixed-citation xml:lang="ru">Singh N, Saraya A. Roles of cathepsins in pancreatic cancer. Trop Gastroenterol. 2016; 37(2): 77-85.</mixed-citation><mixed-citation xml:lang="en">Singh N, Saraya A. Roles of cathepsins in pancreatic cancer. Trop Gastroenterol. 2016; 37(2): 77-85.</mixed-citation></citation-alternatives></ref><ref id="cit39"><label>39</label><citation-alternatives><mixed-citation xml:lang="ru">Fernández PL, Farré X, Nadal A, Fernández E, Peiró N, Sloane BF, et al. Expression of cathepsins B and S in the progression of prostate carcinoma. Int J Cancer. 2001; 95(1): 51-55. doi: 10.1002/1097-0215(20010120)95:1&lt;51::aid-ijc1009&gt;3.0.co;2-j</mixed-citation><mixed-citation xml:lang="en">Fernández PL, Farré X, Nadal A, Fernández E, Peiró N, Sloane BF, et al. Expression of cathepsins B and S in the progression of prostate carcinoma. Int J Cancer. 2001; 95(1): 51-55. doi: 10.1002/1097-0215(20010120)95:1&lt;51::aid-ijc1009&gt;3.0.co;2-j</mixed-citation></citation-alternatives></ref><ref id="cit40"><label>40</label><citation-alternatives><mixed-citation xml:lang="ru">Wang J, Chen L, Li Y, Guan XY. Overexpression of cathepsin Z contributes to tumor metastasis by inducing epithelialmesenchymal transition in hepatocellular carcinoma. PLoS One. 2011; 6(9): e24967. doi: 10.1371/journal.pone.0024967</mixed-citation><mixed-citation xml:lang="en">Wang J, Chen L, Li Y, Guan XY. Overexpression of cathepsin Z contributes to tumor metastasis by inducing epithelialmesenchymal transition in hepatocellular carcinoma. PLoS One. 2011; 6(9): e24967. doi: 10.1371/journal.pone.0024967</mixed-citation></citation-alternatives></ref><ref id="cit41"><label>41</label><citation-alternatives><mixed-citation xml:lang="ru">Kuester D, Lippert H, Roessner A, Krueger S. The cathepsin family and their role in colorectal cancer. Pathol Res Pract. 2008; 204(7): 491-500. doi: 10.1016/j.prp.2008.04.010</mixed-citation><mixed-citation xml:lang="en">Kuester D, Lippert H, Roessner A, Krueger S. The cathepsin family and their role in colorectal cancer. Pathol Res Pract. 2008; 204(7): 491-500. doi: 10.1016/j.prp.2008.04.010</mixed-citation></citation-alternatives></ref><ref id="cit42"><label>42</label><citation-alternatives><mixed-citation xml:lang="ru">Hölzen L, Parigiani MA, Reinheckel T. Tumor cell- and microenvironment-specific roles of cysteine cathepsins in mouse models of human cancers. Biochim Biophys Acta Proteins Proteom. 2020; 1868(7): 140423. doi: 10.1016/j.bbapap.2020.140423</mixed-citation><mixed-citation xml:lang="en">Hölzen L, Parigiani MA, Reinheckel T. Tumor cell- and microenvironment-specific roles of cysteine cathepsins in mouse models of human cancers. Biochim Biophys Acta Proteins Proteom. 2020; 1868(7): 140423. doi: 10.1016/j.bbapap.2020.140423</mixed-citation></citation-alternatives></ref><ref id="cit43"><label>43</label><citation-alternatives><mixed-citation xml:lang="ru">Maacha S, Hong J, von Lersner A, Zijlstra A, Belkhiri A. AXL mediates esophageal adenocarcinoma cell invasion through regulation of extracellular acidification and lysosome trafficking. Neoplasia. 2018; 20(10): 1008-1022. doi: 10.1016/j.neo.2018.08.005</mixed-citation><mixed-citation xml:lang="en">Maacha S, Hong J, von Lersner A, Zijlstra A, Belkhiri A. AXL mediates esophageal adenocarcinoma cell invasion through regulation of extracellular acidification and lysosome trafficking. Neoplasia. 2018; 20(10): 1008-1022. doi: 10.1016/j.neo.2018.08.005</mixed-citation></citation-alternatives></ref><ref id="cit44"><label>44</label><citation-alternatives><mixed-citation xml:lang="ru">Mijanović O, Branković A, Panin AN, Savchuk S, Timashev P, Ulasov I, et al. Cathepsin B: A sellsword of cancer progression. Cancer Lett. 2019; 449: 207-214. doi: 10.1016/j.canlet.2019.02.035</mixed-citation><mixed-citation xml:lang="en">Mijanović O, Branković A, Panin AN, Savchuk S, Timashev P, Ulasov I, et al. Cathepsin B: A sellsword of cancer progression. Cancer Lett. 2019; 449: 207-214. doi: 10.1016/j.canlet.2019.02.035</mixed-citation></citation-alternatives></ref><ref id="cit45"><label>45</label><citation-alternatives><mixed-citation xml:lang="ru">Liaudet-Coopman E, Beaujouin M, Derocq D, Garcia M, Glondu-Lassis M, Laurent-Matha V, et al. Cathepsin D: Newly discovered functions of a long-standing aspartic protease in cancer and apoptosis. Cancer Lett. 2006; 237(2): 167-179. doi: 10.1016/j.canlet.2005.06.007</mixed-citation><mixed-citation xml:lang="en">Liaudet-Coopman E, Beaujouin M, Derocq D, Garcia M, Glondu-Lassis M, Laurent-Matha V, et al. Cathepsin D: Newly discovered functions of a long-standing aspartic protease in cancer and apoptosis. Cancer Lett. 2006; 237(2): 167-179. doi: 10.1016/j.canlet.2005.06.007</mixed-citation></citation-alternatives></ref><ref id="cit46"><label>46</label><citation-alternatives><mixed-citation xml:lang="ru">Korkmaz B, Horwitz MS, Jenne DE, Gauthier F. Neutrophil elastase, proteinase 3, and cathepsin G as therapeutic targets in human diseases. Pharmacol Rev. 2010; 62(4): 726-759. doi: 10.1124/pr.110.002733</mixed-citation><mixed-citation xml:lang="en">Korkmaz B, Horwitz MS, Jenne DE, Gauthier F. Neutrophil elastase, proteinase 3, and cathepsin G as therapeutic targets in human diseases. Pharmacol Rev. 2010; 62(4): 726-759. doi: 10.1124/pr.110.002733</mixed-citation></citation-alternatives></ref><ref id="cit47"><label>47</label><citation-alternatives><mixed-citation xml:lang="ru">Kozlowski L, Wojtukiewicz MZ, Ostrowska H. Cathepsin A activity in primary and metastatic human melanocytic tumors. Arch Dermatol Res. 2000; 292(2-3): 68-71. doi: 10.1007/s004030050012</mixed-citation><mixed-citation xml:lang="en">Kozlowski L, Wojtukiewicz MZ, Ostrowska H. Cathepsin A activity in primary and metastatic human melanocytic tumors. Arch Dermatol Res. 2000; 292(2-3): 68-71. doi: 10.1007/s004030050012</mixed-citation></citation-alternatives></ref><ref id="cit48"><label>48</label><citation-alternatives><mixed-citation xml:lang="ru">Hu B, Zhu X, Lu J. Cathepsin A knockdown decreases the proliferation and invasion of A549 lung adenocarcinoma cells. Mol Med Rep. 2020; 21(6): 2553-2559. doi: 10.3892/mmr.2020.11068</mixed-citation><mixed-citation xml:lang="en">Hu B, Zhu X, Lu J. Cathepsin A knockdown decreases the proliferation and invasion of A549 lung adenocarcinoma cells. Mol Med Rep. 2020; 21(6): 2553-2559. doi: 10.3892/mmr.2020.11068</mixed-citation></citation-alternatives></ref><ref id="cit49"><label>49</label><citation-alternatives><mixed-citation xml:lang="ru">Ni S, Weng W, Xu M, Wang Q, Tan C, Sun H, et al. miR-106b-5p inhibits the invasion and metastasis of colorectal cancer by targeting CTSA. Onco Targets Ther. 2018; 11: 3835-3845. doi: 10.2147/OTT.S172887</mixed-citation><mixed-citation xml:lang="en">Ni S, Weng W, Xu M, Wang Q, Tan C, Sun H, et al. miR-106b-5p inhibits the invasion and metastasis of colorectal cancer by targeting CTSA. Onco Targets Ther. 2018; 11: 3835-3845. doi: 10.2147/OTT.S172887</mixed-citation></citation-alternatives></ref><ref id="cit50"><label>50</label><citation-alternatives><mixed-citation xml:lang="ru">Toss MS, Miligy IM, Haj-Ahmad R, Gorringe KL, AlKawaz A, Mittal K, et al. The prognostic significance of lysosomal protective protein (cathepsin A) in breast ductal carcinoma in situ. Histopathology. 2019; 74(7): 1025-1035. doi: 10.1111/his.13835</mixed-citation><mixed-citation xml:lang="en">Toss MS, Miligy IM, Haj-Ahmad R, Gorringe KL, AlKawaz A, Mittal K, et al. The prognostic significance of lysosomal protective protein (cathepsin A) in breast ductal carcinoma in situ. Histopathology. 2019; 74(7): 1025-1035. doi: 10.1111/his.13835</mixed-citation></citation-alternatives></ref><ref id="cit51"><label>51</label><citation-alternatives><mixed-citation xml:lang="ru">Du Z, Liu X, Wei X, Luo H, Li P, Shi M, et al. Quantitative proteomics identifies a plasma multi-protein model for detection of hepatocellular carcinoma. Sci Rep. 2020; 10(1): 15552. doi: 10.1038/s41598-020-72510-9</mixed-citation><mixed-citation xml:lang="en">Du Z, Liu X, Wei X, Luo H, Li P, Shi M, et al. Quantitative proteomics identifies a plasma multi-protein model for detection of hepatocellular carcinoma. Sci Rep. 2020; 10(1): 15552. doi: 10.1038/s41598-020-72510-9</mixed-citation></citation-alternatives></ref><ref id="cit52"><label>52</label><citation-alternatives><mixed-citation xml:lang="ru">Burster T, Macmillan H, Hou T, Boehm BO, Mellins ED. Cathepsin G: Roles in antigen presentation and beyond. Mol Immunol. 2010; 47(4): 658-665. doi: 10.1016/j.molimm.2009.10.003</mixed-citation><mixed-citation xml:lang="en">Burster T, Macmillan H, Hou T, Boehm BO, Mellins ED. Cathepsin G: Roles in antigen presentation and beyond. Mol Immunol. 2010; 47(4): 658-665. doi: 10.1016/j.molimm.2009.10.003</mixed-citation></citation-alternatives></ref><ref id="cit53"><label>53</label><citation-alternatives><mixed-citation xml:lang="ru">Gao S, Zhu H, Zuo X, Luo H. Cathepsin G and its role in inflammation and autoimmune diseases. Arch Rheumatol. 2018; 33(4): 498-504. doi: 10.5606/ArchRheumatol.2018.6595</mixed-citation><mixed-citation xml:lang="en">Gao S, Zhu H, Zuo X, Luo H. Cathepsin G and its role in inflammation and autoimmune diseases. Arch Rheumatol. 2018; 33(4): 498-504. doi: 10.5606/ArchRheumatol.2018.6595</mixed-citation></citation-alternatives></ref><ref id="cit54"><label>54</label><citation-alternatives><mixed-citation xml:lang="ru">Yui S, Osawa Y, Ichisugi T, Morimoto-Kamata R. Neutrophil cathepsin G, but not elastase, induces aggregation of MCF-7 mammary carcinoma cells by a protease activity-dependent cell-oriented mechanism. Mediators Inflamm. 2014; 2014: 971409. doi: 10.1155/2014/971409</mixed-citation><mixed-citation xml:lang="en">Yui S, Osawa Y, Ichisugi T, Morimoto-Kamata R. Neutrophil cathepsin G, but not elastase, induces aggregation of MCF-7 mammary carcinoma cells by a protease activity-dependent cell-oriented mechanism. Mediators Inflamm. 2014; 2014: 971409. doi: 10.1155/2014/971409</mixed-citation></citation-alternatives></ref><ref id="cit55"><label>55</label><citation-alternatives><mixed-citation xml:lang="ru">Maksimowicz T, Chyczewska E, Chyczewski L, Nikliński J, Ostrowska H, Szyszko J, et al. Activity and tissue localization of cathepsin G in non-small cell lung cancer. Rocz Akad Med Bialymst. 1997; 42(Suppl 1): 199-216.</mixed-citation><mixed-citation xml:lang="en">Maksimowicz T, Chyczewska E, Chyczewski L, Nikliński J, Ostrowska H, Szyszko J, et al. Activity and tissue localization of cathepsin G in non-small cell lung cancer. Rocz Akad Med Bialymst. 1997; 42(Suppl 1): 199-216.</mixed-citation></citation-alternatives></ref><ref id="cit56"><label>56</label><citation-alternatives><mixed-citation xml:lang="ru">Morimoto-Kamata R, Mizoguchi S, Ichisugi T, Yui S. Cathepsin G induces cell aggregation of human breast cancer MCF-7 cells via a 2-step mechanism: Catalytic site-independent binding to the cell surface and enzymatic activity-dependent induction of the cell aggregation. Mediators Inflamm. 2012; 2012: 456462. doi: 10.1155/2012/456462</mixed-citation><mixed-citation xml:lang="en">Morimoto-Kamata R, Mizoguchi S, Ichisugi T, Yui S. Cathepsin G induces cell aggregation of human breast cancer MCF-7 cells via a 2-step mechanism: Catalytic site-independent binding to the cell surface and enzymatic activity-dependent induction of the cell aggregation. Mediators Inflamm. 2012; 2012: 456462. doi: 10.1155/2012/456462</mixed-citation></citation-alternatives></ref><ref id="cit57"><label>57</label><citation-alternatives><mixed-citation xml:lang="ru">Kim J, Bae JS. Tumor-associated macrophages and neutrophils in tumor microenvironment. Mediators Inflamm. 2016; 2016: 6058147. doi: 10.1155/2016/6058147</mixed-citation><mixed-citation xml:lang="en">Kim J, Bae JS. Tumor-associated macrophages and neutrophils in tumor microenvironment. Mediators Inflamm. 2016; 2016: 6058147. doi: 10.1155/2016/6058147</mixed-citation></citation-alternatives></ref><ref id="cit58"><label>58</label><citation-alternatives><mixed-citation xml:lang="ru">Wilson TJ, Nannuru KC, Singh RK. Cathepsin G-mediated activation of pro-matrix metalloproteinase 9 at the tumor-bone interface promotes transforming growth factor-beta signaling and bone destruction. Mol Cancer Res. 2009; 7(8): 1224-1233. doi: 10.1158/1541-7786.MCR-09-0028</mixed-citation><mixed-citation xml:lang="en">Wilson TJ, Nannuru KC, Singh RK. Cathepsin G-mediated activation of pro-matrix metalloproteinase 9 at the tumor-bone interface promotes transforming growth factor-beta signaling and bone destruction. Mol Cancer Res. 2009; 7(8): 1224-1233. doi: 10.1158/1541-7786.MCR-09-0028</mixed-citation></citation-alternatives></ref><ref id="cit59"><label>59</label><citation-alternatives><mixed-citation xml:lang="ru">Shamamian P, Schwartz JD, Pocock BJ, Monea S, Whiting D, Marcus SG, et al. Activation of progelatinase A (MMP-2) by neutrophil elastase, cathepsin G, and proteinase-3: A role for inflammatory cells in tumor invasion and angiogenesis. J Cell Physiol. 2001; 189(2): 197-206. doi: 10.1002/jcp.10014</mixed-citation><mixed-citation xml:lang="en">Shamamian P, Schwartz JD, Pocock BJ, Monea S, Whiting D, Marcus SG, et al. Activation of progelatinase A (MMP-2) by neutrophil elastase, cathepsin G, and proteinase-3: A role for inflammatory cells in tumor invasion and angiogenesis. J Cell Physiol. 2001; 189(2): 197-206. doi: 10.1002/jcp.10014</mixed-citation></citation-alternatives></ref><ref id="cit60"><label>60</label><citation-alternatives><mixed-citation xml:lang="ru">Drag B, Petersen LC. Activation of pro-urokinase by cathepsin G in the presence of glucosaminoglycans. Fibrinolysis. 1994; 8: 192-199.</mixed-citation><mixed-citation xml:lang="en">Drag B, Petersen LC. Activation of pro-urokinase by cathepsin G in the presence of glucosaminoglycans. Fibrinolysis. 1994; 8: 192-199.</mixed-citation></citation-alternatives></ref><ref id="cit61"><label>61</label><citation-alternatives><mixed-citation xml:lang="ru">Bastos P, Magalhães S, Santos LL, Ferreira R, Vitorino R. The role of urinary proteases in bladder cancer. In: Chakraborti S, Dhalla N. Pathophysiological aspects of proteases. Singapore: Springer; 2017. doi: 10.1007/978-981-10-6141-7_4</mixed-citation><mixed-citation xml:lang="en">Bastos P, Magalhães S, Santos LL, Ferreira R, Vitorino R. The role of urinary proteases in bladder cancer. In: Chakraborti S, Dhalla N. Pathophysiological aspects of proteases. Singapore: Springer; 2017. doi: 10.1007/978-981-10-6141-7_4</mixed-citation></citation-alternatives></ref><ref id="cit62"><label>62</label><citation-alternatives><mixed-citation xml:lang="ru">Leto G, Tumminello FM, Crescimanno M, Flandina C, Gebbia N. Cathepsin D expression levels in nongynecological solid tumors: Clinical and therapeutic implications. Clin Exp Metastasis. 2004; 21(2): 91-106. doi: 10.1023/b:clin.0000024740.44602.b7</mixed-citation><mixed-citation xml:lang="en">Leto G, Tumminello FM, Crescimanno M, Flandina C, Gebbia N. Cathepsin D expression levels in nongynecological solid tumors: Clinical and therapeutic implications. Clin Exp Metastasis. 2004; 21(2): 91-106. doi: 10.1023/b:clin.0000024740.44602.b7</mixed-citation></citation-alternatives></ref><ref id="cit63"><label>63</label><citation-alternatives><mixed-citation xml:lang="ru">Masson O, Bach AS, Derocq D, Prébois C, LaurentMatha V, Pattingre S, et al. Pathophysiological functions of cathepsin D: Targeting its catalytic activity versus its protein binding activity? Biochimie. 2010; 92(11): 1635-1643. doi: 10.1016/j.biochi.2010.05.009</mixed-citation><mixed-citation xml:lang="en">Masson O, Bach AS, Derocq D, Prébois C, LaurentMatha V, Pattingre S, et al. Pathophysiological functions of cathepsin D: Targeting its catalytic activity versus its protein binding activity? Biochimie. 2010; 92(11): 1635-1643. doi: 10.1016/j.biochi.2010.05.009</mixed-citation></citation-alternatives></ref><ref id="cit64"><label>64</label><citation-alternatives><mixed-citation xml:lang="ru">O’Donoghue AJ, Ivry SL, Chaudhury C, Hostetter DR, Hanahan D, Craik CS. Procathepsin E is highly abundant but minimally active in pancreatic ductal adenocarcinoma tumors. Biol Chem. 2016; 397(9): 871-881. doi: 10.1515/hsz-2016-0138</mixed-citation><mixed-citation xml:lang="en">O’Donoghue AJ, Ivry SL, Chaudhury C, Hostetter DR, Hanahan D, Craik CS. Procathepsin E is highly abundant but minimally active in pancreatic ductal adenocarcinoma tumors. Biol Chem. 2016; 397(9): 871-881. doi: 10.1515/hsz-2016-0138</mixed-citation></citation-alternatives></ref><ref id="cit65"><label>65</label><citation-alternatives><mixed-citation xml:lang="ru">Pontious C, Kaul S, Hong M, Hart PA, Krishna SG, Lara LF, et al. Cathepsin E expression and activity: Role in the detection and treatment of pancreatic cancer. Pancreatology. 2019; 19(7): 951-956. doi: 10.1016/j.pan.2019.09.009</mixed-citation><mixed-citation xml:lang="en">Pontious C, Kaul S, Hong M, Hart PA, Krishna SG, Lara LF, et al. Cathepsin E expression and activity: Role in the detection and treatment of pancreatic cancer. Pancreatology. 2019; 19(7): 951-956. doi: 10.1016/j.pan.2019.09.009</mixed-citation></citation-alternatives></ref><ref id="cit66"><label>66</label><citation-alternatives><mixed-citation xml:lang="ru">Benes P, Vetvicka V, Fusek M. Cathepsin D – many functions of one aspartic protease. Crit Rev Oncol Hematol. 2008; 68(1): 12-28. doi: 10.1016/j.critrevonc.2008.02.008</mixed-citation><mixed-citation xml:lang="en">Benes P, Vetvicka V, Fusek M. Cathepsin D – many functions of one aspartic protease. Crit Rev Oncol Hematol. 2008; 68(1): 12-28. doi: 10.1016/j.critrevonc.2008.02.008</mixed-citation></citation-alternatives></ref><ref id="cit67"><label>67</label><citation-alternatives><mixed-citation xml:lang="ru">Garcia M, Platet N, Liaudet E, Laurent V, Derocq D, Brouillet JP, et al. Biological and clinical significance of cathepsin D in breast cancer metastasis. Stem Cells. 1996; 14(6): 642-650. doi: 10.1002/stem.140642</mixed-citation><mixed-citation xml:lang="en">Garcia M, Platet N, Liaudet E, Laurent V, Derocq D, Brouillet JP, et al. Biological and clinical significance of cathepsin D in breast cancer metastasis. Stem Cells. 1996; 14(6): 642-650. doi: 10.1002/stem.140642</mixed-citation></citation-alternatives></ref><ref id="cit68"><label>68</label><citation-alternatives><mixed-citation xml:lang="ru">Pranjol ZI, Whatmore JL. Cathepsin D in the tumor microenvironment of breast and ovarian cancers. Adv Exp Med Biol. 2020; 1259: 1-16. doi: 10.1007/978-3-030-43093-1_1</mixed-citation><mixed-citation xml:lang="en">Pranjol ZI, Whatmore JL. Cathepsin D in the tumor microenvironment of breast and ovarian cancers. Adv Exp Med Biol. 2020; 1259: 1-16. doi: 10.1007/978-3-030-43093-1_1</mixed-citation></citation-alternatives></ref><ref id="cit69"><label>69</label><citation-alternatives><mixed-citation xml:lang="ru">Laurent-Matha V, Maruani-Herrmann S, Prébois C, Beaujouin M, Glondu M, Noël A, et al. Catalytically inactive human cathepsin D triggers fibroblast invasive growth. J Cell Biol. 2005; 168(3): 489-499. doi: 10.1083/jcb.200403078</mixed-citation><mixed-citation xml:lang="en">Laurent-Matha V, Maruani-Herrmann S, Prébois C, Beaujouin M, Glondu M, Noël A, et al. Catalytically inactive human cathepsin D triggers fibroblast invasive growth. J Cell Biol. 2005; 168(3): 489-499. doi: 10.1083/jcb.200403078</mixed-citation></citation-alternatives></ref><ref id="cit70"><label>70</label><citation-alternatives><mixed-citation xml:lang="ru">Vetvicka V, Vetvickova J, Fusek M. Role of procathepsin D activation peptide in prostate cancer growth. Prostate. 2000; 44(1): 1-7. doi: 10.1002/1097-0045(20000615)44:1&lt;1::aidpros1&gt;3.0.co;2-4</mixed-citation><mixed-citation xml:lang="en">Vetvicka V, Vetvickova J, Fusek M. Role of procathepsin D activation peptide in prostate cancer growth. Prostate. 2000; 44(1): 1-7. doi: 10.1002/1097-0045(20000615)44:1&lt;1::aidpros1&gt;3.0.co;2-4</mixed-citation></citation-alternatives></ref><ref id="cit71"><label>71</label><citation-alternatives><mixed-citation xml:lang="ru">Yang L, Cui M, Zhang L, Song L. FOXM1 facilitates gastric cancer cell migration and invasion by inducing cathepsin D. Oncotarget. 2017; 8(40): 68180-68190. doi: 10.18632/oncotarget.19254</mixed-citation><mixed-citation xml:lang="en">Yang L, Cui M, Zhang L, Song L. FOXM1 facilitates gastric cancer cell migration and invasion by inducing cathepsin D. Oncotarget. 2017; 8(40): 68180-68190. doi: 10.18632/oncotarget.19254</mixed-citation></citation-alternatives></ref><ref id="cit72"><label>72</label><citation-alternatives><mixed-citation xml:lang="ru">Kang J, Yu Y, Jeong S, Lee H, Heo HJ, Park JJ, et al. Prognostic role of high cathepsin D expression in breast cancer: A systematic review and meta-analysis. Ther Adv Med Oncol. 2020; 12: 1758835920927838. doi: 10.1177/1758835920927838</mixed-citation><mixed-citation xml:lang="en">Kang J, Yu Y, Jeong S, Lee H, Heo HJ, Park JJ, et al. Prognostic role of high cathepsin D expression in breast cancer: A systematic review and meta-analysis. Ther Adv Med Oncol. 2020; 12: 1758835920927838. doi: 10.1177/1758835920927838</mixed-citation></citation-alternatives></ref><ref id="cit73"><label>73</label><citation-alternatives><mixed-citation xml:lang="ru">Gemoll T, Epping F, Heinrich L, Fritzsche B, Roblick UJ, Szymczak S, et al. Increased cathepsin D protein expression is a biomarker for osteosarcomas, pulmonary metastases and other bone malignancies. Oncotarget. 2015; 6(18): 16517-16526. doi: 10.18632/oncotarget.4140</mixed-citation><mixed-citation xml:lang="en">Gemoll T, Epping F, Heinrich L, Fritzsche B, Roblick UJ, Szymczak S, et al. Increased cathepsin D protein expression is a biomarker for osteosarcomas, pulmonary metastases and other bone malignancies. Oncotarget. 2015; 6(18): 16517-16526. doi: 10.18632/oncotarget.4140</mixed-citation></citation-alternatives></ref><ref id="cit74"><label>74</label><citation-alternatives><mixed-citation xml:lang="ru">Mehrotra S, Wickremesekera SK, Brasch HD, Van Schaijik B, Marsh RW, Tan ST, et al. Expression and localization of cathepsins B, D and G in cancer stem cells in liver metastasis from colon adenocarcinoma. Front Surg. 2018; 5: 40. doi: 10.3389/fsurg.2018.00040</mixed-citation><mixed-citation xml:lang="en">Mehrotra S, Wickremesekera SK, Brasch HD, Van Schaijik B, Marsh RW, Tan ST, et al. Expression and localization of cathepsins B, D and G in cancer stem cells in liver metastasis from colon adenocarcinoma. Front Surg. 2018; 5: 40. doi: 10.3389/fsurg.2018.00040</mixed-citation></citation-alternatives></ref><ref id="cit75"><label>75</label><citation-alternatives><mixed-citation xml:lang="ru">Basu S, Cheriyamundath S, Gavert N, Brabletz T, Haase G, Ben-Ze›ev A. Increased expression of cathepsin D is required for L1-mediated colon cancer progression. Oncotarget. 2019; 10(50): 5217-5228. doi: 10.18632/oncotarget.27155</mixed-citation><mixed-citation xml:lang="en">Basu S, Cheriyamundath S, Gavert N, Brabletz T, Haase G, Ben-Ze›ev A. Increased expression of cathepsin D is required for L1-mediated colon cancer progression. Oncotarget. 2019; 10(50): 5217-5228. doi: 10.18632/oncotarget.27155</mixed-citation></citation-alternatives></ref><ref id="cit76"><label>76</label><citation-alternatives><mixed-citation xml:lang="ru">Pruitt FL, He Y, Franco OE, Jiang M, Cates JM, Hayward SW. Cathepsin D acts as an essential mediator to promote malignancy of benign prostatic epithelium. Prostate. 2013; 73(5): 476-488. doi: 10.1002/pros.22589. Epub 2012 Sep 19</mixed-citation><mixed-citation xml:lang="en">Pruitt FL, He Y, Franco OE, Jiang M, Cates JM, Hayward SW. Cathepsin D acts as an essential mediator to promote malignancy of benign prostatic epithelium. Prostate. 2013; 73(5): 476-488. doi: 10.1002/pros.22589. Epub 2012 Sep 19</mixed-citation></citation-alternatives></ref><ref id="cit77"><label>77</label><citation-alternatives><mixed-citation xml:lang="ru">Osmak M, Niksíc D, Brozović A, Ristov AA, Vrhovec I, Skrk J. Drug resistant tumor cells have increased levels of tumor markers for invasion and metastasis. Anticancer Res. 1999; 19(4B): 3193-3197.</mixed-citation><mixed-citation xml:lang="en">Osmak M, Niksíc D, Brozović A, Ristov AA, Vrhovec I, Skrk J. Drug resistant tumor cells have increased levels of tumor markers for invasion and metastasis. Anticancer Res. 1999; 19(4B): 3193-3197.</mixed-citation></citation-alternatives></ref><ref id="cit78"><label>78</label><citation-alternatives><mixed-citation xml:lang="ru">Roger P, Montcourrier P, Maudelonde T, Brouillet JP, Pages A, Laffargue F, et al. Cathepsin D immunostaining in paraffin-embedded breast cancer cells and macrophages: Correlation with cytosolic assay. Hum Pathol. 1994; 25(9): 863-871. doi: 10.1016/0046-8177(94)90004-3</mixed-citation><mixed-citation xml:lang="en">Roger P, Montcourrier P, Maudelonde T, Brouillet JP, Pages A, Laffargue F, et al. Cathepsin D immunostaining in paraffin-embedded breast cancer cells and macrophages: Correlation with cytosolic assay. Hum Pathol. 1994; 25(9): 863-871. doi: 10.1016/0046-8177(94)90004-3</mixed-citation></citation-alternatives></ref><ref id="cit79"><label>79</label><citation-alternatives><mixed-citation xml:lang="ru">Kirana C, Shi H, Laing E, Hood K, Miller R, Bethwaite P, et al. Cathepsin D expression in colorectal cancer: From proteomic discovery through validation using Western blotting, immunohistochemistry, and tissue microarrays. Int J Proteomics. 2012; 2012: 245819. doi: 10.1155/2012/245819</mixed-citation><mixed-citation xml:lang="en">Kirana C, Shi H, Laing E, Hood K, Miller R, Bethwaite P, et al. Cathepsin D expression in colorectal cancer: From proteomic discovery through validation using Western blotting, immunohistochemistry, and tissue microarrays. Int J Proteomics. 2012; 2012: 245819. doi: 10.1155/2012/245819</mixed-citation></citation-alternatives></ref><ref id="cit80"><label>80</label><citation-alternatives><mixed-citation xml:lang="ru">Montcourrier P, Mangeat PH, Valembois C, Salazar G, Sahuquet A, Duperray C, et al. Characterization of very acidic phagosomes in breast cancer cells and their association with invasion. J Cell Sci. 1994; 107(Pt 9): 2381-2391.</mixed-citation><mixed-citation xml:lang="en">Montcourrier P, Mangeat PH, Valembois C, Salazar G, Sahuquet A, Duperray C, et al. Characterization of very acidic phagosomes in breast cancer cells and their association with invasion. J Cell Sci. 1994; 107(Pt 9): 2381-2391.</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>
