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Volumn 7, Issue 8, 1997, Pages 1053-1060

Charge distribution of flanking amino acids inhibits O-glycosylation of several single-site acceptors in vivo

Author keywords

Glycosyltransferases; Mucins; O glycosylation

Indexed keywords

AMINO ACID; SERINE; THREONINE; VON WILLEBRAND FACTOR;

EID: 0031442648     PISSN: 09596658     EISSN: None     Source Type: Journal    
DOI: 10.1093/glycob/7.8.1053-c     Document Type: Article
Times cited : (28)

References (32)
  • 2
    • 0025779449 scopus 로고
    • Generation of high efficiency, single-stranded DNA hybridization probes by PCR
    • Bednarczuk, T.A., Wiggins, R.C. and Konat, G.W. (1991) Generation of high efficiency, single-stranded DNA hybridization probes by PCR. Biotechniques, 10, 478.
    • (1991) Biotechniques , vol.10 , pp. 478
    • Bednarczuk, T.A.1    Wiggins, R.C.2    Konat, G.W.3
  • 3
    • 0030035111 scopus 로고    scopus 로고
    • cDNA cloning and expression of a novel human UDP-N-acetyl-α-D-galactosamine
    • Bennett, E.P., Hassan, H. and Clausen, H. (1996) cDNA cloning and expression of a novel human UDP-N-acetyl-α-D-galactosamine. J. Biol. Chem., 271, 17006-17012.
    • (1996) J. Biol. Chem. , vol.271 , pp. 17006-17012
    • Bennett, E.P.1    Hassan, H.2    Clausen, H.3
  • 4
    • 0027291520 scopus 로고
    • Assignment of O-glycan attachment sites to the hinge-like regions of human lysosomal membrane glycoproteins Lamp-1 and Lamp-2
    • Carlsson, S.R., Lycksell, P.-O. and Fukuda, M. (1993) Assignment of O-glycan attachment sites to the hinge-like regions of human lysosomal membrane glycoproteins Lamp-1 and Lamp-2. Arch. Biochem. Biophys., 304, 65-73.
    • (1993) Arch. Biochem. Biophys. , vol.304 , pp. 65-73
    • Carlsson, S.R.1    Lycksell, P.-O.2    Fukuda, M.3
  • 5
    • 0028800739 scopus 로고
    • A vector projection method for predicting the specificity of GalNAc-transferase
    • Chou, K.-C., Zhang, C.-T., Kézdy, F.J. and Poorman, R.A. (1995) A vector projection method for predicting the specificity of GalNAc-transferase. Proteins Struct. Funct. Genet., 21, 118-126.
    • (1995) Proteins Struct. Funct. Genet. , vol.21 , pp. 118-126
    • Chou, K.-C.1    Zhang, C.-T.2    Kézdy, F.J.3    Poorman, R.A.4
  • 6
    • 0018110116 scopus 로고
    • Prediction of the secondary structure of proteins from their amino acid sequences
    • Chou, P.Y. and Fasman, G.D. (1978) Prediction of the secondary structure of proteins from their amino acid sequences. Adv. Enzymol., 47, 45-147.
    • (1978) Adv. Enzymol. , vol.47 , pp. 45-147
    • Chou, P.Y.1    Fasman, G.D.2
  • 7
    • 0027280810 scopus 로고
    • The specificity of UDP-GalNAc:polypeptide N-Acetylgalactosaminyltransferase as inferred from a database on in vivo substrates and from the in vitro glycosylation of proteins and peptides
    • Elhammer, A.P., Poorman, R.A., Brown, E., Maggiora, L.L., Hoogerheide, J.G. and Kézdy, F.J. (1993) The specificity of UDP-GalNAc:polypeptide N-Acetylgalactosaminyltransferase as inferred from a database on in vivo substrates and from the in vitro glycosylation of proteins and peptides. J. Biol. Chem., 268, 10029-10038.
    • (1993) J. Biol. Chem. , vol.268 , pp. 10029-10038
    • Elhammer, A.P.1    Poorman, R.A.2    Brown, E.3    Maggiora, L.L.4    Hoogerheide, J.G.5    Kézdy, F.J.6
  • 9
    • 0017873321 scopus 로고
    • Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins
    • Garnier, J., Osguthorpe, D.J. and Robson, B. (1978) Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins. J. Mol. Biol., 120, 97-120.
    • (1978) J. Mol. Biol. , vol.120 , pp. 97-120
    • Garnier, J.1    Osguthorpe, D.J.2    Robson, B.3
  • 10
    • 0027374598 scopus 로고
    • Identification of the predominant glycosaminoglycan-attachment site in soluble recombinant human thrombomodulin: Potential regulation of functionality by glycosyltransferase competition for serine 474
    • Gerlitz, B., Hassell, T., Vlahos, C.J., Parkinson, J.F., Bang, N.U. and Grinnell, B.W. (1993) Identification of the predominant glycosaminoglycan-attachment site in soluble recombinant human thrombomodulin: potential regulation of functionality by glycosyltransferase competition for serine 474. Biochem. J., 295, 131-140.
    • (1993) Biochem. J. , vol.295 , pp. 131-140
    • Gerlitz, B.1    Hassell, T.2    Vlahos, C.J.3    Parkinson, J.F.4    Bang, N.U.5    Grinnell, B.W.6
  • 11
    • 0028107095 scopus 로고
    • Towards characterizing O-glycans: The relative merits of in vivo and in vitro approaches in seeking peptide motifs specifying O-glycosylation sites
    • Gooley, A.A. and Williams, K.L. (1994) Towards characterizing O-glycans: the relative merits of in vivo and in vitro approaches in seeking peptide motifs specifying O-glycosylation sites. Glycobiology, 4, 413-417.
    • (1994) Glycobiology , vol.4 , pp. 413-417
    • Gooley, A.A.1    Williams, K.L.2
  • 12
    • 0029621863 scopus 로고
    • Cloning and sequence homology of a rat UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase
    • Hagen, F.K., Gregoire, C.A. and Tabak, L.A. (1995) Cloning and sequence homology of a rat UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase. Glycoconjugate J., 12, 901-909.
    • (1995) Glycoconjugate J. , vol.12 , pp. 901-909
    • Hagen, F.K.1    Gregoire, C.A.2    Tabak, L.A.3
  • 13
    • 0030922124 scopus 로고    scopus 로고
    • cDNA cloning and expression of a novel UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase
    • Hagen, F.K., Ten Hagen, K.G., Beres, T.M., Balys, M., VanWuyckhuyse, B.C. and Tabak, L.A. (1997) cDNA cloning and expression of a novel UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase. J. Biol. Chem., 272, 13843-13848.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13843-13848
    • Hagen, F.K.1    Ten Hagen, K.G.2    Beres, T.M.3    Balys, M.4    VanWuyckhuyse, B.C.5    Tabak, L.A.6
  • 14
    • 0029003322 scopus 로고
    • Prediction of O-glycosylation of mammalian protein: Specificity patterns of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase
    • Hansen, J.E., Lund, O., Engelbrecht, J., Bohr, H., Nielsen, J.O., Hansen, J.-E. S. and Brunak, S. (1995) Prediction of O-glycosylation of mammalian protein: specificity patterns of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase. Biochem. J., 308, 801-813.
    • (1995) Biochem. J. , vol.308 , pp. 801-813
    • Hansen, J.E.1    Lund, O.2    Engelbrecht, J.3    Bohr, H.4    Nielsen, J.O.5    Hansen, J.-E.S.6    Brunak, S.7
  • 16
    • 0029556979 scopus 로고
    • T cell-specific deletion of the polypeptide N-acetylgalactosaminyltransferase gene by site-directed recombination
    • Hennet, T., Hagen, F.K., Tabak, L.A. and Marth, J.D. (1995) T cell-specific deletion of the polypeptide N-acetylgalactosaminyltransferase gene by site-directed recombination. Proc. Natl. Acad. Sci. USA, 92, 12070-12074.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 12070-12074
    • Hennet, T.1    Hagen, F.K.2    Tabak, L.A.3    Marth, J.D.4
  • 17
    • 0025297888 scopus 로고
    • Why are proteins glycosylated?
    • Jentoft, N. (1990) Why are proteins glycosylated? Trends Biochem. Sci., 15, 291-294.
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 291-294
    • Jentoft, N.1
  • 18
    • 0029862980 scopus 로고    scopus 로고
    • Charge distribution of flanking amino acids and Golgi transit time influence O-glycan acquisition in vivo
    • Nehrke, K., Hagen, F.K. and Tabak, L.A. (1996) Charge distribution of flanking amino acids and Golgi transit time influence O-glycan acquisition in vivo. J. Biol. Chem., 271, 7061-7065.
    • (1996) J. Biol. Chem. , vol.271 , pp. 7061-7065
    • Nehrke, K.1    Hagen, F.K.2    Tabak, L.A.3
  • 19
    • 0028289734 scopus 로고
    • Influence of acceptor substrate primary amino acid sequence on the activity of human UDP-N-acetylgalactosamine:polypeptide N-acetylgalactosaminyltransferase
    • Nishimori, I., Johnson, N.R., Sanderson, S.D., Perini, F., Mountjoy, K., Cerny, R.L., Gross, M.L. and Hollingsworth, M.A. (1994) Influence of acceptor substrate primary amino acid sequence on the activity of human UDP-N-acetylgalactosamine:polypeptide N-acetylgalactosaminyltransferase. J. Biol. Chem., 269, 16123-16130.
    • (1994) J. Biol. Chem. , vol.269 , pp. 16123-16130
    • Nishimori, I.1    Johnson, N.R.2    Sanderson, S.D.3    Perini, F.4    Mountjoy, K.5    Cerny, R.L.6    Gross, M.L.7    Hollingsworth, M.A.8
  • 21
    • 0026470310 scopus 로고
    • The influence of flanking sequence on the O-glycosylation of threonine in vitro
    • O'Connell, B., Hagen, F.K. and Tabak, L.A. (1992) The influence of flanking sequence on the O-glycosylation of threonine in vitro. J. Biol. Chem., 267, 25010-25018.
    • (1992) J. Biol. Chem. , vol.267 , pp. 25010-25018
    • O'Connell, B.1    Hagen, F.K.2    Tabak, L.A.3
  • 22
    • 0025284968 scopus 로고
    • O-linked sugar chain of human gramilocyte colony-stimulating factor protects it against polymerization and denaturation allowing it to retain its biological activity
    • Oh-eda, M., Hasegawa, M., Hattori, K., Kuboniwa, H., Kojima, T., Orita, T., Tomonou, K., Yamazaki, T. and Ochi, N. (1990) O-linked sugar chain of human gramilocyte colony-stimulating factor protects it against polymerization and denaturation allowing it to retain its biological activity. J. Biol. Chem., 265, 11432-11435.
    • (1990) J. Biol. Chem. , vol.265 , pp. 11432-11435
    • Oh-eda, M.1    Hasegawa, M.2    Hattori, K.3    Kuboniwa, H.4    Kojima, T.5    Orita, T.6    Tomonou, K.7    Yamazaki, T.8    Ochi, N.9
  • 23
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schagger, H. and von Jagow, G. (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem., 166, 368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schagger, H.1    Von Jagow, G.2
  • 25
    • 0028963728 scopus 로고
    • Studies on the order and site specificity of GalNAc transfer to MUC1 tandem repeats by UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase from milk or mammary carcinoma cells
    • Stadie, T.R.E., Chai, W., Lawson, A.M., Byfield, P.G.H. and Hanisch, F.-G. (1995) Studies on the order and site specificity of GalNAc transfer to MUC1 tandem repeats by UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase from milk or mammary carcinoma cells. Eur. J. Biochem., 229, 140-147.
    • (1995) Eur. J. Biochem. , vol.229 , pp. 140-147
    • Stadie, T.R.E.1    Chai, W.2    Lawson, A.M.3    Byfield, P.G.H.4    Hanisch, F.-G.5
  • 26
    • 0030924831 scopus 로고    scopus 로고
    • Phosphorylation and O-glycosylation sites of bovine chromogranin A from adrenal medullary chromaffin granules and their relationship with biological activities
    • Strub, J.-M., Sorokine, O., Van Dorsselaer, A., Aunis, D. and Metz-Boutigue, M.-H. (1997) Phosphorylation and O-glycosylation sites of bovine chromogranin A from adrenal medullary chromaffin granules and their relationship with biological activities. J. Biol. Chem., 272, 11928-11936.
    • (1997) J. Biol. Chem. , vol.272 , pp. 11928-11936
    • Strub, J.-M.1    Sorokine, O.2    Van Dorsselaer, A.3    Aunis, D.4    Metz-Boutigue, M.-H.5
  • 27
    • 0029814423 scopus 로고    scopus 로고
    • Characterization of the O-glycosylation sites in the chorionic gonadotropin β subunit in vivo using site-directed mutagenesis and gene transfer
    • Sugahara, T., Pixley, M.R., Fares, F. and Boime, I. (1996) Characterization of the O-glycosylation sites in the chorionic gonadotropin β subunit in vivo using site-directed mutagenesis and gene transfer. J. Biol. Chem., 271, 20797-20804.
    • (1996) J. Biol. Chem. , vol.271 , pp. 20797-20804
    • Sugahara, T.1    Pixley, M.R.2    Fares, F.3    Boime, I.4
  • 28
    • 0028942854 scopus 로고
    • In defense of the oral cavity: Structure, biosynthesis, and function of salivary mucins
    • Tabak, L.A. (1995) In defense of the oral cavity: structure, biosynthesis, and function of salivary mucins. Annu. Rev. Physiol., 57, 547-564.
    • (1995) Annu. Rev. Physiol. , vol.57 , pp. 547-564
    • Tabak, L.A.1
  • 29
    • 0028803582 scopus 로고
    • Purification and cDNA cloning of a human UDP-N-acetyl-α-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase
    • White, T., Bennet, E.P., Takiol, K., Sorensen, T., Bonding, N. and Clausen, H. (1995) Purification and cDNA cloning of a human UDP-N-acetyl-α-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase. J. Biol. Chem., 270, 24156-24165.
    • (1995) J. Biol. Chem. , vol.270 , pp. 24156-24165
    • White, T.1    Bennet, E.P.2    Takiol, K.3    Sorensen, T.4    Bonding, N.5    Clausen, H.6
  • 30
    • 0025865091 scopus 로고
    • Amino acid distributions around O-linked glycosylation sites
    • Wilson, I.B., Gavel, Y. and von Heigne, G. (1991) Amino acid distributions around O-linked glycosylation sites. Biochem. J., 275, 529-534.
    • (1991) Biochem. J. , vol.275 , pp. 529-534
    • Wilson, I.B.1    Gavel, Y.2    Von Heigne, G.3


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