메뉴 건너뛰기




Volumn 131, Issue 1, 2012, Pages 117-128

Differential glycosylation of MUC1 and CEACAM5 between normal mucosa and tumour tissue of colon cancer patients

Author keywords

CEACAM5; colon carcinoma; DC SIGN; glycosylation; MGL; MUC1

Indexed keywords

CARCINOEMBRYONIC ANTIGEN; CARCINOEMBRYONIC ANTIGEN RELATED CELL ADHESION MOLECULE 5; CD209 ANTIGEN; CORE 1 ANTIGEN; GALECTIN 3; LECTIN; LEWIS Y ANTIGEN; MANNOSE; MUCIN 1; PEANUT AGGLUTININ; PLANT LECTIN; SIALYL LEWIS X ANTIGEN; THOMSEN FRIEDENREICH ANTIGEN; TUMOR ANTIGEN; UNCLASSIFIED DRUG;

EID: 84860214318     PISSN: 00207136     EISSN: 10970215     Source Type: Journal    
DOI: 10.1002/ijc.26354     Document Type: Article
Times cited : (91)

References (49)
  • 1
    • 44049095632 scopus 로고    scopus 로고
    • Protein-glycan interactions in the control of innate and adaptive immune responses
    • van Kooyk Y, Rabinovich GA,. Protein-glycan interactions in the control of innate and adaptive immune responses. Nat Immunol 2008; 9: 593-601.
    • (2008) Nat Immunol , vol.9 , pp. 593-601
    • Van Kooyk, Y.1    Rabinovich, G.A.2
  • 2
    • 84860222212 scopus 로고    scopus 로고
    • Golgi pH, its regulation and roles in human disease
    • [Epub ahead of print]. DOI: 10.3109/07853890.2011.579150.
    • Rovinoja A, Pujol FM, Hassinen A, Kellokumpu S,. Golgi pH, its regulation and roles in human disease. Ann Med 2011. [Epub ahead of print]. DOI: 10.3109/07853890.2011.579150.
    • (2011) Ann Med
    • Rovinoja, A.1    Pujol, F.M.2    Hassinen, A.3    Kellokumpu, S.4
  • 3
    • 0033977912 scopus 로고    scopus 로고
    • The involvement of Helix pomatia lectin (HPA) binding N-acetylgalactosamine glycans in cancer progression
    • Brooks SA,. The involvement of Helix pomatia lectin (HPA) binding N-acetylgalactosamine glycans in cancer progression. Histol Histopathol 2000; 15: 143-58.
    • (2000) Histol Histopathol , vol.15 , pp. 143-158
    • Brooks, S.A.1
  • 4
    • 33644874643 scopus 로고    scopus 로고
    • High expression of Lewis y/b antigens is associated with decreased survival in lymph node negative breast carcinomas
    • Madjd Z, Parsons T, Watson NF, Spendlove I, Ellis I, Durrant LG,. High expression of Lewis y/b antigens is associated with decreased survival in lymph node negative breast carcinomas. Breast Cancer Res 2005; 7: R780-R787.
    • (2005) Breast Cancer Res , vol.7
    • Madjd, Z.1    Parsons, T.2    Watson, N.F.3    Spendlove, I.4    Ellis, I.5    Durrant, L.G.6
  • 6
    • 0024619236 scopus 로고
    • Expression of Lewisa, Lewisb, Lewisx, Lewisy, siayl-Lewisa, and sialyl-Lewisx blood group antigens in human gastric carcinoma and in normal gastric tissue
    • Sakamoto S, Watanabe T, Tokumaru T, Takagi H, Nakazato H, Lloyd KO,. Expression of Lewisa, Lewisb, Lewisx, Lewisy, siayl-Lewisa, and sialyl-Lewisx blood group antigens in human gastric carcinoma and in normal gastric tissue. Cancer Res 1989; 49: 745-52.
    • (1989) Cancer Res , vol.49 , pp. 745-752
    • Sakamoto, S.1    Watanabe, T.2    Tokumaru, T.3    Takagi, H.4    Nakazato, H.5    Lloyd, K.O.6
  • 7
    • 0022559251 scopus 로고
    • Expression of Lewisa, Lewisb, X, and y blood group antigens in human colonic tumours and normal tissue and in human tumour-derived cell lines
    • Sakamoto J, Furukawa K, Cordon-Cardo C, Yin BW, Rettig WJ, Oettgen HF, Old LJ, Lloyd KO,. Expression of Lewisa, Lewisb, X, and Y blood group antigens in human colonic tumours and normal tissue and in human tumour-derived cell lines. Cancer Res 1986; 46: 1553-61.
    • (1986) Cancer Res , vol.46 , pp. 1553-1561
    • Sakamoto, J.1    Furukawa, K.2    Cordon-Cardo, C.3    Yin, B.W.4    Rettig, W.J.5    Oettgen, H.F.6    Old, L.J.7    Lloyd, K.O.8
  • 8
    • 0028988064 scopus 로고
    • Expression of sialyl Lewis(a) as a new prognostic factor for patients with advanced colorectal carcinoma
    • Nakayama T, Watanabe M, Katsumata T, Teramoto T, Kitajima M,. Expression of sialyl Lewis(a) as a new prognostic factor for patients with advanced colorectal carcinoma. Cancer 1995; 75: 2051-6.
    • (1995) Cancer , vol.75 , pp. 2051-2056
    • Nakayama, T.1    Watanabe, M.2    Katsumata, T.3    Teramoto, T.4    Kitajima, M.5
  • 9
    • 63849339429 scopus 로고    scopus 로고
    • The high affinity selectin glycan ligand C2-O-sLex and mRNA transcripts of the core 2 β-1,6-N-acetylglucosaminyltrans ferase (C2GnT1) gene are highly expressed in human colorectal adenocarcinomas
    • St Hill CA, Farooqui M, Mitcheltree G, Gulbahce HE, Jessurun J, Cao Q, Walcheck B,. The high affinity selectin glycan ligand C2-O-sLex and mRNA transcripts of the core 2 β-1,6-N-acetylglucosaminyltrans ferase (C2GnT1) gene are highly expressed in human colorectal adenocarcinomas. BMC Cancer 2009; 9: 79.
    • (2009) BMC Cancer , vol.9 , pp. 79
    • St Hill, C.A.1    Farooqui, M.2    Mitcheltree, G.3    Gulbahce, H.E.4    Jessurun, J.5    Cao, Q.6    Walcheck, B.7
  • 10
    • 53049084874 scopus 로고    scopus 로고
    • N-Glycans in cancer progression
    • Lau KS, Dennis JW,. N-Glycans in cancer progression. Glycobiology 2008; 18: 750-60.
    • (2008) Glycobiology , vol.18 , pp. 750-760
    • Lau, K.S.1    Dennis, J.W.2
  • 12
    • 21344449731 scopus 로고    scopus 로고
    • Dendritic cells recognize tumour-specific glycosylation of carcinoembryonic antigen on colorectal cancer cells through dendritic cell-specific intercellular adhesion molecule-3-grabbing nonintegrin
    • van Gisbergen KP, Aarnoudse CA, Meijer GA, Geijtenbeek TB, van Kooyk Y,. Dendritic cells recognize tumour-specific glycosylation of carcinoembryonic antigen on colorectal cancer cells through dendritic cell-specific intercellular adhesion molecule-3-grabbing nonintegrin. Cancer Res 2005; 65: 5935-44.
    • (2005) Cancer Res , vol.65 , pp. 5935-5944
    • Van Gisbergen, K.P.1    Aarnoudse, C.A.2    Meijer, G.A.3    Geijtenbeek, T.B.4    Van Kooyk, Y.5
  • 13
    • 0033057177 scopus 로고    scopus 로고
    • The carcinoembryonic antigen (CEA) family: Structures, suggested functions and expression in normal and malignant tissues
    • Hammarstrom S,. The carcinoembryonic antigen (CEA) family: structures, suggested functions and expression in normal and malignant tissues. Semin Cancer Biol 1999; 9: 67-81.
    • (1999) Semin Cancer Biol , vol.9 , pp. 67-81
    • Hammarstrom, S.1
  • 15
    • 0037442109 scopus 로고    scopus 로고
    • Cutting edge: Carbohydrate profiling identifies new pathogens that interact with dendritic cell-specific ICAM-3-grabbing nonintegrin on dendritic cells
    • Appelmelk BJ, van Die I, van Vliet SJ, Vandenbroucke-Grauls CM, Geijtenbeek TB, van Kooyk Y,. Cutting edge: carbohydrate profiling identifies new pathogens that interact with dendritic cell-specific ICAM-3-grabbing nonintegrin on dendritic cells. J Immunol 2003; 170: 1635-9.
    • (2003) J Immunol , vol.170 , pp. 1635-1639
    • Appelmelk, B.J.1    Van Die, I.2    Van Vliet, S.J.3    Vandenbroucke-Grauls, C.M.4    Geijtenbeek, T.B.5    Van Kooyk, Y.6
  • 16
    • 0026264928 scopus 로고
    • Carbohydrate antigens on cancer-associated mucin-like molecules
    • Ho SB, Kim YS,. Carbohydrate antigens on cancer-associated mucin-like molecules. Semin Cancer Biol 1991; 2: 389-400.
    • (1991) Semin Cancer Biol , vol.2 , pp. 389-400
    • Ho, S.B.1    Kim, Y.S.2
  • 17
    • 0347123435 scopus 로고    scopus 로고
    • Mucins in cancer: Protection and control of the cell surface
    • Hollingsworth MA, Swanson BJ,. Mucins in cancer: protection and control of the cell surface. Nat Rev Cancer 2004; 4: 45-60.
    • (2004) Nat Rev Cancer , vol.4 , pp. 45-60
    • Hollingsworth, M.A.1    Swanson, B.J.2
  • 18
    • 38749105791 scopus 로고    scopus 로고
    • Sweet preferences of MGL: Carbohydrate specificity and function
    • van Vliet SJ, Saeland E, van Kooyk Y,. Sweet preferences of MGL: carbohydrate specificity and function. Trends Immunol 2008; 29: 83-90.
    • (2008) Trends Immunol , vol.29 , pp. 83-90
    • Van Vliet, S.J.1    Saeland, E.2    Van Kooyk, Y.3
  • 21
    • 0014949657 scopus 로고
    • Specific inhibition by N-acetyl- D -galactosamine of the interaction between soybean agglutinin and animal cell surfaces
    • Lis H, Sela BA, Sachs L, Sharon N,. Specific inhibition by N-acetyl- D -galactosamine of the interaction between soybean agglutinin and animal cell surfaces. Biochim Biophys Acta 1970; 211: 582-5.
    • (1970) Biochim Biophys Acta , vol.211 , pp. 582-585
    • Lis, H.1    Sela, B.A.2    Sachs, L.3    Sharon, N.4
  • 22
    • 0016702060 scopus 로고
    • The purification, composition, and specificity of the anti-T lectin from peanut (Arachis hypogaea)
    • Lotan R, Skutelsky E, Danon D, Sharon N,. The purification, composition, and specificity of the anti-T lectin from peanut (Arachis hypogaea). J Biol Chem 1975; 250: 8518-23.
    • (1975) J Biol Chem , vol.250 , pp. 8518-8523
    • Lotan, R.1    Skutelsky, E.2    Danon, D.3    Sharon, N.4
  • 23
    • 0025187201 scopus 로고
    • Difference in the ability of blood group-specific lectins and monoclonal antibodies to recognize the ABH antigens in human tissues
    • Ito N, Nishi K, Kawahara S, Okamura Y, Hirota T, Rand S, Fechner G, Brinkmann B,. Difference in the ability of blood group-specific lectins and monoclonal antibodies to recognize the ABH antigens in human tissues. Histochem J 1990; 22: 604-14.
    • (1990) Histochem J , vol.22 , pp. 604-614
    • Ito, N.1    Nishi, K.2    Kawahara, S.3    Okamura, Y.4    Hirota, T.5    Rand, S.6    Fechner, G.7    Brinkmann, B.8
  • 24
    • 0031059280 scopus 로고    scopus 로고
    • Immobilized Lotus tetragonolobus agglutinin binds oligosaccharides containing the Le(x) determinant
    • Yan L, Wilkins PP, varez-Manilla G, Do SI, Smith DF, Cummings RD,. Immobilized Lotus tetragonolobus agglutinin binds oligosaccharides containing the Le(x) determinant. Glycoconj J 1997; 14: 45-55.
    • (1997) Glycoconj J , vol.14 , pp. 45-55
    • Yan, L.1    Wilkins, P.P.2    Varez-Manilla, G.3    Do, S.I.4    Smith, D.F.5    Cummings, R.D.6
  • 25
    • 0029765516 scopus 로고    scopus 로고
    • Characterization of the binding specificity of Anguilla anguilla agglutinin (AAA) in comparison to Ulex europaeus agglutinin i (UEA-I)
    • Baldus SE, Thiele J, Park YO, Hanisch FG, Bara J, Fischer R,. Characterization of the binding specificity of Anguilla anguilla agglutinin (AAA) in comparison to Ulex europaeus agglutinin I (UEA-I). Glycoconj J 1996; 13: 585-90.
    • (1996) Glycoconj J , vol.13 , pp. 585-590
    • Baldus, S.E.1    Thiele, J.2    Park, Y.O.3    Hanisch, F.G.4    Bara, J.5    Fischer, R.6
  • 26
    • 0025333981 scopus 로고
    • Carbohydrate-binding specificity of the daffodil (Narcissus pseudonarcissus) and amaryllis (Hippeastrum hybr.) bulb lectins
    • Kaku H, Van Damme EJ, Peumans WJ, Goldstein IJ,. Carbohydrate-binding specificity of the daffodil (Narcissus pseudonarcissus) and amaryllis (Hippeastrum hybr.) bulb lectins. Arch Biochem Biophys 1990; 279: 298-304.
    • (1990) Arch Biochem Biophys , vol.279 , pp. 298-304
    • Kaku, H.1    Van Damme, E.J.2    Peumans, W.J.3    Goldstein, I.J.4
  • 28
    • 0020479688 scopus 로고
    • Characterization of the structural determinants required for the high affinity interaction of asparagine-linked oligosaccharides with immobilized Phaseolus vulgaris leukoagglutinating and erythroagglutinating lectins
    • Cummings RD, Kornfeld S,. Characterization of the structural determinants required for the high affinity interaction of asparagine-linked oligosaccharides with immobilized Phaseolus vulgaris leukoagglutinating and erythroagglutinating lectins. J Biol Chem 1982; 257: 11230-4.
    • (1982) J Biol Chem , vol.257 , pp. 11230-11234
    • Cummings, R.D.1    Kornfeld, S.2
  • 30
    • 0028895533 scopus 로고
    • Direct demonstration of increased expression of Thomsen-Friedenreich (TF) antigen in colonic adenocarcinoma and ulcerative colitis mucin and its concealment in normal mucin
    • Campbell BJ, Finnie IA, Hounsell EF, Rhodes JM,. Direct demonstration of increased expression of Thomsen-Friedenreich (TF) antigen in colonic adenocarcinoma and ulcerative colitis mucin and its concealment in normal mucin. J Clin Invest 1995; 95: 571-6.
    • (1995) J Clin Invest , vol.95 , pp. 571-576
    • Campbell, B.J.1    Finnie, I.A.2    Hounsell, E.F.3    Rhodes, J.M.4
  • 32
    • 77953627018 scopus 로고    scopus 로고
    • Interaction between circulating galectin-3 and cancer-associated MUC1 enhances tumour cell homotypic aggregation and prevents anoikis
    • Zhao Q, Barclay M, Hilkens J, Guo X, Barrow H, Rhodes JM, Yu LG,. Interaction between circulating galectin-3 and cancer-associated MUC1 enhances tumour cell homotypic aggregation and prevents anoikis. Mol Cancer 2010; 9: 154.
    • (2010) Mol Cancer , vol.9 , pp. 154
    • Zhao, Q.1    Barclay, M.2    Hilkens, J.3    Guo, X.4    Barrow, H.5    Rhodes, J.M.6    Yu, L.G.7
  • 35
    • 0028961151 scopus 로고
    • Distribution of Tn antigen recognized by an anti-Tn monoclonal antibody (MLS128) in normal and malignant tissues of the digestive tract
    • Ohshio G, Imamura T, Imamura M, Yamabe H, Sakahara H, Nakada H, Yamashina I,. Distribution of Tn antigen recognized by an anti-Tn monoclonal antibody (MLS128) in normal and malignant tissues of the digestive tract. J Cancer Res Clin Oncol 1995; 121: 247-52.
    • (1995) J Cancer Res Clin Oncol , vol.121 , pp. 247-252
    • Ohshio, G.1    Imamura, T.2    Imamura, M.3    Yamabe, H.4    Sakahara, H.5    Nakada, H.6    Yamashina, I.7
  • 37
    • 79551477301 scopus 로고    scopus 로고
    • Tumour-associated glycan modifications of antigen enhance MGL2 dependent uptake and MHC class i restricted CD8 T cell responses
    • Singh SK, Streng-Ouwehand I, Litjens M, Kalay H, Saeland E, van Kooyk Y,. Tumour-associated glycan modifications of antigen enhance MGL2 dependent uptake and MHC class I restricted CD8 T cell responses. Int J Cancer 2011; 128: 1371-83.
    • (2011) Int J Cancer , vol.128 , pp. 1371-1383
    • Singh, S.K.1    Streng-Ouwehand, I.2    Litjens, M.3    Kalay, H.4    Saeland, E.5    Van Kooyk, Y.6
  • 38
    • 30044448792 scopus 로고    scopus 로고
    • Autoproteolysis coupled to protein folding in the SEA domain of the membrane-bound MUC1 mucin
    • Macao B, Johansson DG, Hansson GC, Hard T,. Autoproteolysis coupled to protein folding in the SEA domain of the membrane-bound MUC1 mucin. Nat Struct Mol Biol 2006; 13: 71-6.
    • (2006) Nat Struct Mol Biol , vol.13 , pp. 71-76
    • MacAo, B.1    Johansson, D.G.2    Hansson, G.C.3    Hard, T.4
  • 39
    • 0035526270 scopus 로고    scopus 로고
    • Tumour cell MUC1 and CD43 are glycosylated differently with sialyl-Lewis a and x epitopes and show variable interactions with E-selectin under physiological flow conditions
    • Fernandez-Rodriguez J, Dwir O, Alon R, Hansson GC,. Tumour cell MUC1 and CD43 are glycosylated differently with sialyl-Lewis a and x epitopes and show variable interactions with E-selectin under physiological flow conditions. Glycoconj J 2001; 18: 925-30.
    • (2001) Glycoconj J , vol.18 , pp. 925-930
    • Fernandez-Rodriguez, J.1    Dwir, O.2    Alon, R.3    Hansson, G.C.4
  • 40
    • 0022382629 scopus 로고
    • Carbohydrate determinants associated with carcinoembryonic antigen (CEA)
    • Nichols EJ, Kannagi R, Hakomori SI, Krantz MJ, Fuks A,. Carbohydrate determinants associated with carcinoembryonic antigen (CEA). J Immunol 1985; 135: 1911-13.
    • (1985) J Immunol , vol.135 , pp. 1911-1913
    • Nichols, E.J.1    Kannagi, R.2    Hakomori, S.I.3    Krantz, M.J.4    Fuks, A.5
  • 41
    • 0023221836 scopus 로고
    • Structural studies of the carbohydrate moieties of carcinoembryonic antigens
    • Yamashita K, Totani K, Kuroki M, Matsuoka Y, Ueda I, Kobata A,. Structural studies of the carbohydrate moieties of carcinoembryonic antigens. Cancer Res 1987; 47: 3451-9.
    • (1987) Cancer Res , vol.47 , pp. 3451-3459
    • Yamashita, K.1    Totani, K.2    Kuroki, M.3    Matsuoka, Y.4    Ueda, I.5    Kobata, A.6
  • 42
    • 34447345132 scopus 로고    scopus 로고
    • Biosynthesis and expression of the Sda and sialyl Lewis x antigens in normal and cancer colon
    • Malagolini N, Santini D, Chiricolo M, Dall'Olio F,. Biosynthesis and expression of the Sda and sialyl Lewis x antigens in normal and cancer colon. Glycobiology 2007; 17: 688-97.
    • (2007) Glycobiology , vol.17 , pp. 688-697
    • Malagolini, N.1    Santini, D.2    Chiricolo, M.3    Dall'Olio, F.4
  • 44
    • 49149107798 scopus 로고    scopus 로고
    • Knockdown of Mgat5 inhibits breast cancer cell growth with activation of CD4+ T cells and macrophages
    • Li D, Li Y, Wu X, Li Q, Yu J, Gen J, Zhang XL,. Knockdown of Mgat5 inhibits breast cancer cell growth with activation of CD4+ T cells and macrophages. J Immunol 2008; 180: 3158-65.
    • (2008) J Immunol , vol.180 , pp. 3158-3165
    • Li, D.1    Li, Y.2    Wu, X.3    Li, Q.4    Yu, J.5    Gen, J.6    Zhang, X.L.7
  • 45
    • 0029021007 scopus 로고
    • Reduced contact-inhibition and substratum adhesion in epithelial cells expressing GlcNAc-transferase v
    • Demetriou M, Nabi IR, Coppolino M, Dedhar S, Dennis JW, Reduced contact-inhibition and substratum adhesion in epithelial cells expressing GlcNAc-transferase V. J Cell Biol 1995; 130: 383-92.
    • (1995) J Cell Biol , vol.130 , pp. 383-392
    • Demetriou, M.1    Nabi, I.R.2    Coppolino, M.3    Dedhar, S.4    Dennis, J.W.5
  • 46
    • 0020373041 scopus 로고
    • Control of glycoprotein synthesis. UDP-GlcNAc:glycopeptide β 4-N-acetylglucosaminyltransferase III, an enzyme in hen oviduct which adds GlcNAc in β 1-4 linkage to the beta-linked mannose of the trimannosyl core of N-glycosyl oligosaccharides
    • Narasimhan S,. Control of glycoprotein synthesis. UDP-GlcNAc:glycopeptide β 4-N-acetylglucosaminyltransferase III, an enzyme in hen oviduct which adds GlcNAc in β 1-4 linkage to the beta-linked mannose of the trimannosyl core of N-glycosyl oligosaccharides. J Biol Chem 1982; 257: 10235-42.
    • (1982) J Biol Chem , vol.257 , pp. 10235-10242
    • Narasimhan, S.1
  • 47
    • 77951072143 scopus 로고    scopus 로고
    • The bisecting GlcNAc on N-glycans inhibits growth factor signaling and retards mammary tumour progression
    • Song Y, Aglipay JA, Bernstein JD, Goswami S, Stanley P,. The bisecting GlcNAc on N-glycans inhibits growth factor signaling and retards mammary tumour progression. Cancer Res 2010; 70: 3361-71.
    • (2010) Cancer Res , vol.70 , pp. 3361-3371
    • Song, Y.1    Aglipay, J.A.2    Bernstein, J.D.3    Goswami, S.4    Stanley, P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.