Progression of hepatic neoplasms is severely retarded in mice lacking the bisecting N-acetylglucosamine on N-glycans: Evidence for a glycoprotein factor that facilitates hepatic tumor progression

Cancer Research

Volumn 58, Issue 13, 1998, Pages 2881-2887

  Bhaumik, Mantu ^a   Harris, Thomas ^a   Sundaram, Subha ^a   Johnson, Linda ^a   Guttenplan, Joseph ^b   Rogler, Charles ^a   Stanley, Pamela ^a  

^a ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

^b NEW YORK UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DIETHYLNITROSAMINE; GLYCOPROTEIN; N ACETYLGLUCOSAMINE; PHENOBARBITAL;

ANIMAL CELL; ANIMAL MODEL; ARTICLE; CANCER INHIBITION; CARCINOGENESIS; CELL ACTIVITY; ENZYME ACTIVITY; GENE EXPRESSION; GENE TARGETING; HISTOLOGY; LIVER TUMOR; MOLECULAR CLONING; MOUSE; NONHUMAN; PRIORITY JOURNAL; TUMOR GROWTH;

ACETYLGLUCOSAMINE; ANIMALS; CARCINOGENS; DIETHYLNITROSAMINE; DISEASE PROGRESSION; FEMALE; GENETIC VECTORS; LIVER NEOPLASMS, EXPERIMENTAL; MALE; MICE; N-ACETYLGLUCOSAMINYLTRANSFERASES; NEOPLASM PROTEINS; PHENOBARBITAL; POLYSACCHARIDES;

EID: 0032126529     PISSN: 00085472     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (46)

1. Narasimhan, S. 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, 1982.
2. Ihara, Y., Nishikawa, A., Tohma, T., Soejima, H., Niikawa, N., and Taniguchi, N. cDNA cloning, expression, and chromosomal localization of human N-acetylglucosaminyltransferase III (GnT-III). J. Biochem. (Tokyo), 113: 692-698, 1993.
3. Bhaumik, M., Seldin, M. F., and Stanley, P. Cloning and chromosomal mapping of the mouse Mgat3 gene encoding (N-acetylglucosaminyltransferase III. Gene (Amst.), 164: 295-300, 1995.
4. Priatel, J. J., Sarkar. M., Schachter, H., and Marth, J. D. Isolation, characterization and inactivation of the mouse Mgat3 gene: the bisecting N-acetylglucosamine in asparagine-linked oligosaccharides appears dispensable for viability and reproduction. Glycobiology, 7: 45-56, 1997.
5. Campbell, C., and Stanley, P. A dominant mutation to ricin resistance in Chinese hamster ovary cells induces UDP-GlcNAc:glycopeptide β4-N-acetylglucosaminyltransferase III activity. J. Biol. Chem., 259: 13370-13378, 1984.
6. Sallustio, S., and Stanley, P. Novel genetic instability associated with a developmentally regulated glycosyltransferase locus in Chinese hamster ovary cells. Somatic Cell Mol. Genet., 15: 387-400, 1989.
7. Stanley, P., Sundaram, S., and Sallustio, S. A subclass of cell surface carbohydrates revealed by a CHO mutant with two glycosylation mutations. Glycobiology, 1: 307-314, 1991.
8. Tanemura, M., Miyagawa, S., Ihara, Y., Mikata, S., Matsuda, H., Shirakura, R., and Taniguchi, N. Reduction of the major swine xenoantigen Gal α(1,3)Gal by transfection of N-acetylglucosaminyl transferase III (GnT-III) gene. Transplant. Proc., 29: 891-892, 1997.
9. Narasimhan, S., Schachter, H., and Rajalakshmi, S. Expression of N-acetylglucosaminyltransferase III in hepatic nodules during rat liver carcinogenesis promoted by orotic acid. J. Biol. Chem., 263: 1273-1281, 1988.
10. Nishikawa, A., Fujii, S., Sugiyama, T., Hayashi, N., and Taniguchi, N. High expression of an N-acetylglucosaminyltransferase III in 3′-methyl DAB-induced hepatoma and ascites hepatoma. Biochem. Biophys. Res. Commun., 152: 107-112, 1988.
11. Pascale, R., Narasimhan, S., and Rajalakshmi, S. Expression of N-acetylglucosaminyltransferase III in hepatic nodules generated by different models of rat liver carcinogenesis. Carcinogenesis (Lond.), 10: 961-964, 1989.
12. Nishikawa, A., Gu, J., Fujii, S., and Taniguchi, N. Determination of N-acetylglucosaminyltransferases III, IV and V in normal and hepatoma tissues of rats. Biochim. Biophys. Acta, 1035: 313-318, 1990.
13. Miyoshi, E., Nishikawa, A., Ihara, Y., Gu, J., Sugiyama, T., Hayashi, N., Fusamoto, H., Kamada, T., and Taniguchi, N. N-Acetylglucosaminyltransferase III and V messenger RNA levels in LEC rats during hepatocarcinogenesis. Cancer Res., 53: 3899-3902, 1993.
14. Ishibashi, K., Nishikawa, A., Hayashi, N., Kasahara, A., Sato, N., Fujii, S., Kamada, T., and Taniguchi, N. 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.
15. Narasimhan, S., Lee, J. W., Cheung, R. K., Gelfand, E. W., and Schachter, H. β-1,4-Mannosyl-glycoprotein β-1,4-N-acetylglucosaminyltransferase III activity in human B and T lymphocyte lines and in tonsillar B and T lymphocytes. Biochem. Cell Biol., 66: 889-900, 1988.
16. Yoshimura, M., Ihara, Y., and Taniguchi, N. Changes of β-1,4-N-acetylglucosaminyltransferase III (GnT-III) in patients with leukaemia. Glycoconj. J., 12: 234-240, 1995.
17. Yoshimura, M., Nishikawa, A., Ihara, Y., Nishiura, T., Nakao, H., Kanayama, Y., Matsuzawa, Y., and Taniguchi, N. High expression of UDP-N-acetylglucosamine: β-D-mannoside β1,4-N-acetylglucosaminyltransferase III (GnT-III) in chronic myelogenous leukemia in blast crisis. Int. J. Cancer, 60: 443-449, 1995.
18. Sultan, A. S., Miyoshi, E., Ihara, Y., Nishikawa, A., Tsukada, Y., and Taniguchi, N. Bisecting GlcNAc structures act as negative sorting signals for cell surface glycoproteins in forskolin-treated rat hepatoma cells. J. Biol. Chem., 272: 2866-2872, 1997.
19. Taniguchi, N., Yoshimura, M., Miyoshi, E., Ihara, Y., Nishikawa, A., and Fujii, S. 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.
20. Yoshimura, M., Ihara, Y., Ohnishi, A., Ijuhin, N., Nishiura, T., Kanakura, Y., Matsuzawa, Y., and Taniguchi, N. Bisecting N-acetylglucosamine on K562 cells suppresses natural killer cytotoxicity and promotes spleen colonization. Cancer Res., 56: 412-418, 1996.
21. Yoshimura, M., Nishikawa, A., Ihara, Y., Taniguchi, S., and Taniguchi, N. Suppression of lung metastasis of B16 mouse melanoma by N-acetylglucosaminyltransferase III gene transfection. Proc. Natl. Acad. Sci. USA, 92: 8754-8758, 1995.
22. Ihara, Y., Sakamoto, Y., Mihara, M., Shimizu, K., and Taniguchi, N. 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.
23. Rebbaa, A., Yamamoto, H., Saito, T., Meuillet, E., Kim, P., Kersey, D. S., Bremer. E. G., Taniguchi, N., and Moskal, J. R. Gene transfection-mediated Overexpression of β1,4-N-acetylglucosamine bisecting oligosaccharides in glioma cell line U373 MG inhibits epidermal growth factor receptor function. J. Biol. Chem., 272: 9275-9279, 1997.
24. Rudnicki, M. A., Braun, T., Hinuma, S., and Jaenisch, R. Inactivation of MyoD in mice leads to up-regulation of the myogenic HLH gene Myf-5 and results in apparently normal muscle development. Cell, 71: 383-390, 1992.
25. Ioffe, E., Liu, Y., Bhaumik, M., Poirier, F., Factor, S. M., and Stanley, P. WW6: an embryonic stem cell line with an inert genetic marker that can be traced in chimeras. Proc. Natl. Acad. Sci. USA, 92: 7357-7361, 1995.
26. Chancy, W., and Stanley, P. Lec1A Chinese hamster ovary cell mutants appear to arise from a structural alteration in N-acetylglucosaminyltransferase I. J. Biol. Chem., 261: 10551-10557, 1986.
27. Zielenska, M., Beranek, D., and Guttenplan, J. B. Different mutational profiles induced by N-nitroso-N-ethylurea: effects of dose and error-prone DNA repair and correlations with DNA adducts. Environ. Mol. Mutagen., 11: 473-485, 1988.
28. Hammarstrom, S., Hammarstrom, M. L., Sundblad, G., Arnarp, J., and Lonngren, J. Mitogenic leukoagglutinin from Phaseolus vulgaris binds to a pentasaccharide unit in N-acetyllactosamine-type glycoprotein glycans. Proc. Natl. Acad. Sci. USA, 79: 1611-1615, 1982.
29. Cummings, R. D., and Kornfeld, S. 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., 257: 11230-11234, 1982.
30. Baenziger, J. U., and Fiete, D. Structural determinants of Ricinus communis agglutinin and toxin specificity for oligosaccharides. J. Biol. Chem., 254: 9795-9799, 1979.
31. Stevenson, D. E., McClain, R. M., Popp, J. A. Slaga, T. J., Ward, J. M., and Pilot, H. C. Mouse liver carcinogenesis. Mechanism and species comparison. Prog. Clin. Biol. Res., 331: 1990.
32. Goldfarb, S., Pugh, T. D., Koen, H., and He, Y. Z. Preneoplastic and neoplastic progression during hepatocarcinogenesis in mice injected with diethylnitrosamine in infancy. Environ. Health Perspect., 50: 149-161, 1983.
33. Ihara, Y., Yoshimura, M., Miyoshi, E., Nishikawa, A., Sultan, A. S., Toyosawa, S., Ohnishi, A., Suzuki, M., Yamamura Ki, Ijuhin, N., and Taniguchi, N. 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.
34. Kleene, R., and Berger, E. G. The molecular and cell biology of glycosyltransferases. Biochim. Biophys. Acta, 1154: 283-325, 1993.
35. Schachter, H., Chen, S. H., Zhou, S., Tan, J., Yip, B., Sarkar, M., and Spence, A. Structure and function of the genes encoding N-acetylglucosaminyltransferases which initiate N-glycan antennae. Biochem. Soc. Trans., 25: 875-880, 1997.
36. Ioffe, E., and Stanley, P. 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, 1994.
37. Metzler, M., Gertz, A., Sarkar, M., Schachter, H., Schrader, J. W., and Marth, J. D. Complex asparagine-linked oligosaccharides are required for morphogenic events during post-implantation development. EMBO J., 13: 2056-2065, 1994.
38. Thall, A. D., Maly, P., and Lowe, J. B. Oocyte Gal α1,3Gal epitopes implicated in sperm adhesion to the zona pellucida glycoprotein ZP3 are not required for fertilization in the mouse. J. Biol. Chem., 270: 21437-21440, 1995.
39. Lu, Q., Hasty, P., and Shur, B. D. Targeted mutation in β1,4-galactosyltransferase leads to pituitary insufficiency and neonatal lethality. Dev. Biol., 181: 257-267, 1997.
40. Asano, M., Furukawa, K., Kido, M.. Matsumoto, S., Umesaki, Y., Kochibe, N., and Iwakura, Y. Growth retardation and early death of β-1,4-galactosyltransferase knockout mice with augmented proliferation and abnormal differentiation of epithelial cells. EMBO J., 16: 1850-1857, 1997.
41. Chui, D., Oh-Eda, M., Liao, Y. F., Panneerselvam, K., Lal, A., Marek, K. W., Freeze, H. H., Moremen, K. W., Fukuda, M. N., and Marth, J. D. α-Mannosidase-II deficiency results in dyserythropoiesis and unveils an alternate pathway in oligosaccharide biosynthesis. Cell, 90: 157-167, 1997.
42. Ioffe, E., Liu, Y., and Stanley, P. Essential role for complex N-glycans in forming an organized layer of bronchial epithelium. Proc. Natl. Acad. Sci. USA, 93: 11041-11046, 1996.
43. Suzuki, Y., Ishizuka, H., Kaneda, H., and Taniguchi, N. γ-Glutamyl transpeptidase in rat liver during 3′-Me-DAB hepatocarcinogenesis: immunohistochemical and enzyme histochemical study. J. Histochem. Cytochem., 35: 3-7, 1987.
44. Vesselinovitch, S. D., Hacker, H. J., and Bannasch, P. Histochemical characterization of focal hepatic lesions induced by single diethylnitrosamine treatment in infant mice. Cancer Res., 45: 2774-2780, 1985.
45. Petersen, J., Dandri, M., Gupta, S., and Rogler, C. E. Liver repopulation with xenogenic hepatocytes in B and T cell-deficient mice leads to chronic hepadnavirus infection and clonal growth of hepatocellular carcinoma. Proc. Natl. Acad. Sci. USA, 95: 310-315, 1998.
46. Rhim, J. A., Sandgren, E. P., Palmiter, R. D., and Brinster, R. L. Complete reconstitution of mouse liver with xenogeneic hepatocytes. Proc. Natl. Acad. Sci. USA, 92: 4942-4946, 1995.