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Volumn 103, Issue 1, 2014, Pages 37-49

Overexpression of N-acetylglucosaminyltransferases III and v in human melanoma cells. Implications for MCAM N-glycosylation

Author keywords

Activity assay; Glycosyltransferases; MCAM; Melanoma; N glycosylation; Transendothelial migration

Indexed keywords

ALPHA 1,3(6) MANNOSYLGLYCOPROTEIN BETA 1,6 N ACETYLGLUCOSAMINYLTRANSFERASE; CD146 ANTIGEN; N ACETYLGLUCOSAMINYLTRANSFERASE; N ACETYLGLUCOSAMINYLTRANSFERASE III; UNCLASSIFIED DRUG; 2-ACYLGLYCEROL O-ACYLTRANSFERASE; ACYLTRANSFERASE; ALPHA-1,6-MANNOSYLGLYCOPROTEIN BETA 1,6-N-ACETYLGLUCOSAMINYLTRANSFERASE; MCAM PROTEIN, HUMAN; POLYSACCHARIDE;

EID: 84903693482     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2014.04.003     Document Type: Article
Times cited : (23)

References (87)
  • 1
    • 0034441282 scopus 로고    scopus 로고
    • The joys of HexNAc. The synthesis and function of N- and O-glycan branches
    • H. Schachter The joys of HexNAc. The synthesis and function of N- and O-glycan branches Glycoconj. J. 17 2000 465 483
    • (2000) Glycoconj. J. , vol.17 , pp. 465-483
    • Schachter, H.1
  • 2
    • 0035937505 scopus 로고    scopus 로고
    • Intracellular functions of N-linked glycans
    • A. Helenius, and M. Aebi Intracellular functions of N-linked glycans Science 291 2001 2364 2369
    • (2001) Science , vol.291 , pp. 2364-2369
    • Helenius, A.1    Aebi, M.2
  • 3
    • 0021891884 scopus 로고
    • Assembly of asparagine-linked oligosaccharides
    • R. Kornfeld, and S. Kornfeld Assembly of asparagine-linked oligosaccharides Annu. Rev. Biochem. 54 1985 631 664
    • (1985) Annu. Rev. Biochem. , vol.54 , pp. 631-664
    • Kornfeld, R.1    Kornfeld, S.2
  • 4
    • 33748195979 scopus 로고    scopus 로고
    • Glycosylation in cellular mechanisms of health and disease
    • K. Ohtsubo, and J.D. Marth Glycosylation in cellular mechanisms of health and disease Cell 126 2006 855 867
    • (2006) Cell , vol.126 , pp. 855-867
    • Ohtsubo, K.1    Marth, J.D.2
  • 5
    • 72249094196 scopus 로고    scopus 로고
    • Metabolism, cell surface organization, and disease
    • J.W. Dennis, I.R. Nabi, and M. Demetriou Metabolism, cell surface organization, and disease Cell 139 2009 1229 1241
    • (2009) Cell , vol.139 , pp. 1229-1241
    • Dennis, J.W.1    Nabi, I.R.2    Demetriou, M.3
  • 6
    • 0021107923 scopus 로고
    • Solution conformation of asparagine-linked oligosaccharides: Alpha(1-2)-, alpha(1-3)-, beta(1-2)-, and beta(1-4)-linked units
    • J.R. Brisson, and J.P. Carver Solution conformation of asparagine-linked oligosaccharides: alpha(1-2)-, alpha(1-3)-, beta(1-2)-, and beta(1-4)-linked units Biochemistry 22 1983 3671 3680
    • (1983) Biochemistry , vol.22 , pp. 3671-3680
    • Brisson, J.R.1    Carver, J.P.2
  • 7
    • 1642499128 scopus 로고    scopus 로고
    • Determination of modulation of ligand properties of synthetic complex-type biantennary N-glycans by introduction of bisecting GlcNAc in silico, in vitro and in vivo
    • S. André, C. Unverzagt, S. Kojima, M. Frank, J. Seifert, C. Fink, K. Kayser, C.W. von der Lieth, and H.J. Gabius Determination of modulation of ligand properties of synthetic complex-type biantennary N-glycans by introduction of bisecting GlcNAc in silico, in vitro and in vivo Eur. J. Biochem. 271 2004 118 134
    • (2004) Eur. J. Biochem. , vol.271 , pp. 118-134
    • André, S.1    Unverzagt, C.2    Kojima, S.3    Frank, M.4    Seifert, J.5    Fink, C.6    Kayser, K.7    Von Der Lieth, C.W.8    Gabius, H.J.9
  • 8
    • 0027289374 scopus 로고
    • CDNA cloning, expression, and chromosomal localization of human N-acetylglucosaminyltransferase III (GnT-III)
    • Y. Ihara, A. Nishikawa, T. Tohma, H. Soejima, N. Niikawa, and N. Taniguchi cDNA cloning, expression, and chromosomal localization of human N-acetylglucosaminyltransferase III (GnT-III) J. Biochem. 113 1993 692 698
    • (1993) J. Biochem. , vol.113 , pp. 692-698
    • Ihara, Y.1    Nishikawa, A.2    Tohma, T.3    Soejima, H.4    Niikawa, N.5    Taniguchi, N.6
  • 9
    • 0020356007 scopus 로고
    • A mouse lymphoma cell line resistant to the leukoagglutinating lectin from Phaseolus vulgaris is deficient in UDP-GlcNAc: Alpha-d-mannoside beta 1,6 N-acetylglucosaminyltransferase
    • R.D. Cummings, I.S. Trowbridge, and S. Kornfeld A mouse lymphoma cell line resistant to the leukoagglutinating lectin from Phaseolus vulgaris is deficient in UDP-GlcNAc: alpha-d-mannoside beta 1,6 N- acetylglucosaminyltransferase J. Biol. Chem. 257 1982 13421 13427
    • (1982) J. Biol. Chem. , vol.257 , pp. 13421-13427
    • Cummings, R.D.1    Trowbridge, I.S.2    Kornfeld, S.3
  • 10
    • 0033546414 scopus 로고    scopus 로고
    • Poly-N-acetyllactosamine synthesis in branched N-glycans is controlled by complemental branch specificity of I-extension enzyme and beta1,4- galactosyltransferase i
    • M. Ujita, J. McAuliffe, O. Hindsgaul, K. Sasaki, M.N. Fukuda, and M. Fukuda Poly-N-acetyllactosamine synthesis in branched N-glycans is controlled by complemental branch specificity of I-extension enzyme and beta1,4- galactosyltransferase I J. Biol. Chem. 274 1999 16717 16726
    • (1999) J. Biol. Chem. , vol.274 , pp. 16717-16726
    • Ujita, M.1    McAuliffe, J.2    Hindsgaul, O.3    Sasaki, K.4    Fukuda, M.N.5    Fukuda, M.6
  • 11
    • 0024215478 scopus 로고
    • Biosynthesis of blood group i-active polylactosaminoglycans. Partial purification and properties of an UDP-GlcNAc:N-acetyllactosaminide beta 1-3-N-acetylglucosaminyltransferase from Novikoff tumor cell ascites fluid
    • D.H. van den Eijnden, A.H. Koenderman, and W.E. Schiphorst Biosynthesis of blood group i-active polylactosaminoglycans. Partial purification and properties of an UDP-GlcNAc:N-acetyllactosaminide beta 1-3-N- acetylglucosaminyltransferase from Novikoff tumor cell ascites fluid J. Biol. Chem. 263 1988 12461 12471
    • (1988) J. Biol. Chem. , vol.263 , pp. 12461-12471
    • Van Den Eijnden, D.H.1    Koenderman, A.H.2    Schiphorst, W.E.3
  • 15
    • 0029911075 scopus 로고    scopus 로고
    • Transcriptional regulation of the N-acetylglucosaminyltransferase v gene in human bile duct carcinoma cells (HuCC-T1) is mediated by Ets-1
    • R. Kang, H. Saito, Y. Ihara, E. Miyoshi, N. Koyama, Y. Sheng, and N. Taniguchi Transcriptional regulation of the N-acetylglucosaminyltransferase V gene in human bile duct carcinoma cells (HuCC-T1) is mediated by Ets-1 J. Biol. Chem. 271 1996 26706 26712
    • (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    Taniguchi, N.7
  • 16
    • 0000656065 scopus 로고    scopus 로고
    • Regulation of the GnT-V promoter by transcription factor Ets-1 in various cancer cell lines
    • J.H. Ko, E. Miyoshi, K. Noda, A. Ekuni, R. Kang, Y. Ikeda, and N. Taniguchi Regulation of the GnT-V promoter by transcription factor Ets-1 in various cancer cell lines J. Biol. Chem. 274 1999 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    Taniguchi, N.7
  • 17
    • 0030754637 scopus 로고    scopus 로고
    • Transcriptional regulation of N-acetylglucosaminyltransferase v by the src oncogene
    • P. Buckhaults, L. Chen, N. Fregien, and M. Pierce Transcriptional regulation of N-acetylglucosaminyltransferase V by the src oncogene J. Biol. Chem. 272 1997 19575 19581
    • (1997) J. Biol. Chem. , vol.272 , pp. 19575-19581
    • Buckhaults, P.1    Chen, L.2    Fregien, N.3    Pierce, M.4
  • 18
    • 0032558738 scopus 로고    scopus 로고
    • The her-2/neu oncogene stimulates the transcription of N-acetylglucosaminyltransferase v and expression of its cell surface oligosaccharide products
    • L. Chen, W. Zhang, N. Fregien, and M. Pierce The her-2/neu oncogene stimulates the transcription of N-acetylglucosaminyltransferase V and expression of its cell surface oligosaccharide products Oncogene 17 1998 2087 2093
    • (1998) Oncogene , vol.17 , pp. 2087-2093
    • Chen, L.1    Zhang, W.2    Fregien, N.3    Pierce, M.4
  • 19
    • 0026014062 scopus 로고
    • Beta 1-6 branched oligosaccharides as a marker of tumor progression in human breast and colon neoplasia
    • B. Fernandes, U. Sagman, M. Auger, M. Demetrio, and J.W. Dennis Beta 1-6 branched oligosaccharides as a marker of tumor progression in human breast and colon neoplasia Cancer Res. 51 1991 718 723
    • (1991) Cancer Res. , vol.51 , pp. 718-723
    • Fernandes, B.1    Sagman, U.2    Auger, M.3    Demetrio, M.4    Dennis, J.W.5
  • 21
    • 0034061923 scopus 로고    scopus 로고
    • Suppression of tumor growth and metastasis in Mgat-5 deficient mice
    • M. Granovsky, J. Fata, J. Pawling, W. Muller, R. Khokha, and W. Dennis Suppression of tumor growth and metastasis in Mgat-5 deficient mice Nature 6 2000 306 312
    • (2000) Nature , vol.6 , pp. 306-312
    • Granovsky, M.1    Fata, J.2    Pawling, J.3    Muller, W.4    Khokha, R.5    Dennis, W.6
  • 22
    • 1842583688 scopus 로고    scopus 로고
    • Expression of N-acetylglucosaminyltransferase v is associated with prognosis and histology in non-small cell lung cancers
    • H. Dosaka-Akita, E. Miyoshi, O. Suzuki, T. Itoh, H. Katoh, and N. Taniguchi Expression of N-acetylglucosaminyltransferase V is associated with prognosis and histology in non-small cell lung cancers Clin. Cancer Res. 10 2004 1773 1779
    • (2004) Clin. Cancer Res. , vol.10 , pp. 1773-1779
    • Dosaka-Akita, H.1    Miyoshi, E.2    Suzuki, O.3    Itoh, T.4    Katoh, H.5    Taniguchi, N.6
  • 24
    • 0032753478 scopus 로고    scopus 로고
    • Expression of bisecting GlcNAc in pediatric brain tumors and its association with tumor cell response to vinblastine
    • A. Rebbaa, P.M. Chou, I. Vucic, B.L. Mirkin, T. Tomita, and E.G. Bremer Expression of bisecting GlcNAc in pediatric brain tumors and its association with tumor cell response to vinblastine Clin. Cancer Res. 5 1999 3661 3668
    • (1999) Clin. Cancer Res. , vol.5 , pp. 3661-3668
    • Rebbaa, A.1    Chou, P.M.2    Vucic, I.3    Mirkin, B.L.4    Tomita, T.5    Bremer, E.G.6
  • 25
  • 26
    • 77951072143 scopus 로고    scopus 로고
    • The bisecting GlcNAc on N-glycans inhibits growth factor signaling and retards mammary tumor progression
    • Y. Song, J.A. Aglipay, J.D. Bernstein, S. Goswami, and P. Stanley The bisecting GlcNAc on N-glycans inhibits growth factor signaling and retards mammary tumor progression Cancer Res. 70 2010 3361 3371
    • (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
  • 27
    • 0031564104 scopus 로고    scopus 로고
    • Remodeling of glycoconjugates on CD44 enhances cell adhesion to hyaluronate, tumor growth and metastasis in B16 melanoma cells expressing beta1,4-N-acetylglucosaminyltransferase III
    • Y. Sheng, M. Yoshimura, S. Inoue, K. Oritani, T. Nishiura, H. Yoshida, M. Ogawa, Y. Okajima, Y. Matsuzawa, and N. Taniguchi Remodeling of glycoconjugates on CD44 enhances cell adhesion to hyaluronate, tumor growth and metastasis in B16 melanoma cells expressing beta1,4-N-acetylglucosaminyltransferase III Int. J. Cancer 73 1997 850 858
    • (1997) Int. J. Cancer , vol.73 , pp. 850-858
    • Sheng, Y.1    Yoshimura, M.2    Inoue, S.3    Oritani, K.4    Nishiura, T.5    Yoshida, H.6    Ogawa, M.7    Okajima, Y.8    Matsuzawa, Y.9    Taniguchi, N.10
  • 28
    • 0029027831 scopus 로고
    • Supression of lung metastasis of B16 mouse melanoma by N-acetylglucosaminyltransferase III gene transfection
    • M. Yoshimura, A. Nishikawa, Y. Ihara, S. Taniguchi, and N. Taniguchi Supression of lung metastasis of B16 mouse melanoma by N- acetylglucosaminyltransferase III gene transfection Proc. Natl. Acad. Sci. U.S.A. 92 1995 8754 8758
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 8754-8758
    • Yoshimura, M.1    Nishikawa, A.2    Ihara, Y.3    Taniguchi, S.4    Taniguchi, N.5
  • 29
    • 34547844244 scopus 로고    scopus 로고
    • Identification of proteins bearing beta1-6 branched N-glycans in human melanoma cell lines from different progression stages by tandem mass spectrometry analysis
    • M. Przybyło, D. Martuszewska, E. Pocheć, D. Hoja-Łukowicz, and A. Lityńska Identification of proteins bearing beta1-6 branched N-glycans in human melanoma cell lines from different progression stages by tandem mass spectrometry analysis Biochim. Biophys. Acta 1770 2007 1427 1435
    • (2007) Biochim. Biophys. Acta , vol.1770 , pp. 1427-1435
    • Przybyło, M.1    Martuszewska, D.2    Pocheć, E.3    Hoja-Łukowicz, D.4    Lityńska, A.5
  • 32
    • 84876487888 scopus 로고    scopus 로고
    • L1CAM from human melanoma carries a novel type of N-glycan with Galβ1-4Galβ1- motif. Involvement of N-linked glycans in migratory and invasive behaviour of melanoma cells
    • D. Hoja-Łukowicz, P. Link-Lenczowski, A. Carpentieri, A. Amoresano, E. Pocheć, K.A. Artemenko, J. Bergquist, and A. Lityńska L1CAM from human melanoma carries a novel type of N-glycan with Galβ1-4Galβ1- motif. Involvement of N-linked glycans in migratory and invasive behaviour of melanoma cells Glycoconj. J. 30 2013 205 225
    • (2013) Glycoconj. J. , vol.30 , pp. 205-225
    • Hoja-Łukowicz, D.1    Link-Lenczowski, P.2    Carpentieri, A.3    Amoresano, A.4    Pocheć, E.5    Artemenko, K.A.6    Bergquist, J.7    Lityńska, A.8
  • 34
    • 34547610472 scopus 로고    scopus 로고
    • Inhibition of a specific N-glycosylation activity results in attenuation of breast carcinoma cell invasiveness-related phenotypes: Inhibition of epidermal growth factor-induced dephosphorylation of focal adhesion kinase
    • H.B. Guo, M. Randolph, and M. Pierce Inhibition of a specific N-glycosylation activity results in attenuation of breast carcinoma cell invasiveness-related phenotypes: inhibition of epidermal growth factor-induced dephosphorylation of focal adhesion kinase J. Biol. Chem. 282 2007 22150 22162
    • (2007) J. Biol. Chem. , vol.282 , pp. 22150-22162
    • Guo, H.B.1    Randolph, M.2    Pierce, M.3
  • 35
    • 57649219437 scopus 로고    scopus 로고
    • CCL2 increases X4-tropic HIV-1 entry into resting CD4+ T cells
    • G.R. Campbell, and S.A. Spector CCL2 increases X4-tropic HIV-1 entry into resting CD4+ T cells J. Biol. Chem. 283 2008 30745 30753
    • (2008) J. Biol. Chem. , vol.283 , pp. 30745-30753
    • Campbell, G.R.1    Spector, S.A.2
  • 36
    • 0017613512 scopus 로고
    • A simplification of the protein assay method of Lowry et al which is more generally applicable
    • G.L. Peterson A simplification of the protein assay method of Lowry et al. which is more generally applicable Anal. Biochem. 83 1977 346 356
    • (1977) Anal. Biochem. , vol.83 , pp. 346-356
    • Peterson, G.L.1
  • 37
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 38
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • H. Towbin, T. Staehelin, and J. Gordon Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications Proc. Natl. Acad. Sci. U.S.A. 76 1979 4350 4354
    • (1979) Proc. Natl. Acad. Sci. U.S.A. , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 39
    • 13544255695 scopus 로고    scopus 로고
    • N-glycoproteins bearing β-1,6 branched oligosaccharides from A375 human melanoma cell line analysed by tandem mass spectrometry
    • D. Ochwat, D. Hoja-Łukowicz, and A. Lityńska N-glycoproteins bearing β-1,6 branched oligosaccharides from A375 human melanoma cell line analysed by tandem mass spectrometry Melanoma Res. 14 2004 479 485
    • (2004) Melanoma Res. , vol.14 , pp. 479-485
    • Ochwat, D.1    Hoja-Łukowicz, D.2    Lityńska, A.3
  • 40
    • 0025226048 scopus 로고
    • Structural characterization of glycoprotein carbohydrate chains by using digoxigenin-labeled lectins on blots
    • A. Haselbeck, E. Schickaneder, H. von der Eltz, and W. Hösel Structural characterization of glycoprotein carbohydrate chains by using digoxigenin-labeled lectins on blots Anal. Biochem. 191 1990 25 30
    • (1990) Anal. Biochem. , vol.191 , pp. 25-30
    • Haselbeck, A.1    Schickaneder, E.2    Von Der Eltz, H.3    Hösel, W.4
  • 41
    • 0024840851 scopus 로고
    • Glycosyltransferase assays using pyridylaminated acceptors: N-acetylglucosaminyltransferase III, IV, and v
    • N. Taniguchi, A. Nishikawa, S. Fujii, and J.G. Gu Glycosyltransferase assays using pyridylaminated acceptors: N-acetylglucosaminyltransferase III, IV, and V Methods Enzymol. 179 1989 397 408
    • (1989) Methods Enzymol. , vol.179 , pp. 397-408
    • Taniguchi, N.1    Nishikawa, A.2    Fujii, S.3    Gu, J.G.4
  • 42
    • 0031734879 scopus 로고    scopus 로고
    • A general approach to desalting oligosaccharides released from glycoproteins
    • N.H. Packer, M.A. Lawson, D.R. Jardine, and J.W. Redmond A general approach to desalting oligosaccharides released from glycoproteins Glycoconj. J. 15 1998 737 747
    • (1998) Glycoconj. J. , vol.15 , pp. 737-747
    • Packer, N.H.1    Lawson, M.A.2    Jardine, D.R.3    Redmond, J.W.4
  • 43
    • 0029164230 scopus 로고
    • Nonselective and efficient fluorescent labeling of glycans using 2-amino benzamide and anthranilic acid
    • J.C. Bigge, T.P. Patel, J.A. Bruce, P.N. Goulding, S.M. Charles, and R.B. Parekh Nonselective and efficient fluorescent labeling of glycans using 2-amino benzamide and anthranilic acid Anal. Biochem 230 1995 229 238
    • (1995) Anal. Biochem , vol.230 , pp. 229-238
    • Bigge, J.C.1    Patel, T.P.2    Bruce, J.A.3    Goulding, P.N.4    Charles, S.M.5    Parekh, R.B.6
  • 44
    • 3242730231 scopus 로고    scopus 로고
    • Analysis of fluorescently labeled glycosphingolipid-derived oligosaccharides following ceramide glycanase digestion and anthranilic acid labeling
    • D.C. Neville, V. Coquard, D.A. Priestman, D.J. Te Vruchte, D.J. Sillence, R.A. Dwek, F.M. Platt, and T.D. Butters Analysis of fluorescently labeled glycosphingolipid-derived oligosaccharides following ceramide glycanase digestion and anthranilic acid labeling Anal. Biochem. 331 2004 275 282
    • (2004) Anal. Biochem. , vol.331 , pp. 275-282
    • Neville, D.C.1    Coquard, V.2    Priestman, D.A.3    Te Vruchte, D.J.4    Sillence, D.J.5    Dwek, R.A.6    Platt, F.M.7    Butters, T.D.8
  • 45
    • 0242551684 scopus 로고    scopus 로고
    • Ras oncogene directs expression of a differentially sialylated, functionally altered beta1 integrin
    • E.C. Seales, G.A. Jurado, A. Singhal, and S.L. Bellis Ras oncogene directs expression of a differentially sialylated, functionally altered beta1 integrin Oncogene 22 2003 7137 7145
    • (2003) Oncogene , vol.22 , pp. 7137-7145
    • Seales, E.C.1    Jurado, G.A.2    Singhal, A.3    Bellis, S.L.4
  • 47
    • 0030884364 scopus 로고    scopus 로고
    • N-glycosylation is requisite for the enzyme activity and Golgi retention of N-acetylglucosaminyltransferase III
    • K. Nagai, Y. Ihara, Y. Wada, and N. Taniguchi N-glycosylation is requisite for the enzyme activity and Golgi retention of N- acetylglucosaminyltransferase III Glycobiology 7 1997 769 776
    • (1997) Glycobiology , vol.7 , pp. 769-776
    • Nagai, K.1    Ihara, Y.2    Wada, Y.3    Taniguchi, N.4
  • 48
    • 0037478593 scopus 로고    scopus 로고
    • Caveolin-1 regulates the functional localization of N- acetylglucosaminyltransferase III within the golgi apparatus
    • K. Sasai, Y. Ikeda, H. Ihara, K. Honke, and N. Taniguchi Caveolin-1 regulates the functional localization of N- acetylglucosaminyltransferase III within the golgi apparatus J. Biol. Chem. 278 2003 25295 25301
    • (2003) J. Biol. Chem. , vol.278 , pp. 25295-25301
    • Sasai, K.1    Ikeda, Y.2    Ihara, H.3    Honke, K.4    Taniguchi, N.5
  • 49
    • 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
    • R.D. Cummings, and S. Kornfeld 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. 57 1982 11230 11234
    • (1982) J. Biol. Chem. , vol.57 , pp. 11230-11234
    • Cummings, R.D.1    Kornfeld, S.2
  • 50
    • 1642309129 scopus 로고    scopus 로고
    • Glycosylation defining cancer cell motility and invasiveness
    • M. Ono, and S. Hakomori Glycosylation defining cancer cell motility and invasiveness Glycoconj. J. 20 2004 71 78
    • (2004) Glycoconj. J. , vol.20 , pp. 71-78
    • Ono, M.1    Hakomori, S.2
  • 52
    • 0030913615 scopus 로고    scopus 로고
    • Expression of MCAM/MUC18 by human melanoma cells leads to increased tumor growth and metastasis
    • S. Xie, M. Luca, S. Huang, M. Gutman, R. Reich, J.P. Johnson, and M. Bar-Eli Expression of MCAM/MUC18 by human melanoma cells leads to increased tumor growth and metastasis Cancer Res. 57 1997 2295 2303
    • (1997) Cancer Res. , vol.57 , pp. 2295-2303
    • Xie, S.1    Luca, M.2    Huang, S.3    Gutman, M.4    Reich, R.5    Johnson, J.P.6    Bar-Eli, M.7
  • 53
    • 0020491419 scopus 로고
    • Sialylation of glycoprotein oligosaccharides N-linked to asparagine. Enzymatic characterization of a Gal beta 1 to 3(4)GlcNAc alpha 2 to 3 sialyltransferase and a Gal beta 1 to 4GlcNAc alpha 2 to 6 sialyltransferase from rat liver
    • J. Weinstein, U. de Souza-e-Silva, and J.C. Paulson Sialylation of glycoprotein oligosaccharides N-linked to asparagine. Enzymatic characterization of a Gal beta 1 to 3(4)GlcNAc alpha 2 to 3 sialyltransferase and a Gal beta 1 to 4GlcNAc alpha 2 to 6 sialyltransferase from rat liver J. Biol. Chem. 257 1982 13845 13853
    • (1982) J. Biol. Chem. , vol.257 , pp. 13845-13853
    • Weinstein, J.1    De Souza-E-Silva, U.2    Paulson, J.C.3
  • 54
    • 0037016738 scopus 로고    scopus 로고
    • Purification, characterization, and subunit structure of rat core 1 Beta1,3-galactosyltransferase
    • T. Ju, R.D. Cummings, and W.M. Canfield Purification, characterization, and subunit structure of rat core 1 Beta1,3-galactosyltransferase J. Biol. Chem. 277 2002 169 177
    • (2002) J. Biol. Chem. , vol.277 , pp. 169-177
    • Ju, T.1    Cummings, R.D.2    Canfield, W.M.3
  • 57
    • 0029665858 scopus 로고    scopus 로고
    • Human N-acetylglucosaminyltransferase III gene is transcribed from multiple promoters
    • N. Koyama, E. Miyoshi, Y. Ihara, R. Kang, A. Nishikawa, and N. Taniguchi Human N-acetylglucosaminyltransferase III gene is transcribed from multiple promoters Eur. J. Biochem. 238 1996 853 861
    • (1996) Eur. J. Biochem. , vol.238 , pp. 853-861
    • Koyama, N.1    Miyoshi, E.2    Ihara, Y.3    Kang, R.4    Nishikawa, A.5    Taniguchi, N.6
  • 58
    • 33646686860 scopus 로고    scopus 로고
    • GnT-V expression and metastatic phenotypes in macrophage-melanoma fusion hybrids is down-regulated by 5-Aza-dC: Evidence for methylation sensitive, extragenic regulation of GnT-V transcription
    • A.K. Chakraborty, F. Sousa Jde, D. Chakraborty, Y. Funasaka, M. Bhattacharya, A. Chatterjee, and J. Pawelek GnT-V expression and metastatic phenotypes in macrophage-melanoma fusion hybrids is down-regulated by 5-Aza-dC: evidence for methylation sensitive, extragenic regulation of GnT-V transcription Gene 7 2006 166 173
    • (2006) Gene , vol.7 , pp. 166-173
    • Chakraborty, A.K.1    Sousa Jde, F.2    Chakraborty, D.3    Funasaka, Y.4    Bhattacharya, M.5    Chatterjee, A.6    Pawelek, J.7
  • 59
    • 84858138360 scopus 로고    scopus 로고
    • Loss and recovery of Mgat3 and GnT-III Mediated E-cadherin N-glycosylation is a mechanism involved in epithelial-mesenchymal-epithelial transitions
    • S.S. Pinho, P. Oliveira, J. Cabral, S. Carvalho, D. Huntsman, F. Gärtner, R. Seruca, C.A. Reis, and C. Oliveira Loss and recovery of Mgat3 and GnT-III Mediated E-cadherin N-glycosylation is a mechanism involved in epithelial-mesenchymal-epithelial transitions PLoS One 7 2012 e33191
    • (2012) PLoS One , vol.7 , pp. 33191
    • Pinho, S.S.1    Oliveira, P.2    Cabral, J.3    Carvalho, S.4    Huntsman, D.5    Gärtner, F.6    Seruca, R.7    Reis, C.A.8    Oliveira, C.9
  • 60
    • 84857692860 scopus 로고    scopus 로고
    • Branched N-glycans and their implications for cell adhesion, signaling and clinical applications for cancer biomarkers and in therapeutics
    • N. Taniguchi, and H. Korekane Branched N-glycans and their implications for cell adhesion, signaling and clinical applications for cancer biomarkers and in therapeutics BMB Rep. 44 2011 772 781
    • (2011) BMB Rep. , vol.44 , pp. 772-781
    • Taniguchi, N.1    Korekane, H.2
  • 61
    • 39149093366 scopus 로고    scopus 로고
    • Loss of expression of N-acetylglucosaminyltransferase Va results in altered gene expression of glycosyltransferases and galectins
    • H.B. Guo, A. Nairn, K. Harris, M. Randolph, G. Alvarez-Manilla, K. Moremen, and M. Pierce Loss of expression of N-acetylglucosaminyltransferase Va results in altered gene expression of glycosyltransferases and galectins FEBS Lett. 582 2008 527 535
    • (2008) FEBS Lett. , vol.582 , pp. 527-535
    • Guo, H.B.1    Nairn, A.2    Harris, K.3    Randolph, M.4    Alvarez-Manilla, G.5    Moremen, K.6    Pierce, M.7
  • 63
    • 0035980062 scopus 로고    scopus 로고
    • Down-regulation 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
    • S. Koyota, Y. Ikeda, S. Miyagawa, H. Ihara, M. Koma, K. Honke, R. Shirakura, and N. Taniguchi Down-regulation 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 2001 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    Taniguchi, N.8
  • 64
    • 0021152175 scopus 로고
    • Control of glycoprotein synthesis. The in vitro synthesis by hen oviduct membrane preparations of hybrid asparagine-linked oligosaccharides containing 5 mannose residues
    • S.D. Allen, D. Tsai, and H. Schachter Control of glycoprotein synthesis. The in vitro synthesis by hen oviduct membrane preparations of hybrid asparagine-linked oligosaccharides containing 5 mannose residues J. Biol. Chem. 259 1984 6984 6990
    • (1984) J. Biol. Chem. , vol.259 , pp. 6984-6990
    • Allen, S.D.1    Tsai, D.2    Schachter, H.3
  • 65
    • 0024236138 scopus 로고
    • Control of glycoprotein synthesis. The use of oligosaccharide substrates and HPLC to study the sequential pathway for N-acetylglucosaminyltransferases I, II, III, IV, V, and VI in the biosynthesis of highly branched N-glycans by hen oviduct membranes
    • I. Brockhausen, J.P. Carver, and H. Schachter Control of glycoprotein synthesis. The use of oligosaccharide substrates and HPLC to study the sequential pathway for N-acetylglucosaminyltransferases I, II, III, IV, V, and VI in the biosynthesis of highly branched N-glycans by hen oviduct membranes Biochem. Cell Biol. 66 1988 1134 1151
    • (1988) Biochem. Cell Biol. , vol.66 , pp. 1134-1151
    • Brockhausen, I.1    Carver, J.P.2    Schachter, H.3
  • 66
    • 0037014655 scopus 로고    scopus 로고
    • The action of N-acetylglucosaminyltransferase-V is prevented by the bisecting GlcNAc residue at the catalytic step
    • K. Sasai, Y. Ikeda, H. Eguchi, T. Tsuda, K. Honke, and N. Taniguchi The action of N-acetylglucosaminyltransferase-V is prevented by the bisecting GlcNAc residue at the catalytic step FEBS Lett. 522 2002 151 155
    • (2002) FEBS Lett. , vol.522 , pp. 151-155
    • Sasai, K.1    Ikeda, Y.2    Eguchi, H.3    Tsuda, T.4    Honke, K.5    Taniguchi, N.6
  • 67
    • 0020108081 scopus 로고
    • Product-identification and substrate-specificity studies of the GDP-L-fucose:2-acetamido-2-deoxy-beta-D-glucoside (FUC goes to Asn-linked GlcNAc) 6-alpha-L-fucosyltransferase in a Golgi-rich fraction from porcine liver
    • G.D. Longmore, and H. Schachter Product-identification and substrate-specificity studies of the GDP-L-fucose:2-acetamido-2-deoxy-beta-D- glucoside (FUC goes to Asn-linked GlcNAc) 6-alpha-L-fucosyltransferase in a Golgi-rich fraction from porcine liver Carbohydr. Res. 100 1982 365 392
    • (1982) Carbohydr. Res. , vol.100 , pp. 365-392
    • Longmore, G.D.1    Schachter, H.2
  • 69
    • 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
    • K. Inamori, T. Endo, Y. Ide, S. Fujii, J. Gu, K. Honke, and N. Taniguchi 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 2003 43102 43109
    • (2003) J. Biol. Chem. , vol.278 , pp. 43102-43109
    • Inamori, K.1    Endo, T.2    Ide, Y.3    Fujii, S.4    Gu, J.5    Honke, K.6    Taniguchi, N.7
  • 71
    • 84865229984 scopus 로고    scopus 로고
    • Developmental expression of the neuron-specific N- acetylglucosaminyltransferase Vb (GnT-Vb/IX) and identification of its in vivo glycan products in comparison with those of its paralog, GnT-V
    • J.K. Lee, R.T. Matthews, J.M. Lim, K. Swanier, L. Wells, and J.M. Pierce Developmental expression of the neuron-specific N-acetylglucosaminyltransferase Vb (GnT-Vb/IX) and identification of its in vivo glycan products in comparison with those of its paralog, GnT-V J. Biol. Chem. 287 2012 28526 28536
    • (2012) J. Biol. Chem. , vol.287 , pp. 28526-28536
    • Lee, J.K.1    Matthews, R.T.2    Lim, J.M.3    Swanier, K.4    Wells, L.5    Pierce, J.M.6
  • 72
    • 0029933659 scopus 로고    scopus 로고
    • Aberrant glycosylation of E-cadherin enhances cell-cell binding to suppress metastasis
    • M. Yoshimura, Y. Ihara, Y. Matsuzawa, and N. Taniguchi Aberrant glycosylation of E-cadherin enhances cell-cell binding to suppress metastasis J. Biol. Chem. 271 1996 13811 13815
    • (1996) J. Biol. Chem. , vol.271 , pp. 13811-13815
    • Yoshimura, M.1    Ihara, Y.2    Matsuzawa, Y.3    Taniguchi, N.4
  • 73
    • 61849164561 scopus 로고    scopus 로고
    • Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry
    • R. Chen, X. Jiang, D. Sun, G. Han, F. Wang, M. Ye, L. Wang, and H. Zou Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry J. Proteome Res. 8 2009 651 661
    • (2009) J. Proteome Res. , vol.8 , pp. 651-661
    • Chen, R.1    Jiang, X.2    Sun, D.3    Han, G.4    Wang, F.5    Ye, M.6    Wang, L.7    Zou, H.8
  • 74
    • 0028330535 scopus 로고
    • Isolation and functional characterization of the A32 melanoma-associated antigen
    • I.M. Shih, D.E. Elder, D. Speicher, J.P. Johnson, and M. Herlyn Isolation and functional characterization of the A32 melanoma-associated antigen Cancer Res. 54 1994 2514 2520
    • (1994) Cancer Res. , vol.54 , pp. 2514-2520
    • Shih, I.M.1    Elder, D.E.2    Speicher, D.3    Johnson, J.P.4    Herlyn, M.5
  • 76
    • 0031035420 scopus 로고    scopus 로고
    • Bisecting GlcNAc structures act as negative sorting signals for cell surface glycoproteins in forskolin-treated rat hepatoma cells
    • A.S. Sultan, E. Miyoshi, Y. Ihara, A. Nishikawa, Y. Tsukada, and N. Taniguchi Bisecting GlcNAc structures act as negative sorting signals for cell surface glycoproteins in forskolin-treated rat hepatoma cells J. Biol. Chem. 272 1997 2866 2872
    • (1997) J. Biol. Chem. , vol.272 , pp. 2866-2872
    • Sultan, A.S.1    Miyoshi, E.2    Ihara, Y.3    Nishikawa, A.4    Tsukada, Y.5    Taniguchi, N.6
  • 77
    • 0024791128 scopus 로고
    • MUC18, a marker of tumor progression in human melanoma, shows sequence similarity to the neural cell adhesion molecules of the immunoglobulin superfamily
    • J.M. Lehmann, G. Riethmüller, and J.P. Johnson MUC18, a marker of tumor progression in human melanoma, shows sequence similarity to the neural cell adhesion molecules of the immunoglobulin superfamily Proc. Natl. Acad. Sci. U.S.A. 86 1989 9891 9895
    • (1989) Proc. Natl. Acad. Sci. U.S.A. , vol.86 , pp. 9891-9895
    • Lehmann, J.M.1    Riethmüller, G.2    Johnson, J.P.3
  • 78
    • 84855946358 scopus 로고    scopus 로고
    • Recognition of CD146 as an ERM-binding protein offers novel mechanisms for melanoma cell migration
    • Y. Luo, C. Zheng, J. Zhang, D. Lu, J. Zhuang, S. Xing, J. Feng, D. Yang, and X. Yan Recognition of CD146 as an ERM-binding protein offers novel mechanisms for melanoma cell migration Oncogene 31 2012 306 321
    • (2012) Oncogene , vol.31 , pp. 306-321
    • Luo, Y.1    Zheng, C.2    Zhang, J.3    Lu, D.4    Zhuang, J.5    Xing, S.6    Feng, J.7    Yang, D.8    Yan, X.9
  • 80
    • 0033031839 scopus 로고    scopus 로고
    • Control of metastasis by Asn-linked, beta1-6 branched oligosaccharides in mouse mammary cancer cells
    • P.J. Seberger, and W.G. Chaney Control of metastasis by Asn-linked, beta1-6 branched oligosaccharides in mouse mammary cancer cells Glycobiology 9 1999 235 241
    • (1999) Glycobiology , vol.9 , pp. 235-241
    • Seberger, P.J.1    Chaney, W.G.2
  • 82
    • 0030031865 scopus 로고    scopus 로고
    • Circulating malignant lymphocytes from Sezary syndrome express high level of glycoproteins carrying beta (1-6)N-acetylglucosamine-branched N-linked oligosaccharides
    • C. Derappe, G. Haentjens, S. Lemaire, J.P. Feugeas, C. Lebbe, V. Pasqualetto, A. Bussel, M. Aubery, and D. Néel Circulating malignant lymphocytes from Sezary syndrome express high level of glycoproteins carrying beta (1-6)N-acetylglucosamine-branched N-linked oligosaccharides Leukemia 10 1996 138 141
    • (1996) Leukemia , vol.10 , pp. 138-141
    • Derappe, C.1    Haentjens, G.2    Lemaire, S.3    Feugeas, J.P.4    Lebbe, C.5    Pasqualetto, V.6    Bussel, A.7    Aubery, M.8    Néel, D.9
  • 83
    • 3042520927 scopus 로고    scopus 로고
    • Transfection of 2,6 and 2,3-sialyltransferase genes and GlcNAc-transferase genes into human glioma cell line U-373 MG affects glycoconjugate expression and enhances cell death
    • G. Dawson, J.R. Moskal, and S.A. Dawson Transfection of 2,6 and 2,3-sialyltransferase genes and GlcNAc-transferase genes into human glioma cell line U-373 MG affects glycoconjugate expression and enhances cell death J. Neurochem. 89 2004 1436 1444
    • (2004) J. Neurochem. , vol.89 , pp. 1436-1444
    • Dawson, G.1    Moskal, J.R.2    Dawson, S.A.3
  • 84
    • 0026101344 scopus 로고
    • N-linked oligosaccharide processing and autocrine stimulation of tumor cell proliferation
    • I. VanderElst, and J.W. Dennis N-linked oligosaccharide processing and autocrine stimulation of tumor cell proliferation Exp. Cell Res. 192 1991 612 621
    • (1991) Exp. Cell Res. , vol.192 , pp. 612-621
    • Vanderelst, I.1    Dennis, J.W.2
  • 85
    • 84871597069 scopus 로고    scopus 로고
    • All-trans-retinoic acid modulates ICAM-1 N-glycan composition by influencing GnT-III levels and inhibits cell adhesion and trans-endothelial migration
    • C. Chen, D. Diao, L. Guo, M. Shi, J. Gao, M. Hu, M. Yu, L. Qian, and N. Guo All-trans-retinoic acid modulates ICAM-1 N-glycan composition by influencing GnT-III levels and inhibits cell adhesion and trans-endothelial migration PLoS One 7 2012 e52975
    • (2012) PLoS One , vol.7 , pp. 52975
    • Chen, C.1    Diao, D.2    Guo, L.3    Shi, M.4    Gao, J.5    Hu, M.6    Yu, M.7    Qian, L.8    Guo, N.9
  • 87
    • 21744431575 scopus 로고    scopus 로고
    • The sweet and sour of cancer: Glycans as novel therapeutic targets
    • M.M. Fuster, and J.D. Esko The sweet and sour of cancer: glycans as novel therapeutic targets Nat. Rev. Cancer 5 2005 526 542
    • (2005) Nat. Rev. Cancer , vol.5 , pp. 526-542
    • Fuster, M.M.1    Esko, J.D.2


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