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Volumn 44, Issue 12, 2011, Pages 772-781

Branched N-glycans and their implications for cell adhesion, signaling and clinical applications for cancer biomarkers and in therapeutics

Author keywords

Antibody therapy; Branched N glycans; Cancer biomarker; Growth factor receptors; N acetylglucosaminyltransferases

Indexed keywords

POLYSACCHARIDE; TUMOR MARKER;

EID: 84857692860     PISSN: 19766696     EISSN: 1976670X     Source Type: Journal    
DOI: 10.5483/BMBRep.2011.44.12.772     Document Type: Short Survey
Times cited : (102)

References (100)
  • 1
    • 0032754473 scopus 로고    scopus 로고
    • On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database
    • Apweiler, R., Hermjakob, H. and Sharon, N. (1999) On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database. Biochim. Biopys. Acta. 1473, 4-8.
    • (1999) Biochim. Biopys. Acta. , vol.1473 , pp. 4-8
    • Apweiler, R.1    Hermjakob, H.2    Sharon, N.3
  • 2
    • 0035260226 scopus 로고    scopus 로고
    • A glycomic approach to the identification and characterization of glycoprotein function in cells transfected with glycosyltransferase genes
    • Tanichi, N., Ekuni, A., Ko, J. H., Miyoshi, E., Ikeda, Y., Ihara, Y., Nishikawa, A., Honke, K. and Takahashi, M. (2001) A glycomic approach to the identification and characterization of glycoprotein function in cells transfected with glycosyltransferase genes. Proteomics 1, 239-247.
    • (2001) Proteomics , vol.1 , pp. 239-247
    • Tanichi, N.1    Ekuni, A.2    Ko, J.H.3    Miyoshi, E.4    Ikeda, Y.5    Ihara, Y.6    Nishikawa, A.7    Honke, K.8    Takahashi, M.9
  • 3
    • 2342504656 scopus 로고    scopus 로고
    • Functional glycomics and evidence for gain- and loss-of-functions of target proteins for glycosyltransferases involved in N-glycan biosynthesis: their pivotal roles in growth and development, cancer metastasis and antibody therapy against cancer proceedings of the Japan Academy
    • Tanichi, N., Takahashi, M., Miyoshi, E., , J. and Matsumoto, A. (2004) Functional glycomics and evidence for gain- and loss-of-functions of target proteins for glycosyltransferases involved in N-glycan biosynthesis: their pivotal roles in growth and development, cancer metastasis and antibody therapy against cancer proceedings of the Japan Academy. Series B 80, 82-91.
    • (2004) Series B , vol.80 , pp. 82-91
    • Tanichi, N.1    Takahashi, M.2    Miyoshi, E.J.3    Matsumoto, A.4
  • 4
    • 0035526266 scopus 로고    scopus 로고
    • Implication of GnT-V in cancer metastasis: a glycomic approach for identification of a target protein and its unique function as an angiogenic cofactor
    • Tanichi, N., Ihara, S., Saito, T., Miyoshi, E., Ikeda, Y. and Honke, K. (2001) Implication of GnT-V in cancer metastasis: a glycomic approach for identification of a target protein and its unique function as an angiogenic cofactor. Glycoconj. J. 18, 859-865.
    • (2001) Glycoconj. J. , vol.18 , pp. 859-865
    • Tanichi, N.1    Ihara, S.2    Saito, T.3    Miyoshi, E.4    Ikeda, Y.5    Honke, K.6
  • 5
    • 84857762965 scopus 로고    scopus 로고
    • Implication of N-acetylglucosaminyltransferases III and V in Cancer: Gene relation and signaling mechanism
    • Tanichi, N., Miyoshi, E., Ko, J. H., Ikeda, Y. and Ihara, Y. (1999) Implication of N-acetylglucosaminyltransferases III and V in Cancer: Gene relation and signaling mechanism. Biochim. Biophys. Acta (Review). 1473, 9-20.
    • (1999) Biochim. Biophys. Acta (Review). , vol.1473 , pp. 9-20
    • Tanichi, N.1    Miyoshi, E.2    Ko, J.H.3    Ikeda, Y.4    Ihara, Y.5
  • 6
    • 42449143890 scopus 로고    scopus 로고
    • Branched N-glycans relate the biological functions of integrins and cadherins
    • Zhao, Y., Sato, Y., Isaji, T., Fukuda, T., Matsumoto, A., Miyoshi, E., , J. and Tanichi, N. (2008) Branched N-glycans relate the biological functions of integrins and cadherins. FEBS J. 275, 1939-1948.
    • (2008) FEBS J , vol.275 , pp. 1939-1948
    • Zhao, Y.1    Sato, Y.2    Isaji, T.3    Fukuda, T.4    Matsumoto, A.5    Miyoshi, E.J.6    Tanichi, N.7
  • 7
  • 8
    • 71749098786 scopus 로고    scopus 로고
    • From the gamma-glutamyl cycle to the glycan cycle: a road with many turns and pleasant surprises
    • Tanichi, N. (2009) From the gamma-glutamyl cycle to the glycan cycle: a road with many turns and pleasant surprises. J. Biol. Chem. 284, 34469-34478.
    • (2009) J. Biol. Chem. , vol.284 , pp. 34469-34478
    • Tanichi, N.1
  • 9
    • 0022462129 scopus 로고
    • Biosynthetic controls that determine the branching and microheterogeneity of protein-bound oligosaccharides
    • Schachter, H. (1986) Biosynthetic controls that determine the branching and microheterogeneity of protein-bound oligosaccharides. Biochem. Cell Biol. 64, 163-181.
    • (1986) Biochem. Cell Biol. , vol.64 , pp. 163-181
    • Schachter, H.1
  • 10
    • 67649839223 scopus 로고    scopus 로고
    • N-Glycans
    • 2nd ed. Cold Spring Harbor Laboratory Press, New York, USA
    • Stanley, P., Schachter, H. and Tanichi, N. (2009) N-Glycans; In Essentials of Glycobiology. 2nd ed: pp. 101-114 Cold Spring Harbor Laboratory Press, New York, USA.
    • (2009) Essentials of Glycobiology , pp. 101-114
    • Stanley, P.1    Schachter, H.2    Tanichi, N.3
  • 11
    • 0020373041 scopus 로고
    • Control of glycoprotein synthesis. UDP-GlcNAc: glycopeptide beta 4-N-acetylglucosaminyltransferase III, an enzyme in hen oviduct which adds GlcNAc in beta 1-4 linkage to the beta-linked mannose of the trimannosyl core of N-glycosyl oligosaccharides
    • Narasimhan, S. (1982) Control of glycoprotein synthesis. UDP-GlcNAc: glycopeptide beta 4-N-acetylglucosaminyltransferase III, an enzyme in hen oviduct which adds GlcNAc in beta 1-4 linkage to the beta-linked mannose of the trimannosyl core of N-glycosyl oligosaccharides. J. Biol. Chem. 257, 10235-10242.
    • (1982) J. Biol. Chem. , vol.257 , pp. 10235-10242
    • Narasimhan, S.1
  • 12
    • 0021112027 scopus 로고
    • Oligosaccharide branching of glycoproteins: biosynthetic mechanisms and possible biological functions
    • Gleeson, P. A. and Schachter, H. (1983) Oligosaccharide branching of glycoproteins: biosynthetic mechanisms and possible biological functions. J. Biol. Chem. 258, 6162-6173.
    • (1983) J. Biol. Chem. , vol.258 , pp. 6162-6173
    • Gleeson, P.A.1    Schachter, H.2
  • 13
    • 0031627519 scopus 로고    scopus 로고
    • Gamma-Glutamyl transpeptidase: catalytic mechanism and gene expression
    • Tanichi, N. and Ikeda, Y. (1998) Gamma-Glutamyl transpeptidase: catalytic mechanism and gene expression. Adv. Enzymol. Related Areas Mol. Biol. 72, 239-278.
    • (1998) Adv. Enzymol. Related Areas Mol. Biol. , vol.72 , pp. 239-278
    • Tanichi, N.1    Ikeda, Y.2
  • 14
    • 0019393291 scopus 로고
    • Physiochemical and immunochemical characterization of gamma-glutamyl transpeptidase from yolk sak tumor and ascitic hepatoma (AH-66) cells
    • Yokosawa, N., Tanichi, N., Tsukada, Y. and Makita, A. (1981) Physiochemical and immunochemical characterization of gamma-glutamyl transpeptidase from yolk sak tumor and ascitic hepatoma (AH-66) cells. Oncodev. Biol. Med. 2, 165-177.
    • (1981) Oncodev. Biol. Med. , vol.2 , pp. 165-177
    • Yokosawa, N.1    Tanichi, N.2    Tsukada, Y.3    Makita, A.4
  • 15
    • 0021039987 scopus 로고
    • Comparative study of the sugar chains of gamma-glutamyltranspeptidases purified from rat liver and rat AH-66 hepatoma cells
    • Yamashita, K., Hitoi, A., Tanichi, N., Yokosawa, N., Tsukada, Y. and Kobata, A. (1983) Comparative study of the sugar chains of gamma-glutamyltranspeptidases purified from rat liver and rat AH-66 hepatoma cells. Cancer Res. 43, 5059-5063.
    • (1983) Cancer Res , vol.43 , pp. 5059-5063
    • Yamashita, K.1    Hitoi, A.2    Tanichi, N.3    Yokosawa, N.4    Tsukada, Y.5    Kobata, A.6
  • 16
    • 0021308647 scopus 로고
    • Reexamination of the pyridylamination used for fluorescence labeling of oligosaccharides and its application to glycoproteins
    • Hase, S., Ibuki, T. and Ikenaka, T. (1984) Reexamination of the pyridylamination used for fluorescence labeling of oligosaccharides and its application to glycoproteins. J. Biochem. 95, 197-203.
    • (1984) J. Biochem. , vol.95 , pp. 197-203
    • Hase, S.1    Ibuki, T.2    Ikenaka, T.3
  • 17
    • 0023917263 scopus 로고
    • A method for the determination of N-acetylglucosaminyltransferase III activity in rat tissues involving HPLC
    • Nishikawa, A., Fujii, S., Sugiyama, T. and Tanichi, N. (1988) A method for the determination of N-acetylglucosaminyltransferase III activity in rat tissues involving HPLC. Anal. Biochem. 170, 349-354.
    • (1988) Anal. Biochem. , vol.170 , pp. 349-354
    • Nishikawa, A.1    Fujii, S.2    Sugiyama, T.3    Tanichi, N.4
  • 18
    • 0024840851 scopus 로고
    • Glycosyltransferase assays using pyridylaminated acceptors: N-acetylglucosaminyltransferase III, IV, and V
    • Tanichi, N., Nishikawa, A., Fujii, S. and , J. (1989) Glycosyltransferase assays using pyridylaminated acceptors: N-acetylglucosaminyltransferase III, IV, and V. Methods Enzymol. 179, 397-408.
    • (1989) Methods Enzymol , vol.179 , pp. 397-408
    • Tanichi, N.1    Nishikawa, A.2    Fujii, S.J.3
  • 19
    • 0025002487 scopus 로고
    • Determination of N-acetylglucosaminyltransferases III IV and V in normal and hepatoma tissues of rats
    • Nishikawa, A., , J., Fujii, S. and Tanichi, N. (1990) Determination of N-acetylglucosaminyltransferases III, IV and V in normal and hepatoma tissues of rats. Biochim. Biophys. Acta 1035, 313-318.
    • (1990) Biochim. Biophys. Acta , vol.1035 , pp. 313-318
    • Nishikawa, A.J.1    Fujii, S.2    Tanichi, N.3
  • 20
    • 0026705382 scopus 로고
    • Purification, cDNA cloning, and expression of UDP-N-acetylglucosamine: alpha-D-mannoside beta-1 4N-acetylglucosaminyltransferase III from rat kidney
    • Nishikawa, A., Ihara, Y., Hatakeyama, M., Kangawa, K. and Tanichi, N. (1992) Purification, cDNA cloning, and expression of UDP-N-acetylglucosamine: alpha-D-mannoside beta-1, 4N-acetylglucosaminyltransferase III from rat kidney. J. Biol. Chem. 267, 18199-18204.
    • (1992) J. Biol. Chem. , vol.267 , pp. 18199-18204
    • Nishikawa, A.1    Ihara, Y.2    Hatakeyama, M.3    Kangawa, K.4    Tanichi, N.5
  • 22
    • 0029027831 scopus 로고
    • Suppression of lung metastasis of B16 mouse melanoma by N-acetylglucosaminyltransferase III gene transfection
    • Yoshimura, M., Nishikawa, A., Ihara, Y., Tanichi, S. and Tanichi, N. (1995) Suppression of lung metastasis of B16 mouse melanoma by N-acetylglucosaminyltransferase III gene transfection. Proc. Natl. Acad. Sci. U.S.A. 92, 8754-8758.
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 8754-8758
    • Yoshimura, M.1    Nishikawa, A.2    Ihara, Y.3    Tanichi, S.4    Tanichi, N.5
  • 23
    • 0029933659 scopus 로고    scopus 로고
    • Aberrant glycosylation of E-cadherin enhances cell-cell binding to suppress metastasis
    • Yoshimura, M., Ihara, Y., Matsuzawa, Y. and Tanichi, N. (1996) Aberrant glycosylation of E-cadherin enhances cell-cell binding to suppress metastasis. J. Biol. Chem. 271, 13811-13815.
    • (1996) J. Biol. Chem. , vol.271 , pp. 13811-13815
    • Yoshimura, M.1    Ihara, Y.2    Matsuzawa, Y.3    Tanichi, N.4
  • 25
    • 33744958178 scopus 로고    scopus 로고
    • Cell-cell interaction-dependent relation of N-acetylglucosaminyltransferase III and the bisected N-glycans in GEii epithelial cells. Involvement of E-cadherin-mediated cell adhesion
    • Iijima, J., Zhao, Y., Isaji, T., Kameyama, A., Nakaya, S., Wang, X., Ihara, H., Cheng, X., Nakagawa, T., Miyoshi, E. and Kondo, A. (2006) Cell-cell interaction-dependent relation of N-acetylglucosaminyltransferase III and the bisected N-glycans in GEii epithelial cells. Involvement of E-cadherin-mediated cell adhesion. J. Biol. Chem. 281, 13038-13046.
    • (2006) J. Biol. Chem. , vol.281 , pp. 13038-13046
    • Iijima, J.1    Zhao, Y.2    Isaji, T.3    Kameyama, A.4    Nakaya, S.5    Wang, X.6    Ihara, H.7    Cheng, X.8    Nakagawa, T.9    Miyoshi, E.10    Kondo, A.11
  • 26
    • 77956160590 scopus 로고    scopus 로고
    • Functional roles of the bisecting GlcNAc in integrinmediated cell adhesion
    • Isaji, T., Kariya, Y., Xu, Q., Fukuda, T., Tanichi, N. and , J. (2010) Functional roles of the bisecting GlcNAc in integrinmediated cell adhesion. Methods Enzymol. 480, 445-459.
    • (2010) Methods Enzymol , vol.480 , pp. 445-459
    • Isaji, T.1    Kariya, Y.2    Xu, Q.3    Fukuda, T.4    Tanichi, N.J.5
  • 27
    • 33845961737 scopus 로고    scopus 로고
    • N-acetylglucosaminyltransferase III antagonizes the effect of N-acetylglucosaminyltransferase V on alpha3beta1 integrin-mediated cell migration
    • Zhao, Y., Nakagawa, T., Itoh, S., Inamori, K., Isaji, T., Kariya, Y., Kondo, A., Miyoshi, E., Miyazaki, K., Kawasaki, N., Tanichi, N. and , J.(2006) N-acetylglucosaminyltransferase III antagonizes the effect of N-acetylglucosaminyltransferase V on alpha3beta1 integrin-mediated cell migration. J. Biol. Chem. 281, 32122-32130.
    • (2006) J. Biol. Chem. , vol.281 , pp. 32122-32130
    • Zhao, Y.1    Nakagawa, T.2    Itoh, S.3    Inamori, K.4    Isaji, T.5    Kariya, Y.6    Kondo, A.7    Miyoshi, E.8    Miyazaki, K.9    Kawasaki, N.10    Tanichi, N.J.11
  • 28
    • 0035853845 scopus 로고    scopus 로고
    • An N-glycosylation site on the beta-propeller domain of the integrin alpha5 subunit plays key roles in both its function and site-specific modification by beta1, 4-N-acetylglucosaminyltransferase III
    • Sato, Y., Isaji, T., Tajiri, M., Yoshida-Yamamoto, S., Yoshinaka, T., Somehara, T., Fukuda, T., Wada, Y. and , J. (2001) An N-glycosylation site on the beta-propeller domain of the integrin alpha5 subunit plays key roles in both its function and site-specific modification by beta1,4-N-acetylglucosaminyltransferase III. J. Biol. Chem. 276, 11956-11962.
    • (2001) J. Biol. Chem. , vol.276 , pp. 11956-11962
    • Sato, Y.1    Isaji, T.2    Tajiri, M.3    Yoshida-Yamamoto, S.4    Yoshinaka, T.5    Somehara, T.6    Fukuda, T.7    Wada, Y.J.8
  • 29
    • 84857715276 scopus 로고    scopus 로고
    • Bisecting GlcNAc residues on laminin-332 down-relate galectin-3-dependent keratinocyte motility
    • Kariya, Y., Kawamura, C., Tabei, T. and , J. (2010) Bisecting GlcNAc residues on laminin-332 down-relate galectin-3-dependent keratinocyte motility. J. Biol. Chem. 286, 4310-4318.
    • (2010) J. Biol. Chem. , vol.286 , pp. 4310-4318
    • Kariya, Y.1    Kawamura, C.2    Tabei, T.J.3
  • 30
    • 0035853845 scopus 로고    scopus 로고
    • Overexpression of N-acetylglucosaminyltransferase III enhances the epidermal growth factor-induced phosphorylation of ERK in HeLaS3 cells by up-relation of the internalization rate of the receptors
    • Sato, Y., Takahashi, M., Shibukawa, Y., Jain, S. K., Hamaoka, R., Miyagawa, J., Yaginuma, Y., Honke, K., Ishikawa, M. and Tanichi, N. (2001) Overexpression of N-acetylglucosaminyltransferase III enhances the epidermal growth factor-induced phosphorylation of ERK in HeLaS3 cells by up-relation of the internalization rate of the receptors. J. Biol. Chem. 276, 11956-11962.
    • (2001) J. Biol. Chem. , vol.276 , pp. 11956-11962
    • Sato, Y.1    Takahashi, M.2    Shibukawa, Y.3    Jain, S.K.4    Hamaoka, R.5    Miyagawa, J.6    Yaginuma, Y.7    Honke, K.8    Ishikawa, M.9    Tanichi, N.10
  • 32
    • 68249103612 scopus 로고    scopus 로고
    • Core fucose and bisecting GlcNAc, the direct modifiers of the N-glycan core: their functions and target proteins
    • Takahashi, M., Kuroki, Y., Ohtsubo, K. and Tanichi, N. (2009) Core fucose and bisecting GlcNAc, the direct modifiers of the N-glycan core: their functions and target proteins. Carbohydr. Res. 344, 1387-1390.
    • (2009) Carbohydr. Res. , vol.344 , pp. 1387-1390
    • Takahashi, M.1    Kuroki, Y.2    Ohtsubo, K.3    Tanichi, N.4
  • 33
    • 0030970043 scopus 로고    scopus 로고
    • Overexpression of N-acetylglucosaminyltransferase III disrupts the tyrosine phosphorylation of Trk with resultant signaling dysfunction in PC12 cells treated with nerve growth factor
    • Ihara, Y., Sakamoto, Y., Mihara, M., Shimizu, K. and Tanichi, N. (1997) Overexpression of N-acetylglucosaminyltransferase III disrupts the tyrosine phosphorylation of Trk with resultant signaling dysfunction in PC12 cells treated with nerve growth factor. J. Biol. Chem. 272, 9629-9634.
    • (1997) J. Biol. Chem. , vol.272 , pp. 9629-9634
    • Ihara, Y.1    Sakamoto, Y.2    Mihara, M.3    Shimizu, K.4    Tanichi, N.5
  • 34
    • 79953006880 scopus 로고    scopus 로고
    • Wnt/beta-catenin signaling down-relates N-acetylglucosaminyltransferase III expression: the implications of two mutually exclusive pathways for relation
    • Xu, Q., Akama, R., Isaji, T., Lu, Y., Hashimoto, H., Kariya, Y., Fukuda, T., Du, Y. and , J. (2011) Wnt/beta-catenin signaling down-relates N-acetylglucosaminyltransferase III expression: the implications of two mutually exclusive pathways for relation. J. Biol. Chem. 286, 4310-4318.
    • (2011) J. Biol. Chem. , vol.286 , pp. 4310-4318
    • Xu, Q.1    Akama, R.2    Isaji, T.3    Lu, Y.4    Hashimoto, H.5    Kariya, Y.6    Fukuda, T.7    Du, Y.J.8
  • 35
    • 0037474262 scopus 로고    scopus 로고
    • Down-relation of hydrogen peroxide-induced PKC delta activation in N-acetylglucosaminyltransferase III-transfected HeLaS3 cells
    • Shibukawa, Y., Takahashi, M., Laffont, I., Honke, K. and Tanichi, N. (2003) Down-relation of hydrogen peroxide-induced PKC delta activation in N-acetylglucosaminyltransferase III-transfected HeLaS3 cells. J. Biol. Chem. 278, 3197-3203.
    • (2003) J. Biol. Chem. , vol.278 , pp. 3197-3203
    • Shibukawa, Y.1    Takahashi, M.2    Laffont, I.3    Honke, K.4    Tanichi, N.5
  • 37
    • 0030068748 scopus 로고    scopus 로고
    • Bisecting N-acetylglucosamine on K562 cells suppresses natural killer cytotoxicity and promotes spleen colonization
    • Yoshimura, M., Ihara, Y., Ohnishi, A., Ijuhin, N., Nishiura, T., Kanakura, Y., Matsuzawa, Y. and Tanichi, N. (1996) Bisecting N-acetylglucosamine on K562 cells suppresses natural killer cytotoxicity and promotes spleen colonization. Cancer Res. 56, 412-418.
    • (1996) Cancer Res , vol.56 , pp. 412-418
    • Yoshimura, M.1    Ihara, Y.2    Ohnishi, A.3    Ijuhin, N.4    Nishiura, T.5    Kanakura, Y.6    Matsuzawa, Y.7    Tanichi, N.8
  • 38
    • 5144224424 scopus 로고    scopus 로고
    • beta1 4-N-Acetylglucosaminyltransferase III down-relates neurite outgrowth induced by costimulation of epidermal growth factor and integrins through the Ras/ERK signaling pathway in PC12 cells
    • , J., Zhao, Y., Isaji, T., Shibukawa, Y., Ihara, H., Takahashi, M., Ikeda, Y., Miyoshi, E., Honke, K. and Tanichi, N. (2004) beta1,4-N-Acetylglucosaminyltransferase III down-relates neurite outgrowth induced by costimulation of epidermal growth factor and integrins through the Ras/ERK signaling pathway in PC12 cells. Glycobiology 14, 177-186.
    • (2004) Glycobiology , vol.14 , pp. 177-186
    • Zhao, Y.J.1    Isaji, T.2    Shibukawa, Y.3    Ihara, H.4    Takahashi, M.5    Ikeda, Y.6    Miyoshi, E.7    Honke, K.8    Tanichi, N.9
  • 39
    • 0033951459 scopus 로고    scopus 로고
    • Opposing changes in N-acetylglucosaminyltransferase-V and -III during the cell cycle and all-trans retinoic acid treatment of hepatocarcinoma cell line
    • Guo, H. B., Jiang, A. L., Ju, T. Y. and Chen, H. L. (2000) Opposing changes in N-acetylglucosaminyltransferase-V and -III during the cell cycle and all-trans retinoic acid treatment of hepatocarcinoma cell line. Biochim. Biophys. Acta 1495, 297-307.
    • (2000) Biochim. Biophys. Acta , vol.1495 , pp. 297-307
    • Guo, H.B.1    Jiang, A.L.2    Ju, T.Y.3    Chen, H.L.4
  • 41
    • 0035980062 scopus 로고    scopus 로고
    • Down-relation of the alpha-Gal epitope expression in N-glycans of swine endothelial cells by transfection with the N-acetylglucosaminyltransferase III gene Modulation of the biosynthesis of terminal structures by a bisecting GlcNAc
    • Koyota, S., Ikeda, Y., Miyagawa, S., Ihara, H., Koma, M., Honke, K., Shirakura, R. and Tanichi, N. (2001) Down-relation of the alpha-Gal epitope expression in N-glycans of swine endothelial cells by transfection with the N-acetylglucosaminyltransferase III gene. Modulation of the biosynthesis of terminal structures by a bisecting GlcNAc. J. Biol. Chem. 276, 32867-32874.
    • (2001) J. Biol. Chem. , vol.276 , pp. 32867-32874
    • Koyota, S.1    Ikeda, Y.2    Miyagawa, S.3    Ihara, H.4    Koma, M.5    Honke, K.6    Shirakura, R.7    Tanichi, N.8
  • 43
    • 0030884451 scopus 로고    scopus 로고
    • Purification and characterization of UDP-N-acetylglucosamine: alpha 1,3-D-mannoside beta 1 4- N-acetylglucosaminyltransferase (N-acetylglucosaminyltransferase-IV) from bovine small intestine
    • Ori, S., Minowa, M. T., Ihara, Y., Tanichi, N., Ikenaga, H. and Takeuchi, M. (1997) Purification and characterization of UDP-N-acetylglucosamine: alpha 1,3-D-mannoside beta 1,4- N-acetylglucosaminyltransferase (N-acetylglucosaminyltransferase-IV) from bovine small intestine. J. Biol. Chem. 272, 22721-22727.
    • (1997) J. Biol. Chem. , vol.272 , pp. 22721-22727
    • Ori, S.1    Minowa, M.T.2    Ihara, Y.3    Tanichi, N.4    Ikenaga, H.5    Takeuchi, M.6
  • 44
    • 0032496151 scopus 로고    scopus 로고
    • cDNA cloning and expression of bovine UDP-N-acetylglucosamine: alpha1,3-D-mannoside beta1 4-N-acetylglucosaminyltransferase IV
    • Minowa, M. T., Ori, S., Yoshida, A., Hara, T., Iwamatsu, A., Ikenaga, H. and Takeuchi, M. (1998) cDNA cloning and expression of bovine UDP-N-acetylglucosamine: alpha1,3-D-mannoside beta1,4-N-acetylglucosaminyltransferase IV. J. Biol. Chem. 273, 11556-11562.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11556-11562
    • Minowa, M.T.1    Ori, S.2    Yoshida, A.3    Hara, T.4    Iwamatsu, A.5    Ikenaga, H.6    Takeuchi, M.7
  • 45
    • 0024358246 scopus 로고
    • Comparative study of the sugar chains of gamma-glutamyltranspeptidases purified from human hepatocellular carcinoma and from human liver
    • Yamashita, K., Totani, K., Iwaki, Y., Takamisawa, I., Tateishi, N., Higashi, T., Sakamoto, Y. and Kobata, A.(1989) Comparative study of the sugar chains of gamma-glutamyltranspeptidases purified from human hepatocellular carcinoma and from human liver. J. Biochem. 1105, 728-735.
    • (1989) J. Biochem. , vol.1105 , pp. 728-735
    • Yamashita, K.1    Totani, K.2    Iwaki, Y.3    Takamisawa, I.4    Tateishi, N.5    Higashi, T.6    Sakamoto, Y.7    Kobata, A.8
  • 46
    • 0023232348 scopus 로고
    • Structural differences found in the asparaginelinked sugar chains of human chorionic gonadotropins purified from the urine of patients with invasive mole and with choriocarcinoma
    • Endo, T., Nishimura, R., Kawano, T., Mochizuki, M. and Kobata, A. (1987) Structural differences found in the asparaginelinked sugar chains of human chorionic gonadotropins purified from the urine of patients with invasive mole and with choriocarcinoma. Cancer Res. 47, 5242-5245.
    • (1987) Cancer Res , vol.47 , pp. 5242-5245
    • Endo, T.1    Nishimura, R.2    Kawano, T.3    Mochizuki, M.4    Kobata, A.5
  • 47
    • 0024371459 scopus 로고
    • N-acetylglucosaminyltransferase III, IV and V activities in Novikoff ascites tumour cells, mouse lymphoma cells and hen oviduct Application of a sensitive and specific assay by use of high-performance liquid chromatography
    • Koenderman, A. H., Koppen, P. L., Koeleman, C. A. and van den Eijnden, D. H. (1989) N-acetylglucosaminyltransferase III, IV and V activities in Novikoff ascites tumour cells, mouse lymphoma cells and hen oviduct. Application of a sensitive and specific assay by use of high-performance liquid chromatography. Eur. J. Biochem. 181, 651-655.
    • (1989) Eur. J. Biochem. , vol.181 , pp. 651-655
    • Koenderman, A.H.1    Koppen, P.L.2    Koeleman, C.A.3    van den Eijnden, D.H.4
  • 48
    • 0025243494 scopus 로고
    • Modulation of N-acetylglucosaminyltransferase III IV and V activities and alteration of the surface oligosaccharide structure of a myeloma cell line by interleukin 6
    • Nakao, H., Nishikawa, A., Karasuno, T., Nishiura, T., Iida, M., Kanayama, Y., Yonezawa, T., Tarui, S. and Tanichi, N. (1990) Modulation of N-acetylglucosaminyltransferase III, IV and V activities and alteration of the surface oligosaccharide structure of a myeloma cell line by interleukin 6. Biochem. Biophys. Res. Commun. 172, 1260-1266.
    • (1990) Biochem. Biophys. Res. Commun. , vol.172 , pp. 1260-1266
    • Nakao, H.1    Nishikawa, A.2    Karasuno, T.3    Nishiura, T.4    Iida, M.5    Kanayama, Y.6    Yonezawa, T.7    Tarui, S.8    Tanichi, N.9
  • 50
    • 77956205008 scopus 로고    scopus 로고
    • Targeted genetic inactivation N-acetylglucosaminyltransferase-IVa impairs insulin secretion from pancreatic beta cells and evokes type 2 diabetes
    • Ohtsubo, K. (2010) Targeted genetic inactivation N-acetylglucosaminyltransferase-IVa impairs insulin secretion from pancreatic beta cells and evokes type 2 diabetes. Methods Enzymol. 479, 205-222.
    • (2010) Methods Enzymol , vol.479 , pp. 205-222
    • Ohtsubo, K.1
  • 51
    • 80052433997 scopus 로고    scopus 로고
    • Pathway to diabetes through attenuation of pancreatic beta cell glycosylation and glucose transport
    • Ohtsubo, K., Chen, M. Z., Olefsky, J. M. and Marth, J. D. (2011) Pathway to diabetes through attenuation of pancreatic beta cell glycosylation and glucose transport. Nat. Med. 17, 1067-1075.
    • (2011) Nat. Med. , vol.17 , pp. 1067-1075
    • Ohtsubo, K.1    Chen, M.Z.2    Olefsky, J.M.3    Marth, J.D.4
  • 54
    • 0027196125 scopus 로고
    • Purification and characterization of UDP-N-acetylglucosamine: alpha-6-Dmannoside beta 1-6N-acetylglucosaminyltransferase (N-acetylglucosaminyltransferase V) from a human lung cancer cell line
    • , J., Nishikawa, A., Tsuruoka, N., Ohno, M., Yamachi, N., Kangawa, K. and Tanichi, N. (1993) Purification and characterization of UDP-N-acetylglucosamine: alpha-6-Dmannoside beta 1-6N-acetylglucosaminyltransferase (N-acetylglucosaminyltransferase V) from a human lung cancer cell line. J. Biochem. 113, 614-619.
    • (1993) J. Biochem. , vol.113 , pp. 614-619
    • Nishikawa, A.J.1    Tsuruoka, N.2    Ohno, M.3    Yamachi, N.4    Kangawa, K.5    Tanichi, N.6
  • 57
    • 33947724303 scopus 로고    scopus 로고
    • Complex N-glycan number and degree of branching cooperate to relate cell proliferation and differentiation
    • Lau, K. S., Partridge, E. A., Grigorian, A., Silvescu, C. I., Reinhold, V. N., Demetriou, M. and Dennis, J. W. (2007) Complex N-glycan number and degree of branching cooperate to relate cell proliferation and differentiation. Cell 129, 123-134.
    • (2007) Cell , vol.129 , pp. 123-134
    • Lau, K.S.1    Partridge, E.A.2    Grigorian, A.3    Silvescu, C.I.4    Reinhold, V.N.5    Demetriou, M.6    Dennis, J.W.7
  • 58
    • 0035526266 scopus 로고    scopus 로고
    • Implication of GnT-V in cancer metastasis: a glycomic approach for identification of a target protein and its unique function as an angiogenic cofactor
    • Tanichi, N., Ihara, S., Saito, T., Miyoshi, E., Ikeda, Y. and Honke, K. (2001) Implication of GnT-V in cancer metastasis: a glycomic approach for identification of a target protein and its unique function as an angiogenic cofactor. Glycoconj. J. 18, 859-865.
    • (2001) Glycoconj. J. , vol.18 , pp. 859-865
    • Tanichi, N.1    Ihara, S.2    Saito, T.3    Miyoshi, E.4    Ikeda, Y.5    Honke, K.6
  • 59
    • 0029911075 scopus 로고    scopus 로고
    • Transcriptional relation of the N-acetylglucosaminyltransferase V gene in human bile duct carcinoma cells (HuCC-T1) is mediated by Ets-1
    • Erratum in: J. Biol. Chem. (1999) 274, 554
    • Kang, R., Saito, H., Ihara, Y., Miyoshi, E., Koyama, N., Sheng, Y. and Tanichi, N. (1996) Transcriptional relation of the N-acetylglucosaminyltransferase V gene in human bile duct carcinoma cells (HuCC-T1) is mediated by Ets-1. J. Biol. Chem. 271, 26706-26712. Erratum in: J. Biol. Chem. (1999) 274, 554.
    • (1996) J. Biol. Chem. , vol.271 , pp. 26706-26712
    • Kang, R.1    Saito, H.2    Ihara, Y.3    Miyoshi, E.4    Koyama, N.5    Sheng, Y.6    Tanichi, N.7
  • 60
    • 0000656065 scopus 로고    scopus 로고
    • Relation of the GnT-V promoter by transcription factor Ets-1 in various cancer cell lines
    • Ko, J. H., Miyoshi, E., Noda, K., Ekuni, A., Kang, R., Ikeda, Y. and Tanichi, N. (1999) Relation of the GnT-V promoter by transcription factor Ets-1 in various cancer cell lines. J. Biol. Chem. 274, 22941-22948.
    • (1999) J. Biol. Chem. , vol.274 , pp. 22941-22948
    • Ko, J.H.1    Miyoshi, E.2    Noda, K.3    Ekuni, A.4    Kang, R.5    Ikeda, Y.6    Tanichi, N.7
  • 61
    • 0028970268 scopus 로고
    • Transforming growth factor beta up-relates expression of the N-acetylglucosaminyltransferase V gene in mouse melanoma cells
    • Miyoshi, E., Nishikawa, A., Ihara, Y., Saito, H., Uozumi, N., Hayashi, N., Fusamoto, H., Kamada, T. and Tanichi, N. (1995) Transforming growth factor beta up-relates expression of the N-acetylglucosaminyltransferase V gene in mouse melanoma cells. J. Biol. Chem. 270, 6216-6220.
    • (1995) J. Biol. Chem. , vol.270 , pp. 6216-6220
    • Miyoshi, E.1    Nishikawa, A.2    Ihara, Y.3    Saito, H.4    Uozumi, N.5    Hayashi, N.6    Fusamoto, H.7    Kamada, T.8    Tanichi, N.9
  • 62
    • 0347993082 scopus 로고    scopus 로고
    • N-acetylglucosaminyltransferase V expression levels relate cadherin-associated homotypic cell-cell adhesion and intracellular signaling pathways
    • o, HB., Lee, I., Kamar, M. and Pierce, M. (2003) N-acetylglucosaminyltransferase V expression levels relate cadherin-associated homotypic cell-cell adhesion and intracellular signaling pathways. J. Biol. Chem. 278, 52412-52424.
    • (2003) J. Biol. Chem. , vol.278 , pp. 52412-52424
    • o, H.B.1    Lee, I.2    Kamar, M.3    Pierce, M.4
  • 63
    • 84857737111 scopus 로고
    • Sequential action of Ets-1 and Sp1 in the activation of the human beta-1 4-galactosyltransferase V gene involved in abnormal glycosylation characteristic of cancer cells
    • Sato, T. and Furukawa, K. (1995) Sequential action of Ets-1 and Sp1 in the activation of the human beta-1,4-galactosyltransferase V gene involved in abnormal glycosylation characteristic of cancer cells. J. Biol. Chem. 270, 6216-6220.
    • (1995) J. Biol. Chem. , vol.270 , pp. 6216-6220
    • Sato, T.1    Furukawa, K.2
  • 64
    • 0034655858 scopus 로고    scopus 로고
    • Relation of expression of the human beta-1 2-N-acetylglucosaminyltransferase II gene (MGAT2) by Ets transcription factors
    • Zhang, W., Revers, L., Pierce, M. and Schachter, H. (2000) Relation of expression of the human beta-1, 2-N-acetylglucosaminyltransferase II gene (MGAT2) by Ets transcription factors. Biochem. J. 347(Pt 2), 511-518.
    • (2000) Biochem. J. , vol.347 , Issue.PART 2 , pp. 511-518
    • Zhang, W.1    Revers, L.2    Pierce, M.3    Schachter, H.4
  • 65
    • 0037053318 scopus 로고    scopus 로고
    • Prometastatic effect of N-acetylglucosaminyltransferase V is due to modification and stabilization of active matriptase by adding beta 1-6 GlcNAc branching
    • Ihara, S., Miyoshi, E., Ko, J. H., Murata, K., Nakahara, S., Honke, K., Dickson, R. B., Lin, C. Y. and Tanichi, N. (2002) Prometastatic effect of N-acetylglucosaminyltransferase V is due to modification and stabilization of active matriptase by adding beta 1-6 GlcNAc branching. J. Biol. Chem. 277, 16960-16967.
    • (2002) J. Biol. Chem. , vol.277 , pp. 16960-16967
    • Ihara, S.1    Miyoshi, E.2    Ko, J.H.3    Murata, K.4    Nakahara, S.5    Honke, K.6    Dickson, R.B.7    Lin, C.Y.8    Tanichi, N.9
  • 66
    • 5144234312 scopus 로고    scopus 로고
    • Addition of beta1-6 GlcNAc branching to the oligosaccharide attached to Asn 772 in the serine protease domain of matriptase plays a pivotal role in its stability and resistance against trypsin
    • Ihara, S., Miyoshi, E., Nakahara, S., Sakiyama, H., Ihara, H., Akinaga, A., Honke, K., Dickson, RB, Lin, C. Y. and Tanichi, N. (2004) Addition of beta1-6 GlcNAc branching to the oligosaccharide attached to Asn 772 in the serine protease domain of matriptase plays a pivotal role in its stability and resistance against trypsin. Glycobiology 14, 139-146.
    • (2004) Glycobiology , vol.14 , pp. 139-146
    • Ihara, S.1    Miyoshi, E.2    Nakahara, S.3    Sakiyama, H.4    Ihara, H.5    Akinaga, A.6    Honke, K.7    Dickson, R.B.8    Lin, C.Y.9    Tanichi, N.10
  • 67
    • 0038026134 scopus 로고    scopus 로고
    • Roles of hepatocyte growth factor (HGF) activator and HGF activator inhibitor in the pericellular activation of HGF/scatter factor
    • Kataoka, H., Miyata, S., Uchinokura, S. and Itoh, H. (2003) Roles of hepatocyte growth factor (HGF) activator and HGF activator inhibitor in the pericellular activation of HGF/scatter factor. Cancer Metastasis Rev. 22, 223-236.
    • (2003) Cancer Metastasis Rev , vol.22 , pp. 223-236
    • Kataoka, H.1    Miyata, S.2    Uchinokura, S.3    Itoh, H.4
  • 68
    • 0142243202 scopus 로고    scopus 로고
    • The novel serine protease tumor-associated differentially expressed gene-15 (matriptase/MT-SP1) is highly overexpressed in cervical carcinoma
    • Santin, A. D., Cane', S., Bellone, S., Bignotti, E., Palmieri, M., De Las Casas, L. E., Anfossi, S., Roman, J. J., O'Brien, T. and Pecorelli, S. (2003) The novel serine protease tumor-associated differentially expressed gene-15 (matriptase/MT-SP1) is highly overexpressed in cervical carcinoma. Cancer 98, 1898-1904.
    • (2003) Cancer , vol.98 , pp. 1898-1904
    • Santin, A.D.1    Cane', S.2    Bellone, S.3    Bignotti, E.4    Palmieri, M.5    De Las Casas, L.E.6    Anfossi, S.7    Roman, J.J.8    O'Brien, T.9    Pecorelli, S.10
  • 69
    • 0037053299 scopus 로고    scopus 로고
    • A secreted type of beta 1 6-N-acetylglucosaminyltransferase V (GnT-V) induces tumor angiogenesis without mediation of glycosylation: a novel function of GnT-V distinct from the original glycosyltransferase activity
    • Saito, T., Miyoshi, E., Sasai, K., Nakano, N., Echi, H., Honke, K. and Tanichi, N. (2002) A secreted type of beta 1, 6-N-acetylglucosaminyltransferase V (GnT-V) induces tumor angiogenesis without mediation of glycosylation: a novel function of GnT-V distinct from the original glycosyltransferase activity. J. Biol. Chem. 277, 17002-17008.
    • (2002) J. Biol. Chem. , vol.277 , pp. 17002-17008
    • Saito, T.1    Miyoshi, E.2    Sasai, K.3    Nakano, N.4    Echi, H.5    Honke, K.6    Tanichi, N.7
  • 72
    • 39049105125 scopus 로고    scopus 로고
    • Functional proteomics study reveals that N-Acetylglucosaminyltransferase V reinforces the invasive/metastatic potential of colon cancer through aberrant glycosylation on tissue inhibitor of metalloproteinase-1
    • Kim, Y. S., Hwang, S. Y., Kang, H. Y., Sohn, H., Oh, S., Kim, J. Y., Yoo, J. S., Kim, Y. H., Kim, C. H., Jeon, J. H., Lee, J. M., Kang, H. A., Miyoshi, E., Tanichi, N., Yoo, H. S. and Ko, J. H. (2008) Functional proteomics study reveals that N-Acetylglucosaminyltransferase V reinforces the invasive/metastatic potential of colon cancer through aberrant glycosylation on tissue inhibitor of metalloproteinase-1. Mol. Cell Proteomics. 7, 1-14.
    • (2008) Mol. Cell Proteomics. , vol.7 , pp. 1-14
    • Kim, Y.S.1    Hwang, S.Y.2    Kang, H.Y.3    Sohn, H.4    Oh, S.5    Kim, J.Y.6    Yoo, J.S.7    Kim, Y.H.8    Kim, C.H.9    Jeon, J.H.10    Lee, J.M.11    Kang, H.A.12    Miyoshi, E.13    Tanichi, N.14    Yoo, H.S.15    Ko, J.H.16
  • 73
    • 0242322005 scopus 로고    scopus 로고
    • Molecular cloning and characterization of human GnT-IX, a novel beta1 6-N-acetylglucosaminyltransferase that is specifically expressed in the brain
    • Inamori, K., Endo, T., Ide, Y., Fujii, S., , J., Honke, K. and Tanichi, N. (2003) Molecular cloning and characterization of human GnT-IX, a novel beta1, 6-N-acetylglucosaminyltransferase that is specifically expressed in the brain. J. Biol. Chem. 278, 43102-43109.
    • (2003) J. Biol. Chem. , vol.278 , pp. 43102-43109
    • Inamori, K.1    Endo, T.2    Ide, Y.3    Fujii, S.J.4    Honke, K.5    Tanichi, N.6
  • 75
    • 9144252532 scopus 로고    scopus 로고
    • N-Acetylglucosaminyltransferase IX acts on the GlcNAc beta 1, 2-Man alpha 1-Ser/Thr moiety, forming a 2, 6-branched structure in brain O-mannosyl glycan
    • Inamori, K., Endo, T., , J., Matsuo, I., Ito, Y., Fujii, S., Iwasaki, H., Narimatsu, H., Miyoshi, E., Honke, K. and Tanichi, N. (2004) N-Acetylglucosaminyltransferase IX acts on the GlcNAc beta 1, 2-Man alpha 1-Ser/Thr moiety, forming a 2, 6-branched structure in brain O-mannosyl glycan. J. Biol. Chem. 279, 2337-2340.
    • (2004) J. Biol. Chem. , vol.279 , pp. 2337-2340
    • Inamori, K.1    Endo, T.J.2    Matsuo, I.3    Ito, Y.4    Fujii, S.5    Iwasaki, H.6    Narimatsu, H.7    Miyoshi, E.8    Honke, K.9    Tanichi, N.10
  • 76
    • 30644475356 scopus 로고    scopus 로고
    • High expression of N-acetylglucosaminyltransferase V in favorable neuroblastomas: Involvement of its effect on apoptosis
    • Inamori, K., , J., Ohira, M., Kawasaki, A., Nakamura, Y., Nakagawa, T., Kondo, A., Miyoshi, E., Nakagawara, A. and Tanichi, N. (2006) High expression of N-acetylglucosaminyltransferase V in favorable neuroblastomas: Involvement of its effect on apoptosis. FEBS Lett. 580, 627-632.
    • (2006) FEBS Lett , vol.580 , pp. 627-632
    • Inamori, K.J.1    Ohira, M.2    Kawasaki, A.3    Nakamura, Y.4    Nakagawa, T.5    Kondo, A.6    Miyoshi, E.7    Nakagawara, A.8    Tanichi, N.9
  • 77
    • 33646510540 scopus 로고    scopus 로고
    • Demonstration of the expression and the enzymatic activity of N-acetylglucosaminyltransferase IX in the mouse brain
    • Inamori, K., Mita, S., , J., Mizuno-Horikawa, Y., Miyoshi, E., Dennis, J. W. and Tanichi, N. (2006) Demonstration of the expression and the enzymatic activity of N-acetylglucosaminyltransferase IX in the mouse brain. Biochim. Biophys. Acta 60, 678-684.
    • (2006) Biochim. Biophys. Acta , vol.60 , pp. 678-684
    • Inamori, K.1    Mita, S.J.2    Mizuno-Horikawa, Y.3    Miyoshi, E.4    Dennis, J.W.5    Tanichi, N.6
  • 78
    • 80052415923 scopus 로고    scopus 로고
    • Brain-specific expression of N-acetylglucosaminyltransferase IX (GnT-IX) is related by epigenetic histone modifications
    • Kizuka, Y., Kitazume, S., Yoshida, M. and Tanichi, N. (2011) Brain-specific expression of N-acetylglucosaminyltransferase IX (GnT-IX) is related by epigenetic histone modifications. J. Biol. Chem. 286, 31875-31884.
    • (2011) J. Biol. Chem. , vol.286 , pp. 31875-31884
    • Kizuka, Y.1    Kitazume, S.2    Yoshida, M.3    Tanichi, N.4
  • 79
    • 0031026624 scopus 로고    scopus 로고
    • Structures of sialylated O-linked oligosaccharides of bovine peripheral nerve alpha-dystroglycan The role of a novel Omannosyl-type oligosaccharide in the binding of alpha-dystroglycan with laminin
    • Chiba, A., Matsumura, K., Yamada, H., Inazu, T., Shimizu, T., Kusunoki, S., Kanazawa, I., Kobata, A. and Endo, T. (1997) Structures of sialylated O-linked oligosaccharides of bovine peripheral nerve alpha-dystroglycan. The role of a novel Omannosyl-type oligosaccharide in the binding of alpha-dystroglycan with laminin. J. Biol. Chem. 272, 2156-2162.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2156-2162
    • Chiba, A.1    Matsumura, K.2    Yamada, H.3    Inazu, T.4    Shimizu, T.5    Kusunoki, S.6    Kanazawa, I.7    Kobata, A.8    Endo, T.9
  • 80
    • 0028047235 scopus 로고
    • Dystrophin-glycoprotein complex: its role in the molecular pathogenesis of muscular dystrophies
    • Matsumura, K. and Campbell, K. P. (1994) Dystrophin-glycoprotein complex: its role in the molecular pathogenesis of muscular dystrophies. Muscle Nerve 1, 2-15.
    • (1994) Muscle Nerve , vol.1 , pp. 2-15
    • Matsumura, K.1    Campbell, K.P.2
  • 82
    • 57749114758 scopus 로고    scopus 로고
    • Receptor tyrosine phosphatase beta (RPTPbeta) activity and signaling are attenuated by glycosylation and subsequent cell surface galectin-1 binding
    • Abbott, K. L., Matthews, R. T. and Pierce, M. (2008) Receptor tyrosine phosphatase beta (RPTPbeta) activity and signaling are attenuated by glycosylation and subsequent cell surface galectin-1 binding. J. Biol. Chem. 283, 33026-33035.
    • (2008) J. Biol. Chem. , vol.283 , pp. 33026-33035
    • Abbott, K.L.1    Matthews, R.T.2    Pierce, M.3
  • 83
    • 0032906430 scopus 로고    scopus 로고
    • Divergent evolution of fucosyltransferase genes from vertebrates, invertebrates, and bacteria
    • Oriol, R., Mollicone, R., Cailleau, A., Balanzino, L. and Breton, C. (1999) Divergent evolution of fucosyltransferase genes from vertebrates, invertebrates, and bacteria. Glycobiology 9, 323-334.
    • (1999) Glycobiology , vol.9 , pp. 323-334
    • Oriol, R.1    Mollicone, R.2    Cailleau, A.3    Balanzino, L.4    Breton, C.5
  • 84
    • 0025789667 scopus 로고
    • Purification and characterization of GDP-L-fucose-Nacetyl beta-D-glucosaminide alpha 1-6fucosyltransferase from cultured human skin fibroblasts Requirement of a specific biantennary oligosaccharide as substrate
    • Voynow, J. A., Kaiser, R. S., Scanlin, T. F. and Glick, M. C. (1991) Purification and characterization of GDP-L-fucose-Nacetyl beta-D-glucosaminide alpha 1-6fucosyltransferase from cultured human skin fibroblasts. Requirement of a specific biantennary oligosaccharide as substrate. J. Biol. Chem. 266, 21572-21577.
    • (1991) J. Biol. Chem. , vol.266 , pp. 21572-21577
    • Voynow, J.A.1    Kaiser, R.S.2    Scanlin, T.F.3    Glick, M.C.4
  • 86
    • 0030897673 scopus 로고    scopus 로고
    • Purification and cDNA cloning of GDP-L-Fuc:N-acetyl-beta-D-glucosaminide:alpha1-6 fucosyltransferase (alpha1-6 FucT) from human gastric cancer MKN45 cells
    • Yanagidani, S., Uozumi, N., Ihara, Y., Miyoshi, E., Yamachi, N. and Tanichi, N. (1997) Purification and cDNA cloning of GDP-L-Fuc:N-acetyl-beta-D-glucosaminide:alpha1-6 fucosyltransferase (alpha1-6 FucT) from human gastric cancer MKN45 cells. J. Biochem. 121, 626-632.
    • (1997) J. Biochem. , vol.121 , pp. 626-632
    • Yanagidani, S.1    Uozumi, N.2    Ihara, Y.3    Miyoshi, E.4    Yamachi, N.5    Tanichi, N.6
  • 89
    • 79956299332 scopus 로고    scopus 로고
    • Alpha1 6-fucosyltransferase-deficient mice exhibit multiple behavioral abnormalities associated with a schizophrenia-like phenotype: importance of the balance between the dopamine and serotonin systems
    • Fukuda, T., Hashimoto, H., Okayasu, N., Kameyama, A., Onogi, H., Nakagawasai, O., Nakazawa, T., Kurosawa, T., Hao, Y., Isaji, T., Tadano, T., Narimatsu, H., Tanichi, N. and , J. (2011) Alpha1, 6-fucosyltransferase-deficient mice exhibit multiple behavioral abnormalities associated with a schizophrenia-like phenotype: importance of the balance between the dopamine and serotonin systems. J. Biol. Chem. 286, 18434-18443.
    • (2011) J. Biol. Chem. , vol.286 , pp. 18434-18443
    • Fukuda, T.1    Hashimoto, H.2    Okayasu, N.3    Kameyama, A.4    Onogi, H.5    Nakagawasai, O.6    Nakazawa, T.7    Kurosawa, T.8    Hao, Y.9    Isaji, T.10    Tadano, T.11    Narimatsu, H.12    Tanichi, N.J.13
  • 90
    • 0023836388 scopus 로고
    • The fucosylation index of alpha-fetoprotein and its usefulness in the early diagnosis of hepatocellular carcinoma
    • Aoyagi, Y., Suzuki, Y., Isemura, M., Nomoto, M., Sekine, C., Igarashi, K. and Ichida, F. (1988) The fucosylation index of alpha-fetoprotein and its usefulness in the early diagnosis of hepatocellular carcinoma. Cancer 61, 769-774.
    • (1988) Cancer , vol.61 , pp. 769-774
    • Aoyagi, Y.1    Suzuki, Y.2    Isemura, M.3    Nomoto, M.4    Sekine, C.5    Igarashi, K.6    Ichida, F.7
  • 91
    • 0027422524 scopus 로고
    • A collaborative study for the evaluation of lectin-reactive alpha-fetoproteins in early detection of hepatocellular carcinoma
    • Taketa, K., Endo, Y., Sekiya, C., Tanikawa, K., Koji, T., Taga, H., Satomura, S., Matsuura, S., Kawai, T. and Hirai, H. (1993) A collaborative study for the evaluation of lectin-reactive alpha-fetoproteins in early detection of hepatocellular carcinoma. Cancer Res. 53, 5419-5423.
    • (1993) Cancer Res , vol.53 , pp. 5419-5423
    • Taketa, K.1    Endo, Y.2    Sekiya, C.3    Tanikawa, K.4    Koji, T.5    Taga, H.6    Satomura, S.7    Matsuura, S.8    Kawai, T.9    Hirai, H.10
  • 94
    • 84857699951 scopus 로고    scopus 로고
    • Fucosylated haptoglobin is a novel type of cancer biomarker linked to the prognosis after an operation in colorectal cancer
    • (in press)
    • Takeda, Y., Shinzaki, S., Okudo, K., Moriwaki, K., Murata, K. and Miyoshi, E. (2011) Fucosylated haptoglobin is a novel type of cancer biomarker linked to the prognosis after an operation in colorectal cancer. Cancer (in press).
    • (2011) Cancer
    • Takeda, Y.1    Shinzaki, S.2    Okudo, K.3    Moriwaki, K.4    Murata, K.5    Miyoshi, E.6
  • 96
    • 0037178791 scopus 로고    scopus 로고
    • Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human Fcgamma RIII and antibody-dependent cellular toxicity
    • Shields, R. L., Lai, J., Keck, R., O'Connell, L. Y., Hong, K., Meng, Y. G., Weikert, S. H. and Presta, L. G. (2002) Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human Fcgamma RIII and antibody-dependent cellular toxicity. J. Biol. Chem. 277, 26733-26740.
    • (2002) J. Biol. Chem. , vol.277 , pp. 26733-26740
    • Shields, R.L.1    Lai, J.2    Keck, R.3    O'Connell, L.Y.4    Hong, K.5    Meng, Y.G.6    Weikert, S.H.7    Presta, L.G.8
  • 97
    • 0037474276 scopus 로고    scopus 로고
    • The absence of fucose but not the presence of galactose or bisecting N-acetylglucosamine of human IgG1 complex-type oligosaccharides shows the critical role of enhancing antibody-dependent cellular cytotoxicity
    • Shinkawa, T., Nakamura, K., Yamane, N., Shoji-Hosaka, E., Kanda, Y., Sakurada, M., Uchida, K., Anazawa, H., Satoh, M., Yamasaki, M., Hanai, N. and Shitara, K. (2003) The absence of fucose but not the presence of galactose or bisecting N-acetylglucosamine of human IgG1 complex-type oligosaccharides shows the critical role of enhancing antibody-dependent cellular cytotoxicity. J. Biol. Chem. 278, 3466-3473.
    • (2003) J. Biol. Chem. , vol.278 , pp. 3466-3473
    • Shinkawa, T.1    Nakamura, K.2    Yamane, N.3    Shoji-Hosaka, E.4    Kanda, Y.5    Sakurada, M.6    Uchida, K.7    Anazawa, H.8    Satoh, M.9    Yamasaki, M.10    Hanai, N.11    Shitara, K.12
  • 100
    • 33745078347 scopus 로고    scopus 로고
    • From glycobiology to systems glycobiology: International network with Japanese scientists through consortia
    • Tanichi, N. (2006) From glycobiology to systems glycobiology: International network with Japanese scientists through consortia. IUBMB Life 58, 1-4.
    • (2006) IUBMB Life , vol.58 , pp. 1-4
    • Tanichi, N.1


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