메뉴 건너뛰기




Volumn 7, Issue 6, 1997, Pages 769-776

N-Glycosylation is requisite for the enzyme activity and Golgi retention of N-acetylglucosaminyltransferase III

Author keywords

Glycoprotein; Golgi apparatus; N acetylglucosaminyltransferase III; N glycosylation; Protein folding

Indexed keywords

CASTANOSPERMINE; GLYCOPROTEIN; N ACETYLGLUCOSAMINYLTRANSFERASE; TUNICAMYCIN;

EID: 0030884364     PISSN: 09596658     EISSN: None     Source Type: Journal    
DOI: 10.1093/glycob/7.6.769     Document Type: Article
Times cited : (64)

References (26)
  • 1
    • 0025736106 scopus 로고
    • Effects of inhibitors of N-linked oligosaccharide processing on the secretion, stability, and activity of lecithin:cholesterol acyltransferase
    • Collet, X. and Fielding, C. J. (1991) Effects of inhibitors of N-linked oligosaccharide processing on the secretion, stability, and activity of lecithin:cholesterol acyltransferase. Biochemistry, 30, 3228-3234.
    • (1991) Biochemistry , vol.30 , pp. 3228-3234
    • Collet, X.1    Fielding, C.J.2
  • 2
    • 0025739245 scopus 로고
    • Acquisition of the functional properties of the transferrin receptor during its biosynthesis
    • Enns, C.A., Clinton, E.M., Reckhow, C.L., Root, B.J., Do, S.-I. and Cook, C. (1991) Acquisition of the functional properties of the transferrin receptor during its biosynthesis. J. Biol. Chem., 266, 13272-13277.
    • (1991) J. Biol. Chem. , vol.266 , pp. 13272-13277
    • Enns, C.A.1    Clinton, E.M.2    Reckhow, C.L.3    Root, B.J.4    Do, S.-I.5    Cook, C.6
  • 3
    • 0027449104 scopus 로고
    • The role of the carbohydrate chains of Galβ-1,4-GlcNAcα2,6-sialytransferase for enzyme activity
    • Fast, D.G., Jamieson, J.C. and McCaffey, G. (1993) The role of the carbohydrate chains of Galβ-1,4-GlcNAcα2,6-sialytransferase for enzyme activity. Biochim. Biophys. Acta, 1202, 325-330.
    • (1993) Biochim. Biophys. Acta , vol.1202 , pp. 325-330
    • Fast, D.G.1    Jamieson, J.C.2    McCaffey, G.3
  • 4
    • 0029144380 scopus 로고
    • Molecular cloning of eukaryotic glycoprotein and glycolipid glycosyltransferases: A survey
    • Field, M.C. and Wainwright, L.J. (1995) Molecular cloning of eukaryotic glycoprotein and glycolipid glycosyltransferases: a survey. Glycobiology, 5, 463-472.
    • (1995) Glycobiology , vol.5 , pp. 463-472
    • Field, M.C.1    Wainwright, L.J.2
  • 5
    • 0021079440 scopus 로고
    • 1-Deoxynojirimycin impairs oligosaccharide processing of a1-protease inhibitor and inhibits its secretion in primary cultures of rat hepatocytes
    • Gross, V., Andus, T., Tran-Thi, T.-A., Schwarz, R.T., Decker, K. and Heinrich, P.C. (1983) 1-Deoxynojirimycin impairs oligosaccharide processing of a1-protease inhibitor and inhibits its secretion in primary cultures of rat hepatocytes. J. Biol. Chem., 258, 12203-12209.
    • (1983) J. Biol. Chem. , vol.258 , pp. 12203-12209
    • Gross, V.1    Andus, T.2    Tran-Thi, T.-A.3    Schwarz, R.T.4    Decker, K.5    Heinrich, P.C.6
  • 6
    • 0028880799 scopus 로고
    • The effects of the site-directed removal of N-glycosylation sites from β-1,4-N-acetylgalactosaminyltransferase on its function
    • Hiraguchi, M., Yamashiro, S., Furukawa, K., Takamiya, K., Shiku, H. and Furukawa, K. (1995) The effects of the site-directed removal of N-glycosylation sites from β-1,4-N-acetylgalactosaminyltransferase on its function. Biochem. J., 312, 273-280.
    • (1995) Biochem. J. , vol.312 , pp. 273-280
    • Hiraguchi, M.1    Yamashiro, S.2    Furukawa, K.3    Takamiya, K.4    Shiku, H.5    Furukawa, K.6
  • 7
    • 0021308647 scopus 로고
    • Reexamination of the pyridylamina-licn used for fluorescence labeling of oligosaccharides and its application to siKcoproteins
    • Hase, S., Ibuki, T. and Ikenaka, T. (1984) Reexamination of the pyridylamina-licn used for fluorescence labeling of oligosaccharides and its application to siKcoproteins. J. Biochem., 95, 197-203.
    • (1984) J. Biochem. , vol.95 , pp. 197-203
    • Hase, S.1    Ibuki, T.2    Ikenaka, T.3
  • 8
    • 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
    • Kang, R., Saito, H., Ihara, Y., Miyoshi, E., Koyama, N., Sheng, Y. and Taniguchi, N. (1996) 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, 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
  • 9
    • 0024371459 scopus 로고
    • N-Acetylglucosaminyltransferase III, IV and V activities in Novikoff ascites tumor cells, mouse lymphoma cells and hen oviduct
    • Koenderraan, A.H.L., Koppen, P.L., Koeleman, C.A.M. and van den Eijnden, D.H. (1989) N-Acetylglucosaminyltransferase III, IV and V activities in Novikoff ascites tumor cells, mouse lymphoma cells and hen oviduct. Eur. J. Biochem., 181, 651-655.
    • (1989) Eur. J. Biochem. , vol.181 , pp. 651-655
    • Koenderraan, A.H.L.1    Koppen, P.L.2    Koeleman, C.A.M.3    Van Den Eijnden, D.H.4
  • 10
    • 0023635575 scopus 로고
    • Changes in the expression of N-acetylglucosaminyltransferase III, IV, V associated with the differentiation of HL-60 cells
    • Koenderman, A.H.L., Wijermans, P.W. and van den Eijnden, D.H. (1987) Changes in the expression of N-acetylglucosaminyltransferase III, IV, V associated with the differentiation of HL-60 cells. FEBS Lett., 222, 42-46.
    • (1987) FEBS Lett. , vol.222 , pp. 42-46
    • Koenderman, A.H.L.1    Wijermans, P.W.2    Van Den Eijnden, D.H.3
  • 11
    • 0025638959 scopus 로고
    • Cloning and expression of N-acetylglucosaminyltransferase I. the medial Golgi transferase that initiates complex N-linked carbohydrate formation
    • 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.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 9948-9952
    • Kumar, R.1    Yang, J.2    Larsen, R.D.3    Stanley, P.4
  • 12
    • 2642699794 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel, T.A. (1985) Rapid and efficient site-specific mutagenesis without phenotypic selection. Proc. Natl. Acad. Sci. USA, 82, 488-492.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 488-492
    • Kunkel, T.A.1
  • 13
    • 0021280849 scopus 로고
    • Glucose removal from N-linked oligosaccharides is required for efficient maturation of certain secretory glycoproteins from the rough endoplasmic reticulum to the Golgi complex
    • Lodish, H.F. and Kong, N. (1984) Glucose removal from N-linked oligosaccharides is required for efficient maturation of certain secretory glycoproteins from the rough endoplasmic reticulum to the Golgi complex. J. Cell Biol., 98, 1720-1729.
    • (1984) J. Cell Biol. , vol.98 , pp. 1720-1729
    • Lodish, H.F.1    Kong, N.2
  • 15
    • 0027401887 scopus 로고
    • Inhibition of glucose trimming by castanospermine results in rapid degradation of unassembled major histocompatibility complex class I molecules
    • Moore, S.E.H. and Spiro, R.G. (1993) Inhibition of glucose trimming by castanospermine results in rapid degradation of unassembled major histocompatibility complex class I molecules. J. Biol. Chem., 268, 3809-3812.
    • (1993) J. Biol. Chem. , vol.268 , pp. 3809-3812
    • Moore, S.E.H.1    Spiro, R.G.2
  • 16
    • 0025990802 scopus 로고
    • Sequences within and adjacent to the transmembrane segment of α-2,6-sialyltransferase specify Golgi retention
    • Munro, S. (1991) Sequences within and adjacent to the transmembrane segment of α-2,6-sialyltransferase specify Golgi retention. EMBO J., 10, 3577-3588.
    • (1991) EMBO J. , vol.10 , pp. 3577-3588
    • Munro, S.1
  • 17
    • 0029165107 scopus 로고
    • An investigation of the role of transmembrane domains in Golgi protein retention
    • Munro, S. (1995) An investigation of the role of transmembrane domains in Golgi protein retention. EMBO J., 14, 4695-4704.
    • (1995) EMBO J. , vol.14 , pp. 4695-4704
    • Munro, S.1
  • 18
    • 0027732562 scopus 로고
    • Role of intramolecular high-mannose chains in the folding and assembly of soybean (Glycine max) lectin polypeptides: Studies by the combined use of spectroscopy and gel-filtration size analysis
    • Nagai, K., Shibata, K. and Yamaguchi, H. (1993) Role of intramolecular high-mannose chains in the folding and assembly of soybean (Glycine max) lectin polypeptides: studies by the combined use of spectroscopy and gel-filtration size analysis. J. Biochem., 114, 830-834.
    • (1993) J. Biochem. , vol.114 , pp. 830-834
    • Nagai, K.1    Shibata, K.2    Yamaguchi, H.3
  • 20
    • 0025002487 scopus 로고
    • Determination of N-acetylglucosaminyltransferases III, IV and V in normal and hepatoma tissues of rats
    • Nishikawa, A., Gu, J., Fujii, S. and Taniguchi, 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.1    Gu, J.2    Fujii, S.3    Taniguchi, N.4
  • 21
    • 0026705382 scopus 로고
    • Purification, cDNA cloning, and expression of UDP-N-acetylglucosamine: β-D-mannoside β-1,4 N-acetylglucosaminyltransferase III from rat kidney
    • Nishikawa, A., Ihara, Y., Hatakeyama, M., Kangawa, K., and Taniguchi, N. (1992) Purification, cDNA cloning, and expression of UDP-N-acetylglucosamine: β-D-mannoside β-1,4 N-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    Taniguchi, N.5
  • 23
    • 0026007853 scopus 로고
    • Molecular cloning and expression of cDNA encoding the enzyme that controls conversion of high-mannose to hybrid and complex N-glycans UDP-N-acetylglucosamine: α-3-D-mannoside β-1,2-N-acetylglucosaminyltransferasse I
    • Sarkar, M., Hull, E., Nishikawa, Y., Simpson, R.J., Moritz, R.L., Dunn, R. and Schachler, H. (1991) Molecular cloning and expression of cDNA encoding the enzyme that controls conversion of high-mannose to hybrid and complex N-glycans UDP-N-acetylglucosamine: α-3-D-mannoside β-1,2-N-acetylglucosaminyltransferasse I. Proc. Natl. Acad. Sci. USA, 88, 234-238.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 234-238
    • Sarkar, M.1    Hull, E.2    Nishikawa, Y.3    Simpson, R.J.4    Moritz, R.L.5    Dunn, R.6    Schachler, H.7
  • 24
    • 0021250549 scopus 로고
    • The formation of vesicular stomatitis virus (San Juan strain) becomes temperature-sensitive when glucose residues are retained on the oligosaccharides of the glycoprotein
    • Schlesinger, S., Malfer, C. and Schlesingeer, M.J. (1984) The formation of vesicular stomatitis virus (San Juan strain) becomes temperature-sensitive when glucose residues are retained on the oligosaccharides of the glycoprotein. J. Biol. Chem., 259, 7597-7601.
    • (1984) J. Biol. Chem. , vol.259 , pp. 7597-7601
    • Schlesinger, S.1    Malfer, C.2    Schlesingeer, M.J.3
  • 25
    • 0027318961 scopus 로고
    • Biological roles of oligosaccharides: All of the theories are correct
    • Varki, A. (1993) Biological roles of oligosaccharides: all of the theories are correct. Glycobiology, 3, 97-130.
    • (1993) Glycobiology , vol.3 , pp. 97-130
    • Varki, A.1
  • 26
    • 0028931837 scopus 로고
    • High expression of UDP-N-acetylglucosamine: β-D mannoside β-1,4-N-acetylglucosaminyltrnsferase III (GnT-III) in chronic myelogenous leukemia in blast crisis
    • Yoshimura, M., Nishikawa, A., Ihara, Y., Nishiura, T., Nakao, H., Kanayama, Y., Matuzawa, Y. and Taniguchi, N. (1995) High expression of UDP-N-acetylglucosamine: β-D mannoside β-1,4-N-acetylglucosaminyltrnsferase III (GnT-III) in chronic myelogenous leukemia in blast crisis. Int. J. Cancer, 60, 443-449.
    • (1995) Int. J. Cancer , vol.60 , pp. 443-449
    • Yoshimura, M.1    Nishikawa, A.2    Ihara, Y.3    Nishiura, T.4    Nakao, H.5    Kanayama, Y.6    Matuzawa, Y.7    Taniguchi, N.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.