REFERENCES
1. Jeppesen DK, Zhang Q, Franklin JL, Coffey RJ. Extracellular vesicles and nanoparticles: emerging complexities. Trends Cell Biol ;2023:S0962-8924(23)00005.
2. Jeppesen DK, Fenix AM, Franklin JL, et al. Reassessment of exosome composition. Cell 2019;177:428-445.e18.
3. Niel G, D'Angelo G, Raposo G. Shedding light on the cell biology of extracellular vesicles. Nat Rev Mol Cell Biol 2018;19:213-28.
4. Mathivanan S, Ji H, Simpson RJ. Exosomes: extracellular organelles important in intercellular communication. J Proteomics 2010;73:1907-20.
5. Kharaziha P, Ceder S, Li Q, Panaretakis T. Tumor cell-derived exosomes: a message in a bottle. Biochim Biophys Acta 2012;1826:103-11.
6. Valadi H, Ekström K, Bossios A, Sjöstrand M, Lee JJ, Lötvall JO. Exosome-mediated transfer of mRNAs and microRNAs is a novel mechanism of genetic exchange between cells. Nat Cell Biol 2007;9:654-9.
7. Тамкович СН, Тутанов ОС, Лактионов ПП, Tamkovich SN, Tutanov OS, Laktionov PP. Экзосомы: механизмы возникновения, состав, транспорт, биологическая активность, использование в диагностике. Биол мембраны 2016;33:163-75.
8. Glass SE, Coffey RJ. Recent advances in the study of extracellular vesicles in colorectal cancer. Gastroenterology 2022;163:1188-97.
9. Cocucci E, Meldolesi J. Ectosomes and exosomes: shedding the confusion between extracellular vesicles. Trends Cell Biol 2015;25:364-72.
10. Sun H, Burrola S, Wu J, Ding WQ. Extracellular vesicles in the development of cancer therapeutics. Int J Mol Sci 2020;21:6097.
11. Zhang H, Freitas D, Kim HS, et al. Identification of distinct nanoparticles and subsets of extracellular vesicles by asymmetric flow field-flow fractionation. Nat Cell Biol 2018;20:332-43.
12. Zhang Q, Higginbotham JN, Jeppesen DK, et al. Transfer of functional cargo in exomeres. Cell Rep 2019;27:940-954.e6.
13. Zhang Q, Jeppesen DK, Higginbotham JN, et al. Supermeres are functional extracellular nanoparticles replete with disease biomarkers and therapeutic targets. Nat Cell Biol 2021;23:1240-54.
14. Tosar JP, Cayota A, Witwer K. Exomeres and supermeres: monolithic or diverse? J Extracell Biol 2022;1:e45.
15. Zhang Q, Jeppesen DK, Higginbotham JN, Franklin JL, Coffey RJ. Comprehensive isolation of extracellular vesicles and nanoparticles. Nat Protoc ;2023:1462-87.
16. Vidal M. Exosomes and GPI-anchored proteins: judicious pairs for investigating biomarkers from body fluids. Adv Drug Deliv Rev 2020;161-162:110-23.
17. Sangiorgio V, Pitto M, Palestini P, Masserini M. GPI-anchored proteins and lipid rafts. Ital J Biochem :53, 98-111.
18. Dolezal S, Hester S, Kirby PS, Nairn A, Pierce M, Abbott KL. Elevated levels of glycosylphosphatidylinositol (GPI) anchored proteins in plasma from human cancers detected by C. septicum alpha toxin. Cancer Biomark 2014;14:55-62.
19. Wang M, Jia J, Cui Y, Peng Y, Jiang Y. CD73-positive extracellular vesicles promote glioblastoma immunosuppression by inhibiting T-cell clonal expansion. Cell Death Dis 2021;12:1065.
20. Igami K, Uchiumi T, Shiota M, et al. Extracellular vesicles expressing CEACAM proteins in the urine of bladder cancer patients. Cancer Sci 2022;113:3120-33.
21. Hussein NH, Amin NS, El Tayebi HM. GPI-AP: unraveling a new class of malignancy mediators and potential immunotherapy targets. Front Oncol 2020;10:537311.
22. Kooijmans SA, Aleza CG, Roffler SR, van Solinge WW, Vader P, Schiffelers RM. Display of GPI-anchored anti-EGFR nanobodies on extracellular vesicles promotes tumour cell targeting. J Extracell Vesicles 2016;5:31053.
23. Choi H, Choi Y, Yim HY, Mirzaaghasi A, Yoo JK, Choi C. Biodistribution of exosomes and engineering strategies for targeted delivery of therapeutic exosomes. Tissue Eng Regen Med 2021;18:499-511.
24. Brewis IA, Ferguson MA, Mehlert A, Turner AJ, Hooper NM. Structures of the glycosyl-phosphatidylinositol anchors of porcine and human renal membrane dipeptidase. comprehensive structural studies on the porcine anchor and interspecies comparison of the glycan core structures. J Biol Chem 1995;270:22946-56.
25. Kinoshita T. Glycosylphosphatidylinositol (GPI) anchors: biochemistry and cell biology: introduction to a thematic review series. J Lipid Res 2016;57:4-5.
26. Kinoshita T, Fujita M. Biosynthesis of GPI-anchored proteins: special emphasis on GPI lipid remodeling. J Lipid Res 2016;57:6-24.
27. Homans SW, Ferguson MA, Dwek RA, Rademacher TW, Anand R, Williams AF. Complete structure of the glycosyl phosphatidylinositol membrane anchor of rat brain Thy-1 glycoprotein. Nature 1988;333:269-72.
28. Ferguson MA, Homans SW, Dwek RA, Rademacher TW. Glycosyl-phosphatidylinositol moiety that anchors trypanosoma brucei variant surface glycoprotein to the membrane. Science 1988;239:753-9.
29. Fankhauser, C, et al. J Biol Chem 1993. pp. 26365-74. Structures of glycosylphosphatidylinositol membrane anchors from Saccharomyces cerevisiae.
30. Available from: https://www.uniprot.org/uniprotkb?facets=reviewed%3Atrue%2Cmodel_organism%3A9606&query=%28cc_scl_term%3ASL-9902%29 [Last accessed on 11 May 2023].
31. Kalra H, Simpson RJ, Ji H, et al. Vesiclepedia: a compendium for extracellular vesicles with continuous community annotation. PLoS Biol 2012;10:e1001450.
32. Fujihara Y, Ikawa M. GPI-AP release in cellular, developmental, and reproductive biology. J Lipid Res 2016;57:538-45.
33. Saha S, Anilkumar AA, Mayor S. GPI-anchored protein organization and dynamics at the cell surface. J Lipid Res 2016;57:159-75.
34. Brown DA, Rose JK. Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface. Cell 1992;68:533-44.
38. Muñiz M, Riezman H. Trafficking of glycosylphosphatidylinositol anchored proteins from the endoplasmic reticulum to the cell surface. J Lipid Res 2016;57:352-60.
40. Huang K, Park S. Affinity purification of glycosylphosphatidylinositol-anchored proteins by alpha-toxin. methods mol biol 2022;2303:251-7.
41. Fujita M, Kinoshita T. GPI-anchor remodeling: potential functions of GPI-anchors in intracellular trafficking and membrane dynamics. Biochim Biophys Acta 2012;1821:1050-8.
42. Nagpal JK, Dasgupta S, Jadallah S, et al. Profiling the expression pattern of GPI transamidase complex subunits in human cancer. Mod Pathol 2008;21:979-91.
43. Sahu PK, Tomar RS. The natural anticancer agent cantharidin alters GPI-anchored protein sorting by targeting Cdc1-mediated remodeling in endoplasmic reticulum. J Biol Chem 2019;294:3837-52.
44. Kinoshita T. Biosynthesis and biology of mammalian GPI-anchored proteins. Open Biol 2020;10:190290.
45. Galian C, Björkholm P, Bulleid N, von Heijne G. Efficient glycosylphosphatidylinositol (GPI) modification of membrane proteins requires a C-terminal anchoring signal of marginal hydrophobicity. J Biol Chem 2012;287:16399-409.
46. Howell S, Lanctôt C, Boileau G, Crine P. A cleavable N-terminal signal peptide is not a prerequisite for the biosynthesis of glycosylphosphatidylinositol-anchored proteins. J Biol Chem 1994;269:16993-6.
47. Barlowe CK, Miller EA. Secretory protein biogenesis and traffic in the early secretory pathway. Genetics 2013;193:383-410.
48. Rivier AS, Castillon GA, Michon L, et al. Exit of GPI-anchored proteins from the ER differs in yeast and mammalian cells. Traffic 2010;11:1017-33.
49. Fujita M, Watanabe R, Jaensch N, et al. Sorting of GPI-anchored proteins into ER exit sites by p24 proteins is dependent on remodeled GPI. J Cell Biol 2011;194:61-75.
50. Castillon GA, Aguilera-Romero A, Manzano-Lopez J, et al. The yeast p24 complex regulates GPI-anchored protein transport and quality control by monitoring anchor remodeling. Mol Biol Cell 2011;22:2924-36.
51. Surma MA, Klose C, Simons K. Lipid-dependent protein sorting at the trans-Golgi network. Biochim Biophys Acta 2012;1821:1059-67.
52. Maeda Y, Tashima Y, Houjou T, et al. Fatty acid remodeling of GPI-anchored proteins is required for their raft association. Mol Biol Cell 2007;18:1497-506.
53. Tashima Y, Taguchi R, Murata C, et al. PGAP2 is essential for correct processing and stable expression of GPI-anchored proteins. Mol Biol Cell 2006;17:1410-20.
54. Keller P, Toomre D, Díaz E, White J, Simons K. Multicolour imaging of post-Golgi sorting and trafficking in live cells. Nat Cell Biol 2001;3:140-9.
55. Hua W, Sheff D, Toomre D, Mellman I. Vectorial insertion of apical and basolateral membrane proteins in polarized epithelial cells revealed by quantitative 3D live cell imaging. J Cell Biol 2006;172:1035-44.
56. Paladino S, Pocard T, Catino MA, Zurzolo C. GPI-anchored proteins are directly targeted to the apical surface in fully polarized MDCK cells. J Cell Biol 2006;172:1023-34.
57. Ledesma MD, Simons K, Dotti CG. Neuronal polarity: essential role of protein-lipid complexes in axonal sorting. Proc Natl Acad Sci U S A 1998;95:3966-71.
58. Lisanti MP, Caras IW, Davitz MA, Rodriguez-Boulan E. A glycophospholipid membrane anchor acts as an apical targeting signal in polarized epithelial cells. J Cell Biol 1989;109:2145-56.
59. Kokkonen N, Khosrowabadi E, Hassinen A, et al. Abnormal golgi pH homeostasis in cancer cells impairs apical targeting of carcinoembryonic antigen by inhibiting its glycosyl-phosphatidylinositol anchor-Mediated association with lipid rafts. Antioxid Redox Signal 2019;30:5-21.
60. Meer G, Stelzer EH, Wijnaendts-van-Resandt RW, Simons K. Sorting of sphingolipids in epithelial (Madin-Darby canine kidney) cells. J Cell Biol 1987;105:1623-35.
61. Mays RW, Siemers KA, Fritz BA, et al. Hierarchy of mechanisms involved in generating Na/K-ATPase polarity in MDCK epithelial cells. J Cell Biol 1995;130:1105-15.
62. Paladino S, Sarnataro D, Pillich R, et al. Protein oligomerization modulates raft partitioning and apical sorting of GPI-anchored proteins. J Cell Biol 2004;167:699-709.
63. Jaensch N, Corrêa IR Jr, Watanabe R. Stable cell surface expression of GPI-anchored proteins, but not intracellular transport, depends on their fatty acid structure. Traffic 2014;15:1305-29.
64. Paladino S, Sarnataro D, Tivodar S, Zurzolo C. Oligomerization is a specific requirement for apical sorting of glycosyl-phosphatidylinositol-anchored proteins but not for non-raft-associated apical proteins. Traffic 2007;8:251-8.
65. Paladino S, Lebreton S, Tivodar S, et al. Different GPI-attachment signals affect the oligomerisation of GPI-anchored proteins and their apical sorting. J Cell Sci 2008;121:4001-7.
66. Paladino S, Lebreton S, Tivodar S, et al. Golgi sorting regulates organization and activity of GPI proteins at apical membranes. Nat Chem Biol 2014;10:350-7.
67. Benting JH, Rietveld AG, Simons K. N-Glycans mediate the apical sorting of a GPI-anchored, raft-associated protein in Madin-Darby canine kidney cells. J Cell Biol 1999;146:313-20.
68. Cheong KH, Zacchetti D, Schneeberger EE, Simons K. VIP17/MAL, a lipid raft-associated protein, is involved in apical transport in MDCK cells. Proc Natl Acad Sci USA 1999;96:6241-8.
69. Martín-Belmonte F, Puertollano R, Millán J, Alonso MA. The MAL proteolipid is necessary for the overall apical delivery of membrane proteins in the polarized epithelial Madin-Darby canine kidney and fischer rat thyroid cell lines. Mol Biol Cell 2000;11:2033-45.
70. Lafont F, Lecat S, Verkade P, Simons K. Annexin XIIIb associates with lipid microdomains to function in apical delivery. J Cell Biol 1998;142:1413-27.
71. Jacob R, Heine M, Eikemeyer J, et al. Annexin II is required for apical transport in polarized epithelial cells. J Biol Chem 2004;279:3680-4.
72. Snyers L, Umlauf E, Prohaska R. Association of stomatin with lipid-protein complexes in the plasma membrane and the endocytic compartment. Eur J Cell Biol 1999;78:802-12.
73. Neumann-Giesen C, Falkenbach B, Beicht P, et al. Membrane and raft association of reggie-1/flotillin-2: role of myristoylation, palmitoylation and oligomerization and induction of filopodia by overexpression. Biochem J 2004;378:509-18.
74. Zurzolo C, Lisanti MP, Caras IW, Nitsch L, Rodriguez-Boulan E. Glycosylphosphatidylinositol-anchored proteins are preferentially targeted to the basolateral surface in Fischer rat thyroid epithelial cells. J Cell Biol 1993;121:1031-9.
75. Sarnataro D, Paladino S, Campana V, Grassi J, Nitsch L, Zurzolo C. PrPC is sorted to the basolateral membrane of epithelial cells independently of its association with rafts. Traffic 2002;3:810-21.
76. Puig B, Altmeppen H, Glatzel M. The GPI-anchoring of PrP: implications in sorting and pathogenesis. Prion 2014;8:11-8.
77. Young SG, Davies BS, Voss CV, et al. GPIHBP1, an endothelial cell transporter for lipoprotein lipase. J Lipid Res 2011;52:1869-84.
78. Müller GA. The release of glycosylphosphatidylinositol-anchored proteins from the cell surface. Arch Biochem Biophys 2018;656:1-18.
79. Low MG. Glycosyl-phosphatidylinositol: a versatile anchor for cell surface proteins. FASEB J 1989;3:1600-8.
80. Lauc G, Heffer-Lauc M. Shedding and uptake of gangliosides and glycosylphosphatidylinositol-anchored proteins. Biochim Biophys Acta 2006;1760:584-602.
81. Kuespert K, Pils S, Hauck CR. CEACAMs: their role in physiology and pathophysiology. Curr Opin Cell Biol 2006;18:565-71.
82. Tchoupa AK, Schuhmacher T, Hauck CR. Signaling by epithelial members of the CEACAM family - mucosal docking sites for pathogenic bacteria. Cell Commun Signal 2014;12:27.
83. Pakdel A, Naghibalhossaini F, Mokarram P, Jaberipour M, Hosseini A. Regulation of carcinoembryonic antigen release from colorectal cancer cells. Mol Biol Rep 2012;39:3695-704.
84. Ferguson MA, Williams AF. Cell-surface anchoring of proteins via glycosyl-phosphatidylinositol structures. Annu Rev Biochem 1988;57:285-320.
85. Cross GA. Cellular and genetic aspects of antigenic variation in trypanosomes. Annu Rev Immunol 1990;8:83-110.
86. Low MG, Prasad AR. A phospholipase D specific for the phosphatidylinositol anchor of cell-surface proteins is abundant in plasma. Proc Natl Acad Sci U S A 1988;85:980-4.
87. Stieger S, Diem S, Jakob A, Brodbeck U. Enzymatic properties of phosphatidylinositol-glycan-specific phospholipase C from rat liver and phosphatidylinositol-glycan-specific phospholipase D from rat serum. Eur J Biochem 1991;197:67-73.
88. Deeg MA, Davitz MA. [45] Glycosylphosphatidylinositol-phospholipase D: A tool for glycosylphosphatidylinositol structural analysis. Lipid Modifications of Proteins. Elsevier; 1995. pp. 630-40.
89. Flores-Borja F, Kieszkievicz J, Church V, et al. Genetic regulation of mouse glycosylphosphatidylinositol-phospholipase D. Biochimie 2004;86:275-82.
90. Heller M, Bütikofer P, Brodbeck U. Generation by limited proteolysis of a catalytically active 39-kDa protein from the 115-kDa form of phosphatidylinositol-glycan-specific phospholipase D from bovine serum. Eur J Biochem 1994;224:823-33.
91. Springer TA. Folding of the N-terminal, ligand-binding region of integrin alpha-subunits into a beta-propeller domain. Proc Natl Acad Sci USA 1997;94:65-72.
92. Wilhelm OG, Wilhelm S, Escott GM, et al. Cellular glycosylphosphatidylinositol-specific phospholipase D regulates urokinase receptor shedding and cell surface expression. J Cell Physiol 1999;180:225-35.
93. Bugge TH, Suh TT, Flick MJ, et al. The receptor for urokinase-type plasminogen activator is not essential for mouse development or fertility. J Biol Chem 1995;270:16886-94.
94. Yamamoto Y, Hirakawa E, Mori S, Hamada Y, Kawaguchi N, Matsuura N. Cleavage of carcinoembryonic antigen induces metastatic potential in colorectal carcinoma. Biochem Biophys Res Commun 2005;333:223-9.
95. Verghese GM, Gutknecht MF, Caughey GH. Prostasin regulates epithelial monolayer function: cell-specific Gpld1-mediated secretion and functional role for GPI anchor. Am J Physiol Cell Physiol 2006;291:C1258-70.
96. Hummler E, Dousse A, Rieder A, et al. The channel-activating protease CAP1/Prss8 is required for placental labyrinth maturation. PLoS One 2013;8:e55796.
97. Watanabe K, Bianco C, Strizzi L, et al. Growth factor induction of Cripto-1 shedding by glycosylphosphatidylinositol-phospholipase D and enhancement of endothelial cell migration. J Biol Chem 2007;282:31643-55.
98. Ding J, Yang L, Yan YT, et al. Cripto is required for correct orientation of the anterior-posterior axis in the mouse embryo. Nature 1998;395:702-7.
99. Mateescu B, Jones JC, Alexander RP, et al. Phase 2 of extracellular RNA communication consortium charts next-generation approaches for extracellular RNA research. iScience 2022;25:104653.
100. Tauro BJ, Greening DW, Mathias RA, Mathivanan S, Ji H, Simpson RJ. Two distinct populations of exosomes are released from LIM1863 colon carcinoma cell-derived organoids. Mol Cell Proteomics 2013;12:587-98.
101. Thompson A, Nessler R, Wisco D, Anderson E, Winckler B, Sheff D. Recycling endosomes of polarized epithelial cells actively sort apical and basolateral cargos into separate subdomains. Mol Biol Cell 2007;18:2687-97.
102. Chen Y, Zhao Y, Yin Y, Jia X, Mao L. Mechanism of cargo sorting into small extracellular vesicles. Bioengineered 2021;12:8186-201.
103. Andreu Z, Yáñez-Mó M. Tetraspanins in extracellular vesicle formation and function. Front Immunol 2014;5:442.
104. Apodaca G, Gallo LI, Bryant DM. Role of membrane traffic in the generation of epithelial cell asymmetry. Nat Cell Biol 2012;14:1235-43.
105. Adachi H, Kubota I, Okamura N, et al. Purification and characterization of human microsomal dipeptidase. J Biochem 1989;105:957-61.
106. Buckhaults, P, et al. Secreted and cell surface genes expressed in benign and malignant colorectal tumors. Cancer Res :61, 6996-7001.
107. Zhao ZW, Fan XX, Yang LL, et al. The identification of a common different gene expression signature in patients with colorectal cancer. Math Biosci Eng 2019;16:2942-58.
108. Tachibana K, Saito M, Imai JI, et al. Clinicopathological examination of dipeptidase 1 expression in colorectal cancer. Biomed Rep 2017;6:423-8.
109. Liu Q, Deng J, Yang C, et al. DPEP1 promotes the proliferation of colon cancer cells via the DPEP1/MYC feedback loop regulation. Biochem Biophys Res Commun 2020;532:520-7.
110. Toiyama Y, Inoue Y, Yasuda H, et al. DPEP1, expressed in the early stages of colon carcinogenesis, affects cancer cell invasiveness. J Gastroenterol 2011;46:153-63.
111. Park SY, Lee SJ, Cho HJ, et al. Dehydropeptidase 1 promotes metastasis through regulation of E-cadherin expression in colon cancer. Oncotarget 2016;7:9501-12.
112. Zeng C, Qi G, Shen Y, et al. DPEP1 promotes drug resistance in colon cancer cells by forming a positive feedback loop with ASCL2. Cancer Med 2023;12:412-24.
113. Liu Z, Cauvi DM, Bernardino EMA, et al. Isolation and characterization of human urine extracellular vesicles. Cell Stress Chaperones 2018;23:943-53.
114. Stokman MF, Bijnsdorp IV, Schelfhorst T, et al. Changes in the urinary extracellular vesicle proteome are associated with nephronophthisis-related ciliopathies. J Proteomics 2019;192:27-36.
115. Choi DS, Choi DY, Hong BS, et al. Quantitative proteomics of extracellular vesicles derived from human primary and metastatic colorectal cancer cells. J Extracell Vesicles 2012;1:18704.
116. Choudhury SR, Babes L, Rahn JJ, et al. Dipeptidase-1 Is an Adhesion Receptor for Neutrophil Recruitment in Lungs and Liver. Cell 2019;178:1205-1221.e17.
117. Lau A, Rahn JJ, Chappellaz M, et al. Dipeptidase-1 governs renal inflammation during ischemia reperfusion injury. Sci Adv 2022;8:eabm0142.
118. Zhang Q, Jeppesen DK, Higginbotham JN, Franklin JL, Crowe JE Jr, Coffey RJ. Angiotensin-converting Enzyme 2-containing Small Extracellular Vesicles and Exomeres Bind the Severe Acute Respiratory Syndrome Coronavirus 2 Spike Protein. Gastroenterology 2021;160:958-961.e3.
119. Roh M, Wainwright DA, Wu JD, Wan Y, Zhang B. Targeting CD73 to augment cancer immunotherapy. Curr Opin Pharmacol 2020;53:66-76.
120. Airas L, Niemelä J, Jalkanen S. CD73 engagement promotes lymphocyte binding to endothelial cells via a lymphocyte function-associated antigen-1-dependent mechanism. J Immunol 2000;165:5411-7.
122. Zhang F, Li R, Yang Y, et al. Specific Decrease in B-Cell-Derived Extracellular Vesicles Enhances Post-Chemotherapeutic CD8(+) T Cell Responses. Immunity 2019;50:738-750.e7.
123. Clayton A, Al-Taei S, Webber J, Mason MD, Tabi Z. Cancer exosomes express CD39 and CD73, which suppress T cells through adenosine production. J Immunol 2011;187:676-83.
124. Ludwig N, Yerneni SS, Azambuja JH, et al. Tumor-derived exosomes promote angiogenesis via adenosine A(2B) receptor signaling. Angiogenesis 2020;23:599-610.
125. Turiello R, Capone M, Morretta E, et al. Exosomal CD73 from serum of patients with melanoma suppresses lymphocyte functions and is associated with therapy resistance to anti-PD-1 agents. J Immunother Cancer 2022;10:e004043.
126. Ploeg EM, Ke X, Britsch I, et al. Bispecific antibody CD73xEpCAM selectively inhibits the adenosine-mediated immunosuppressive activity of carcinoma-derived extracellular vesicles. Cancer Lett 2021;521:109-18.
127. Harvey JB, Phan LH, Villarreal OE, Bowser JL. CD73's Potential as an Immunotherapy Target in Gastrointestinal Cancers. Front Immunol 2020;11:508.
128. Hammarström S. The carcinoembryonic antigen (CEA) family: structures, suggested functions and expression in normal and malignant tissues. Semin Cancer Biol 1999;9:67-81.
129. Johnson B, Mahadevan D. Emerging role and targeting of carcinoembryonic antigen-related cell adhesion Molecule 6 (CEACAM6) in human malignancies. Clin Cancer Drugs 2015;2:100-11.
130. Benchimol S, Fuks A, Jothy S, Beauchemin N, Shirota K, Stanners CP. Carcinoembryonic antigen, a human tumor marker, functions as an intercellular adhesion molecule. Cell 1989;57:327-34.
131. Chan CH, Stanners CP. Recent advances in the tumour biology of the GPI-anchored carcinoembryonic antigen family members CEACAM5 and CEACAM6. Curr Oncol 2007;14:70-3.
132. Blumenthal RD, Hansen HJ, Goldenberg DM. Inhibition of adhesion, invasion, and metastasis by antibodies targeting CEACAM6 (NCA-90) and CEACAM5 (Carcinoembryonic Antigen). Cancer Res 2005;65:8809-17.
133. Beauchemin N, Arabzadeh A. Carcinoembryonic antigen-related cell adhesion molecules (CEACAMs) in cancer progression and metastasis. Cancer Metastasis Rev 2013;32:643-71.
134. Gemei M, Mirabelli P, Di Noto R, et al. CD66c is a novel marker for colorectal cancer stem cell isolation, and its silencing halts tumor growth in vivo. Cancer 2013;119:729-38.
135. Pinkert J, Boehm HH, Trautwein M, et al. T cell-mediated elimination of cancer cells by blocking CEACAM6-CEACAM1 interaction. Oncoimmunology 2022;11:2008110.
136. Sørensen CG, Karlsson WK, Pommergaard HC, Burcharth J, Rosenberg J. The diagnostic accuracy of carcinoembryonic antigen to detect colorectal cancer recurrence - A systematic review. Int J Surg 2016;25:134-44.
137. Kang Y, Zhu X, Lin Z, et al. Compare the diagnostic and prognostic value of MLR, NLR and PLR in CRC patients. Clin Lab 2021:67.
138. Ma Y, Zhang Y, Bi Y, et al. Diagnostic value of carcinoembryonic antigen combined with cytokines in serum of patients with colorectal cancer. Medicine 2022;101:e30787.
139. Wang, J, et al. Combined detection of preoperative serum CEA, CA19-9 and CA242 improve prognostic prediction of surgically treated colorectal cancer patients. Int J Clin Exp Pathol 2015;8:14853-63.
140. Xu Z, Wang H, Gao L, Zhang H, Wang X. YAP levels combined with plasma CEA levels are prognostic biomarkers for early-clinical-stage patients of colorectal cancer. Biomed Res Int 2019;2019:2170830.
141. Belov L, Matic KJ, Hallal S, Best OG, Mulligan SP, Christopherson RI. Extensive surface protein profiles of extracellular vesicles from cancer cells may provide diagnostic signatures from blood samples. J Extracell Vesicles 2016;5:25355.
142. Yokoyama S, Takeuchi A, Yamaguchi S, et al. Clinical implications of carcinoembryonic antigen distribution in serum exosomal fraction-Measurement by ELISA. PLoS One 2017;12:e0183337.
143. Eddama MMR, Gurung R, Fragkos K, et al. The role of microvesicles as biomarkers in the screening of colorectal neoplasm. Cancer Med 2022;11:2957-68.
144. Lee CH, Im EJ, Moon PG, Baek MC. Discovery of a diagnostic biomarker for colon cancer through proteomic profiling of small extracellular vesicles. BMC Cancer 2018;18:1058.
145. Sun B, Li Y, Zhou Y, et al. Circulating exosomal CPNE3 as a diagnostic and prognostic biomarker for colorectal cancer. J Cell Physiol 2019;234:1416-25.
146. Xiao Y, Zhong J, Zhong B, et al. Exosomes as potential sources of biomarkers in colorectal cancer. Cancer Lett 2020;476:13-22.
147. Ikeda A, Nagayama S, Sumazaki M, et al. Colorectal cancer-derived CAT1-positive extracellular vesicles alter nitric oxide metabolism in endothelial cells and promote angiogenesis. Mol Cancer Res 2021;19:834-46.
148. Keyhani G, Mahmoodzadeh Hosseini H, Salimi A. Effect of extracellular vesicles of Lactobacillus rhamnosus GG on the expression of CEA gene and protein released by colorectal cancer cells. Iran J Microbiol 2022;14:90-6.
149. Wang S, Qiu Y, Bai B. The expression, regulation, and biomarker potential of glypican-1 in cancer. Front Oncol 2019;9:614.
150. Lu F, Chen S, Shi W, Su X, Wu H, Liu M. GPC1 promotes the growth and migration of colorectal cancer cells through regulating the TGF-β1/SMAD2 signaling pathway. PLoS One 2022;17:e0269094.
151. Melo SA, Luecke LB, Kahlert C, et al. Glypican-1 identifies cancer exosomes and detects early pancreatic cancer. Nature 2015;523:177-82.
152. Papiewska-Pająk I, Krzyżanowski D, Katela M, et al. Glypican-1 level is elevated in extracellular vesicles released from MC38 colon adenocarcinoma cells overexpressing snail. Cells 2020;9:1585.
153. Li J, Chen Y, Guo X, et al. GPC1 exosome and its regulatory miRNAs are specific markers for the detection and target therapy of colorectal cancer. J Cell Mol Med 2017;21:838-47.
154. L Ramos T, Sánchez-Abarca LI, Muntión S, et al. MSC surface markers (CD44, CD73, and CD90) can identify human MSC-derived extracellular vesicles by conventional flow cytometry. Cell Commun Signal 2016;14:2.
155. Rabesandratana H, Toutant JP, Reggio H, Vidal M. Decay-accelerating factor (CD55) and membrane inhibitor of reactive lysis (CD59) are released within exosomes during in vitro maturation of reticulocytes. Blood 1998; 91:2573-80.
156. Liu D, Liu F, Song YK. Recognition and clearance of liposomes containing phosphatidylserine are mediated by serum opsonin. Biochim Biophys Acta 1995;1235:140-6.
157. Wassef NM, Matyas GR, Alving CR. Complement-dependent phagocytosis of liposomes by macrophages: suppressive effects of "stealth" lipids. Biochem Biophys Res Commun 1991;176:866-74.
158. López-Cobo S, Campos-Silva C, Valés-Gómez M. Glycosyl-phosphatidyl-inositol (GPI)-anchors and metalloproteases: their roles in the regulation of exosome composition and NKG2D-mediated immune recognition. Front Cell Dev Biol 2016;4:97.
159. Laulagnier K, Motta C, Hamdi S, et al. Mast cell- and dendritic cell-derived exosomes display a specific lipid composition and an unusual membrane organization. Biochem J 2004;380:161-71.
160. Stalder D, Gershlick DC. Direct trafficking pathways from the Golgi apparatus to the plasma membrane. Semin Cell Dev Biol 2020;107:112-25.
161. Vidal M, Mangeat P, Hoekstra D. Aggregation reroutes molecules from a recycling to a vesicle-mediated secretion pathway during reticulocyte maturation. J Cell Sci 1997;110 ( Pt 16):1867-77.
162. Edgar JR, Manna PT, Nishimura S, Banting G, Robinson MS. Tetherin is an exosomal tether. Elife 2016;5:e17180.
163. Tanaka Y, Okada Y, Hirokawa N. FGF-induced vesicular release of Sonic hedgehog and retinoic acid in leftward nodal flow is critical for left-right determination. Nature 2005;435:172-7.
164. Panáková D, Sprong H, Marois E, Thiele C, Eaton S. Lipoprotein particles are required for Hedgehog and Wingless signalling. Nature 2005;435:58-65.
165. Eliakim R, DeSchryver-Kecskemeti K, Nogee L, Stenson WF, Alpers DH. Isolation and characterization of a small intestinal surfactant-like particle containing alkaline phosphatase and other digestive enzymes. J Biol Chem 1989;264:20614-19.
166. Strybel U, Marczak L, Zeman M, et al. Molecular Composition of Serum Exosomes Could Discriminate Rectal Cancer Patients with Different Responses to Neoadjuvant Radiotherapy. Cancers (Basel) 2022;14:993.
167. Chen Q, Takada R, Noda C, Kobayashi S, Takada S. Different populations of Wnt-containing vesicles are individually released from polarized epithelial cells. Sci Rep 2016;6:35562.
168. Théry C, Witwer KW, Aikawa E, et al. 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 2018;7:1535750.
169. Wei D, Zhan W, Gao Y, et al. RAB31 marks and controls an ESCRT-independent exosome pathway. Cell Res 2021;31:157-77.
