메뉴 건너뛰기




Volumn 74, Issue 6, 2000, Pages 2359-2364

Effect of N-glycosylation on turnover and subcellular distribution of N- acetylgalactosaminyltransferase I and sialyltransferase II in neuroblastoma cells

Author keywords

Chaperones; Gangliosides; Glycosylation; Glycosyltransferases; Posttranslational modification; Subcellular localization

Indexed keywords

CALNEXIN; CASTANOSPERMINE; CHAPERONE; GANGLIOSIDE; GLYCOPROTEIN; GLYCOSPHINGOLIPID; GLYCOSYLTRANSFERASE; N ACETYLGALACTOSAMINYLTRANSFERASE; SIALYLTRANSFERASE;

EID: 0034073590     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.2000.0742359.x     Document Type: Article
Times cited : (26)

References (22)
  • 1
    • 0028972747 scopus 로고
    • 9-mannosidase from human kidney is expressed in COS-cells as a Golgi resident type II transmembrane N-glycoprotein
    • 9-mannosidase from human kidney is expressed in COS-cells as a Golgi resident type II transmembrane N-glycoprotein. Eur. J. Biochem. 233, 644-649.
    • (1995) Eur. J. Biochem. , vol.233 , pp. 644-649
    • Bieberich, E.1    Bause, E.2
  • 2
    • 0033040971 scopus 로고    scopus 로고
    • Multi-enzyme kinetic analysis (MEKA) of ganglioside metabolism
    • Bieberich E. and Yu R. K. (1999) Multi-enzyme kinetic analysis (MEKA) of ganglioside metabolism. Biochim. Biophys. Acta 1432, 113-124.
    • (1999) Biochim. Biophys. Acta , vol.1432 , pp. 113-124
    • Bieberich, E.1    Yu, R.K.2
  • 3
    • 0031846525 scopus 로고    scopus 로고
    • Inhibition of N-linked glycosylation results in retention of intracellular apo[a] in hepatoma cells, although nonglycosylated and immature forms of apolipoprotein[a] are competent to associate with apolipoprotein B-100 in vitro
    • Bonen D. K., Nassir F., Hausman A. M., and Davidson N. O. (1998) Inhibition of N-linked glycosylation results in retention of intracellular apo[a] in hepatoma cells, although nonglycosylated and immature forms of apolipoprotein[a] are competent to associate with apolipoprotein B-100 in vitro. J. Lipid Res. 39, 1629-1640.
    • (1998) J. Lipid Res. , vol.39 , pp. 1629-1640
    • Bonen, D.K.1    Nassir, F.2    Hausman, A.M.3    Davidson, N.O.4
  • 4
    • 0033548479 scopus 로고    scopus 로고
    • Trimming and readdition of glucose to N-linked oligosaccharides determines calnexin association of a substrate glycoprotein in living cells
    • Cannon K. S. and Helenius A. (1999) Trimming and readdition of glucose to N-linked oligosaccharides determines calnexin association of a substrate glycoprotein in living cells. J. Biol. Chem. 274, 7537-7544.
    • (1999) J. Biol. Chem. , vol.274 , pp. 7537-7544
    • Cannon, K.S.1    Helenius, A.2
  • 5
    • 0029049090 scopus 로고
    • Cotranslational folding and calnexin binding during glycoprotein synthesis
    • Chen W., Helenius J., Braakman I., and Helenius A. (1995) Cotranslational folding and calnexin binding during glycoprotein synthesis. Proc. Natl. Acad. Sci. USA 92, 6229-6233.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 6229-6233
    • Chen, W.1    Helenius, J.2    Braakman, I.3    Helenius, A.4
  • 6
    • 0033521072 scopus 로고    scopus 로고
    • Setting the standards: Quality control in the secretory pathway
    • Ellgaard L., Molinari M., and Helenius A. (1999) Setting the standards: quality control in the secretory pathway. Science 286, 1882-1888.
    • (1999) Science , vol.286 , pp. 1882-1888
    • Ellgaard, L.1    Molinari, M.2    Helenius, A.3
  • 7
    • 0020579390 scopus 로고
    • Protein blotting: Principles and applications
    • Gershoni J. M. and Palade G. E. (1983) Protein blotting: principles and applications. Anal. Biochem. 13, 1-15.
    • (1983) Anal. Biochem. , vol.13 , pp. 1-15
    • Gershoni, J.M.1    Palade, G.E.2
  • 8
    • 0028918341 scopus 로고
    • Regulation of sialyl-transferase activities by phosphorylation and dephosphorylation
    • Gu X., Preuß U., Gu T., and Yu R. K. (1995) Regulation of sialyl-transferase activities by phosphorylation and dephosphorylation. J. Neurochem. 64, 2295-2302.
    • (1995) J. Neurochem. , vol.64 , pp. 2295-2302
    • Gu, X.1    Preuß, U.2    Gu, T.3    Yu, R.K.4
  • 9
    • 0028103695 scopus 로고
    • Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control
    • Hammond C., Braakman I., and Helenius A. (1994) Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control. Proc. Natl. Acad. Sci. USA 91, 913-917.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 913-917
    • Hammond, C.1    Braakman, I.2    Helenius, A.3
  • 10
    • 0028880799 scopus 로고
    • The effects of site-directed removal of N-glycosylation sites from β-1,4-N-acetylgalactosaminyltransferase on its function
    • Haraguchi M., Yamashiro S., Furukawa K., Takamiya K., Shiku H., and Furukawa K. (1995) The effects of 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
    • Haraguchi, M.1    Yamashiro, S.2    Furukawa, K.3    Takamiya, K.4    Shiku, H.5    Furukawa, K.6
  • 11
    • 0029024748 scopus 로고
    • Glucose trimming and reglucosylation determine glycoprotein association with calnexin in the endoplasmic reticulum
    • Hebert D. N., Foellmer B., and Helenius A. (1995) Glucose trimming and reglucosylation determine glycoprotein association with calnexin in the endoplasmic reticulum. Cell 81, 425-433.
    • (1995) Cell , vol.81 , pp. 425-433
    • Hebert, D.N.1    Foellmer, B.2    Helenius, A.3
  • 12
    • 0028198111 scopus 로고
    • How N-linked oligosaccharides affect glycoprotein folding in the endoplasmic reticulum
    • Helenius A. (1994) How N-linked oligosaccharides affect glycoprotein folding in the endoplasmic reticulum. Mol. Biol. Cell 5, 253-265.
    • (1994) Mol. Biol. Cell , vol.5 , pp. 253-265
    • Helenius, A.1
  • 13
    • 0029035773 scopus 로고
    • Cloning and expression of glucosidase I from human hippocampus
    • Kalz-Füller B., Bieberich E., and Bause E. (1995) Cloning and expression of glucosidase I from human hippocampus. Eur. J. Biochem. 231, 344-351.
    • (1995) Eur. J. Biochem. , vol.231 , pp. 344-351
    • Kalz-Füller, B.1    Bieberich, E.2    Bause, E.3
  • 14
    • 0000960815 scopus 로고    scopus 로고
    • Combinatorial PCR approach to homology-based cloning: Cloning and expression of mouse and human GM3 synthase
    • Kapitonov D., Bieberich E., and Yu R. K. (1999) Combinatorial PCR approach to homology-based cloning: cloning and expression of mouse and human GM3 synthase. Glycoconj. J. 16, 337-350.
    • (1999) Glycoconj. J. , vol.16 , pp. 337-350
    • Kapitonov, D.1    Bieberich, E.2    Yu, R.K.3
  • 15
    • 0021891884 scopus 로고
    • Assembly of asparagine-linked oligosaccharides
    • Kornfeld R. and Kornfeld S. (1985) Assembly of asparagine-linked oligosaccharides. Annu. Rev. Biochem. 54, 631-664.
    • (1985) Annu. Rev. Biochem. , vol.54 , pp. 631-664
    • Kornfeld, R.1    Kornfeld, S.2
  • 16
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 17
    • 0032488983 scopus 로고    scopus 로고
    • Influence of N-glycosylation and N-glycan trimming on the activity and intracellular traffic of GD3-synthase
    • Martina J. A., Daniotti J. L., and Maccioni H. J. F. (1998) Influence of N-glycosylation and N-glycan trimming on the activity and intracellular traffic of GD3-synthase. J. Biol. Chem. 273, 3725-3731.
    • (1998) J. Biol. Chem. , vol.273 , pp. 3725-3731
    • Martina, J.A.1    Daniotti, J.L.2    Maccioni, H.J.F.3
  • 18
    • 0030449989 scopus 로고
    • N-linked oligosaccharides are necessary and sufficient for association of glycosylated forms of bovine RNase with calnexin and calreticulin
    • Rodan A. R., Simons J. F., Trombetta E. S., and Helenius A. (1995) N-linked oligosaccharides are necessary and sufficient for association of glycosylated forms of bovine RNase with calnexin and calreticulin. EMBO J. 15, 6921-6930.
    • (1995) EMBO J. , vol.15 , pp. 6921-6930
    • Rodan, A.R.1    Simons, J.F.2    Trombetta, E.S.3    Helenius, A.4
  • 20
    • 0016637041 scopus 로고
    • Lowry determination of protein in the presence of Triton X-100
    • Wang C.-S. and Smith R. L. (1975) Lowry determination of protein in the presence of Triton X-100. Anal. Biochem. 63, 414-417.
    • (1975) Anal. Biochem. , vol.63 , pp. 414-417
    • Wang, C.-S.1    Smith, R.L.2
  • 21
    • 0021355340 scopus 로고
    • A method for the quantitative recovery of protein in dilute solution in the presence of detergents and lipids
    • Wessel D. and Flügge U. I. (1984) A method for the quantitative recovery of protein in dilute solution in the presence of detergents and lipids. Anal. Biochem. 138, 141-143.
    • (1984) Anal. Biochem. , vol.138 , pp. 141-143
    • Wessel, D.1    Flügge, U.I.2
  • 22
    • 0028212835 scopus 로고
    • Developmental regulation of ganglioside metabolism
    • Yu R. K. (1994) Developmental regulation of ganglioside metabolism. Prog. Brain Res. 101, 31-44.
    • (1994) Prog. Brain Res. , vol.101 , pp. 31-44
    • Yu, R.K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.