{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,18]],"date-time":"2026-04-18T10:59:31Z","timestamp":1776509971409,"version":"3.51.2"},"reference-count":100,"publisher":"Portland Press Ltd.","issue":"2","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2021,4,30]]},"abstract":"<jats:p>Aberrant cell surface glycosylation signatures are currently known to actively drive the neoplastic transformation of healthy cells. By disrupting the homeostatic functions of their protein carriers, cancer-associated glycans mechanistically underpin several molecular hallmarks of human malignancy. Furthermore, such aberrant glycan structures play key roles in the acquisition of molecular resistance to targeted therapeutic agents, which compromises their clinical efficacy, by modulating tumour cell aggressiveness and supporting the establishment of an immunosuppressive microenvironment. Recent advances in the study of the tumour cell glycoproteome have unravelled previously elusive molecular mechanisms of therapeutic resistance, guided the rational design of novel personalized therapeutic strategies, and may further improve the clinical performance of currently approved anti-cancer targeted agents. In this review, we highlight the impact of glycosylation in cancer targeted therapy, with particular focus on receptor tyrosine kinase-targeted therapy, immune checkpoints blockade therapy, and current developments on therapeutic strategies directed to glycan-binding proteins and other innovative glycan therapeutic strategies.<\/jats:p>","DOI":"10.1042\/bst20200763","type":"journal-article","created":{"date-parts":[[2021,3,11]],"date-time":"2021-03-11T13:05:10Z","timestamp":1615467910000},"page":"843-854","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":26,"title":["Aberrant protein glycosylation in cancer: implications in targeted therapy"],"prefix":"10.1042","volume":"49","author":[{"given":"Joana G.","family":"Rodrigues","sequence":"first","affiliation":[{"name":"i3S \u2013 Instituto de Investiga\u00e7\u00e3o e Inova\u00e7\u00e3o em Sa\u00fade, Universidade do Porto, 4200-135 Porto, Portugal"},{"name":"IPATIMUP \u2013 Institute of Molecular Pathology and Immunology of the University of Porto, 4200-135 Porto, Portugal"},{"name":"ICBAS - Institute of Biomedical Sciences Abel Salazar, University of Porto, 4050-313 Porto, Portugal"}]},{"given":"Henrique O.","family":"Duarte","sequence":"additional","affiliation":[{"name":"i3S \u2013 Instituto de Investiga\u00e7\u00e3o e Inova\u00e7\u00e3o em Sa\u00fade, Universidade do Porto, 4200-135 Porto, Portugal"},{"name":"IPATIMUP \u2013 Institute of Molecular Pathology and Immunology of the University of Porto, 4200-135 Porto, Portugal"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0286-6639","authenticated-orcid":false,"given":"Celso A.","family":"Reis","sequence":"additional","affiliation":[{"name":"i3S \u2013 Instituto de Investiga\u00e7\u00e3o e Inova\u00e7\u00e3o em Sa\u00fade, Universidade do Porto, 4200-135 Porto, Portugal"},{"name":"IPATIMUP \u2013 Institute of Molecular Pathology and Immunology of the University of Porto, 4200-135 Porto, Portugal"},{"name":"ICBAS - Institute of Biomedical Sciences Abel Salazar, University of Porto, 4050-313 Porto, Portugal"},{"name":"Faculty of Medicine, University of Porto, 4200-319 Porto, Portugal"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8832-2703","authenticated-orcid":false,"given":"Joana","family":"Gomes","sequence":"additional","affiliation":[{"name":"i3S \u2013 Instituto de Investiga\u00e7\u00e3o e Inova\u00e7\u00e3o em Sa\u00fade, Universidade do Porto, 4200-135 Porto, Portugal"},{"name":"IPATIMUP \u2013 Institute of Molecular Pathology and Immunology of the University of Porto, 4200-135 Porto, Portugal"}]}],"member":"288","published-online":{"date-parts":[[2021,3,11]]},"reference":[{"key":"2021111916093236700_BST-2020-0763CC1","volume-title":"Essentials of Glycobiology"},{"key":"2021111916093236700_BST-2020-0763CC2","doi-asserted-by":"publisher","first-page":"540","DOI":"10.1038\/nrc3982","article-title":"Glycosylation in cancer: mechanisms and clinical implications","volume":"15","year":"2015","journal-title":"Nat. Rev. Cancer"},{"key":"2021111916093236700_BST-2020-0763CC3","doi-asserted-by":"publisher","first-page":"11","DOI":"10.1016\/bs.acr.2014.11.001","article-title":"Glycans and cancer: role of N-glycans in cancer biomarker, progression and metastasis, and therapeutics","volume":"126","year":"2015","journal-title":"Adv. Cancer Res."},{"key":"2021111916093236700_BST-2020-0763CC4","doi-asserted-by":"publisher","first-page":"E4066","DOI":"10.1073\/pnas.1406619111","article-title":"Immature truncated O-glycophenotype of cancer directly induces oncogenic features","volume":"111","year":"2014","journal-title":"Proc. Natl Acad. Sci. U.S.A."},{"key":"2021111916093236700_BST-2020-0763CC5","doi-asserted-by":"publisher","first-page":"53","DOI":"10.1016\/bs.acr.2014.11.002","article-title":"Simple sugars to complex disease\u2013mucin-type O-glycans in cancer","volume":"126","year":"2015","journal-title":"Adv. Cancer Res."},{"key":"2021111916093236700_BST-2020-0763CC6","doi-asserted-by":"publisher","first-page":"335","DOI":"10.1007\/s10719-008-9181-1","article-title":"Complex N-glycans or core 1-derived O-glycans are not required for the expression of stage-specific antigens SSEA-1, SSEA-3, SSEA-4, or Le(Y) in the preimplantation mouse embryo","volume":"26","year":"2009","journal-title":"Glycoconj J."},{"key":"2021111916093236700_BST-2020-0763CC7","doi-asserted-by":"publisher","first-page":"46","DOI":"10.1016\/j.cellimm.2018.03.007","article-title":"Glycosylation in cancer: selected roles in tumour progression, immune modulation and metastasis","volume":"333","year":"2018","journal-title":"Cell Immunol."},{"key":"2021111916093236700_BST-2020-0763CC8","doi-asserted-by":"publisher","first-page":"322","DOI":"10.1136\/jcp.2009.071035","article-title":"Alterations in glycosylation as biomarkers for cancer detection","volume":"63","year":"2010","journal-title":"J. Clin. Pathol."},{"key":"2021111916093236700_BST-2020-0763CC9","doi-asserted-by":"publisher","first-page":"iv238","DOI":"10.1093\/annonc\/mdy308","article-title":"Hepatocellular carcinoma: ESMO clinical practice guidelines for diagnosis, treatment and follow-up","volume":"29","year":"2018","journal-title":"Ann. Oncol."},{"key":"2021111916093236700_BST-2020-0763CC10","doi-asserted-by":"publisher","first-page":"2732","DOI":"10.1038\/s41598-018-21048-y","article-title":"Evaluation of serum CEA, CA19-9, CA72-4, CA125 and ferritin as diagnostic markers and factors of clinical parameters for colorectal cancer","volume":"8","year":"2018","journal-title":"Sci Rep."},{"key":"2021111916093236700_BST-2020-0763CC11","first-page":"2903","article-title":"Prognostic value of preoperative serum levels of CEA, CA 19-9 and CA 72-4 in gastric carcinoma","volume":"17","year":"1997","journal-title":"Anticancer Res."},{"key":"2021111916093236700_BST-2020-0763CC12","doi-asserted-by":"publisher","first-page":"6","DOI":"10.1016\/j.ccell.2019.06.006","article-title":"Glycosylation in the era of cancer-targeted therapy: where are we heading?","volume":"36","year":"2019","journal-title":"Cancer Cell"},{"key":"2021111916093236700_BST-2020-0763CC13","doi-asserted-by":"publisher","first-page":"204","DOI":"10.1038\/nri.2018.3","article-title":"The tumour glyco-code as a novel immune checkpoint for immunotherapy","volume":"18","year":"2018","journal-title":"Nat. Rev. Immunol."},{"key":"2021111916093236700_BST-2020-0763CC14","doi-asserted-by":"publisher","first-page":"1117","DOI":"10.1016\/j.cell.2010.06.011","article-title":"Cell signaling by receptor tyrosine kinases","volume":"141","year":"2010","journal-title":"Cell"},{"key":"2021111916093236700_BST-2020-0763CC15","doi-asserted-by":"publisher","first-page":"729","DOI":"10.1038\/s41580-020-00294-x","article-title":"Global view of human protein glycosylation pathways and functions","volume":"21","year":"2020","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"2021111916093236700_BST-2020-0763CC16","doi-asserted-by":"publisher","first-page":"3803","DOI":"10.1158\/0008-5472.CAN-07-6389","article-title":"Inhibition of N-linked glycosylation disrupts receptor tyrosine kinase signaling in tumor cells","volume":"68","year":"2008","journal-title":"Cancer Res."},{"key":"2021111916093236700_BST-2020-0763CC17","doi-asserted-by":"publisher","first-page":"4334","DOI":"10.1073\/pnas.1503262112","article-title":"N-Glycosylation as determinant of epidermal growth factor receptor conformation in membranes","volume":"112","year":"2015","journal-title":"Proc. Natl Acad. Sci. U.S.A."},{"key":"2021111916093236700_BST-2020-0763CC18","doi-asserted-by":"publisher","first-page":"11332","DOI":"10.1073\/pnas.1107385108","article-title":"Sialylation and fucosylation of epidermal growth factor receptor suppress its dimerization and activation in lung cancer cells","volume":"108","year":"2011","journal-title":"Proc. Natl Acad. Sci. U.S.A."},{"key":"2021111916093236700_BST-2020-0763CC19","doi-asserted-by":"publisher","first-page":"e66737","DOI":"10.1371\/journal.pone.0066737","article-title":"Expression of ST3GAL4 leads to SLex expression and induces c-Met activation and an invasive phenotype in gastric carcinoma cells","volume":"8","year":"2013","journal-title":"PLoS ONE"},{"key":"2021111916093236700_BST-2020-0763CC20","doi-asserted-by":"publisher","first-page":"1795","DOI":"10.1016\/j.bbagen.2015.12.016","article-title":"Glycomic analysis of gastric carcinoma cells discloses glycans as modulators of RON receptor tyrosine kinase activation in cancer","volume":"1860","year":"2016","journal-title":"Biochim. Biophys. Acta"},{"key":"2021111916093236700_BST-2020-0763CC21","doi-asserted-by":"publisher","first-page":"5580","DOI":"10.1158\/0008-5472.CAN-13-0869","article-title":"C1GALT1 enhances proliferation of hepatocellular carcinoma cells via modulating MET glycosylation and dimerization","volume":"73","year":"2013","journal-title":"Cancer Res."},{"key":"2021111916093236700_BST-2020-0763CC22","doi-asserted-by":"publisher","first-page":"1376","DOI":"10.1038\/bjc.2016.116","article-title":"Loss of N-acetylgalactosaminyltransferase 3 in poorly differentiated pancreatic cancer: augmented aggressiveness and aberrant ErbB family glycosylation","volume":"114","year":"2016","journal-title":"Br. J. Cancer"},{"key":"2021111916093236700_BST-2020-0763CC23","doi-asserted-by":"publisher","first-page":"349","DOI":"10.1016\/j.ebiom.2019.01.017","article-title":"O-glycans truncation modulates gastric cancer cell signaling and transcription leading to a more aggressive phenotype","volume":"40","year":"2019","journal-title":"EBioMedicine"},{"key":"2021111916093236700_BST-2020-0763CC24","doi-asserted-by":"publisher","first-page":"1087","DOI":"10.1158\/0008-5472.CAN-03-2435","article-title":"Antibodies directed against Lewis-Y antigen inhibit signaling of Lewis-Y modified ErbB receptors","volume":"64","year":"2004","journal-title":"Cancer Res."},{"key":"2021111916093236700_BST-2020-0763CC25","doi-asserted-by":"publisher","first-page":"2262","DOI":"10.3390\/ijms18112262","article-title":"Gastric cancer cell glycosylation as a modulator of the ErbB2 oncogenic receptor","volume":"18","year":"2017","journal-title":"Int. J. Mol. Sci."},{"key":"2021111916093236700_BST-2020-0763CC26","doi-asserted-by":"publisher","first-page":"38912","DOI":"10.18632\/oncotarget.5334","article-title":"Tunicamycin enhances the antitumor activity of trastuzumab on breast cancer in vitro and in vivo","volume":"6","year":"2015","journal-title":"Oncotarget"},{"key":"2021111916093236700_BST-2020-0763CC27","doi-asserted-by":"publisher","first-page":"43006","DOI":"10.1038\/srep43006","article-title":"Cellular glycosylation affects herceptin binding and sensitivity of breast cancer cells to doxorubicin and growth factors","volume":"7","year":"2017","journal-title":"Sci. Rep."},{"key":"2021111916093236700_BST-2020-0763CC28","doi-asserted-by":"publisher","first-page":"7342","DOI":"10.1038\/s41388-019-0946-8","article-title":"Therapeutic anti-cancer activity of antibodies targeting sulfhydryl bond constrained epitopes on unglycosylated RON receptor tyrosine kinase","volume":"38","year":"2019","journal-title":"Oncogene"},{"key":"2021111916093236700_BST-2020-0763CC29","doi-asserted-by":"publisher","first-page":"10304","DOI":"10.1073\/pnas.1608069113","article-title":"Precision glycocalyx editing as a strategy for cancer immunotherapy","volume":"113","year":"2016","journal-title":"Proc. Natl Acad. Sci. U.S.A."},{"key":"2021111916093236700_BST-2020-0763CC30","doi-asserted-by":"publisher","first-page":"744","DOI":"10.1016\/j.cell.2014.01.043","article-title":"Glycosylation-dependent lectin-receptor interactions preserve angiogenesis in anti-VEGF refractory tumors","volume":"156","year":"2014","journal-title":"Cell"},{"key":"2021111916093236700_BST-2020-0763CC31","doi-asserted-by":"publisher","first-page":"1023","DOI":"10.1038\/nchembio.2194","article-title":"Oligosaccharyltransferase inhibition induces senescence in RTK-driven tumor cells","volume":"12","year":"2016","journal-title":"Nat. Chem. Biol."},{"key":"2021111916093236700_BST-2020-0763CC32","doi-asserted-by":"publisher","first-page":"5094","DOI":"10.1158\/0008-5472.CAN-18-0505","article-title":"Oligosaccharyltransferase inhibition overcomes therapeutic resistance to EGFR tyrosine kinase inhibitors","volume":"78","year":"2018","journal-title":"Cancer Res."},{"key":"2021111916093236700_BST-2020-0763CC33","doi-asserted-by":"publisher","first-page":"6955","DOI":"10.1073\/pnas.1507329112","article-title":"Effect of sialylation on EGFR phosphorylation and resistance to tyrosine kinase inhibition","volume":"112","year":"2015","journal-title":"Proc. Natl Acad. Sci. U.S.A."},{"key":"2021111916093236700_BST-2020-0763CC34","doi-asserted-by":"publisher","first-page":"12","DOI":"10.1186\/s13048-018-0385-0","article-title":"Sialylation of EGFR by the ST6Gal-I sialyltransferase promotes EGFR activation and resistance to gefitinib-mediated cell death","volume":"11","year":"2018","journal-title":"J. Ovarian Res."},{"key":"2021111916093236700_BST-2020-0763CC35","doi-asserted-by":"publisher","first-page":"2997","DOI":"10.3892\/or.2018.6680","article-title":"Increasing HER2 \u03b12,6 sialylation facilitates gastric cancer progression and resistance via the Akt and ERK pathways","volume":"40","year":"2018","journal-title":"Oncol. Rep."},{"key":"2021111916093236700_BST-2020-0763CC36","doi-asserted-by":"publisher","first-page":"1027","DOI":"10.1084\/jem.192.7.1027","article-title":"Engagement of the PD-1 immunoinhibitory receptor by a novel B7 family member leads to negative regulation of lymphocyte activation","volume":"192","year":"2000","journal-title":"J. Exp. Med."},{"key":"2021111916093236700_BST-2020-0763CC37","doi-asserted-by":"publisher","first-page":"550","DOI":"10.3389\/fimmu.2016.00550","article-title":"The PD1:PD-L1\/2 pathway from discovery to clinical implementation","volume":"7","year":"2016","journal-title":"Front. Immunol."},{"key":"2021111916093236700_BST-2020-0763CC38","doi-asserted-by":"publisher","first-page":"12293","DOI":"10.1073\/pnas.192461099","article-title":"Involvement of PD-L1 on tumor cells in the escape from host immune system and tumor immunotherapy by PD-L1 blockade","volume":"99","year":"2002","journal-title":"Proc. Natl Acad. Sci. U.S.A."},{"key":"2021111916093236700_BST-2020-0763CC39","doi-asserted-by":"crossref","first-page":"1089","DOI":"10.1158\/0008-5472.1089.65.3","article-title":"Blockade of B7-H1 and PD-1 by monoclonal antibodies potentiates cancer therapeutic immunity","volume":"65","year":"2005","journal-title":"Cancer Res."},{"key":"2021111916093236700_BST-2020-0763CC40","first-page":"727","article-title":"PD-1\/PD-L1 pathway: current researches in cancer","volume":"10","year":"2020","journal-title":"Am. J. Cancer Res."},{"key":"2021111916093236700_BST-2020-0763CC41","doi-asserted-by":"publisher","first-page":"24","DOI":"10.1016\/j.molmed.2014.10.009","article-title":"Human cancer immunotherapy with antibodies to the PD-1 and PD-L1 pathway","volume":"21","year":"2015","journal-title":"Trends Mol. Med."},{"key":"2021111916093236700_BST-2020-0763CC42","doi-asserted-by":"publisher","first-page":"1758835920937612","DOI":"10.1177\/1758835920937612","article-title":"Efficacy of PD-1\/PD-L1 blockade monotherapy in clinical trials","volume":"12","year":"2020","journal-title":"Ther. Adv. Med. Oncol."},{"key":"2021111916093236700_BST-2020-0763CC43","doi-asserted-by":"publisher","first-page":"854","DOI":"10.1038\/nrd.2018.210","article-title":"The clinical trial landscape for PD1\/PDL1 immune checkpoint inhibitors","volume":"17","year":"2018","journal-title":"Nat. Rev. Drug Discov."},{"key":"2021111916093236700_BST-2020-0763CC44","doi-asserted-by":"publisher","first-page":"707","DOI":"10.1016\/j.cell.2017.01.017","article-title":"Primary, adaptive, and acquired resistance to cancer immunotherapy","volume":"168","year":"2017","journal-title":"Cell"},{"key":"2021111916093236700_BST-2020-0763CC45","doi-asserted-by":"publisher","first-page":"6349","DOI":"10.1158\/0008-5472.CAN-18-1892","article-title":"Posttranslational modifications of PD-L1 and their applications in cancer therapy","volume":"78","year":"2018","journal-title":"Cancer Res."},{"key":"2021111916093236700_BST-2020-0763CC46","doi-asserted-by":"publisher","first-page":"77","DOI":"10.1186\/s12929-020-00670-x","article-title":"The impact of PD-L1 N-linked glycosylation on cancer therapy and clinical diagnosis","volume":"27","year":"2020","journal-title":"J. Biomed. Sci."},{"key":"2021111916093236700_BST-2020-0763CC47","doi-asserted-by":"publisher","first-page":"12632","DOI":"10.1038\/ncomms12632","article-title":"Glycosylation and stabilization of programmed death ligand-1 suppresses T-cell activity","volume":"7","year":"2016","journal-title":"Nat. Commun."},{"key":"2021111916093236700_BST-2020-0763CC48","doi-asserted-by":"publisher","first-page":"187","DOI":"10.1016\/j.ccell.2018.01.009","article-title":"Eradication of triple-Negative breast cancer cells by targeting glycosylated PD-L1","volume":"33","year":"2018","journal-title":"Cancer Cell"},{"key":"2021111916093236700_BST-2020-0763CC49","doi-asserted-by":"publisher","first-page":"328rv4","DOI":"10.1126\/scitranslmed.aad7118","article-title":"PD-L1 (B7-H1) and PD-1 pathway blockade for cancer therapy: mechanisms, response biomarkers, and combinations","volume":"8","year":"2016","journal-title":"Sci. Transl. Med."},{"key":"2021111916093236700_BST-2020-0763CC50","doi-asserted-by":"publisher","first-page":"581","DOI":"10.1007\/s10549-018-4874-z","article-title":"Protein N-glycosylation alteration and glycolysis inhibition both contribute to the antiproliferative action of 2-deoxyglucose in breast cancer cells","volume":"171","year":"2018","journal-title":"Breast Cancer Res. Treat."},{"key":"2021111916093236700_BST-2020-0763CC51","first-page":"1837","article-title":"Deglycosylation of PD-L1 by 2-deoxyglucose reverses PARP inhibitor-induced immunosuppression in triple-negative breast cancer","volume":"8","year":"2018","journal-title":"Am. J. Cancer Res."},{"key":"2021111916093236700_BST-2020-0763CC52","doi-asserted-by":"publisher","first-page":"691","DOI":"10.1002\/mc.23170","article-title":"Saccharide analog, 2-deoxy-d-glucose enhances 4-1BB-mediated antitumor immunity via PD-L1 deglycosylation","volume":"59","year":"2020","journal-title":"Mol. Carcinog."},{"key":"2021111916093236700_BST-2020-0763CC53","doi-asserted-by":"publisher","first-page":"5990","DOI":"10.1158\/1078-0432.CCR-20-0778","article-title":"Inhibition of MAN2A1 enhances the immune response to anti-PD-L1 in human tumors","volume":"26","year":"2020","journal-title":"Clin. Cancer Res."},{"key":"2021111916093236700_BST-2020-0763CC54","doi-asserted-by":"publisher","first-page":"8","DOI":"10.18632\/aging.102646","article-title":"Resveratrol targets PD-L1 glycosylation and dimerization to enhance antitumor T-cell immunity","volume":"12","year":"2020","journal-title":"Aging (Albany NY)"},{"key":"2021111916093236700_BST-2020-0763CC55","doi-asserted-by":"publisher","first-page":"243","DOI":"10.1158\/1541-7786.MCR-17-0166","article-title":"Small-molecule sigma1 modulator induces autophagic degradation of PD-L1","volume":"16","year":"2018","journal-title":"Mol. Cancer Res."},{"key":"2021111916093236700_BST-2020-0763CC56","doi-asserted-by":"publisher","first-page":"1908","DOI":"10.1038\/s41467-018-04313-6","article-title":"STT3-dependent PD-L1 accumulation on cancer stem cells promotes immune evasion","volume":"9","year":"2018","journal-title":"Nat Commun."},{"key":"2021111916093236700_BST-2020-0763CC57","doi-asserted-by":"publisher","first-page":"1614","DOI":"10.3389\/fimmu.2018.01614","article-title":"Glyco-Engineered anti-human programmed death-ligand 1 antibody mediates stronger CD8T cell activation than its normal glycosylated and non-glycosylated counterparts","volume":"9","year":"2018","journal-title":"Front. Immunol."},{"key":"2021111916093236700_BST-2020-0763CC58","doi-asserted-by":"publisher","first-page":"168","DOI":"10.1016\/j.ccell.2019.06.008","article-title":"Removal of N-linked glycosylation enhances PD-L1 detection and predicts anti-PD-1\/PD-L1 therapeutic efficacy","volume":"36","year":"2019","journal-title":"Cancer Cell"},{"key":"2021111916093236700_BST-2020-0763CC59","doi-asserted-by":"publisher","first-page":"274","DOI":"10.1016\/j.it.2020.02.001","article-title":"Sialoglycans and siglecs can shape the tumor immune microenvironment","volume":"41","year":"2020","journal-title":"Trends Immunol."},{"key":"2021111916093236700_BST-2020-0763CC60","doi-asserted-by":"publisher","first-page":"593","DOI":"10.1007\/s00018-019-03288-x","article-title":"Sialic acid-binding immunoglobulin-like lectins (Siglecs) detect self-associated molecular patterns to regulate immune responses","volume":"77","year":"2020","journal-title":"Cell. Mol. Life Sci."},{"key":"2021111916093236700_BST-2020-0763CC61","doi-asserted-by":"publisher","first-page":"1810","DOI":"10.1172\/JCI65899","article-title":"Interactions between siglec-7\/9 receptors and ligands influence NK cell-dependent tumor immunosurveillance","volume":"124","year":"2014","journal-title":"J. Clin. Invest."},{"key":"2021111916093236700_BST-2020-0763CC62","doi-asserted-by":"publisher","first-page":"69","DOI":"10.1038\/nchembio.1388","article-title":"Glycocalyx engineering reveals a Siglec-based mechanism for NK cell immunoevasion","volume":"10","year":"2014","journal-title":"Nat. Chem. Biol."},{"key":"2021111916093236700_BST-2020-0763CC63","doi-asserted-by":"publisher","first-page":"1273","DOI":"10.1038\/ni.3552","article-title":"The mucin MUC1 modulates the tumor immunological microenvironment through engagement of the lectin Siglec-9","volume":"17","year":"2016","journal-title":"Nat. Immunol."},{"key":"2021111916093236700_BST-2020-0763CC64","doi-asserted-by":"publisher","first-page":"532","DOI":"10.1016\/j.bbrc.2014.06.009","article-title":"A soluble form of Siglec-9 provides an antitumor benefit against mammary tumor cells expressing MUC1 in transgenic mice","volume":"450","year":"2014","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"2021111916093236700_BST-2020-0763CC65","doi-asserted-by":"publisher","first-page":"707","DOI":"10.1158\/2326-6066.CIR-18-0505","article-title":"Siglec-9 regulates an effector memory CD8(+) T-cell subset that congregates in the melanoma tumor microenvironment","volume":"7","year":"2019","journal-title":"Cancer Immunol. Res."},{"key":"2021111916093236700_BST-2020-0763CC66","doi-asserted-by":"publisher","first-page":"392","DOI":"10.1038\/s41586-019-1456-0","article-title":"CD24 signalling through macrophage Siglec-10 is a target for cancer immunotherapy","volume":"572","year":"2019","journal-title":"Nature"},{"key":"2021111916093236700_BST-2020-0763CC67","doi-asserted-by":"publisher","first-page":"656","DOI":"10.1038\/s41591-019-0374-x","article-title":"Siglec-15 as an immune suppressor and potential target for normalization cancer immunotherapy","volume":"25","year":"2019","journal-title":"Nat. Med."},{"key":"2021111916093236700_BST-2020-0763CC68","doi-asserted-by":"publisher","first-page":"3574","DOI":"10.1158\/0008-5472.CAN-17-3376","article-title":"Sialic acid blockade suppresses tumor growth by enhancing T-cell-mediated tumor immunity","volume":"78","year":"2018","journal-title":"Cancer Res."},{"key":"2021111916093236700_BST-2020-0763CC69","doi-asserted-by":"publisher","first-page":"1376","DOI":"10.1038\/s41589-020-0622-x","article-title":"Targeted glycan degradation potentiates the anticancer immune response in vivo","volume":"16","year":"2020","journal-title":"Nat. Chem. Biol."},{"key":"2021111916093236700_BST-2020-0763CC70","doi-asserted-by":"publisher","first-page":"119929","DOI":"10.1016\/j.ijpharm.2020.119929","article-title":"Targeted delivery of zoledronic acid through the sialic acid: Siglec axis for killing and reversal of M2 phenotypic tumor-associated macrophages: a promising cancer immunotherapy","volume":"590","year":"2020","journal-title":"Int. J. Pharm."},{"key":"2021111916093236700_BST-2020-0763CC71","doi-asserted-by":"publisher","first-page":"1500","DOI":"10.3892\/etm.2019.7630","article-title":"Anti-CD22 epratuzumab for systemic lupus erythematosus: a systematic review and meta-analysis of randomized controlled trials","volume":"18","year":"2019","journal-title":"Exp. Ther. Med."},{"key":"2021111916093236700_BST-2020-0763CC72","doi-asserted-by":"publisher","first-page":"1624","DOI":"10.1056\/NEJMoa2012047","article-title":"Anti-Siglec-8 antibody for eosinophilic gastritis and duodenitis","volume":"383","year":"2020","journal-title":"N. Engl. J. Med."},{"key":"2021111916093236700_BST-2020-0763CC73","doi-asserted-by":"publisher","first-page":"2713","DOI":"10.1158\/1538-7445.AM2018-2713","article-title":"Abstract 2713: preclinical development of first-in-class antibodies targeting siglec-9 immune checkpoint for cancer immunotherapy","volume":"78","year":"2018","journal-title":"Cancer Res."},{"key":"2021111916093236700_BST-2020-0763CC74","doi-asserted-by":"publisher","first-page":"5302","DOI":"10.1158\/0008-5472.CAN-16-0784","article-title":"Monocyte induction of E-selectin-mediated endothelial activation releases VE-cadherin junctions to promote tumor cell extravasation in the metastasis cascade","volume":"76","year":"2016","journal-title":"Cancer Res."},{"key":"2021111916093236700_BST-2020-0763CC75","doi-asserted-by":"publisher","first-page":"627","DOI":"10.1038\/s41556-019-0309-2","article-title":"Bone vascular niche E-selectin induces mesenchymal-epithelial transition and Wnt activation in cancer cells to promote bone metastasis","volume":"21","year":"2019","journal-title":"Nat. Cell Biol."},{"key":"2021111916093236700_BST-2020-0763CC76","doi-asserted-by":"publisher","first-page":"2042","DOI":"10.1038\/s41467-020-15817-5","article-title":"Endothelial E-selectin inhibition improves acute myeloid leukaemia therapy by disrupting vascular niche-mediated chemoresistance","volume":"11","year":"2020","journal-title":"Nat. Commun."},{"key":"2021111916093236700_BST-2020-0763CC77","doi-asserted-by":"publisher","first-page":"109","DOI":"10.3389\/fonc.2016.00109","article-title":"Turning-off signaling by siglecs, selectins, and galectins: chemical inhibition of glycan-Dependent interactions in cancer","volume":"6","year":"2016","journal-title":"Front. Oncol."},{"key":"2021111916093236700_BST-2020-0763CC78","doi-asserted-by":"publisher","first-page":"757","DOI":"10.1016\/j.trecan.2020.04.002","article-title":"Targeting glycosylation: a new road for cancer drug discovery","volume":"6","year":"2020","journal-title":"Trends Cancer"},{"key":"2021111916093236700_BST-2020-0763CC79","doi-asserted-by":"publisher","first-page":"eaaz1580","DOI":"10.1126\/sciadv.aaz1580","article-title":"Platelet P-selectin initiates cross-presentation and dendritic cell differentiation in blood monocytes","volume":"6","year":"2020","journal-title":"Sci. Adv."},{"key":"2021111916093236700_BST-2020-0763CC80","doi-asserted-by":"publisher","first-page":"5553","DOI":"10.1172\/JCI129025","article-title":"Galectin-1-driven T cell exclusion in the tumor endothelium promotes immunotherapy resistance","volume":"129","year":"2019","journal-title":"J. Clin. Invest."},{"key":"2021111916093236700_BST-2020-0763CC81","doi-asserted-by":"publisher","first-page":"1937","DOI":"10.1038\/cdd.2017.119","article-title":"Interaction of galectin-3 with MUC1 on cell surface promotes EGFR dimerization and activation in human epithelial cancer cells","volume":"24","year":"2017","journal-title":"Cell Death Differ."},{"key":"2021111916093236700_BST-2020-0763CC82","doi-asserted-by":"publisher","first-page":"1594","DOI":"10.3389\/fimmu.2019.01594","article-title":"The Tim-3-Galectin-9 pathway and Its regulatory mechanisms in human breast cancer","volume":"10","year":"2019","journal-title":"Front. Immunol."},{"key":"2021111916093236700_BST-2020-0763CC83","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1007\/s10456-020-09749-3","article-title":"Characterization of a neutralizing anti-human galectin-1 monoclonal antibody with angioregulatory and immunomodulatory activities","volume":"24","year":"2021","journal-title":"Angiogenesis"},{"key":"2021111916093236700_BST-2020-0763CC84","doi-asserted-by":"publisher","first-page":"1248","DOI":"10.1016\/j.immuni.2016.06.010","article-title":"Driving CARs into sweet roads: targeting glycosylated antigens in cancer","volume":"44","year":"2016","journal-title":"Immunity"},{"key":"2021111916093236700_BST-2020-0763CC85","doi-asserted-by":"publisher","first-page":"656","DOI":"10.1093\/glycob\/cwy008","article-title":"Glycan-directed CAR-T cells","volume":"28","year":"2018","journal-title":"Glycobiology."},{"key":"2021111916093236700_BST-2020-0763CC86","doi-asserted-by":"publisher","first-page":"659","DOI":"10.3390\/vaccines8040659","article-title":"Potential of anti-MUC1 antibodies as a targeted therapy for gastrointestinal cancers","volume":"8","year":"2020","journal-title":"Vaccines"},{"key":"2021111916093236700_BST-2020-0763CC87","doi-asserted-by":"publisher","first-page":"947","DOI":"10.1016\/j.immuni.2016.10.015","article-title":"Distinguishing truncated and normal MUC1 glycoform targeting from Tn-MUC1-specific CAR T cells: specificity Is the Key to safety","volume":"45","year":"2016","journal-title":"Immunity"},{"key":"2021111916093236700_BST-2020-0763CC88","doi-asserted-by":"publisher","first-page":"1444","DOI":"10.1016\/j.immuni.2016.05.014","article-title":"Engineered CAR T cells targeting the cancer-associated Tn-glycoform of the membrane mucin MUC1 control adenocarcinoma","volume":"44","year":"2016","journal-title":"Immunity"},{"key":"2021111916093236700_BST-2020-0763CC89","doi-asserted-by":"publisher","first-page":"96","DOI":"10.1093\/glycob\/cwj044","article-title":"Chemoenzymatically synthesized multimeric Tn\/STn MUC1 glycopeptides elicit cancer-specific anti-MUC1 antibody responses and override tolerance","volume":"16","year":"2006","journal-title":"Glycobiology"},{"key":"2021111916093236700_BST-2020-0763CC90","doi-asserted-by":"publisher","first-page":"15148","DOI":"10.1073\/pnas.1920662117","article-title":"Structure-guided engineering of the affinity and specificity of CARs against Tn-glycopeptides","volume":"117","year":"2020","journal-title":"Proc. Natl Acad. Sci. U.S.A."},{"key":"2021111916093236700_BST-2020-0763CC91","doi-asserted-by":"publisher","first-page":"2268","DOI":"10.3389\/fimmu.2018.02268","article-title":"Effective targeting of TAG72(+) peritoneal ovarian tumors via regional delivery of CAR-engineered T cells","volume":"9","year":"2018","journal-title":"Front. Immunol."},{"key":"2021111916093236700_BST-2020-0763CC92","doi-asserted-by":"publisher","first-page":"22","DOI":"10.1186\/s40425-017-0222-9","article-title":"Safety, tumor trafficking and immunogenicity of chimeric antigen receptor (CAR)-T cells specific for TAG-72 in colorectal cancer","volume":"5","year":"2017","journal-title":"J. Immunother. Cancer"},{"key":"2021111916093236700_BST-2020-0763CC93","first-page":"3254","article-title":"Construction, production, and characterization of humanized anti-Lewis Y monoclonal antibody 3S193 for targeted immunotherapy of solid tumors","volume":"60","year":"2000","journal-title":"Cancer Res."},{"key":"2021111916093236700_BST-2020-0763CC94","doi-asserted-by":"publisher","first-page":"26","DOI":"10.1186\/s13550-016-0180-0","article-title":"Engineering anti-Lewis-Y hu3S193 antibodies with improved therapeutic ratio for radioimmunotherapy of epithelial cancers","volume":"6","year":"2016","journal-title":"EJNMMI Res."},{"key":"2021111916093236700_BST-2020-0763CC95","doi-asserted-by":"publisher","first-page":"19051","DOI":"10.1073\/pnas.0504312102","article-title":"Adoptive transfer of T cells modified with a humanized chimeric receptor gene inhibits growth of Lewis-Y-expressing tumors in mice","volume":"102","year":"2005","journal-title":"Proc. Natl Acad. Sci. U.S.A."},{"key":"2021111916093236700_BST-2020-0763CC96","doi-asserted-by":"publisher","first-page":"2122","DOI":"10.1038\/mt.2013.154","article-title":"Persistence and efficacy of second generation CAR T cell against the LeY antigen in acute myeloid leukemia","volume":"21","year":"2013","journal-title":"Mol. Ther."},{"key":"2021111916093236700_BST-2020-0763CC97","doi-asserted-by":"publisher","first-page":"127","DOI":"10.1186\/s13045-019-0831-5","article-title":"Targeting glycosylation of PD-1 to enhance CAR-T cell cytotoxicity","volume":"12","year":"2019","journal-title":"J. Hematol. Oncol."},{"key":"2021111916093236700_BST-2020-0763CC98","doi-asserted-by":"publisher","first-page":"713","DOI":"10.1002\/mc.23213","article-title":"Targeting glycosylated antigens on cancer cells using siglec-7\/9-based CAR T-cells","volume":"59","year":"2020","journal-title":"Mol. Carcinog."},{"key":"2021111916093236700_BST-2020-0763CC99","doi-asserted-by":"publisher","first-page":"3084","DOI":"10.3389\/fimmu.2018.03084","article-title":"The first step in adoptive cell immunotherapeutics: assuring cell delivery via glycoengineering","volume":"9","year":"2019","journal-title":"Front. Immunol."},{"key":"2021111916093236700_BST-2020-0763CC100","doi-asserted-by":"publisher","first-page":"18465","DOI":"10.1074\/jbc.RA119.011134","article-title":"Glycoengineering of chimeric antigen receptor (CAR) T-cells to enforce E-selectin binding","volume":"294","year":"2019","journal-title":"J. Biol. Chem."}],"container-title":["Biochemical Society Transactions"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemsoctrans\/article-pdf\/49\/2\/843\/909987\/bst-2020-0763c.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemsoctrans\/article-pdf\/49\/2\/843\/909987\/bst-2020-0763c.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,12,21]],"date-time":"2022-12-21T04:53:44Z","timestamp":1671598424000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemsoctrans\/article\/49\/2\/843\/228064\/Aberrant-protein-glycosylation-in-cancer"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,3,11]]},"references-count":100,"journal-issue":{"issue":"2","published-online":{"date-parts":[[2021,3,11]]},"published-print":{"date-parts":[[2021,4,30]]}},"URL":"https:\/\/doi.org\/10.1042\/bst20200763","relation":{},"ISSN":["0300-5127","1470-8752"],"issn-type":[{"value":"0300-5127","type":"print"},{"value":"1470-8752","type":"electronic"}],"subject":[],"published":{"date-parts":[[2021,3,11]]}}}