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Volumn 39, Issue 1, 2011, Pages 388-392

Highly glycosylated tumour antigens: Interactions with the immune system

Author keywords

C type lectin; Cancer; Carcinoembryonic antigen (CEA); Dendritic cell; Glycosylation; Mucin

Indexed keywords

CARBOHYDRATE BINDING PROTEIN; LECTIN RECEPTOR; LECTIN RECEPTOR C TYPE; TUMOR ANTIGEN; UNCLASSIFIED DRUG;

EID: 79551484543     PISSN: 03005127     EISSN: 14708752     Source Type: Journal    
DOI: 10.1042/BST0390388     Document Type: Conference Paper
Times cited : (6)

References (50)
  • 1
    • 33748195979 scopus 로고    scopus 로고
    • Glycosylation in cellular mechanisms of health and disease
    • Ohtsubo, K. and Marth, J.D. (2006) Glycosylation in cellular mechanisms of health and disease. Cell 126, 855-867
    • (2006) Cell , vol.126 , pp. 855-867
    • Ohtsubo, K.1    Marth, J.D.2
  • 2
    • 0018149657 scopus 로고
    • Blood group substances as tumor antigens in the distal colon
    • Cooper, H.S. and Haesler, Jr, W.E. (1978) Blood group substances as tumor antigens in the distal colon. Am. J. Clin. Pathol. 69, 594-598
    • (1978) Am. J. Clin. Pathol. , vol.69 , pp. 594-598
    • Cooper, H.S.1    Haesler Jr., W.E.2
  • 3
    • 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, N.F., Spendlove, I., Ellis, I. and Durrant, L.G. (2005) High expression of Lewis y/b antigens is associated with decreased survival in lymph node negative breast carcinomas. Breast Cancer Res. 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
  • 4
    • 0028988064 scopus 로고
    • Expression of sialyl Lewisa as a new prognostic factor for patients with advanced colorectal carcinoma
    • Nakayama, T., Watanabe, M., Katsumata, T., Teramoto, T. and Kitajima, M. (1995) Expression of sialyl Lewisa as a new prognostic factor for patients with advanced colorectal carcinoma. Cancer 75, 2051-2056
    • (1995) Cancer , vol.75 , pp. 2051-2056
    • Nakayama, T.1    Watanabe, M.2    Katsumata, T.3    Teramoto, T.4    Kitajima, M.5
  • 7
    • 0025765750 scopus 로고
    • Prediction of lymph node involvement in breast cancer by detection of altered glycosylation in the primary tumour
    • Brooks, S.A. and Leathem, A.J. (1991) Prediction of lymph node involvement in breast cancer by detection of altered glycosylation in the primary tumour. Lancet 338, 71-74
    • (1991) Lancet , vol.338 , pp. 71-74
    • Brooks, S.A.1    Leathem, A.J.2
  • 8
    • 0023278648 scopus 로고
    • Helix pomatia and Ulex europaeus lectin binding in human breast carcinoma
    • Fenlon, S., Ellis, I.O., Bell, J., Todd, J.H., Elston, C.W. and Blamey, R.W. (1987) Helix pomatia and Ulex europaeus lectin binding in human breast carcinoma. J. Pathol. 152, 169-176
    • (1987) J. Pathol. , vol.152 , pp. 169-176
    • Fenlon, S.1    Ellis, I.O.2    Bell, J.3    Todd, J.H.4    Elston, C.W.5    Blamey, R.W.6
  • 10
    • 0033057177 scopus 로고    scopus 로고
    • The carcinoembryonic antigen (CEA) family: Structures, suggested functions and expression in normal and malignant tissues
    • Hammarstrom, S. (1999) The carcinoembryonic antigen (CEA) family: structures, suggested functions and expression in normal and malignant tissues. Semin. Cancer Biol. 9, 67-81
    • (1999) Semin. Cancer Biol. , vol.9 , pp. 67-81
    • Hammarstrom, S.1
  • 11
    • 61849174789 scopus 로고    scopus 로고
    • Glycoproteomics for prostate cancer detection: Changes in serum PSA glycosylation patterns
    • Meany, D.L., Zhang, Z., Sokoll, L.J., Zhang, H. and Chan, D.W. (2009) Glycoproteomics for prostate cancer detection: changes in serum PSA glycosylation patterns. J. Proteome Res. 8, 613-619
    • (2009) J. Proteome Res. , vol.8 , pp. 613-619
    • Meany, D.L.1    Zhang, Z.2    Sokoll, L.J.3    Zhang, H.4    Chan, D.W.5
  • 13
    • 1542269032 scopus 로고    scopus 로고
    • High preoperative CA 15-3 concentrations predict adverse outcome in node-negative and node-positive breast cancer: Study of 600 patients with histologically confirmed breast cancer
    • Duffy, M.J., Duggan, C., Keane, R., Hill, A.D., McDermott, E., Crown, J. and O'Higgins, N. (2004) High preoperative CA 15-3 concentrations predict adverse outcome in node-negative and node-positive breast cancer: study of 600 patients with histologically confirmed breast cancer. Clin. Chem. 50, 559-563
    • (2004) Clin. Chem. , vol.50 , pp. 559-563
    • Duffy, M.J.1    Duggan, C.2    Keane, R.3    Hill, A.D.4    McDermott, E.5    Crown, J.6    O'Higgins, N.7
  • 14
    • 0029417269 scopus 로고
    • The epithelial mucin, MUC1, of milk, mammary gland and other tissues
    • Patton, S., Gendler, S.J. and Spicer, A.P. (1995) The epithelial mucin, MUC1, of milk, mammary gland and other tissues. Biochim. Biophys. Acta 1241, 407-423
    • (1995) Biochim. Biophys. Acta , vol.1241 , pp. 407-423
    • Patton, S.1    Gendler, S.J.2    Spicer, A.P.3
  • 16
    • 0026264928 scopus 로고
    • Carbohydrate antigens on cancer-associated mucin-like molecules
    • Ho, S.B. and Kim, Y.S. (1991) Carbohydrate antigens on cancer-associated mucin-like molecules. Semin. Cancer Biol. 2, 389-400
    • (1991) Semin. Cancer Biol. , vol.2 , pp. 389-400
    • Ho, S.B.1    Kim, Y.S.2
  • 17
    • 0030466993 scopus 로고    scopus 로고
    • Comparison of O-linked carbohydrate chains in MUC-1 mucin from normal breast epithelial cell lines and breast carcinoma cell lines: Demonstration of simpler and fewer glycan chains in tumor cells
    • Lloyd, K.O., Burchell, J., Kudryashov, V., Yin, B.W. and Taylor-Papadimitriou, J. (1996) Comparison of O-linked carbohydrate chains in MUC-1 mucin from normal breast epithelial cell lines and breast carcinoma cell lines: demonstration of simpler and fewer glycan chains in tumor cells. J. Biol. Chem. 271, 33325-33334
    • (1996) J. Biol. Chem. , vol.271 , pp. 33325-33334
    • Lloyd, K.O.1    Burchell, J.2    Kudryashov, V.3    Yin, B.W.4    Taylor-Papadimitriou, J.5
  • 18
    • 0023177138 scopus 로고
    • Isolation and characterization of full-length functional cDNA clones for human carcinoembryonic antigen
    • Beauchemin, N., Benchimol, S., Cournoyer, D., Fuks, A. and Stanners, C.P. (1987) Isolation and characterization of full-length functional cDNA clones for human carcinoembryonic antigen. Mol. Cell. Biol. 7, 3221-3230
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 3221-3230
    • Beauchemin, N.1    Benchimol, S.2    Cournoyer, D.3    Fuks, A.4    Stanners, C.P.5
  • 20
    • 0034234257 scopus 로고    scopus 로고
    • Human carcinoembryonic antigen functions as a general inhibitor of anoikis
    • Ordonez, C., Screaton, R.A., Ilantzis, C. and Stanners, C.P. (2000) Human carcinoembryonic antigen functions as a general inhibitor of anoikis. Cancer Res. 60, 3419-3424
    • (2000) Cancer Res. , vol.60 , pp. 3419-3424
    • Ordonez, C.1    Screaton, R.A.2    Ilantzis, C.3    Stanners, C.P.4
  • 21
    • 0344443683 scopus 로고    scopus 로고
    • Tumor markers and colorectal cancer: Utility in management
    • Crawford, N.P., Colliver, D.W. and Galandiuk, S. (2003) Tumor markers and colorectal cancer: utility in management. J. Surg. Oncol. 84, 239-248
    • (2003) J. Surg. Oncol. , vol.84 , pp. 239-248
    • Crawford, N.P.1    Colliver, D.W.2    Galandiuk, S.3
  • 22
    • 33749000327 scopus 로고    scopus 로고
    • Immunomodulatory roles of the carcinoembryonic antigen family of glycoproteins
    • Shao, L., Allez, M., Park, M.S. and Mayer, L. (2006) Immunomodulatory roles of the carcinoembryonic antigen family of glycoproteins. Ann. N.Y. Acad. Sci. 1072, 194-209
    • (2006) Ann. N.Y. Acad. Sci. , vol.1072 , pp. 194-209
    • Shao, L.1    Allez, M.2    Park, M.S.3    Mayer, L.4
  • 23
    • 0022382629 scopus 로고
    • Carbohydrate determinants associated with carcinoembryonic antigen (CEA)
    • Nichols, E.J., Kannagi, R., Hakomori, S.I., Krantz, M.J. and Fuks, A. (1985) Carbohydrate determinants associated with carcinoembryonic antigen (CEA). J. Immunol. 135, 1911-1913
    • (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
  • 24
    • 0023221836 scopus 로고
    • Structural studies of the carbohydrate moieties of carcinoembryonic antigens
    • Yamashita, K., Totani, K., Kuroki, M., Matsuoka, Y., Ueda, I. and Kobata, A. (1987) Structural studies of the carbohydrate moieties of carcinoembryonic antigens. Cancer Res. 47, 3451-3459
    • (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
  • 25
    • 0030745147 scopus 로고    scopus 로고
    • Perspectives on the significance of altered glycosylation of glycoproteins in cancer
    • Kim, Y.J. and Varki, A. (1997) Perspectives on the significance of altered glycosylation of glycoproteins in cancer. Glycoconjugate J. 14, 569-576
    • (1997) Glycoconjugate J. , vol.14 , pp. 569-576
    • Kim, Y.J.1    Varki, A.2
  • 26
    • 0032546352 scopus 로고    scopus 로고
    • Dendritic cells and the control of immunity
    • Banchereau, J. and Steinman, R.M. (1998) Dendritic cells and the control of immunity. Nature 392, 245-252
    • (1998) Nature , vol.392 , pp. 245-252
    • Banchereau, J.1    Steinman, R.M.2
  • 27
    • 44049095632 scopus 로고    scopus 로고
    • Protein-glycan interactions in the control of innate and adaptive immune responses
    • van Kooyk, Y. and Rabinovich, G.A. (2008) Protein-glycan interactions in the control of innate and adaptive immune responses. Nat. Immunol. 9, 593-601
    • (2008) Nat. Immunol. , vol.9 , pp. 593-601
    • Van Kooyk, Y.1    Rabinovich, G.A.2
  • 28
    • 29144452851 scopus 로고    scopus 로고
    • The C-type lectin-like domain superfamily
    • Zelensky, A.N. and Gready, J.E. (2005) The C-type lectin-like domain superfamily. FEBS J. 272, 6179-6217
    • (2005) FEBS J. , vol.272 , pp. 6179-6217
    • Zelensky, A.N.1    Gready, J.E.2
  • 29
    • 21344449731 scopus 로고    scopus 로고
    • Dendritic cells recognize tumor-specific glycosylation of carcinoembryonic antigen on colorectal cancer cells through dendritic cell-specific intercellular adhesion molecule-3-grabbing nonintegrin
    • van Gisbergen, K.P., Aarnoudse, C.A., Meijer, G.A., Geijtenbeek, T.B. and van Kooyk, Y. (2005) Dendritic cells recognize tumor-specific glycosylation of carcinoembryonic antigen on colorectal cancer cells through dendritic cell-specific intercellular adhesion molecule-3-grabbing nonintegrin. Cancer Res. 65, 5935-5944
    • (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
  • 31
    • 67649781789 scopus 로고    scopus 로고
    • Endogenous ligands for C-type lectin receptors: The true regulators of immune homeostasis
    • Garcia-Vallejo, J.J. and van Kooyk, Y. (2009) Endogenous ligands for C-type lectin receptors: the true regulators of immune homeostasis. Immunol. Rev. 230, 22-37
    • (2009) Immunol. Rev. , vol.230 , pp. 22-37
    • Garcia-Vallejo, J.J.1    Van Kooyk, Y.2
  • 33
    • 34548593215 scopus 로고    scopus 로고
    • Tumor-associated Tn-MUC1 glycoform is internalized through the macrophage galactose-type C-type lectin and delivered to the HLA class I and II compartments in dendritic cells
    • Napoletano, C., Rughetti, A., Gervig Tarp, M.P., Coleman, J., Bennett, E.P., Picco, G., Sale, P., da-Nagai, K., Irimura, T., Mandel, U. et al. (2007) Tumor-associated Tn-MUC1 glycoform is internalized through the macrophage galactose-type C-type lectin and delivered to the HLA class I and II compartments in dendritic cells. Cancer Res. 67, 8358-8367
    • (2007) Cancer Res. , vol.67 , pp. 8358-8367
    • Napoletano, C.1    Rughetti, A.2    Gervig Tarp, M.P.3    Coleman, J.4    Bennett, E.P.5    Picco, G.6    Sale, P.7    Da-Nagai, K.8    Irimura, T.9    Mandel, U.10
  • 34
    • 67649840704 scopus 로고    scopus 로고
    • Signalling through C-type lectin receptors: Shaping immune responses
    • Geijtenbeek, T.B. and Gringhuis, S.I. (2009) Signalling through C-type lectin receptors: shaping immune responses. Nat. Rev. Immunol. 9, 465-479
    • (2009) Nat. Rev. Immunol. , vol.9 , pp. 465-479
    • Geijtenbeek, T.B.1    Gringhuis, S.I.2
  • 35
    • 34248544993 scopus 로고    scopus 로고
    • C-type lectin DC-SIGN modulates Toll-like receptor signaling via Raf-1 kinase-dependent acetylation of transcription factor NF-κB
    • Gringhuis, S.I., den Dunnen, J., Litjens, M., van het Hof, B., van Kooyk, Y. and Geijtenbeek, T.B. (2007) C-type lectin DC-SIGN modulates Toll-like receptor signaling via Raf-1 kinase-dependent acetylation of transcription factor NF-κB. Immunity 26, 605-616
    • (2007) Immunity , vol.26 , pp. 605-616
    • Gringhuis, S.I.1    Den Dunnen, J.2    Litjens, M.3    Van Het Hof, B.4    Van Kooyk, Y.5    Geijtenbeek, T.B.6
  • 36
    • 23744481998 scopus 로고    scopus 로고
    • Effective induction of naive and recall T-cell responses by targeting antigen to human dendritic cells via a humanized anti-DC-SIGN antibody
    • Tacken, P.J., de Vries, I., Gijzen, K., Joosten, B., Wu, D., Rother, R.P., Faas, S.J., Punt, C.J., Torensma, R., Adema, G.J. and Figdor, C.G. (2005) Effective induction of naive and recall T-cell responses by targeting antigen to human dendritic cells via a humanized anti-DC-SIGN antibody. Blood 106, 1278-1285
    • (2005) Blood , vol.106 , pp. 1278-1285
    • Tacken, P.J.1    De Vries, I.2    Gijzen, K.3    Joosten, B.4    Wu, D.5    Rother, R.P.6    Faas, S.J.7    Punt, C.J.8    Torensma, R.9    Adema, G.J.10    Figdor, C.G.11
  • 40
    • 71649109998 scopus 로고    scopus 로고
    • Dendritic cells integrate signals from the tumor microenvironment to modulate immunity and tumor growth
    • Lin, A., Schildknecht, A., Nguyen, L.T. and Ohashi, P.S. (2010) Dendritic cells integrate signals from the tumor microenvironment to modulate immunity and tumor growth. Immunol. Lett. 127, 77-84
    • (2010) Immunol. Lett. , vol.127 , pp. 77-84
    • Lin, A.1    Schildknecht, A.2    Nguyen, L.T.3    Ohashi, P.S.4
  • 43
    • 0037047438 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a novel mouse macrophage C-type lectin, mMGL2, which has a distinct carbohydrate specificity from mMGL1
    • Tsuiji, M., Fujimori, M., Ohashi, Y., Higashi, N., Onami, T.M., Hedrick, S.M. and Irimura, T. (2002) Molecular cloning and characterization of a novel mouse macrophage C-type lectin, mMGL2, which has a distinct carbohydrate specificity from mMGL1. J. Biol. Chem. 277, 28892-28901
    • (2002) J. Biol. Chem. , vol.277 , pp. 28892-28901
    • Tsuiji, M.1    Fujimori, M.2    Ohashi, Y.3    Higashi, N.4    Onami, T.M.5    Hedrick, S.M.6    Irimura, T.7
  • 44
    • 79551477301 scopus 로고    scopus 로고
    • Tumour-associated glycan modifications of antigen enhance MGL2 dependent uptake and MHC class I restricted CD8 T cell responses
    • doi:10.1002/ijc.25458
    • Singh, S.K., Streng-Ouwehand, I., Litjens, M., Kalay, H., Saeland, E. and van Kooyk, Y. (2010) Tumour-associated glycan modifications of antigen enhance MGL2 dependent uptake and MHC class I restricted CD8 T cell responses. Int. J. Cancer, doi:10.1002/ijc.25458
    • (2010) Int. J. Cancer
    • Singh, S.K.1    Streng-Ouwehand, I.2    Litjens, M.3    Kalay, H.4    Saeland, E.5    Van Kooyk, Y.6
  • 45
    • 33747366158 scopus 로고    scopus 로고
    • Differential regulation of C-type lectin expression on tolerogenic dendritic cell subsets
    • van Vliet, S.J., van Liempt, E., Geijtenbeek, T.B. and van Kooyk, Y. (2006) Differential regulation of C-type lectin expression on tolerogenic dendritic cell subsets. Immunobiology 211, 577-585
    • (2006) Immunobiology , vol.211 , pp. 577-585
    • Van Vliet, S.J.1    Van Liempt, E.2    Geijtenbeek, T.B.3    Van Kooyk, Y.4
  • 46
    • 33646343959 scopus 로고    scopus 로고
    • Fucosylated haptoglobin is a novel marker for pancreatic cancer: A detailed analysis of the oligosaccharide structure and a possible mechanism for fucosylation
    • Okuyama, N., Ide, Y., Nakano, M., Nakagawa, T., Yamanaka, K., Moriwaki, K., Murata, K., Ohigashi, H., Yokoyama, S., Eguchi, H. et al. (2006) Fucosylated haptoglobin is a novel marker for pancreatic cancer: a detailed analysis of the oligosaccharide structure and a possible mechanism for fucosylation. Int. J. Cancer 118, 2803-2808
    • (2006) Int. J. Cancer , vol.118 , pp. 2803-2808
    • Okuyama, N.1    Ide, Y.2    Nakano, M.3    Nakagawa, T.4    Yamanaka, K.5    Moriwaki, K.6    Murata, K.7    Ohigashi, H.8    Yokoyama, S.9    Eguchi, H.10
  • 47
    • 77957750584 scopus 로고    scopus 로고
    • A sensitive assay to measure biomarker glycosylation demonstrates increased fucosylation of prostate-specific antigen (PSA) in patients with prostate cancer compared with benign prostatic hyperplasia
    • Dwek, M.V., Jenks, A. and Leathem, A.J. (2010) A sensitive assay to measure biomarker glycosylation demonstrates increased fucosylation of prostate-specific antigen (PSA) in patients with prostate cancer compared with benign prostatic hyperplasia. Clin. Chim. Acta 411, 1935-1939
    • (2010) Clin. Chim. Acta , vol.411 , pp. 1935-1939
    • Dwek, M.V.1    Jenks, A.2    Leathem, A.J.3
  • 49
    • 77952299239 scopus 로고    scopus 로고
    • α1,2-Fucosylated and β-N-acetylgalactosaminylated prostate-specific antigen as an efficient marker of prostatic cancer
    • Fukushima, K., Satoh, T., Baba, S. and Yamashita, K. (2010) α1,2-Fucosylated and β-N-acetylgalactosaminylated prostate-specific antigen as an efficient marker of prostatic cancer. Glycobiology 20, 452-460
    • (2010) Glycobiology , vol.20 , pp. 452-460
    • Fukushima, K.1    Satoh, T.2    Baba, S.3    Yamashita, K.4
  • 50
    • 70350000599 scopus 로고    scopus 로고
    • Structural insights into what glycan arrays tell us about how glycan-binding proteins interact with their ligands
    • Taylor, M.E. and Drickamer, K. (2009) Structural insights into what glycan arrays tell us about how glycan-binding proteins interact with their ligands. Glycobiology 19, 1155-1162
    • (2009) Glycobiology , vol.19 , pp. 1155-1162
    • Taylor, M.E.1    Drickamer, K.2


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