Remodeling of cell surface glycoproteins by N-acetylglucosaminyltransferase III gene transfection: Modulation of metastatic potentials and down regulation of hepatitis B virus replication

Glycobiology

Volumn 6, Issue 7, 1996, Pages 691-694

  Taniguchi, Naoyuki ^a   Yoshimura, Masafumi ^b   Miyoshi, Eiji ^b   Ihara, Yoshito ^b   Nishikawa, Atsushi ^b   Fujii, Shigeru ^b  

^a OSAKA UNIVERSITY MEDICAL SCHOOL   (Japan)

^b NONE

Author keywords

B virus; Gene transfection; Hepatitis; Melanomal; N acetylglucosaminyltransferase III; N acetylglucosaminyltransferase V

Indexed keywords

CELL SURFACE PROTEIN; N ACETYLGLUCOSAMINYLTRANSFERASE; UVOMORULIN;

ANIMAL CELL; ANIMAL MODEL; CELL ADHESION; CELL SURFACE; CONTROLLED STUDY; CYTOCHEMISTRY; GENE THERAPY; GENETIC TRANSFECTION; HEPATITIS B; HEPATITIS B VIRUS; HUMAN; LUNG METASTASIS; METASTASIS POTENTIAL; NONHUMAN; PRIORITY JOURNAL; SHORT SURVEY;

ANIMALIA; HEPATITIS B VIRUS;

EID: 0029956556     PISSN: 09596658     EISSN: None     Source Type: Journal    
DOI: 10.1093/glycob/6.7.691     Document Type: Short Survey

References (55)

1. Beyer,T-A., Rearick,J.I., Paulson,J.C., Prieels,J.P., Sadler,J.E. and Hill,R.L. (1979) Biosynthesis of mammalian glycoproteins. Glycosylation pathways in the synthesis of the nonreducing terminal sequences. J. Biol. Chem., 254, 12531-12534
2. Bhaumik,M. and Stanley,P. (1995) Develpmental roles of N-linked carbohydrates: generation of mice lacking GlcNAc-TIII. Glycoconj. J., 12, 489.
3. 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.
4. Bierhuizen,M.F., Maemuram,K., Kudo,S and Fukuda,M. (1995) Genomic organization of core 2 and 1 branching β-1,6-N-acetylglucosaminyltransferases. Implication for evolution of the β-1,6-N-acetylglucosaminyltransferase gene family. Glycobiology, 5, 417-425.
5. Briles,E.B. (1982) Lectin-resistant cell surface variants of eukaryotic cells. Int. Rev. Cytol., 75, 101-165.
6. Brisson,J.R. and Carver,J.P. (1983) The relation of three-dimensional structure to biosynthesis in the N-linked oligosaccharides. Can. J. Biochem. Cell Biol., 61, 1067-1078.
7. Campbell,C. and Stanley,P. (1983) Regulatory mutations in CHO cells induce expression of the mouse embryonic antigen SSEA-1. Cell, 35, 303-309.
8. Campbell,C. and Stanley,P. (1984) A dominant mutation to ricin resistance in Chinese hamster ovary cells induces UDP-GlcNAc:glycopeptide β-4-N-acetylglucosaminyltransferase III activity. J. Biol. Chem., 259, 13370-13378.
9. Chaney,W. and Stanley,P. (1986) Lec1A Chinese hamster ovary cell mutants appear to arise from a structural alteration in N-acetylglucosaminyltransferase I. J. Biol. Chem., 261, 10551-10557.
10. Chaney,W., Sundaram,S., Friedman,N. and Stanley,P. (1989) The Lec4A CHO glycosylation mutant arises from miscompartmentalization of a Golgi glycosyltransferase. J. Cell Biol., 109, 2089-2096.
11. Cummings,L., Warren,C.E., Granovsky,M. and Dennis,J.W (1993) Antisense and sense cDNA expression cloning using autonomously replicating vectors and toxic lectin selection. Biochem. Biophys. Res. Commun., 195, 814-822.
12. Eckhardt,M., Muhlenhoff,M., Bethe,A., Koopman,J., Frosch,M. and Gerardy-Schahn,R. (1995) Molecular characterization of eukaryotic polysalyltransferase-1. Nature, 373, 715-718.
13. Finne,J., Tao,T.W. and Burger,M.M. (1980) Carbohydrate changes in glycoproteins of a poorly metastasizing wheat germ agglutmin-resistant melanoma clone. Cancer Res., 40, 2580-2587.
14. Finne,J., Burger,M.M. and Prieels,J.P. (1982) Enzymatic basis for a lectin-resistant phenotype: increase in a fucosyltransferase in mouse melanoma cells. J. Cell Biol., 92, 277-282.
15. Gottlieb,C. Baenziger,J. and Kornfeld,S. (1975) Deficient uridine diphosphate-N-acetylglucosamine:glycoprotein N-acetylglucosaminyltransferase activity in a clone of Chinese hamster ovary cells with altered surface glycoproteins. J. Biol. Chem., 250, 3303-3309.
16. Hakomori,S. (1984) Tumor-associated carbohydrate antigens. Annu. Rev. Immunol., 2, 103-126.
17. Harduin-Lepers,A., Shaper,J.H. and Shaper,N.L. (1993) Characterization of two cis-regulatory regions in the murine β1,4-galactosyltransferase gene. Evidence for a negative regulatory element that controls initiation at the proximal site. J. Biol Chem., 268, 14348-14359.
18. Herscovics,A. and Orlean,P. (1993) Glycoprotein biosynthesis in yeast. FASEB J., 7, 540-550.
19. Howard,D.R., Fukuda,M., Fukuda,M.N. and Stanley,P. (1987) The GDP-fucose:N-acetylglucosaminide 3-α-L-fucosyltransferases of LEC11 and LEC12 Chinese hamster ovary mutants exhibit novel specificities for glycolipid substrates. J. Biol. Chem., 262, 16830-16837.
20. Ihara,Y., Nishikawa,A., Tohma,T., Soejima,H., Niikawa,N. and Taniguchi,N. (1993) cDNA cloning, expression, and chromosomal localization of human N-acetylglucosaminyltransferase III (GnT-III). J. Biochem. (Tokyo), 113, 692-698.
21. Ioffe,E. and Stanley,P. (1994) Mice lacking N-acetylglucosaminyltransferase I activity die at mid-gestation, revealing an essential role for complex or hybrid N-linked carbohydrates. Proc. Natl. Acad. Sci. USA, 91, 728-732.
22. Joziasse,D.H. (1992) Mammalian glycosyltransferases: genomic organization and protein structure. Glycobiology, 2, 271-277.
23. Kleene,R. and Berger,E.G. (1993) The molecular and cell biology of glycosyltransferases. Biochim. Biophys. Acta. 1154, 283-325.
24. Kornfeld,R. and Kornfeld,S (1985) Assembly of asparagine-linked oligosaccharides. Annu. Rev. Biochem., 54, 631-664
25. Kumar,R., Yang,J., Larsen,R.D. and Stanley,P. (1990) Cloning and expression of N-acetylglucosaminyltransferase I. the medial Golgi transferase that initiates complex N-linked carbohydrate formation. Proc. Natl. Acad. Sci. USA, 87, 9948-9952.
26. Kumar,R., Potvin,B., Muller,W.A. and Stanley,P. (1991) Cloning of a human α(1,3)-fucosyltransferase gene that encodes ELFT but does not confer ELAM-1 recognition on Chinese hamster ovary cell transfectants. J. Biol. Chem. 266, 21777-21783.
27. Kumar,R., Yang,J., Eddy,R.L., Byers,M.G., Shows,T.B. and Stanley,P. (1992) Cloning and expression of the murine gene and chromosomal location of the human gene encoding N-acetylglucosaminyltransferase I. Glycobiology, 2, 383-393.
28. Lasky,L.A. (1995) Selectin-carbohydrate interactions and the initiation of the inflammatory response. Annu. Rev. Biochem., 64, 113-139.
29. Lowe,J.B. (1991) Molecular cloning, expression, and uses of mammalian glycosyltransferases Semin. Cell Biol., 2, 289-307.
30. Lowe,J.B., Kukowska-Latallo,J F., Nair,R.P., Larsen,R.D., Marks,R.M., Macher,B.A., Kelly,R.J. and Ernst,L.K. (1991) Molecular cloning of a human fucosyltransferase gene that determines expression of the Lewis and VIM-2 epitopes but not ELAM-1-dependent cell adhesion J. Biol. Chem., 266, 17467-17477.
31. Metzler,M., Gertz,A., Sarkar,M , Schachter,H., Schrader,J W. and Marth,L.D. (1994) Complex asparagine-linked oligosaccharides are required for morphogenic events during post-implantation development. EMBO J., 13, 2056-2065.
32. Narasimhan,S. (1982) Control of glycoprotein synthesis. UDP-GlcNAc:glycopeptide β4-N-acetylglucosaminyltransferase III, an enzyme in hen oviduct which adds GlcNAc in β1-4 linkage to the β-linked mannose of the trimannosyl core of N-glycosyl oligosaccharides. J. Biol Chem., 257, 10235-10242.
33. Narasimhan,S., Stanley,P. and Schachter,H. (1977) Control of glycoprotein synthesis. Lectin-resistant mutant containing only one of two distinct N-acetylglucosaminyltransferase activities present in wild type Chinese hamster ovary cells. J. Biol. Chem., 252, 3926-3933.
34. Potvin,B and Stanley,P. (1991) Activation of two new α(1,3)fucosyltransferase activities in Chinese hamster ovary cells by 5-azacytidine. Cell Regul., 2, 989-1000
35. Puck,T.T., Cieciura,S J. and Robinson,A. (1958) Genetics of somatic mammalian cells III. Long-term cultivation of euploid cell from human and animal subjects. J. Exp. Med., 108, 945-955.
36. Raju,T.S. and Stanley,P. (1996) LEC14, a dominant Chinese hamster ovary glycosylation mutant expresses complex N-glycans with a new N-acetylglucosamine residue in the core region. J. Biol. Chem., 271, 7484-7493.
37. Raju,T.S., Ray,M.K. and Stanley,P. (1995) LEC18, a dominant Chinese hamster ovary glycosylation mutant synthesizes N-linked carbohydrates with a novel core structure. J. Biol. Chem., 270, 30294-30302.
38. Ripka,J. and Stanley,P. (1986) Lectin-resistant CHO cells: selection of four new pea lectin-resistant phenotypes. Somat. Cell Mol. Genet., 12, 51-62.
39. Russo,R.N., Shaper,N.L. and Shaper,J H. (1990) Bovine β1-4-galactosyltransferase: two sets of mRNA transcripts encode two forms of the protein with different amino-terminal domains. In vitro translation experiments demonstrate that both the short and the long forms of the enzyme are type II membrane-bound glycoproteins. J. Biol. Chem., 265, 3324-3331.
40. Sadler,J.E., Beyer,T.A., Oppenheimer,C.L., Paulson,J.C., Prieels,J.P., Rearick,J.I. and Hill,R.L. (1982) Purification of mammalian glycosyltransferases. Methods Enzymol., 83, 458-514.
41. Schachter,H. (1986) Biosynthetic controls that determine the branching and microheterogeneity of protein-bound oligosaccharides. Adv. Exp. Med. Biol., 205, 53-85.
42. Shaper,N.L., Wright,W.W. and Shaper,J.H. (1990) Murine β1,4-galactosyltransferase: both the amounts and structure of the mRNA are regulated during spermatogenesis. Proc. Natl. Acad. Sci. USA, 87, 791-795.
43. Stanley,P. (1983) Lectin-resistant CHO cells: selection of new mutant phenotypes. Somatic. Cell Genet., 9, 593-608.
44. Stanley,P. (1984) Glycosylation mutants of animal cells. Annu. Rev. Genet., 18, 525-552
45. Stanley,P. (1993) Use of mammalian cell mutants to study the function of N-and O-linked glycosylation. In Mecham,R.P. and Roberts,D. (eds), Cell Surface and Extracellular Glycoconjugates: Structure and Function. Academic Press, New York, pp. 181-222.
46. Stanley,P. and Atkinson,P.H. (1988) The LEC11 Chinese hamster ovary mutant synthesizes N-linked carbohydrates containing sialylated, fucosylated lactosamine units. Analysis by one- and two-dimensional 1H NMR spectroscopy [erratum J. Biol. Chem. 1988; 263, 17203]. J. Biol. Chem., 263, 11374-11381.
47. Stanley,P. and Chaney,W. (1985) Control of carbohydrate processing, the lec1A CHO mutation results in partial loss of N-acetylglucosaminyltransferase I activity. Mol. Cell Biol., 5, 1204-1211.
48. Stanley,P. and Ioffe,E. (1995) Glycosyltransferase mutants: key to new insights in glycobiology. FASEB J., 9, 1436-1444.
49. Stanley,P., Narasimhan,S., Siminovitch,L. and Schachter,H. (1975) Chinese hamster ovary cells selected for resistance to the cytotoxicity of phytohemagglutinin are deficient in a UDP-N-acetylglucosamine-glycoprotein N-acetylglucosaminyltransferase activity. Proc. Natl. Acad. Sci. USA, 72, 3323-3327.
50. Tabas,I. and Kornfeld,S. (1978) The synthesis of complex-type oligosaccharides. III. Identification of an α-D-mannosidase activity involved in a late stage of processing of complex-type oligosaccharides. J. Biol. Chem., 253, 7779-7786
51. Tao,T.W. and Burger,M.M. (1977) Non-metastasising variants selected from metastasising melanoma cells. Nature, 270, 437-438.
52. Weinstein,J., Sundaram,S., Wang,X., Delgado,D., Basu,R. and Stanley,P. (1996) A point mutation causes mistargeting of Golgi GlcNAc-TV in the Lec4A CHO glycosylation mutant. J. Biol. Chem., in press.
53. Weston,B.W., Nair,R.P., Larsen,R.D. and Lowe,J.B (1992a) Isolation of a novel human α(1,3)fucosyltransferase gene and molecular comparison to the human Lewis blood group α(1,3/1,4)fucosyltransferase gene. Syntenic, homologous, nonallelic genes encoding enzymes with distinct acceptor substrate specificities. J. Biol. Chem., 267, 4152-4160.
54. Weston,B.W., Smith,P.L., Kelly,R.J. and Lowe,J.B. (1992b) Molecular cloning of a fourth member of a human α(1,3)fucosyltransferase gene family. Multiple homologous sequences that determine expression of the Lewis x, sialyl Lewis x, and difucosyl sialyl Lewis epitopes [erratum: J. Biol. Chem. (1993) 268, 18398]. J. Biol Chem., 267, 24575-24584.
55. Yang,J., Bhaumik,M., Liu,Y. and Stanley,P. (1994) Regulation of N-linked glycosylation. Neuronal cell-specific expression of a 5′ extended transcript from the gene encoding N-acetylglucosaminyltransferase I [erratum: Glycobiology (1995) 5, 279]. Glycobiology, 4, 703-712.