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Volumn 16, Issue 3, 2003, Pages 343-353

Remodeling of the major mouse xenoantigen, Galα1-3Galβ1-4GlcNAc- R, by N-acetylglucosaminyltransferase-III

Author keywords

GnT III; N Acetylglucosamine; N Glycosylation; Transgenic Mice; Xenotransplantation

Indexed keywords

ALBUMIN; ALPHA 1,3 GALACTOSYLTRANSFERASE; ALPHA 6 DEXTRO MANNOSIDE BETA 1,6 N ACETYLGLUCOSAMINYLTRANSFERASE V; BETA DEXTRO MANNOSIDE BETA 1,4 N ACETYLGLUCOSAMINYLTRANSFERASE III; EPITOPE; N ACETYLGLUCOSAMINE; N ACETYLGLUCOSAMINYLTRANSFERASE; UNCLASSIFIED DRUG; BETA 1,4 MANNOSYL GLYCOPROTEIN BETA 1,4 N ACETYLGLUCOSAMINYLTRANSFERASE; BETA-1,4-MANNOSYL-GLYCOPROTEIN BETA-1,4-N-ACETYLGLUCOSAMINYLTRANSFERASE; HETEROPHILE ANTIGEN; OLIGOSACCHARIDE;

EID: 1442307620     PISSN: 10168478     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (6)

References (60)
  • 1
    • 0028871648 scopus 로고
    • Cloning and chromosomal mapping of the mouse Mgat3 gene encoding N-acetylglucosaminyltransferase III
    • Bhaumik, M., Seldin, M. F., and Stanley, P. (1995) Cloning and chromosomal mapping of the mouse Mgat3 gene encoding N- acetylglucosaminyltransferase III. Gene 164, 295-300.
    • (1995) Gene , vol.164 , pp. 295-300
    • Bhaumik, M.1    Seldin, M.F.2    Stanley, P.3
  • 2
    • 0023277545 scopus 로고
    • Single step method of RNA isolation by acid guanidnium thiocyanate-phenolchloroform extraction
    • Chomczynski, P. and Sacchi, N. (1987) Single step method of RNA isolation by acid guanidnium thiocyanate-phenolchloroform extraction. Anal. Biochem. 162, 156-159.
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 3
    • 0030742322 scopus 로고    scopus 로고
    • Down-regulation of Gal α(1,3)Gal expression by α1,2- fucosyltransferase: Further characterization of α1,2-fucosyltransferase transgenic mice
    • Cohney, S., McKenzie, I. F., Patton, K., Prenzoska, J., Ostenreid, K., Fodor, W. L., and Sandrin, M. S. (1997) Down-regulation of Gal α(1,3)Gal expression by α1,2-fucosyltransferase: further characterization of α1,2-fucosyltransferase transgenic mice. Transplantation 64, 495-500.
    • (1997) Transplantation , vol.64 , pp. 495-500
    • Cohney, S.1    McKenzie, I.F.2    Patton, K.3    Prenzoska, J.4    Ostenreid, K.5    Fodor, W.L.6    Sandrin, M.S.7
  • 4
    • 0033208674 scopus 로고    scopus 로고
    • Expression of the human α1,2-fucosyltransferase in transgenic pigs modifies the cell surface carbohydrate phenotype and confers resistance to human serum-mediated cytolysis
    • Costa, C., Zhao, L., Burton, W. V., Bondioli, K. R., Williams, B. L., Hoagland, T. A., Ditullio, P. A., Ebert, K. M., and Fodor, W. L. (1999) Expression of the human α1,2-fucosyltransferase in transgenic pigs modifies the cell surface carbohydrate phenotype and confers resistance to human serum-mediated cytolysis. FASEB J. 13, 1762-1773.
    • (1999) FASEB J. , vol.13 , pp. 1762-1773
    • Costa, C.1    Zhao, L.2    Burton, W.V.3    Bondioli, K.R.4    Williams, B.L.5    Hoagland, T.A.6    Ditullio, P.A.7    Ebert, K.M.8    Fodor, W.L.9
  • 5
    • 0020479688 scopus 로고
    • Characterization of structural determinants required for the high-affinity interaction of asparagine-linked oligosaccharides with immobilized Phaseolus vulgaris leukoagglutinating and erythroagglutinating lectins
    • Cummings, R. D. and Kornfeld, S. (1982) Characterization of structural determinants required for the high-affinity interaction of asparagine-linked oligosaccharides with immobilized Phaseolus vulgaris leukoagglutinating and erythroagglutinating lectins. J. Biol. Chem. 257, 11230-11234.
    • (1982) J. Biol. Chem. , vol.257 , pp. 11230-11234
    • Cummings, R.D.1    Kornfeld, S.2
  • 6
    • 0037349966 scopus 로고    scopus 로고
    • Xenotransplantation: Where are we today?
    • Dooldeniya, M. D. and Warrens, A. N. (2003) Xenotransplantation: where are we today? J. R. Soc. Med. 96, 111-117.
    • (2003) J. R. Soc. Med. , vol.96 , pp. 111-117
    • Dooldeniya, M.D.1    Warrens, A.N.2
  • 7
    • 0021796301 scopus 로고
    • Immunochemistry of I/i-active oligo- and polyglycosylceramides from rabbit erythrocyte membranes. Characterization of linear, di-, and triantennary neolactoglycosphingolipids
    • Egge, H., Kordowicz, M., Peter-Katalinic, J., and Hanfland, P. (1985) Immunochemistry of I/i-active oligo- and polyglycosylceramides from rabbit erythrocyte membranes. Characterization of linear, di-, and triantennary neolactoglycosphingolipids. J. Biol. Chem. 260, 4927-4935.
    • (1985) J. Biol. Chem. , vol.260 , pp. 4927-4935
    • Egge, H.1    Kordowicz, M.2    Peter-Katalinic, J.3    Hanfland, P.4
  • 8
    • 0028080349 scopus 로고
    • Expression of a functional human complement inhibitor in a transgenic pig as a model for the prevention of xenogeneic hyperacute organ rejection
    • Fodor, W. L., Williams, B. L., Matis, L. A., Madri, J. A., Rollins, S. A., Knight, J. W., Velander, W., and Squinto, S. P. (1994) Expression of a functional human complement inhibitor in a transgenic pig as a model for the prevention of xenogeneic hyperacute organ rejection. Proc. Natl. Acad. Sci. USA 91, 11153-11157.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 11153-11157
    • Fodor, W.L.1    Williams, B.L.2    Matis, L.A.3    Madri, J.A.4    Rollins, S.A.5    Knight, J.W.6    Velander, W.7    Squinto, S.P.8
  • 9
    • 0034851054 scopus 로고    scopus 로고
    • The alpha-gal epitope (Galα1-3Galβ1-4Glc NAc-R) in xenotransplantation
    • Galili, U. (2001) The alpha-gal epitope (Galα1-3Galβ1-4Glc NAc-R) in xenotransplantation. Biochimie 83, 557-563
    • (2001) Biochimie , vol.83 , pp. 557-563
    • Galili, U.1
  • 10
    • 0025773203 scopus 로고
    • Gene sequences suggest inactivation of α1,3-galactosyltransferase in catarrhines after the divergence of apes from monkeys
    • Galili, U. and Swanson, K. (1991) Gene sequences suggest inactivation of α1,3-galactosyltransferase in catarrhines after the divergence of apes from monkeys. Proc. Natl. Acad. Sci. USA 88, 7401-7404.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 7401-7404
    • Galili, U.1    Swanson, K.2
  • 11
    • 0021678856 scopus 로고
    • A unique natural human IgG antibody with anti-alpha-galactosyl specificity
    • Galili, U., Rachmilewitz, E. A., Peleg, A., and Flechner, I. (1984) A unique natural human IgG antibody with anti-alpha-galactosyl specificity. J. Exp. Med. 160, 1519-1531.
    • (1984) J. Exp. Med. , vol.160 , pp. 1519-1531
    • Galili, U.1    Rachmilewitz, E.A.2    Peleg, A.3    Flechner, I.4
  • 12
    • 0000665022 scopus 로고
    • Evolutionary relationship between the natural anti-Gal antibody and the Galα1-3Gal epitope in primates
    • Galili, U., Clark, M. R., Shohet, S. B., Buehler, J., and Macher, B. A. (1987) Evolutionary relationship between the natural anti-Gal antibody and the Galα1-3Gal epitope in primates. Proc. Natl. Acad. Sci. USA 84, 1369-1373.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 1369-1373
    • Galili, U.1    Clark, M.R.2    Shohet, S.B.3    Buehler, J.4    Macher, B.A.5
  • 13
    • 0024585483 scopus 로고
    • Aberrant glycosylation in tumors and tumor-associated carbohydrate antigens
    • Hakomori, S. (1989) Aberrant glycosylation in tumors and tumor-associated carbohydrate antigens. Adv. Cancer Res. 52, 257-331.
    • (1989) Adv. Cancer Res. , vol.52 , pp. 257-331
    • Hakomori, S.1
  • 14
    • 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
  • 15
    • 13144259662 scopus 로고    scopus 로고
    • Ectopic expression of N-acetylglucosaminyltransferase III in transgenic hepatocytes disrupts apolipoprotein B secretion and induces aberrant cellular morphology with lipid storage
    • Ihara, Y., Yoshimura, M., Miyoshi, E., Nishikawa, A., Sultan, A. S., Toyosawa, S., Ohnishi, A., Suzuki, M., Yamamura, K., Ijuhin, N., and Taniguchi, N. (1998) Ectopic expression of N-acetylglucosaminyltransferase III in transgenic hepatocytes disrupts apolipoprotein B secretion and induces aberrant cellular morphology with lipid storage. Proc. Natl. Acad. Sci. USA 95, 2526-2530.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 2526-2530
    • Ihara, Y.1    Yoshimura, M.2    Miyoshi, E.3    Nishikawa, A.4    Sultan, A.S.5    Toyosawa, S.6    Ohnishi, A.7    Suzuki, M.8    Yamamura, K.9    Ijuhin, N.10    Taniguchi, N.11
  • 16
    • 0024847844 scopus 로고
    • N-acetylglucosaminyltransferase III in human serum, and liver and hepatoma tissues: Increased activity in liver cirrhosis and hepatoma patients
    • Ishibashi, K., Nishikawa, A., Hayashi, N., Kasahara, A., Sato, N., Fujii, S., Kamada, T., and Taniguchi, N. (1989) N-acetylglucosaminyltransferase III in human serum, and liver and hepatoma tissues: increased activity in liver cirrhosis and hepatoma patients. Clin. Chim. Acta 185, 325-332.
    • (1989) Clin. Chim. Acta , vol.185 , pp. 325-332
    • Ishibashi, K.1    Nishikawa, A.2    Hayashi, N.3    Kasahara, A.4    Sato, N.5    Fujii, S.6    Kamada, T.7    Taniguchi, N.8
  • 18
    • 0037590899 scopus 로고    scopus 로고
    • A Salmonella typhimurium rfaE mutant recovers invasiveness for human epithelial cells when complemented by wild type rfaE (controlling biosynthesis of ADP-L-glycero-D-manno-heptose-containing lipopolysaccharide)
    • Kim, C. H. (2003) A Salmonella typhimurium rfaE mutant recovers invasiveness for human epithelial cells when complemented by wild type rfaE (controlling biosynthesis of ADP-L-glycero-D-manno-heptose-containing lipopolysaccharide). Mol. Cells 15, 226-232.
    • (2003) Mol. Cells , vol.15 , pp. 226-232
    • Kim, C.H.1
  • 19
    • 0029875308 scopus 로고    scopus 로고
    • Sequence analysis of the 5′-flanking region of the gene encoding human N-acetylglucosaminyltransferase III
    • Kim, Y-J., Kim, K.-S., Ko, J.-H., Lee, Y.-C., Chung, T.-W., Choe, I.-S., and Kim, C.-H. (1996) Sequence analysis of the 5′-flanking region of the gene encoding human N-acetylglucosaminyltransferase III. Gene 170, 281-283.
    • (1996) Gene , vol.170 , pp. 281-283
    • Kim, Y.-J.1    Kim, K.-S.2    Ko, J.-H.3    Lee, Y.-C.4    Chung, T.-W.5    Choe, I.-S.6    Kim, C.-H.7
  • 22
    • 0035980062 scopus 로고    scopus 로고
    • Downregulation of the α-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 Taniguchi, N. (2001) Downregulation of the α-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    Taniguchi, N.8
  • 23
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1950) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1950) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 24
    • 0032530610 scopus 로고    scopus 로고
    • Discordant organ xenotransplantation in primates: World experience and current status
    • Lambrigts, D., Sachs, D. H., and Cooper, D. K. (1998) Discordant organ xenotransplantation in primates: world experience and current status. Transplantation 66, 547-561.
    • (1998) Transplantation , vol.66 , pp. 547-561
    • Lambrigts, D.1    Sachs, D.H.2    Cooper, D.K.3
  • 26
    • 71849104860 scopus 로고
    • Protein measurement with the Folin phenol reagent
    • Lowry, O. H., Rosenbrough, N. H., and Farr, A. L. (1951) Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193, 265-275.
    • (1951) J. Biol. Chem. , vol.193 , pp. 265-275
    • Lowry, O.H.1    Rosenbrough, N.H.2    Farr, A.L.3
  • 27
  • 28
    • 0034721846 scopus 로고    scopus 로고
    • Fucosyl transferase (H) transgenic heart transplants to Gal-/-mice
    • McKenzie, I. F., Li, Y. Q., Patton, K., and Sandrin, M. S. (2000) Fucosyl transferase (H) transgenic heart transplants to Gal-/-mice. Transplantation 70, 1205-1209.
    • (2000) Transplantation , vol.70 , pp. 1205-1209
    • McKenzie, I.F.1    Li, Y.Q.2    Patton, K.3    Sandrin, M.S.4
  • 30
    • 0033388438 scopus 로고    scopus 로고
    • Regulation of natural killer cell-mediated swine endothelial cell lysis through genetic remodeling of a glycoantigen
    • Miyagawa, S., Nakai, R., Yamada, M., Tanemura, M., Ikeda, Y., Taniguchi, N., and Shirakura, R. (1999) Regulation of natural killer cell-mediated swine endothelial cell lysis through genetic remodeling of a glycoantigen. J. Biochem. 126, 1067-1073.
    • (1999) J. Biochem. , vol.126 , pp. 1067-1073
    • Miyagawa, S.1    Nakai, R.2    Yamada, M.3    Tanemura, M.4    Ikeda, Y.5    Taniguchi, N.6    Shirakura, R.7
  • 33
    • 0019964513 scopus 로고
    • Isolation of a human erythrocyte membrane glycoprotein with decay-accelerating activity for C3 convertases of the complement system
    • Nicholson-Weller, A., Burge, J., Fearon, D. T., Weller, P. F., and Austen, K. F. (1982) Isolation of a human erythrocyte membrane glycoprotein with decay-accelerating activity for C3 convertases of the complement system. J. Immunol. 129, 184-189.
    • (1982) J. Immunol. , vol.129 , pp. 184-189
    • Nicholson-Weller, A.1    Burge, J.2    Fearon, D.T.3    Weller, P.F.4    Austen, K.F.5
  • 34
    • 0025002487 scopus 로고
    • Determination of N-acetylglucosaminyltransferase III and V in normal and hepatoma tissues of rat
    • Nishikawa, A., Gu, J., Fujii, S., and Taniguchi, N. (1990) Determination of N-acetylglucosaminyltransferase III and V in normal and hepatoma tissues of rat. Biochim. Biophys. Acta 1035, 313-318.
    • (1990) Biochim. Biophys. Acta , vol.1035 , pp. 313-318
    • Nishikawa, A.1    Gu, J.2    Fujii, S.3    Taniguchi, N.4
  • 36
    • 0031460988 scopus 로고    scopus 로고
    • Combined transgenic expression of a-galactosidase and α1,2-fucosyltransferase leads to optimal reduction in the major xenoepitope Galα(1,3)Gal
    • Osman, N., McKenzie, I. F. C., Ostenried, K., Ioannou, Y. A., Desnick, R. J., and Sandrin, M. S. (1998) Combined transgenic expression of a-galactosidase and α1,2-fucosyltransferase leads to optimal reduction in the major xenoepitope Galα(1,3)Gal. Proc. Natl. Acad. Sci. USA 94, 14677-14682.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 14677-14682
    • Osman, N.1    McKenzie, I.F.C.2    Ostenried, K.3    Ioannou, Y.A.4    Desnick, R.J.5    Sandrin, M.S.6
  • 37
    • 0033566066 scopus 로고    scopus 로고
    • Characterization of UDP-N-acetylglucosamine: β-6-D-mannoside β-1,6-N-acetylglucosaminyltransferase-V from a human hepatoma cell line Hep3B
    • Park, C., Jin, U.-H., Lee, Y.-C., Cho, T.-J., and Kim, C.-H. (1999) Characterization of UDP-N-acetylglucosamine: β-6-D-mannoside β-1,6-N-acetylglucosaminyltransferase-V from a human hepatoma cell line Hep3B. Arch. Biochem. Biophys. 367, 281-288.
    • (1999) Arch. Biochem. Biophys. , vol.367 , pp. 281-288
    • Park, C.1    Jin, U.-H.2    Lee, Y.-C.3    Cho, T.-J.4    Kim, C.-H.5
  • 39
    • 0029057985 scopus 로고
    • Tissue expression of human complement inhibitor, decay-accelerating factor, in transgenic pigs. A potential approach for preventing xenograft rejection
    • Rosengard, A. M., Cary, N. R., Langford, G. A., Tucker, A. W., Wallwork, J., and White, D. J. (1995) Tissue expression of human complement inhibitor, decay-accelerating factor, in transgenic pigs. A potential approach for preventing xenograft rejection. Transplantation 59, 1325-1333.
    • (1995) Transplantation , vol.59 , pp. 1325-1333
    • Rosengard, A.M.1    Cary, N.R.2    Langford, G.A.3    Tucker, A.W.4    Wallwork, J.5    White, D.J.6
  • 41
    • 0028811673 scopus 로고
    • Enzymatic remodelling of the carbohydrate surface of a xenogenic cell substantially reduces human antibody binding and complement-mediated cytolysis
    • Sandrin, M. S., Fodor, W. L., Mouhtouris, E., Osman, N., Cohney, S., Rollins, S. A., Guilmette, E. R., Setter, E., Squinto, S. P., and McKenzie, I. F. C. (1995) Enzymatic remodelling of the carbohydrate surface of a xenogenic cell substantially reduces human antibody binding and complement-mediated cytolysis. Nat. Med. 1, 1261-1267.
    • (1995) Nat. Med. , vol.1 , pp. 1261-1267
    • Sandrin, M.S.1    Fodor, W.L.2    Mouhtouris, E.3    Osman, N.4    Cohney, S.5    Rollins, S.A.6    Guilmette, E.R.7    Setter, E.8    Squinto, S.P.9    McKenzie, I.F.C.10
  • 42
    • 0022462129 scopus 로고
    • Biosynthetic controls that determine the branching and microheterogeneity of protein-bound oligosaccharides
    • Schachter, H. (1990) Biosynthetic controls that determine the branching and microheterogeneity of protein-bound oligosaccharides. Biochem. Cell. Biol. 64, 163-181.
    • (1990) Biochem. Cell. Biol. , vol.64 , pp. 163-181
    • Schachter, H.1
  • 43
    • 0030881106 scopus 로고    scopus 로고
    • Expression of α1,3-galactose and other type 2 oligosaccharide structures in a porcine endothelial cell line transfected with human α1,2-fucosyltransferase cDNA
    • Sepp, A., Skacel, P., Lindstedt, R., and Lechler, R. I. (1997) Expression of α1,3-galactose and other type 2 oligosaccharide structures in a porcine endothelial cell line transfected with human α1,2- fucosyltransferase cDNA. J. Biol. Chem. 272, 23104-23110.
    • (1997) J. Biol. Chem. , vol.272 , pp. 23104-23110
    • Sepp, A.1    Skacel, P.2    Lindstedt, R.3    Lechler, R.I.4
  • 44
    • 0018537055 scopus 로고
    • Specific interaction of human Tamm-Horsfall gylcoprotein with leucoagglutinin, a lectin from Phaseolus vulgaris (red kidney bean)
    • Serafini-Cessi, F., Francecshi, C., and Sperti, S. (1979) Specific interaction of human Tamm-Horsfall gylcoprotein with leucoagglutinin, a lectin from Phaseolus vulgaris (red kidney bean). Biochem. J. 183, 381-388.
    • (1979) Biochem. J. , vol.183 , pp. 381-388
    • Serafini-Cessi, F.1    Francecshi, C.2    Sperti, S.3
  • 45
    • 0022517078 scopus 로고
    • Purification and characterization of a membrane protein (gp45-70) that is a cofactor for cleavage of C3b and C4b
    • Seya, T., Turner, J. R., and Atkinson, J. P. (1986) Purification and characterization of a membrane protein (gp45-70) that is a cofactor for cleavage of C3b and C4b. J. Exp. Med. 163, 837-855.
    • (1986) J. Exp. Med. , vol.163 , pp. 837-855
    • Seya, T.1    Turner, J.R.2    Atkinson, J.P.3
  • 46
    • 0029959441 scopus 로고    scopus 로고
    • Reduction in the level of Gal(α1,3)Gal in transgenic mice and pigs by the expression of an α(1,2)fucosyltransferase
    • Sharma, A., Okabe, J., Birch, P., McClellan, S. B., Martin, M. J., Platt, J. L., and Logan, J. S. (1996) Reduction in the level of Gal(α1,3)Gal in transgenic mice and pigs by the expression of an α(1,2)fucosyltransferase. Proc. Natl. Acad. Sci. USA 93, 7190-7195.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 7190-7195
    • Sharma, A.1    Okabe, J.2    Birch, P.3    McClellan, S.B.4    Martin, M.J.5    Platt, J.L.6    Logan, J.S.7
  • 47
    • 0031564104 scopus 로고    scopus 로고
    • Remodeling of glycoconjugates on CD44 enhances cell adhesion to hyaluronate, tumor growth and metastasis in B16 melanoma cells expressing β1,4-N-acetylglueosaminyltransferase III
    • Sheng, Y., Yoshimura, M., Inoue, S., Oritani, K., Nishiura, T., Yoshida, H., Ogawa, M., Okajima, Y., Matsuzawa, Y., and Taniguchi, N. (1997) Remodeling of glycoconjugates on CD44 enhances cell adhesion to hyaluronate, tumor growth and metastasis in B16 melanoma cells expressing β1,4-N- acetylglueosaminyltransferase III. Int. J. Cancer 73, 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
  • 48
    • 0035964441 scopus 로고    scopus 로고
    • Carbon tetrachloride-induced changes in the activity of phase II drug-metabolizing enzyme in the liver of male rats: Role of antioxidants
    • Sheweita, S. A., Abd El-Gabar, M., and Bastawy, M. (2001) Carbon tetrachloride-induced changes in the activity of phase II drug-metabolizing enzyme in the liver of male rats: role of antioxidants. Toxicology 165, 217-224.
    • (2001) Toxicology , vol.165 , pp. 217-224
    • Sheweita, S.A.1    Abd El-Gabar, M.2    Bastawy, M.3
  • 49
    • 0034051786 scopus 로고    scopus 로고
    • A simplified procedure for the purification of human N- acetylglucosaminyltyransferase-III from human hepatocellular carcinoma tissues
    • Song, E.-Y., Kim, K.-A., Kim, Y.-D., Kwon, D.-H., Lee, H.-S., Kim, C.-H., Chung, T.-W., and Byun, S.-M. (2000) A simplified procedure for the purification of human N-acetylglucosaminyltyransferase-III from human hepatocellular carcinoma tissues. Biotechnol. Lett. 22, 201-204.
    • (2000) Biotechnol. Lett. , vol.22 , pp. 201-204
    • Song, E.-Y.1    Kim, K.-A.2    Kim, Y.-D.3    Kwon, D.-H.4    Lee, H.-S.5    Kim, C.-H.6    Chung, T.-W.7    Byun, S.-M.8
  • 50
    • 0035216931 scopus 로고    scopus 로고
    • Expression of bisecting N-acetylglucosaminyltransferase-III in human hepatocarcinoma tissues, fetal liver tissues, and hepatoma cell lines of Hep3B and HepG2
    • Song, E.-Y., Lee, Y.-C., Park, Y.-G., Chung, T.-W., and Kim, C.-H. (2001) Expression of bisecting N-acetylglucosaminyltransferase-III in human hepatocarcinoma tissues, fetal liver tissues, and hepatoma cell lines of Hep3B and HepG2. Cancer Investigation 19, 797-805.
    • (2001) Cancer Investigation , vol.19 , pp. 797-805
    • Song, E.-Y.1    Lee, Y.-C.2    Park, Y.-G.3    Chung, T.-W.4    Kim, C.-H.5
  • 51
    • 27744529371 scopus 로고    scopus 로고
    • (2003a) Transgenic mice for over-expression of human N- acetylglucosamintransferase-III and method for producing of the same. Korean Patent No. 10-02-0033515
    • Song, E.-Y., Chung, T.-H., Yeom, Y.-I., and Kim, C.-H. (2003a) Transgenic mice for over-expression of human N-acetylglucosamintransferase-III and method for producing of the same. Korean Patent No. 10-02-0033515.
    • Song, E.-Y.1    Chung, T.-H.2    Yeom, Y.-I.3    Kim, C.-H.4
  • 52
    • 27744486156 scopus 로고    scopus 로고
    • Evaluation of N-acetylgucosaminyltransferase III-like proteins in the serum of patients with chronic hepatitis and liver cirrhosis
    • in press
    • Song, E.-Y., Kim, K.-S., Kim, K.-A., Kim, Y.-D., Kwon, D.-H., Byun, S.-M., Kim, H.-J., Chung, T.-W., and Kim, C.-H. (2003b) Evaluation of N-acetylgucosaminyltransferase III-like proteins in the serum of patients with chronic hepatitis and liver cirrhosis. Glycoconjugate J. (in press).
    • (2003) Glycoconjugate J.
    • Song, E.-Y.1    Kim, K.-S.2    Kim, K.-A.3    Kim, Y.-D.4    Kwon, D.-H.5    Byun, S.-M.6    Kim, H.-J.7    Chung, T.-W.8    Kim, C.-H.9
  • 53
    • 0016700864 scopus 로고
    • Detection of specific sequences among DNA fragments separated by gel electrophoresis
    • Southern, E. M. (1975) Detection of specific sequences among DNA fragments separated by gel electrophoresis. J. Mol. Biol. 98, 503-505.
    • (1975) J. Mol. Biol. , vol.98 , pp. 503-505
    • Southern, E.M.1
  • 54
    • 0031577182 scopus 로고    scopus 로고
    • Significant downregulation of the major swine xenoantigen by N-acetylglueosaminyltransferase III gene transfection
    • Tanemura, M., Miyagawa, S., Ihara, Y., Matsuda, H., Shirakura, R., and Taniguchi, N. (1997) Significant downregulation of the major swine xenoantigen by N-acetylglueosaminyltransferase III gene transfection. Biochem. Biophys. Res. Commun. 235, 359-364.
    • (1997) Biochem. Biophys. Res. Commun. , vol.235 , pp. 359-364
    • Tanemura, M.1    Miyagawa, S.2    Ihara, Y.3    Matsuda, H.4    Shirakura, R.5    Taniguchi, N.6
  • 55
    • 0032568842 scopus 로고    scopus 로고
    • Reduction of the major swine xenoantigen, the α-galactosyl epitope by transfection of the α2,3-sialyltransferase gene
    • Tanemura, M., Miyagawa, S., Koyota, S., Koma, M., Matsuda, H., Tsuji, S., Shirakura, R., and Taniguchi, N. (1998) Reduction of the major swine xenoantigen, the α-galactosyl epitope by transfection of the α2,3-sialyltransferase gene. J. Biol. Chem. 273, 16421-16425.
    • (1998) J. Biol. Chem. , vol.273 , pp. 16421-16425
    • Tanemura, M.1    Miyagawa, S.2    Koyota, S.3    Koma, M.4    Matsuda, H.5    Tsuji, S.6    Shirakura, R.7    Taniguchi, N.8
  • 56
    • 0034650236 scopus 로고    scopus 로고
    • Differential expression of α-GAL epitopes (Galα1-3Galβ1- 4GlcNAc-R) on pig and mouse organs
    • Tanemura, M., Maruyama, S., and Galili, U. (2000) Differential expression of α-GAL epitopes (Galα1-3Galβ1-4GlcNAc-R) on pig and mouse organs. Transplantation 69, 187-190.
    • (2000) Transplantation , vol.69 , pp. 187-190
    • Tanemura, M.1    Maruyama, S.2    Galili, U.3
  • 57
    • 0029956556 scopus 로고    scopus 로고
    • Remodeling of cell surface glycoproteins by N- acetylglucosaminyltransferase III gene transfection: Modulation of metastatic potentials and down regulation of hepatitis B virus replication
    • Taniguchi, N., Yoshimura, M., Miyoshi, E., Ihara, Y., Nishikawa, A., and Fujii, S. (1996) Remodeling of cell surface glycoproteins by N-acetylglucosaminyltransferase III gene transfection: modulation of metastatic potentials and down regulation of hepatitis B virus replication. Glycobiology 6, 691-694.
    • (1996) Glycobiology , vol.6 , pp. 691-694
    • Taniguchi, N.1    Yoshimura, M.2    Miyoshi, E.3    Ihara, Y.4    Nishikawa, A.5    Fujii, S.6
  • 58
    • 0021112907 scopus 로고
    • Structural determinants of Phaseolus vulgaris erythroagglutinating lectin for oligosaccharides
    • Yamashita, K., Hitoi, A., and Kobata, A. (1983) Structural determinants of Phaseolus vulgaris erythroagglutinating lectin for oligosaccharides. J. Biol. Chem. 258, 14753-14755.
    • (1983) J. Biol. Chem. , vol.258 , pp. 14753-14755
    • Yamashita, K.1    Hitoi, A.2    Kobata, A.3
  • 59
    • 0037442166 scopus 로고    scopus 로고
    • Opportunities and risks of xenogeneic thymus transplantation
    • Yau, Y. and Waer, M. (2003) Opportunities and risks of xenogeneic thymus transplantation. Transplantation 75, 263-264.
    • (2003) Transplantation , vol.75 , pp. 263-264
    • Yau, Y.1    Waer, M.2
  • 60
    • 0029027831 scopus 로고
    • Suppression of lung metastasis of B16 mouse melanoma by N-acetylglucosaminyltransferase III gene transfection
    • Yoshimura, M., Nishikawa, A., Ihara, Y., Taniguchi, S., and Taniguchi, N. (1995) Suppression of lung metastasis of B16 mouse melanoma by N-acetylglucosaminyltransferase III gene transfection. Proc. Natl. Acad. Sci. USA 92, 8754-8758.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8754-8758
    • Yoshimura, M.1    Nishikawa, A.2    Ihara, Y.3    Taniguchi, S.4    Taniguchi, N.5


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