{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,12]],"date-time":"2026-04-12T06:20:49Z","timestamp":1775974849421,"version":"3.50.1"},"reference-count":222,"publisher":"MDPI AG","issue":"1","license":[{"start":{"date-parts":[[2021,1,8]],"date-time":"2021-01-08T00:00:00Z","timestamp":1610064000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"Foundation for Science and Technology (FCT)","award":["PTDC\/BBB-EBI\/0567\/2014"],"award-info":[{"award-number":["PTDC\/BBB-EBI\/0567\/2014"]}]},{"name":"Foundation for Science and Technology (FCT)","award":["2020.04384.CEECIND"],"award-info":[{"award-number":["2020.04384.CEECIND"]}]},{"name":"Foundation for Science and Technology (FCT)","award":["2020.05359.BD"],"award-info":[{"award-number":["2020.05359.BD"]}]},{"name":"Operational Programme for Competitiveness Factors COMPETE 2020","award":["POCI-01-0145-FEDER-016585"],"award-info":[{"award-number":["POCI-01-0145-FEDER-016585"]}]},{"name":"Norte Portugal Regional Programme (NORTE 2020)","award":["NORTE-01-0145-FEDER-000029"],"award-info":[{"award-number":["NORTE-01-0145-FEDER-000029"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Cells"],"abstract":"<jats:p>Glycans are major constituents of extracellular vesicles (EVs). Alterations in the glycosylation pathway are a common feature of cancer cells, which gives rise to de novo or increased synthesis of particular glycans. Therefore, glycans and glycoproteins have been widely used in the clinic as both stratification and prognosis cancer biomarkers. Interestingly, several of the known tumor-associated glycans have already been identified in cancer EVs, highlighting EV glycosylation as a potential source of circulating cancer biomarkers. These particles are crucial vehicles of cell\u2013cell communication, being able to transfer molecular information and to modulate the recipient cell behavior. The presence of particular glycoconjugates has been described to be important for EV protein sorting, uptake and organ-tropism. Furthermore, specific EV glycans or glycoproteins have been described to be able to distinguish tumor EVs from benign EVs. In this review, the application of EV glycosylation in the development of novel EV detection and capture methodologies is discussed. In addition, we highlight the potential of EV glycosylation in the clinical setting for both cancer biomarker discovery and EV therapeutic delivery strategies.<\/jats:p>","DOI":"10.3390\/cells10010109","type":"journal-article","created":{"date-parts":[[2021,1,8]],"date-time":"2021-01-08T08:58:34Z","timestamp":1610096314000},"page":"109","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":115,"title":["Glycosylation of Cancer Extracellular Vesicles: Capture Strategies, Functional Roles and Potential Clinical Applications"],"prefix":"10.3390","volume":"10","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-0266-9093","authenticated-orcid":false,"given":"\u00c1lvaro M.","family":"Martins","sequence":"first","affiliation":[{"name":"Institute for Research and Innovation in Health (i3S), University of Porto, 4200-135 Porto, Portugal"},{"name":"Institute of Molecular Pathology and Immunology (IPATIMUP), University of Porto, 4200-135 Porto, Portugal"},{"name":"Instituto de Ci\u00eancias Biom\u00e9dicas Abel Salazar (ICBAS), University of Porto, 4050-313 Porto, Portugal"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1902-3053","authenticated-orcid":false,"given":"C\u00e1tia C.","family":"Ramos","sequence":"additional","affiliation":[{"name":"Institute for Research and Innovation in Health (i3S), University of Porto, 4200-135 Porto, Portugal"},{"name":"Institute of Molecular Pathology and Immunology (IPATIMUP), University of Porto, 4200-135 Porto, Portugal"},{"name":"Department of Chemistry, University of Aveiro, Campus Universit\u00e1rio de Santiago, 3810-193 Aveiro, Portugal"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7606-1120","authenticated-orcid":false,"given":"Daniela","family":"Freitas","sequence":"additional","affiliation":[{"name":"Institute for Research and Innovation in Health (i3S), University of Porto, 4200-135 Porto, Portugal"},{"name":"Institute of Molecular Pathology and Immunology (IPATIMUP), 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":"Institute for Research and Innovation in Health (i3S), University of Porto, 4200-135 Porto, Portugal"},{"name":"Institute of Molecular Pathology and Immunology (IPATIMUP), University of Porto, 4200-135 Porto, Portugal"},{"name":"Instituto de Ci\u00eancias Biom\u00e9dicas Abel Salazar (ICBAS), University of Porto, 4050-313 Porto, Portugal"},{"name":"Faculty of Medicine of the University of Porto (FMUP), 4200-319 Porto, Portugal"}]}],"member":"1968","published-online":{"date-parts":[[2021,1,8]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"255","DOI":"10.1146\/annurev-cellbio-101512-122326","article-title":"Biogenesis, Secretion, and Intercellular Interactions of Exosomes and Other Extracellular Vesicles","volume":"30","author":"Colombo","year":"2014","journal-title":"Annu. Rev. Cell Dev. Biol."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"525","DOI":"10.1002\/pmic.201300387","article-title":"Cell Surface Protein Glycosylation in Cancer","volume":"14","author":"Christiansen","year":"2014","journal-title":"Proteomics"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"540","DOI":"10.1038\/nrc3982","article-title":"Glycosylation in Cancer: Mechanisms and Clinical Implications","volume":"15","author":"Pinho","year":"2015","journal-title":"Nat. Rev. Cancer"},{"key":"ref_4","doi-asserted-by":"crossref","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","author":"Mereiter","year":"2019","journal-title":"Cancer Cell"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"395","DOI":"10.1016\/j.lfs.2018.06.026","article-title":"Human Melanoma-Derived Ectosomes Are Enriched with Specific Glycan Epitopes","volume":"207","author":"Surman","year":"2018","journal-title":"Life Sci."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"4624","DOI":"10.1021\/pr200434y","article-title":"Identification of a Conserved Glycan Signature for Microvesicles","volume":"10","author":"Batista","year":"2011","journal-title":"J. Proteome Res."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"3183","DOI":"10.1016\/j.jmb.2016.02.030","article-title":"Glycosylation Quality Control by the Golgi Structure","volume":"428","author":"Zhang","year":"2016","journal-title":"J. Mol. Biol."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"11920","DOI":"10.1038\/s41598-019-48499-1","article-title":"Assessing the Role of Surface Glycans of Extracellular Vesicles on Cellular Uptake","volume":"9","author":"Williams","year":"2019","journal-title":"Sci. Rep."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"17380","DOI":"10.1073\/pnas.1304266110","article-title":"Cancer Cell Exosomes Depend on Cell-Surface Heparan Sulfate Proteoglycans for Their Internalization and Functional Activity","volume":"110","author":"Christianson","year":"2013","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"4263","DOI":"10.1002\/1873-3468.12448","article-title":"Integrins and Heparan Sulfate Proteoglycans on Hepatic Stellate Cells (HSC) Are Novel Receptors for HSC-Derived Exosomes","volume":"590","author":"Chen","year":"2016","journal-title":"FEBS Lett."},{"key":"ref_11","doi-asserted-by":"crossref","unstructured":"Franzen, C.A., Simms, P.E., Van Huis, A.F., Foreman, K.E., Kuo, P.C., and Gupta, G.N. (2014). Characterization of Uptake and Internalization of Exosomes by Bladder Cancer Cells. Biomed. Res. Int., 2014.","DOI":"10.1155\/2014\/619829"},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.chembiol.2013.12.010","article-title":"The Challenge and Promise of Glycomics","volume":"21","author":"Cummings","year":"2014","journal-title":"Chem. Biol."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"55","DOI":"10.3389\/fonc.2016.00055","article-title":"Glycomic Approaches for the Discovery of Targets in Gastrointestinal Cancer","volume":"6","author":"Mereiter","year":"2016","journal-title":"Front. Oncol."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1093\/glycob\/cww086","article-title":"Biological Roles of Glycans","volume":"27","author":"Varki","year":"2017","journal-title":"Glycobiology"},{"key":"ref_15","doi-asserted-by":"crossref","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","author":"Rodrigues","year":"2018","journal-title":"Cell Immunol."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"8398","DOI":"10.3390\/ijms13078398","article-title":"Function and 3D Structure of the N-Glycans on Glycoproteins","volume":"13","author":"Nagae","year":"2012","journal-title":"Int. J. Mol. Sci."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1016\/j.tcb.2010.11.004","article-title":"Location, Location, Location: New Insights into O-GalNAc Protein Glycosylation","volume":"21","author":"Gill","year":"2011","journal-title":"Trends Cell Biol."},{"key":"ref_18","first-page":"147","article-title":"The Structural Elucidation of Glycosaminoglycans","volume":"534","author":"Prabhakar","year":"2009","journal-title":"Methods Mol. Biol."},{"key":"ref_19","first-page":"4620","article-title":"Increased Expression of UDP-Galactose Transporter Messenger RNA in Human Colon Cancer Tissues and Its Implication in Synthesis of Thomsen-Friedenreich Antigen and Sialyl Lewis A\/X Determinants","volume":"61","author":"Kumamoto","year":"2001","journal-title":"Cancer Res."},{"key":"ref_20","first-page":"1443","article-title":"ST6GalNAc-I Controls Expression of Sialyl-Tn Antigen in Gastrointestinal Tissues","volume":"3","author":"Marcos","year":"2011","journal-title":"Front. Biosci. (Elite Ed.)"},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"843","DOI":"10.1083\/jcb.201003055","article-title":"Regulation of O-Glycosylation through Golgi-to-ER Relocation of Initiation Enzymes","volume":"189","author":"Gill","year":"2010","journal-title":"J. Cell. Biol."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"9228","DOI":"10.1073\/pnas.0914004107","article-title":"Cosmc Is an Essential Chaperone for Correct Protein O-Glycosylation","volume":"107","author":"Wang","year":"2010","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1016\/j.cell.2007.01.049","article-title":"Complex N-Glycan Number and Degree of Branching Cooperate to Regulate Cell Proliferation and Differentiation","volume":"129","author":"Lau","year":"2007","journal-title":"Cell"},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"1283","DOI":"10.1093\/glycob\/cwu083","article-title":"Regulatory Role of Glycans in the Control of Hypoxia-Driven Angiogenesis and Sensitivity to Anti-Angiogenic Treatment","volume":"24","author":"Croci","year":"2014","journal-title":"Glycobiology"},{"key":"ref_25","doi-asserted-by":"crossref","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","author":"Freitas","year":"2019","journal-title":"EBioMedicine"},{"key":"ref_26","first-page":"28","article-title":"Altered Tumor-Cell Glycosylation Promotes Metastasis","volume":"4","author":"Borsig","year":"2014","journal-title":"Front. Oncol."},{"key":"ref_27","doi-asserted-by":"crossref","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","author":"Contessa","year":"2008","journal-title":"Cancer Res."},{"key":"ref_28","doi-asserted-by":"crossref","unstructured":"Gomes, C., Os\u00f3rio, H., Pinto, M.T., Campos, D., Oliveira, M.J., and Reis, C.A. (2013). Expression of ST3GAL4 Leads to SLe(x) Expression and Induces c-Met Activation and an Invasive Phenotype in Gastric Carcinoma Cells. PLoS One, 8.","DOI":"10.1371\/journal.pone.0066737"},{"key":"ref_29","doi-asserted-by":"crossref","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","author":"Mereiter","year":"2016","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_30","first-page":"2478","article-title":"N-Glycosylation Alters Cadherin-Mediated Intercellular Binding Kinetics","volume":"125","author":"Langer","year":"2012","journal-title":"J. Cell Sci."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"537","DOI":"10.1016\/j.trecan.2018.05.009","article-title":"Glycosylation and Integrin Regulation in Cancer","volume":"4","author":"Marsico","year":"2018","journal-title":"Trends Cancer"},{"key":"ref_32","doi-asserted-by":"crossref","unstructured":"Hang, Q., Isaji, T., Hou, S., Wang, Y., Fukuda, T., and Gu, J. (2017). A Key Regulator of Cell Adhesion: Identification and Characterization of Important N-Glycosylation Sites on Integrin A5 for Cell Migration. Mol. Cell Biol., 37.","DOI":"10.1128\/MCB.00558-16"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"2120","DOI":"10.3389\/fimmu.2019.02120","article-title":"Altered Cell Adhesion and Glycosylation Promote Cancer Immune Suppression and Metastasis","volume":"10","author":"Borsig","year":"2019","journal-title":"Front. Immunol."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"473","DOI":"10.1146\/annurev-pathol-012414-040438","article-title":"Protein Glycosylation in Cancer","volume":"10","author":"Stowell","year":"2015","journal-title":"Annu. Rev. Pathol."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"1117","DOI":"10.1016\/j.cell.2010.06.011","article-title":"Cell Signaling by Receptor Tyrosine Kinases","volume":"141","author":"Lemmon","year":"2010","journal-title":"Cell"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"58","DOI":"10.1186\/s12943-018-0782-4","article-title":"Mechanisms of Receptor Tyrosine Kinase Activation in Cancer","volume":"17","author":"Du","year":"2018","journal-title":"Mol. Cancer"},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"34","DOI":"10.1186\/s12943-018-0797-x","article-title":"Receptor Tyrosine Kinases (RTKs) in Breast Cancer: Signaling, Therapeutic Implications and Challenges","volume":"17","author":"Butti","year":"2018","journal-title":"Mol. Cancer"},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"64","DOI":"10.1016\/j.abb.2009.02.005","article-title":"EGF-Mediated Migration Signaling Activated by N-Acetylglucosaminyltransferase-V via Receptor Protein Tyrosine Phosphatase Kappa","volume":"486","author":"Wang","year":"2009","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"33507","DOI":"10.1038\/srep33507","article-title":"N-Glycosylation of Integrin A5 Acts as a Switch for EGFR-Mediated Complex Formation of Integrin A5\u03b21 to A6\u03b24","volume":"6","author":"Hang","year":"2016","journal-title":"Sci. Rep."},{"key":"ref_40","doi-asserted-by":"crossref","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","author":"Britain","year":"2018","journal-title":"J. Ovarian Res."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"21116","DOI":"10.1073\/pnas.1013405107","article-title":"Specific Posttranslational Modification Regulates Early Events in Mammary Carcinoma Formation","volume":"107","author":"Guo","year":"2010","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"e1800014","DOI":"10.1002\/prca.201800014","article-title":"Increases in Tumor N-Glycan Polylactosamines Associated with Advanced HER2-Positive and Triple-Negative Breast Cancer Tissues","volume":"13","author":"Scott","year":"2019","journal-title":"Proteom. Clin. Appl."},{"key":"ref_43","doi-asserted-by":"crossref","unstructured":"Duarte, H.O., Balma\u00f1a, M., Mereiter, S., Os\u00f3rio, H., Gomes, J., and Reis, C.A. (2017). Gastric Cancer Cell Glycosylation as a Modulator of the ErbB2 Oncogenic Receptor. Int. J. Mol. Sci., 18.","DOI":"10.3390\/ijms18112262"},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"29913","DOI":"10.1074\/jbc.M111.226423","article-title":"Galectin-3 Protein Modulates Cell Surface Expression and Activation of Vascular Endothelial Growth Factor Receptor 2 in Human Endothelial Cells","volume":"286","author":"Markowska","year":"2011","journal-title":"J. Biol. Chem."},{"key":"ref_45","doi-asserted-by":"crossref","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","author":"Croci","year":"2014","journal-title":"Cell"},{"key":"ref_46","doi-asserted-by":"crossref","unstructured":"Ferreira, I.G., Pucci, M., Venturi, G., Malagolini, N., Chiricolo, M., and Dall\u2019Olio, F. (2018). Glycosylation as a Main Regulator of Growth and Death Factor Receptors Signaling. Int. J. Mol. Sci., 19.","DOI":"10.3390\/ijms19020580"},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"250","DOI":"10.1016\/j.ccr.2012.06.029","article-title":"Targeted Disruption of Heparan Sulfate Interaction with Hepatocyte and Vascular Endothelial Growth Factors Blocks Normal and Oncogenic Signaling","volume":"22","author":"Cecchi","year":"2012","journal-title":"Cancer Cell"},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"3045","DOI":"10.1038\/sj.emboj.7601188","article-title":"Glycosaminoglycan Modification of Neuropilin-1 Modulates VEGFR2 Signaling","volume":"25","author":"Shintani","year":"2006","journal-title":"EMBO J."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"1183","DOI":"10.1242\/jcs.064618","article-title":"Integrins and Cadherins Join Forces to Form Adhesive Networks","volume":"124","author":"Weber","year":"2011","journal-title":"J. Cell Sci."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"319","DOI":"10.1038\/nature13535","article-title":"The Cancer Glycocalyx Mechanically Primes Integrin-Mediated Growth and Survival","volume":"511","author":"Paszek","year":"2014","journal-title":"Nature"},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"138","DOI":"10.1016\/j.lfs.2016.02.071","article-title":"Effect of Alpha 2,6 Sialylation on Integrin-Mediated Adhesion of Breast Cancer Cells to Fibronectin and Collagen IV","volume":"149","author":"Yuan","year":"2016","journal-title":"Life Sci."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"5059","DOI":"10.1242\/jcs.01350","article-title":"Expression of Sialyl-Tn Epitopes on Beta1 Integrin Alters Epithelial Cell Phenotype, Proliferation and Haptotaxis","volume":"117","author":"Rocher","year":"2004","journal-title":"J. Cell Sci."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"2690","DOI":"10.1016\/j.bbagen.2012.10.021","article-title":"E-Cadherin and Adherens-Junctions Stability in Gastric Carcinoma: Functional Implications of Glycosyltransferases Involving N-Glycan Branching Biosynthesis, N-Acetylglucosaminyltransferases III and V","volume":"1830","author":"Pinho","year":"2013","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"648","DOI":"10.1093\/glycob\/cwx105","article-title":"Selectins in Cancer Immunity","volume":"28","author":"Borsig","year":"2018","journal-title":"Glycobiology"},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"331","DOI":"10.1093\/cvr\/cvv154","article-title":"Selectins: Initiators of Leucocyte Adhesion and Signalling at the Vascular Wall","volume":"107","author":"McEver","year":"2015","journal-title":"Cardiovasc. Res."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"13","DOI":"10.3892\/ol.2016.5431","article-title":"C-Type Lectins Facilitate Tumor Metastasis","volume":"13","author":"Ding","year":"2017","journal-title":"Oncol. Lett."},{"key":"ref_57","doi-asserted-by":"crossref","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","author":"Esposito","year":"2019","journal-title":"Nat. Cell Biol."},{"key":"ref_58","doi-asserted-by":"crossref","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","author":"Jandus","year":"2014","journal-title":"J. Clin. Investig."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1038\/nchembio.1388","article-title":"Glycocalyx Engineering Reveals a Siglec-Based Mechanism for NK Cell Immunoevasion","volume":"10","author":"Hudak","year":"2014","journal-title":"Nat. Chem. Biol."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"653","DOI":"10.1038\/nri3737","article-title":"Siglec-Mediated Regulation of Immune Cell Function in Disease","volume":"14","author":"Macauley","year":"2014","journal-title":"Nat. Rev. Immunol."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"556","DOI":"10.1038\/nm.4314","article-title":"Dectin 1 Activation on Macrophages by Galectin 9 Promotes Pancreatic Carcinoma and Peritumoral Immune Tolerance","volume":"23","author":"Daley","year":"2017","journal-title":"Nat. Med."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"412","DOI":"10.1158\/2326-6066.CIR-14-0150","article-title":"Galectin-3 Shapes Antitumor Immune Responses by Suppressing CD8+ T Cells via LAG-3 and Inhibiting Expansion of Plasmacytoid Dendritic Cells","volume":"3","author":"Kouo","year":"2015","journal-title":"Cancer Immunol. Res."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"7476","DOI":"10.1158\/0008-5472.CAN-10-0761","article-title":"A Galectin-3 Ligand Corrects the Impaired Function of Human CD4 and CD8 Tumor-Infiltrating Lymphocytes and Favors Tumor Rejection in Mice","volume":"70","author":"Demotte","year":"2010","journal-title":"Cancer Res."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"e1629257","DOI":"10.1080\/2162402X.2019.1629257","article-title":"Aberrant Fucosylation Enables Breast Cancer Clusterin to Interact with Dendritic Cell-Specific ICAM-Grabbing Non-Integrin (DC-SIGN)","volume":"8","author":"Merlotti","year":"2019","journal-title":"Oncoimmunology"},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"615","DOI":"10.1089\/omi.2019.0149","article-title":"Rise of Systems Glycobiology and Personalized Glycomedicine: Why and How to Integrate Glycomics with Multiomics Science?","volume":"23","author":"Kunej","year":"2019","journal-title":"OMICS"},{"key":"ref_66","unstructured":"Rudd, P., Karlsson, N.G., Khoo, K.-H., and Packer, N.H. Glycomics and Glycoproteomics, Cold Spring Harbor Laboratory Press. [3rd ed.]. Chapter 51."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1007\/128_2014_612","article-title":"Development and Applications of the Lectin Microarray","volume":"367","author":"Hirabayashi","year":"2015","journal-title":"Top. Curr. Chem."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1007\/s10719-012-9376-3","article-title":"Glycomics Using Mass Spectrometry","volume":"30","author":"Wuhrer","year":"2013","journal-title":"Glycoconj. J."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"1071","DOI":"10.1039\/C5MB00835B","article-title":"Getting to Know the Extracellular Vesicle Glycome","volume":"12","author":"Gerlach","year":"2016","journal-title":"Mol. Biosyst."},{"key":"ref_70","doi-asserted-by":"crossref","unstructured":"Gerlach, J.Q., Kr\u00fcger, A., Gallogly, S., Hanley, S.A., Hogan, M.C., Ward, C.J., Joshi, L., and Griffin, M.D. (2013). Surface Glycosylation Profiles of Urine Extracellular Vesicles. PLoS ONE, 8.","DOI":"10.1371\/journal.pone.0074801"},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"7871","DOI":"10.1021\/acs.analchem.7b05455","article-title":"N-Glycosylation of Extracellular Vesicles from HEK-293 and Glioma Cell Lines","volume":"90","author":"Costa","year":"2018","journal-title":"Anal. Chem."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"1741","DOI":"10.3390\/biom5031741","article-title":"Extracellular Vesicles from Ovarian Carcinoma Cells Display Specific Glycosignatures","volume":"5","author":"Gomes","year":"2015","journal-title":"Biomolecules"},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"1442985","DOI":"10.1080\/20013078.2018.1442985","article-title":"Glycosylation of Extracellular Vesicles: Current Knowledge, Tools and Clinical Perspectives","volume":"7","author":"Williams","year":"2018","journal-title":"J. Extracell. Vesicles"},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"498","DOI":"10.1016\/j.sbi.2009.05.005","article-title":"Mass Spectrometry in the Analysis of N-Linked and O-Linked Glycans","volume":"19","author":"North","year":"2009","journal-title":"Curr. Opin. Struct. Biol."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"6088","DOI":"10.1021\/ac025890a","article-title":"Small-Scale Analysis of O-Linked Oligosaccharides from Glycoproteins and Mucins Separated by Gel Electrophoresis","volume":"74","author":"Schulz","year":"2002","journal-title":"Anal. Chem."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"1853","DOI":"10.1016\/j.bbapap.2006.10.007","article-title":"Strategies for Analysis of Glycoprotein Glycosylation","volume":"1764","author":"Geyer","year":"2006","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1006\/abio.2002.5620","article-title":"Recovery of Intact 2-Aminobenzamide-Labeled O-Glycans Released from Glycoproteins by Hydrazinolysis","volume":"304","author":"Merry","year":"2002","journal-title":"Anal. Biochem."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1016\/j.ab.2012.01.002","article-title":"Suppression of Peeling during the Release of O-Glycans by Hydrazinolysis","volume":"423","author":"Kozak","year":"2012","journal-title":"Anal. Biochem."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"429","DOI":"10.1182\/bloodadvances.2016002121","article-title":"Characterizing the O-Glycosylation Landscape of Human Plasma, Platelets, and Endothelial Cells","volume":"1","author":"King","year":"2017","journal-title":"Blood Adv."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"1478","DOI":"10.1038\/emboj.2013.79","article-title":"Precision Mapping of the Human O-GalNAc Glycoproteome through SimpleCell Technology","volume":"32","author":"Steentoft","year":"2013","journal-title":"EMBO J."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"902","DOI":"10.1038\/s41592-019-0504-x","article-title":"Glyco-DIA: A Method for Quantitative O-Glycoproteomics with in Silico-Boosted Glycopeptide Libraries","volume":"16","author":"Ye","year":"2019","journal-title":"Nat. Methods"},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"1616","DOI":"10.1074\/mcp.M114.046862","article-title":"Probing the O-Glycoproteome of Gastric Cancer Cell Lines for Biomarker Discovery","volume":"14","author":"Campos","year":"2015","journal-title":"Mol. Cell. Proteom."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"337","DOI":"10.1586\/14789450.2015.1059758","article-title":"Glycoengineered Cell Models for the Characterization of Cancer O-Glycoproteome: An Innovative Strategy for Biomarker Discovery","volume":"12","author":"Campos","year":"2015","journal-title":"Expert. Rev. Proteom."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"942","DOI":"10.1002\/1873-3468.13377","article-title":"N-Glycome Inheritance from Cells to Extracellular Vesicles in B16 Melanomas","volume":"593","author":"Harada","year":"2019","journal-title":"FEBS Lett."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"838","DOI":"10.1136\/jclinpath-2016-204312","article-title":"Release of Urinary Extracellular Vesicles in Prostate Cancer Is Associated with Altered Urinary N-Glycosylation Profile","volume":"70","author":"Vermassen","year":"2017","journal-title":"J. Clin. Pathol."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"1621131","DOI":"10.1080\/20013078.2019.1621131","article-title":"Different Isolation Approaches Lead to Diverse Glycosylated Extracellular Vesicle Populations","volume":"8","author":"Freitas","year":"2019","journal-title":"J. Extracell. Vesicles"},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"108","DOI":"10.1016\/j.aca.2018.07.040","article-title":"Lectin-Mediated in Situ Rolling Circle Amplification on Exosomes for Probing Cancer-Related Glycan Pattern","volume":"1039","author":"Feng","year":"2018","journal-title":"Anal. Chim. Acta"},{"key":"ref_88","first-page":"387","article-title":"Elevated O-GlcNAcylation of Extracellular Vesicle Proteins Derived from Metastatic Colorectal Cancer Cells","volume":"13","author":"Chaiyawat","year":"2016","journal-title":"Cancer Genom. Proteom."},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"5364","DOI":"10.1021\/acs.analchem.7b00062","article-title":"Comprehensive Analytical Approach toward Glycomic Characterization and Profiling in Urinary Exosomes","volume":"89","author":"Zou","year":"2017","journal-title":"Anal. Chem."},{"key":"ref_90","doi-asserted-by":"crossref","unstructured":"Peixoto, A., Relvas-Santos, M., Azevedo, R., Santos, L.L., and Ferreira, J.A. (2019). Protein Glycosylation and Tumor Microenvironment Alterations Driving Cancer Hallmarks. Front. Oncol., 9.","DOI":"10.3389\/fonc.2019.00380"},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"332","DOI":"10.1038\/s41556-018-0040-4","article-title":"Identification of Distinct Nanoparticles and Subsets of Extracellular Vesicles by Asymmetric Flow Field-Flow Fractionation","volume":"20","author":"Zhang","year":"2018","journal-title":"Nat. Cell. Biol."},{"key":"ref_92","doi-asserted-by":"crossref","unstructured":"Doyle, L.M., and Wang, M.Z. (2019). Overview of Extracellular Vesicles, Their Origin, Composition, Purpose, and Methods for Exosome Isolation and Analysis. Cells, 8.","DOI":"10.3390\/cells8070727"},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1038\/nrm.2017.125","article-title":"Shedding Light on the Cell Biology of Extracellular Vesicles","volume":"19","author":"Raposo","year":"2018","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.pharmthera.2018.02.013","article-title":"Biogenesis and Function of Extracellular Vesicles in Cancer","volume":"188","author":"Bebelman","year":"2018","journal-title":"Pharmacol. Ther."},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"22519","DOI":"10.1038\/srep22519","article-title":"Cells Release Subpopulations of Exosomes with Distinct Molecular and Biological Properties","volume":"6","author":"Willms","year":"2016","journal-title":"Sci. Rep."},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1111\/j.1600-0854.2004.0167.x","article-title":"Degradation of AP2 during Reticulocyte Maturation Enhances Binding of Hsc70 and Alix to a Common Site on TFR for Sorting into Exosomes","volume":"5","author":"Blanc","year":"2004","journal-title":"Traffic"},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"925","DOI":"10.1111\/j.1600-0854.2009.00920.x","article-title":"Multivesicular Endosome Biogenesis in the Absence of ESCRTs","volume":"10","author":"Stuffers","year":"2009","journal-title":"Traffic"},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"1244","DOI":"10.1126\/science.1153124","article-title":"Ceramide Triggers Budding of Exosome Vesicles into Multivesicular Endosomes","volume":"319","author":"Trajkovic","year":"2008","journal-title":"Science"},{"key":"ref_99","doi-asserted-by":"crossref","unstructured":"Andreu, Z., and Y\u00e1\u00f1ez-M\u00f3, M. (2014). Tetraspanins in Extracellular Vesicle Formation and Function. Front. Immunol., 5.","DOI":"10.3389\/fimmu.2014.00442"},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"20121","DOI":"10.1074\/jbc.273.32.20121","article-title":"Selective Enrichment of Tetraspan Proteins on the Internal Vesicles of Multivesicular Endosomes and on Exosomes Secreted by Human B-Lymphocytes","volume":"273","author":"Escola","year":"1998","journal-title":"J. Biol. Chem."},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"2154","DOI":"10.1021\/pr200901p","article-title":"Quantitative Proteome Profiling of Normal Human Circulating Microparticles","volume":"11","author":"Nielsen","year":"2012","journal-title":"J. Proteome. Res."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"3791","DOI":"10.1182\/blood.V94.11.3791","article-title":"Activated Platelets Release Two Types of Membrane Vesicles: Microvesicles by Surface Shedding and Exosomes Derived from Exocytosis of Multivesicular Bodies and Alpha-Granules","volume":"94","author":"Heijnen","year":"1999","journal-title":"Blood"},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"7309","DOI":"10.4049\/jimmunol.166.12.7309","article-title":"Proteomic Analysis of Dendritic Cell-Derived Exosomes: A Secreted Subcellular Compartment Distinct from Apoptotic Vesicles","volume":"166","author":"Boussac","year":"2001","journal-title":"J. Immunol."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"309","DOI":"10.1038\/s41419-019-1518-0","article-title":"Cytokine-Induced Translocation of GRP78 to the Plasma Membrane Triggers a pro-Apoptotic Feedback Loop in Pancreatic Beta Cells","volume":"10","author":"Vig","year":"2019","journal-title":"Cell Death Dis."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"28849","DOI":"10.18632\/oncotarget.6680","article-title":"The Histone Deacetylase Inhibitor SAHA Induces HSP60 Nitration and Its Extracellular Release by Exosomal Vesicles in Human Lung-Derived Carcinoma Cells","volume":"7","author":"Campanella","year":"2015","journal-title":"Oncotarget"},{"key":"ref_106","doi-asserted-by":"crossref","unstructured":"Kusuma, G.D., Barabadi, M., Tan, J.L., Morton, D.A.V., Frith, J.E., and Lim, R. (2018). To Protect and to Preserve: Novel Preservation Strategies for Extracellular Vesicles. Front. Pharmacol., 9.","DOI":"10.3389\/fphar.2018.01199"},{"key":"ref_107","doi-asserted-by":"crossref","unstructured":"Kalra, H., Drummen, G.P.C., and Mathivanan, S. (2016). Focus on Extracellular Vesicles: Introducing the Next Small Big Thing. Int. J. Mol. Sci., 17.","DOI":"10.3390\/ijms17020170"},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"585","DOI":"10.1038\/s41580-020-0251-y","article-title":"RNA Delivery by Extracellular Vesicles in Mammalian Cells and Its Applications","volume":"21","author":"Breyne","year":"2020","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"170","DOI":"10.1016\/j.pharmthera.2018.08.002","article-title":"Extracellular Vesicles and Their Nucleic Acids for Biomarker Discovery","volume":"192","author":"Getting","year":"2018","journal-title":"Pharmacol. Ther."},{"key":"ref_110","doi-asserted-by":"crossref","unstructured":"Massaro, C., Sgueglia, G., Frattolillo, V., Baglio, S.R., Altucci, L., and Dell\u2019Aversana, C. (2020). Extracellular Vesicle-Based Nucleic Acid Delivery: Current Advances and Future Perspectives in Cancer Therapeutic Strategies. Pharmaceutics, 12.","DOI":"10.3390\/pharmaceutics12100980"},{"key":"ref_111","doi-asserted-by":"crossref","unstructured":"Escrevente, C., Grammel, N., Kandzia, S., Zeiser, J., Tranfield, E.M., Conradt, H.S., and Costa, J. (2013). Sialoglycoproteins and N-Glycans from Secreted Exosomes of Ovarian Carcinoma Cells. PLoS ONE, 8.","DOI":"10.1371\/journal.pone.0078631"},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"836","DOI":"10.1016\/j.ccell.2016.10.009","article-title":"Extracellular Vesicles in Cancer: Cell-to-Cell Mediators of Metastasis","volume":"30","author":"Becker","year":"2016","journal-title":"Cancer Cell"},{"key":"ref_113","doi-asserted-by":"crossref","unstructured":"King, H.W., Michael, M.Z., and Gleadle, J.M. (2012). Hypoxic Enhancement of Exosome Release by Breast Cancer Cells. BMC Cancer, 12.","DOI":"10.1186\/1471-2407-12-421"},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"1595","DOI":"10.1002\/ijc.24479","article-title":"Lung Cancer Secreted Microvesicles: Underappreciated Modulators of Microenvironment in Expanding Tumors","volume":"125","author":"Wysoczynski","year":"2009","journal-title":"Int. J. Cancer"},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"34211","DOI":"10.1074\/jbc.M109.041152","article-title":"Microenvironmental PH Is a Key Factor for Exosome Traffic in Tumor Cells","volume":"284","author":"Parolini","year":"2009","journal-title":"J. Biol. Chem."},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"230","DOI":"10.1016\/j.isci.2019.05.029","article-title":"Serum Deprivation of Mesenchymal Stem Cells Improves Exosome Activity and Alters Lipid and Protein Composition","volume":"16","author":"Haraszti","year":"2019","journal-title":"iScience"},{"key":"ref_117","doi-asserted-by":"crossref","unstructured":"Garcia, N.A., Ontoria-Oviedo, I., Gonz\u00e1lez-King, H., Diez-Juan, A., and Sep\u00falveda, P. (2015). Glucose Starvation in Cardiomyocytes Enhances Exosome Secretion and Promotes Angiogenesis in Endothelial Cells. PLoS ONE, 10.","DOI":"10.1371\/journal.pone.0138849"},{"key":"ref_118","doi-asserted-by":"crossref","unstructured":"Hedlund, M., Nagaeva, O., Kargl, D., Baranov, V., and Mincheva-Nilsson, L. (2011). Thermal- and Oxidative Stress Causes Enhanced Release of NKG2D Ligand-Bearing Immunosuppressive Exosomes in Leukemia\/Lymphoma T and B Cells. PLoS ONE, 6.","DOI":"10.1371\/journal.pone.0016899"},{"key":"ref_119","doi-asserted-by":"crossref","unstructured":"Eldh, M., Ekstr\u00f6m, K., Valadi, H., Sj\u00f6strand, M., Olsson, B., Jern\u00e5s, M., and L\u00f6tvall, J. (2010). Exosomes Communicate Protective Messages during Oxidative Stress; Possible Role of Exosomal Shuttle RNA. PLoS ONE, 5.","DOI":"10.1371\/journal.pone.0015353"},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"15874","DOI":"10.1074\/jbc.M112.340588","article-title":"Anticancer Drugs Cause Release of Exosomes with Heat Shock Proteins from Human Hepatocellular Carcinoma Cells That Elicit Effective Natural Killer Cell Antitumor Responses in Vitro","volume":"287","author":"Lv","year":"2012","journal-title":"J. Biol. Chem."},{"key":"ref_121","doi-asserted-by":"crossref","unstructured":"Kucharzewska, P., and Belting, M. (2013). Emerging Roles of Extracellular Vesicles in the Adaptive Response of Tumour Cells to Microenvironmental Stress. J. Extracell. Vesicles, 2.","DOI":"10.3402\/jev.v2i0.20304"},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"7404","DOI":"10.1021\/jacs.9b12182","article-title":"Quantitative Localized Analysis Reveals Distinct Exosomal Protein-Specific Glycosignatures: Implications in Cancer Cell Subtyping, Exosome Biogenesis, and Function","volume":"142","author":"Guo","year":"2020","journal-title":"J. Am. Chem. Soc."},{"key":"ref_123","doi-asserted-by":"crossref","unstructured":"Surman, M., Hoja-\u0141ukowicz, D., Szwed, S., K\u0119dracka-Krok, S., Jankowska, U., Kurtyka, M., Dro\u017cd\u017c, A., Lity\u0144ska, A., St\u0119pie\u0144, E., and Przyby\u0142o, M. (2019). An Insight into the Proteome of Uveal Melanoma-Derived Ectosomes Reveals the Presence of Potentially Useful Biomarkers. Int. J. Mol. Sci., 20.","DOI":"10.3390\/ijms20153789"},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"701","DOI":"10.1016\/j.bbrc.2017.07.126","article-title":"Glycan Profiling Analysis Using Evanescent-Field Fluorescence-Assisted Lectin Array: Importance of Sugar Recognition for Cellular Uptake of Exosomes from Mesenchymal Stem Cells","volume":"491","author":"Shimoda","year":"2017","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_125","doi-asserted-by":"crossref","unstructured":"Th\u00e9ry, C., Witwer, K.W., Aikawa, E., Alcaraz, M.J., Anderson, J.D., Andriantsitohaina, R., Antoniou, A., Arab, T., Archer, F., and Atkin-Smith, G.K. (2018). Minimal Information for Studies of Extracellular Vesicles 2018 (MISEV2018): A Position Statement of the International Society for Extracellular Vesicles and Update of the MISEV2014 Guidelines. J. Extracell. Vesicles, 7.","DOI":"10.1080\/20013078.2018.1535750"},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"881","DOI":"10.1039\/C7NR08360B","article-title":"Technical Challenges of Working with Extracellular Vesicles","volume":"10","author":"Ramirez","year":"2018","journal-title":"Nanoscale"},{"key":"ref_127","doi-asserted-by":"crossref","unstructured":"Williams, C., Palviainen, M., Reichardt, N.-C., Siljander, P.R.-M., and Falc\u00f3n-P\u00e9rez, J.M. (2019). Metabolomics Applied to the Study of Extracellular Vesicles. Metabolites, 9.","DOI":"10.3390\/metabo9110276"},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"834","DOI":"10.3892\/ijmm.2017.3080","article-title":"Comparison of Isolation Methods of Exosomes and Exosomal RNA from Cell Culture Medium and Serum","volume":"40","author":"Tang","year":"2017","journal-title":"Int. J. Mol. Med."},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"29497","DOI":"10.3402\/jev.v5.29497","article-title":"Different EV Enrichment Methods Suitable for Clinical Settings Yield Different Subpopulations of Urinary Extracellular Vesicles from Human Samples","volume":"5","author":"Royo","year":"2016","journal-title":"J. Extracell. Vesicles"},{"key":"ref_130","doi-asserted-by":"crossref","unstructured":"Van Deun, J., Mestdagh, P., Sormunen, R., Cocquyt, V., Vermaelen, K., Vandesompele, J., Bracke, M., De Wever, O., and Hendrix, A. (2014). The Impact of Disparate Isolation Methods for Extracellular Vesicles on Downstream RNA Profiling. J. Extracell. Vesicles, 3.","DOI":"10.3402\/jev.v3.24858"},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"2516","DOI":"10.1021\/acs.jproteome.0c00200","article-title":"Comparative Glycomic Analysis of Exosome Subpopulations Derived from Pancreatic Cancer Cell Lines","volume":"19","author":"Matsuda","year":"2020","journal-title":"J. Proteome Res."},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"293","DOI":"10.1016\/j.ymeth.2012.01.002","article-title":"Comparison of Ultracentrifugation, Density Gradient Separation, and Immunoaffinity Capture Methods for Isolating Human Colon Cancer Cell Line LIM1863-Derived Exosomes","volume":"56","author":"Tauro","year":"2012","journal-title":"Methods"},{"key":"ref_133","first-page":"3","article-title":"Isolation and Characterization of Exosomes from Cell Culture Supernatants and Biological Fluids","volume":"30","author":"Amigorena","year":"2006","journal-title":"Curr. Protoc. Cell Biol."},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"F1251","DOI":"10.1152\/ajprenal.00128.2014","article-title":"Urinary Extracellular Vesicles and the Kidney: Biomarkers and Beyond","volume":"306","author":"Salih","year":"2014","journal-title":"Am. J. Physiol. Renal. Physiol."},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1016\/j.ymeth.2015.02.019","article-title":"Methods of Isolating Extracellular Vesicles Impact Down-Stream Analyses of Their Cargoes","volume":"87","author":"Taylor","year":"2015","journal-title":"Methods"},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1007\/978-1-61779-068-3_15","article-title":"Exosome Isolation for Proteomic Analyses and RNA Profiling","volume":"728","author":"Taylor","year":"2011","journal-title":"Methods Mol. Biol."},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"33641","DOI":"10.1038\/srep33641","article-title":"Size-Exclusion Chromatography-Based Isolation Minimally Alters Extracellular Vesicles\u2019 Characteristics Compared to Precipitating Agents","volume":"6","author":"Beyer","year":"2016","journal-title":"Sci. Rep."},{"key":"ref_138","doi-asserted-by":"crossref","unstructured":"Karttunen, J., Heiskanen, M., Navarro-Ferrandis, V., Das Gupta, S., Lipponen, A., Puhakka, N., Rilla, K., Koistinen, A., and Pitk\u00e4nen, A. (2018). Precipitation-Based Extracellular Vesicle Isolation from Rat Plasma Co-Precipitate Vesicle-Free MicroRNAs. J. Extracell. Vesicles, 8.","DOI":"10.1080\/20013078.2018.1555410"},{"key":"ref_139","doi-asserted-by":"crossref","unstructured":"Bickmore, D.C., and Miklavcic, J.J. (2020). Characterization of Extracellular Vesicles Isolated From Human Milk Using a Precipitation-Based Method. Front. Nutr., 7.","DOI":"10.3389\/fnut.2020.00022"},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"3773","DOI":"10.1039\/C4LC00662C","article-title":"Integrated Immunoisolation and Protein Analysis of Circulating Exosomes Using Microfluidic Technology","volume":"14","author":"He","year":"2014","journal-title":"Lab. Chip."},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"1891","DOI":"10.1039\/C4LC00136B","article-title":"Microfluidic Device (ExoChip) for on-Chip Isolation, Quantification and Characterization of Circulating Exosomes","volume":"14","author":"Kanwar","year":"2014","journal-title":"Lab. Chip."},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1007\/978-1-4939-2550-6_15","article-title":"A Protocol for Exosome Isolation and Characterization: Evaluation of Ultracentrifugation, Density-Gradient Separation, and Immunoaffinity Capture Methods","volume":"1295","author":"Greening","year":"2015","journal-title":"Methods Mol. Biol."},{"key":"ref_143","doi-asserted-by":"crossref","first-page":"465","DOI":"10.1007\/978-1-4939-1538-5_27","article-title":"Magnetic Bead-Based Isolation of Exosomes","volume":"1218","author":"Oksvold","year":"2015","journal-title":"Methods Mol. Biol."},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"1217","DOI":"10.2217\/nnm-2017-0016","article-title":"Urinary Nanovesicles Captured by Lectins or Antibodies Demonstrate Variations in Size and Surface Glycosylation Profile","volume":"12","author":"Gerlach","year":"2017","journal-title":"Nanomedicine (Lond.)"},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"1621","DOI":"10.1002\/cbic.201402058","article-title":"Microarray-Based Identification of Lectins for the Purification of Human Urinary Extracellular Vesicles Directly from Urine Samples","volume":"15","author":"Echevarria","year":"2014","journal-title":"Chembiochem"},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"4","DOI":"10.5772\/62579","article-title":"Protein Complexes in Urine Interfere with Extracellular Vesicle Biomarker Studies","volume":"5","author":"Wachalska","year":"2016","journal-title":"J. Circ. Biomark."},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1016\/j.ab.2019.06.001","article-title":"Application of High-Mannose-Type Glycan-Specific Lectin from Oscillatoria Agardhii for Affinity Isolation of Tumor-Derived Extracellular Vesicles","volume":"580","author":"Yamamoto","year":"2019","journal-title":"Anal. Biochem."},{"key":"ref_148","doi-asserted-by":"crossref","first-page":"10038","DOI":"10.1038\/s41598-019-46395-2","article-title":"A Nanoparticle-Based Approach for the Detection of Extracellular Vesicles","volume":"9","author":"Islam","year":"2019","journal-title":"Sci. Rep."},{"key":"ref_149","doi-asserted-by":"crossref","unstructured":"Herrero, C., de la Fuente, A., Casas-Arozamena, C., Sebastian, V., Prieto, M., Arruebo, M., Abalo, A., Col\u00e1s, E., Moreno-Bueno, G., and Gil-Moreno, A. (2019). Extracellular Vesicles-Based Biomarkers Represent a Promising Liquid Biopsy in Endometrial Cancer. Cancers (Basel), 11.","DOI":"10.3390\/cancers11122000"},{"key":"ref_150","doi-asserted-by":"crossref","first-page":"1531","DOI":"10.1039\/C8NR03900C","article-title":"Modification of the Glycosylation of Extracellular Vesicles Alters Their Biodistribution in Mice","volume":"11","author":"Royo","year":"2019","journal-title":"Nanoscale"},{"key":"ref_151","doi-asserted-by":"crossref","first-page":"14339","DOI":"10.1039\/C9CC06742F","article-title":"Reverse Capture for Selectively and Sensitively Revealing the N-Glycome of Serum Exosomes","volume":"55","author":"Lv","year":"2019","journal-title":"Chem. Commun. (Camb.)"},{"key":"ref_152","doi-asserted-by":"crossref","unstructured":"Escrevente, C., Keller, S., Altevogt, P., and Costa, J. (2011). Interaction and Uptake of Exosomes by Ovarian Cancer Cells. BMC Cancer, 11.","DOI":"10.1186\/1471-2407-11-108"},{"key":"ref_153","doi-asserted-by":"crossref","unstructured":"Horrevorts, S.K., Stolk, D.A., van de Ven, R., Hulst, M., van Het Hof, B., Duinkerken, S., Heineke, M.H., Ma, W., Dusoswa, S.A., and Nieuwland, R. (2019). Glycan-Modified Apoptotic Melanoma-Derived Extracellular Vesicles as Antigen Source for Anti-Tumor Vaccination. Cancers (Basel), 11.","DOI":"10.3390\/cancers11091266"},{"key":"ref_154","first-page":"201","article-title":"Proteomic Analysis Reveals Aberrant O-GlcNAcylation of Extracellular Proteins from Breast Cancer Cell Secretion","volume":"12","author":"Netsirisawan","year":"2015","journal-title":"Cancer Genom. Proteom."},{"key":"ref_155","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1038\/nature14581","article-title":"Glypican-1 Identifies Cancer Exosomes and Detects Early Pancreatic Cancer","volume":"523","author":"Melo","year":"2015","journal-title":"Nature"},{"key":"ref_156","doi-asserted-by":"crossref","first-page":"1435138","DOI":"10.1080\/20013078.2018.1435138","article-title":"Immunoaffinity-Based Isolation of Melanoma Cell-Derived Exosomes from Plasma of Patients with Melanoma","volume":"7","author":"Sharma","year":"2018","journal-title":"J. Extracell. Vesicles"},{"key":"ref_157","doi-asserted-by":"crossref","unstructured":"Mulcahy, L.A., Pink, R.C., and Carter, D.R.F. (2014). Routes and Mechanisms of Extracellular Vesicle Uptake. J. Extracell. Vesicles, 3.","DOI":"10.3402\/jev.v3.24641"},{"key":"ref_158","doi-asserted-by":"crossref","first-page":"353","DOI":"10.1007\/s00281-012-0310-3","article-title":"Sialoadhesin in Recognition of Self and Non-Self","volume":"34","author":"Klaas","year":"2012","journal-title":"Semin. Immunopathol."},{"key":"ref_159","doi-asserted-by":"crossref","first-page":"208","DOI":"10.1182\/blood-2013-03-489732","article-title":"CD169 Mediates the Capture of Exosomes in Spleen and Lymph Node","volume":"123","author":"Saunderson","year":"2014","journal-title":"Blood"},{"key":"ref_160","doi-asserted-by":"crossref","unstructured":"Ko, S.Y., and Naora, H. (2020). Extracellular Vesicle Membrane-Associated Proteins: Emerging Roles in Tumor Angiogenesis and Anti-Angiogenesis Therapy Resistance. Int. J. Mol. Sci., 21.","DOI":"10.3390\/ijms21155418"},{"key":"ref_161","doi-asserted-by":"crossref","first-page":"32526","DOI":"10.1074\/jbc.M114.606269","article-title":"Complex N-Linked Glycans Serve as a Determinant for Exosome\/Microvesicle Cargo Recruitment","volume":"289","author":"Liang","year":"2014","journal-title":"J. Biol. Chem."},{"key":"ref_162","doi-asserted-by":"crossref","first-page":"2195","DOI":"10.1021\/acs.jproteome.9b00578","article-title":"Impact of Increased FUT8 Expression on the Extracellular Vesicle Proteome in Prostate Cancer Cells","volume":"19","author":"Clark","year":"2020","journal-title":"J. Proteome Res."},{"key":"ref_163","doi-asserted-by":"crossref","first-page":"514","DOI":"10.1016\/j.bbrc.2019.10.149","article-title":"Disruption of Core 1-Mediated O-Glycosylation Oppositely Regulates CD44 Expression in Human Colon Cancer Cells and Tumor-Derived Exosomes","volume":"521","author":"Gao","year":"2020","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_164","doi-asserted-by":"crossref","first-page":"669","DOI":"10.1023\/A:1011077000164","article-title":"The Sialyl-Alpha2,6-Lactosaminyl-Structure: Biosynthesis and Functional Role","volume":"17","year":"2000","journal-title":"Glycoconj. J."},{"key":"ref_165","doi-asserted-by":"crossref","first-page":"1089","DOI":"10.1093\/carcin\/bgw091","article-title":"Silencing of ST6Gal I Enhances Colorectal Cancer Metastasis by Down-Regulating KAI1 via Exosome-Mediated Exportation and Thereby Rescues Integrin Signaling","volume":"37","author":"Jung","year":"2016","journal-title":"Carcinogenesis"},{"key":"ref_166","doi-asserted-by":"crossref","first-page":"40","DOI":"10.1038\/nrc2543","article-title":"Tetraspanins: Push and Pull in Suppressing and Promoting Metastasis","volume":"9","year":"2009","journal-title":"Nat. Rev. Cancer"},{"key":"ref_167","doi-asserted-by":"crossref","first-page":"426","DOI":"10.3389\/fphar.2018.00426","article-title":"N-Glycosylation of Lipocalin 2 Is Not Required for Secretion or Exosome Targeting","volume":"9","author":"Meurer","year":"2018","journal-title":"Front. Pharmacol."},{"key":"ref_168","doi-asserted-by":"crossref","first-page":"27066","DOI":"10.3402\/jev.v4.27066","article-title":"Biological Properties of Extracellular Vesicles and Their Physiological Functions","volume":"4","author":"Siljander","year":"2015","journal-title":"J. Extracell. Vesicles"},{"key":"ref_169","doi-asserted-by":"crossref","first-page":"617","DOI":"10.1038\/s41571-018-0036-9","article-title":"Extracellular Vesicles in Cancer\u2014Implications for Future Improvements in Cancer Care","volume":"15","author":"Xu","year":"2018","journal-title":"Nat. Rev. Clin. Oncol."},{"key":"ref_170","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1093\/jmcb\/mju047","article-title":"Tumor-Derived Microvesicles Mediate Human Breast Cancer Invasion through Differentially Glycosylated EMMPRIN","volume":"7","author":"Menck","year":"2015","journal-title":"J. Mol. Cell. Biol."},{"key":"ref_171","doi-asserted-by":"crossref","first-page":"6467","DOI":"10.7150\/thno.43865","article-title":"MGAT3-Mediated Glycosylation of Tetraspanin CD82 at Asparagine 157 Suppresses Ovarian Cancer Metastasis by Inhibiting the Integrin Signaling Pathway","volume":"10","author":"Li","year":"2020","journal-title":"Theranostics"},{"key":"ref_172","doi-asserted-by":"crossref","first-page":"940","DOI":"10.1016\/j.celrep.2019.01.009","article-title":"Transfer of Functional Cargo in Exomeres","volume":"27","author":"Zhang","year":"2019","journal-title":"Cell Rep."},{"key":"ref_173","doi-asserted-by":"crossref","first-page":"1282","DOI":"10.1038\/ncomms2282","article-title":"Delivery of Chemotherapeutic Drugs in Tumour Cell-Derived Microparticles","volume":"3","author":"Tang","year":"2012","journal-title":"Nat. Commun."},{"key":"ref_174","doi-asserted-by":"crossref","first-page":"1606","DOI":"10.1038\/mt.2010.105","article-title":"A Novel Nanoparticle Drug Delivery System: The Anti-Inflammatory Activity of Curcumin Is Enhanced When Encapsulated in Exosomes","volume":"18","author":"Sun","year":"2010","journal-title":"Mol. Ther."},{"key":"ref_175","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1021\/acsnano.6b07607","article-title":"Re-Engineering Extracellular Vesicles as Smart Nanoscale Therapeutics","volume":"11","author":"Armstrong","year":"2017","journal-title":"ACS Nano"},{"key":"ref_176","doi-asserted-by":"crossref","unstructured":"Villata, S., Canta, M., and Cauda, V. (2020). EVs and Bioengineering: From Cellular Products to Engineered Nanomachines. Int. J. Mol. Sci., 21.","DOI":"10.3390\/ijms21176048"},{"key":"ref_177","doi-asserted-by":"crossref","first-page":"231","DOI":"10.1016\/j.biomaterials.2015.09.031","article-title":"Plasma Membrane Vesicles Decorated with Glycolipid-Anchored Antigens and Adjuvants via Protein Transfer as an Antigen Delivery Platform for Inhibition of Tumor Growth","volume":"74","author":"Patel","year":"2016","journal-title":"Biomaterials"},{"key":"ref_178","doi-asserted-by":"crossref","first-page":"31053","DOI":"10.3402\/jev.v5.31053","article-title":"Display of GPI-Anchored Anti-EGFR Nanobodies on Extracellular Vesicles Promotes Tumour Cell Targeting","volume":"5","author":"Kooijmans","year":"2016","journal-title":"J. Extracell. Vesicles"},{"key":"ref_179","doi-asserted-by":"crossref","first-page":"2264","DOI":"10.1016\/j.vaccine.2005.11.045","article-title":"Human Tumor Membrane Vesicles Modified to Express Glycolipid-Anchored IL-12 by Protein Transfer Induce T Cell Proliferation in Vitro: A Potential Approach for Local Delivery of Cytokines during Vaccination","volume":"24","author":"Nagarajan","year":"2006","journal-title":"Vaccine"},{"key":"ref_180","doi-asserted-by":"crossref","first-page":"1091","DOI":"10.1016\/j.bbagen.2018.02.001","article-title":"Facile Metabolic Glycan Labeling Strategy for Exosome Tracking","volume":"1862","author":"Lee","year":"2018","journal-title":"Biochim. Biophys. Acta. Gen. Subj."},{"key":"ref_181","doi-asserted-by":"crossref","first-page":"195","DOI":"10.3389\/fonc.2014.00195","article-title":"The Role of Heparanase and Sulfatases in the Modification of Heparan Sulfate Proteoglycans within the Tumor Microenvironment and Opportunities for Novel Cancer Therapeutics","volume":"4","author":"Hammond","year":"2014","journal-title":"Front. Oncol."},{"key":"ref_182","doi-asserted-by":"crossref","first-page":"343","DOI":"10.1007\/s11060-013-1235-y","article-title":"Heparin Blocks Transfer of Extracellular Vesicles between Donor and Recipient Cells","volume":"115","author":"Atai","year":"2013","journal-title":"J. Neurooncol."},{"key":"ref_183","doi-asserted-by":"crossref","unstructured":"Sento, S., Sasabe, E., and Yamamoto, T. (2016). Application of a Persistent Heparin Treatment Inhibits the Malignant Potential of Oral Squamous Carcinoma Cells Induced by Tumor Cell-Derived Exosomes. PLoS ONE, 11.","DOI":"10.1371\/journal.pone.0148454"},{"key":"ref_184","doi-asserted-by":"crossref","first-page":"635","DOI":"10.1038\/bjc.2011.11","article-title":"PG545, a Dual Heparanase and Angiogenesis Inhibitor, Induces Potent Anti-Tumour and Anti-Metastatic Efficacy in Preclinical Models","volume":"104","author":"Dredge","year":"2011","journal-title":"Br. J. Cancer"},{"key":"ref_185","doi-asserted-by":"crossref","unstructured":"Zhou, H., Roy, S., Cochran, E., Zouaoui, R., Chu, C.L., Duffner, J., Zhao, G., Smith, S., Galcheva-Gargova, Z., and Karlgren, J. (2011). M402, a Novel Heparan Sulfate Mimetic, Targets Multiple Pathways Implicated in Tumor Progression and Metastasis. PLoS ONE, 6.","DOI":"10.1371\/journal.pone.0021106"},{"key":"ref_186","doi-asserted-by":"crossref","first-page":"1382","DOI":"10.1158\/1078-0432.CCR-10-2476","article-title":"SST0001, a Chemically Modified Heparin, Inhibits Myeloma Growth and Angiogenesis via Disruption of the Heparanase\/Syndecan-1 Axis","volume":"17","author":"Ritchie","year":"2011","journal-title":"Clin. Cancer Res."},{"key":"ref_187","doi-asserted-by":"crossref","first-page":"5471","DOI":"10.1158\/1078-0432.CCR-05-2423","article-title":"A Phase I Biological and Pharmacologic Study of the Heparanase Inhibitor PI-88 in Patients with Advanced Solid Tumors","volume":"12","author":"Basche","year":"2006","journal-title":"Clin. Cancer Res."},{"key":"ref_188","doi-asserted-by":"crossref","first-page":"958","DOI":"10.1016\/j.jhep.2008.12.023","article-title":"Heparanase Inhibitor PI-88 as Adjuvant Therapy for Hepatocellular Carcinoma after Curative Resection: A Randomized Phase II Trial for Safety and Optimal Dosage","volume":"50","author":"Liu","year":"2009","journal-title":"J. Hepatol."},{"key":"ref_189","doi-asserted-by":"crossref","first-page":"12103","DOI":"10.1074\/jbc.M414217200","article-title":"Modulation of the Heparanase-Inhibiting Activity of Heparin through Selective Desulfation, Graded N-Acetylation, and Glycol Splitting","volume":"280","author":"Naggi","year":"2005","journal-title":"J. Biol. Chem."},{"key":"ref_190","doi-asserted-by":"crossref","first-page":"640","DOI":"10.1093\/glycob\/cww003","article-title":"Kinetic Analysis and Molecular Modeling of the Inhibition Mechanism of Roneparstat (SST0001) on Human Heparanase","volume":"26","author":"Pala","year":"2016","journal-title":"Glycobiology"},{"key":"ref_191","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1016\/j.neo.2014.11.007","article-title":"Heparanase Mediates a Novel Mechanism in Lapatinib-Resistant Brain Metastatic Breast Cancer","volume":"17","author":"Zhang","year":"2015","journal-title":"Neoplasia"},{"key":"ref_192","doi-asserted-by":"crossref","first-page":"1648995","DOI":"10.1080\/20013078.2019.1648995","article-title":"Glycan Modification of Glioblastoma-Derived Extracellular Vesicles Enhances Receptor-Mediated Targeting of Dendritic Cells","volume":"8","author":"Dusoswa","year":"2019","journal-title":"J. Extracell. Vesicles"},{"key":"ref_193","doi-asserted-by":"crossref","first-page":"134","DOI":"10.1186\/1479-5876-10-134","article-title":"Exosome Removal as a Therapeutic Adjuvant in Cancer","volume":"10","author":"Marleau","year":"2012","journal-title":"J. Transl. Med."},{"key":"ref_194","doi-asserted-by":"crossref","first-page":"64","DOI":"10.1159\/000167011","article-title":"Reduction of Hepatitis C Virus Using Lectin Affinity Plasmapheresis in Dialysis Patients","volume":"27","author":"Tullis","year":"2009","journal-title":"Blood Purif."},{"key":"ref_195","doi-asserted-by":"crossref","unstructured":"Samuel, P., Fabbri, M., and Carter, D.R.F. (2017). Mechanisms of Drug Resistance in Cancer: The Role of Extracellular Vesicles. Proteomics, 17.","DOI":"10.1002\/pmic.201600375"},{"key":"ref_196","doi-asserted-by":"crossref","first-page":"10952","DOI":"10.1158\/0008-5472.CAN-05-2021","article-title":"Novel Extracellular Vesicles Mediate an ABCG2-Dependent Anticancer Drug Sequestration and Resistance","volume":"65","author":"Ifergan","year":"2005","journal-title":"Cancer Res."},{"key":"ref_197","first-page":"4331","article-title":"Expulsion of Small Molecules in Vesicles Shed by Cancer Cells: Association with Gene Expression and Chemosensitivity Profiles","volume":"63","author":"Shedden","year":"2003","journal-title":"Cancer Res."},{"key":"ref_198","doi-asserted-by":"crossref","first-page":"50365","DOI":"10.18632\/oncotarget.10395","article-title":"Microvesicle Removal of Anticancer Drugs Contributes to Drug Resistance in Human Pancreatic Cancer Cells","volume":"7","author":"Kohan","year":"2016","journal-title":"Oncotarget"},{"key":"ref_199","doi-asserted-by":"crossref","unstructured":"Corcoran, C., Rani, S., O\u2019Brien, K., O\u2019Neill, A., Prencipe, M., Sheikh, R., Webb, G., McDermott, R., Watson, W., and Crown, J. (2012). Docetaxel-Resistance in Prostate Cancer: Evaluating Associated Phenotypic Changes and Potential for Resistance Transfer via Exosomes. PLoS ONE, 7.","DOI":"10.1371\/journal.pone.0050999"},{"key":"ref_200","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1016\/j.ejphar.2014.05.026","article-title":"Microvesicles Mediate Transfer of P-Glycoprotein to Paclitaxel-Sensitive A2780 Human Ovarian Cancer Cells, Conferring Paclitaxel-Resistance","volume":"738","author":"Zhang","year":"2014","journal-title":"Eur. J. Pharmacol."},{"key":"ref_201","doi-asserted-by":"crossref","first-page":"1643","DOI":"10.1038\/leu.2009.76","article-title":"Membrane Microparticles Mediate Transfer of P-Glycoprotein to Drug Sensitive Cancer Cells","volume":"23","author":"Bebawy","year":"2009","journal-title":"Leukemia"},{"key":"ref_202","doi-asserted-by":"crossref","first-page":"10773","DOI":"10.1007\/s13277-014-2377-z","article-title":"Exosomes Mediate Drug Resistance Transfer in MCF-7 Breast Cancer Cells and a Probable Mechanism Is Delivery of P-Glycoprotein","volume":"35","author":"Lv","year":"2014","journal-title":"Tumour Biol."},{"key":"ref_203","doi-asserted-by":"crossref","first-page":"3227","DOI":"10.1007\/s13277-015-4161-0","article-title":"Exosomes from Adriamycin-Resistant Breast Cancer Cells Transmit Drug Resistance Partly by Delivering MiR-222","volume":"37","author":"Yu","year":"2016","journal-title":"Tumour Biol."},{"key":"ref_204","doi-asserted-by":"crossref","first-page":"42339","DOI":"10.1038\/srep42339","article-title":"MicroRNA-155 Controls Exosome Synthesis and Promotes Gemcitabine Resistance in Pancreatic Ductal Adenocarcinoma","volume":"7","author":"Mikamori","year":"2017","journal-title":"Sci. Rep."},{"key":"ref_205","doi-asserted-by":"crossref","first-page":"1228","DOI":"10.1111\/jcmm.13056","article-title":"Circulating Exosomal MicroRNA-96 Promotes Cell Proliferation, Migration and Drug Resistance by Targeting LMO7","volume":"21","author":"Wu","year":"2017","journal-title":"J. Cell. Mol. Med."},{"key":"ref_206","doi-asserted-by":"crossref","unstructured":"Mittal, S., Gupta, P., Chaluvally-Raghavan, P., and Pradeep, S. (2020). Emerging Role of Extracellular Vesicles in Immune Regulation and Cancer Progression. Cancers (Basel), 12.","DOI":"10.3390\/cancers12123563"},{"key":"ref_207","doi-asserted-by":"crossref","unstructured":"Xie, F., Zhou, X., Fang, M., Li, H., Su, P., Tu, Y., Zhang, L., and Zhou, F. (2019). Extracellular Vesicles in Cancer Immune Microenvironment and Cancer Immunotherapy. Adv. Sci. (Weinh), 6.","DOI":"10.1002\/advs.201901779"},{"key":"ref_208","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1016\/j.bbcan.2017.03.007","article-title":"Glycoconjugates from Extracellular Vesicles: Structures, Functions and Emerging Potential as Cancer Biomarkers","volume":"1868","author":"Costa","year":"2017","journal-title":"Biochim. Biophys. Acta Rev. Cancer"},{"key":"ref_209","doi-asserted-by":"crossref","first-page":"322","DOI":"10.1136\/jcp.2009.071035","article-title":"Alterations in Glycosylation as Biomarkers for Cancer Detection","volume":"63","author":"Reis","year":"2010","journal-title":"J. Clin. Pathol."},{"key":"ref_210","doi-asserted-by":"crossref","first-page":"6445","DOI":"10.7150\/jca.48531","article-title":"Exosomal CA125 as A Promising Biomarker for Ovarian Cancer Diagnosis","volume":"11","author":"Chen","year":"2020","journal-title":"J. Cancer"},{"key":"ref_211","doi-asserted-by":"crossref","unstructured":"Yokose, T., Kabe, Y., Matsuda, A., Kitago, M., Matsuda, S., Hirai, M., Nakagawa, T., Masugi, Y., Hishiki, T., and Nakamura, Y. (2020). O-Glycan-Altered Extracellular Vesicles: A Specific Serum Marker Elevated in Pancreatic Cancer. Cancers (Basel), 12.","DOI":"10.3390\/cancers12092469"},{"key":"ref_212","doi-asserted-by":"crossref","first-page":"150","DOI":"10.1186\/s12951-020-00701-7","article-title":"Isolation of Exosomes from Whole Blood by a New Microfluidic Device: Proof of Concept Application in the Diagnosis and Monitoring of Pancreatic Cancer","volume":"18","author":"Mendoza","year":"2020","journal-title":"J. Nanobiotechnol."},{"key":"ref_213","doi-asserted-by":"crossref","first-page":"198","DOI":"10.1007\/s00795-019-00218-5","article-title":"Glycosylation of Ascites-Derived Exosomal CD133: A Potential Prognostic Biomarker in Patients with Advanced Pancreatic Cancer","volume":"52","author":"Sakaue","year":"2019","journal-title":"Med. Mol. Morphol."},{"key":"ref_214","doi-asserted-by":"crossref","first-page":"1302","DOI":"10.1016\/j.bbalip.2013.04.011","article-title":"Molecular Lipidomics of Exosomes Released by PC-3 Prostate Cancer Cells","volume":"1831","author":"Llorente","year":"2013","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_215","doi-asserted-by":"crossref","first-page":"1044","DOI":"10.1016\/j.cell.2020.07.009","article-title":"Extracellular Vesicle and Particle Biomarkers Define Multiple Human Cancers","volume":"182","author":"Hoshino","year":"2020","journal-title":"Cell"},{"key":"ref_216","doi-asserted-by":"crossref","first-page":"1340745","DOI":"10.1080\/20013078.2017.1340745","article-title":"Characterisation of Tumour-Derived Microvesicles in Cancer Patients\u2019 Blood and Correlation with Clinical Outcome","volume":"6","author":"Menck","year":"2017","journal-title":"J. Extracell. Vesicles"},{"key":"ref_217","doi-asserted-by":"crossref","unstructured":"Walker, S.A., Aguilar D\u00edaz De Le\u00f3n, J.S., Busatto, S., Wurtz, G.A., Zubair, A.C., Borges, C.R., and Wolfram, J. (2020). Glycan Node Analysis of Plasma-Derived Extracellular Vesicles. Cells, 9.","DOI":"10.3390\/cells9091946"},{"key":"ref_218","doi-asserted-by":"crossref","first-page":"150","DOI":"10.1016\/j.matt.2019.10.018","article-title":"Dual-Selective Magnetic Analysis of Extracellular Vesicle Glycans","volume":"2","author":"Wang","year":"2020","journal-title":"Matter"},{"key":"ref_219","doi-asserted-by":"crossref","first-page":"1676","DOI":"10.1016\/j.bbagen.2016.03.003","article-title":"Methods for the Absolute Quantification of N-Glycan Biomarkers","volume":"1860","author":"Etxebarria","year":"2016","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_220","doi-asserted-by":"crossref","first-page":"201","DOI":"10.1093\/glycob\/cwn099","article-title":"Identification and Quantification of N-Linked Oligosaccharides Released from Glycoproteins: An Inter-Laboratory Study","volume":"19","author":"Thobhani","year":"2009","journal-title":"Glycobiology"},{"key":"ref_221","doi-asserted-by":"crossref","unstructured":"Schjoldager, K.T., Narimatsu, Y., Joshi, H.J., and Clausen, H. (2020). Global View of Human Protein Glycosylation Pathways and Functions. Nat. Rev. Mol. Cell. Biol.","DOI":"10.1038\/s41580-020-00294-x"},{"key":"ref_222","doi-asserted-by":"crossref","first-page":"1809766","DOI":"10.1080\/20013078.2020.1809766","article-title":"The Future of Extracellular Vesicles as Theranostics\u2014An ISEV Meeting Report","volume":"9","author":"Soekmadji","year":"2020","journal-title":"J. Extracell. 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