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Volumn 12, Issue 11, 2002, Pages 763-770

O-glycosylation of EGF repeats: Identification and initial characterization of a UDP-glucose: Protein O-glucosyltransferase

Author keywords

Chinese hamster ovary cells; EGF repeats; Glucosyltransferase; Glycosyltransferases; O glucose

Indexed keywords

ALANINE; BLOOD CLOTTING FACTOR 7; BLOOD CLOTTING FACTOR 9; CELL EXTRACT; CYSTEINE; EPIDERMAL GROWTH FACTOR; FATTY ACID BINDING PROTEIN; GLUCOSE; GLUCOSYLTRANSFERASE; MANGANESE; METAL ION; PLASMA PROTEIN; PROTEIN; RECOMBINANT PROTEIN; SERINE; THROMBOSPONDIN; URIDINE DIPHOSPHATE GLUCOSE;

EID: 0036868766     PISSN: 09596658     EISSN: None     Source Type: Journal    
DOI: 10.1093/glycob/cwf085     Document Type: Review
Times cited : (64)

References (45)
  • 1
    • 0025941824 scopus 로고
    • NCAM polysialic acid can regulate both cell-cell and cell-substrate interactions
    • Acheson, A., Sunshine, J.L., and Rutishauser, U. (1991) NCAM polysialic acid can regulate both cell-cell and cell-substrate interactions. J. Cell Biol., 114, 143-153.
    • (1991) J. Cell Biol. , vol.114 , pp. 143-153
    • Acheson, A.1    Sunshine, J.L.2    Rutishauser, U.3
  • 2
    • 0034074901 scopus 로고    scopus 로고
    • The thrombospondin type 1 repeat (TSR) superfamily: Diverse proteins with related roles in neuronal development
    • Adams, J.C. and Tucker, R.P. (2000) The thrombospondin type 1 repeat (TSR) superfamily: diverse proteins with related roles in neuronal development. Dev. Dyn., 218, 280-299.
    • (2000) Dev. Dyn. , vol.218 , pp. 280-299
    • Adams, J.C.1    Tucker, R.P.2
  • 3
    • 0029064102 scopus 로고
    • Catalytic activities of glycogenin additional to autocatalytic self-glucosylation
    • Alonso, M.D., Lomako, J., Lomako, W.M., and Whelan, W.J. (1995) Catalytic activities of glycogenin additional to autocatalytic self-glucosylation. J. Biol. Chem., 270, 15315-15319.
    • (1995) J. Biol. Chem. , vol.270 , pp. 15315-15319
    • Alonso, M.D.1    Lomako, J.2    Lomako, W.M.3    Whelan, W.J.4
  • 4
    • 0033617522 scopus 로고    scopus 로고
    • Notch signaling: Cell fate control and signal integration in development
    • Artavanis-Tsakonas, S., Rand, M.D., and Lake, R.J. (1999) Notch signaling: cell fate control and signal integration in development. Science, 284, 770-776.
    • (1999) Science , vol.284 , pp. 770-776
    • Artavanis-Tsakonas, S.1    Rand, M.D.2    Lake, R.J.3
  • 5
    • 0018702930 scopus 로고
    • Chicken hematopoietic cells transformed by seven strains of defective avian leukemia viruses display three distinct phenotypes of differentiation
    • Beug, H., von Kirchbach, A., Doderlein, G., Conscience, J.F., and Graf, T. (1979) Chicken hematopoietic cells transformed by seven strains of defective avian leukemia viruses display three distinct phenotypes of differentiation. Cell, 18, 375-390.
    • (1979) Cell , vol.18 , pp. 375-390
    • Beug, H.1    von Kirchbach, A.2    Doderlein, G.3    Conscience, J.F.4    Graf, T.5
  • 6
    • 0025764566 scopus 로고
    • Human plasma and recombinant factor VII: Characterization of o-glycosylation at serine residues 52 and 60 and effects of site-directed mutagenesis of serine 52 to alanine
    • Bjoem, S., Foster, D.C., Thim, L., Wiberg, F.C., Christensen, M., Komiyama, Y., Pedersen, A.H., and Kisiel, W. (1991) Human plasma and recombinant factor VII: characterization of o-glycosylation at serine residues 52 and 60 and effects of site-directed mutagenesis of serine 52 to alanine. J. Biol. Chem., 266, 11051-11057.
    • (1991) J. Biol. Chem. , vol.266 , pp. 11051-11057
    • Bjoem, S.1    Foster, D.C.2    Thim, L.3    Wiberg, F.C.4    Christensen, M.5    Komiyama, Y.6    Pedersen, A.H.7    Kisiel, W.8
  • 7
    • 0242593940 scopus 로고    scopus 로고
    • Glycosyltransferase activity of Fringe modulates Notch-Delta interactions
    • Bruckner, K., Perez, L., Clausen, H., and Cohen, S. (2000) Glycosyltransferase activity of Fringe modulates Notch-Delta interactions. Nature, 406, 411-415.
    • (2000) Nature , vol.406 , pp. 411-415
    • Bruckner, K.1    Perez, L.2    Clausen, H.3    Cohen, S.4
  • 10
    • 0025856717 scopus 로고
    • TAN-1, the human homolog of the Drosophila Notch gene, is broken by chromosomal translocations in T lymphoblastic neoplasms
    • Ellisen, L.W., Bird, J., West, D.C., Soreng, A.L., Reynolds, T.C., Smith, S.D., and Sklar, J. (1991) TAN-1, the human homolog of the Drosophila Notch gene, is broken by chromosomal translocations in T lymphoblastic neoplasms. Cell, 66, 649-661.
    • (1991) Cell , vol.66 , pp. 649-661
    • Ellisen, L.W.1    Bird, J.2    West, D.C.3    Soreng, A.L.4    Reynolds, T.C.5    Smith, S.D.6    Sklar, J.7
  • 11
    • 0025193520 scopus 로고
    • Enzymatic addition of O-GlcNAc to nuclear and cytoplasmic proteins. Identification of a uridine diphospho-N-acetylglucosamine:peptide β-N-acetylglucosaminyl-transferase
    • Haltiwanger, R.S., Holt, G.D., and Hart, G.W. (1990) Enzymatic addition of O-GlcNAc to nuclear and cytoplasmic proteins. Identification of a uridine diphospho-N-acetylglucosamine:peptide β-N-acetylglucosaminyl-transferase. J. Biol. Chem., 265, 2563-2568.
    • (1990) J. Biol. Chem. , vol.265 , pp. 2563-2568
    • Haltiwanger, R.S.1    Holt, G.D.2    Hart, G.W.3
  • 12
    • 0027205366 scopus 로고
    • O-linked fucose and other post-translational modifications unique to EGF modules
    • Harris, R.J. and Spellman, M.W. (1993) O-linked fucose and other post-translational modifications unique to EGF modules. Glycobiology, 3, 219-224.
    • (1993) Glycobiology , vol.3 , pp. 219-224
    • Harris, R.J.1    Spellman, M.W.2
  • 14
    • 0025192470 scopus 로고
    • 2glucose-O-serine 53 found in the first epidermal growth factor-like domain of bovine blood clotting factor IX
    • 2glucose-O-serine 53 found in the first epidermal growth factor-like domain of bovine blood clotting factor IX. J. Biol. Chem., 265, 1858-1861.
    • (1990) J. Biol. Chem. , vol.265 , pp. 1858-1861
    • Hase, S.1    Nishimura, H.2    Kawabata, S.3    Iwanaga, S.4    Ikenaka, T.5
  • 15
    • 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
  • 17
    • 0023037076 scopus 로고
    • The subcellular distribution of terminal N-acetylglucosamine moieties. Localization of a novel protein-saccharide likage, O-linked GlcNAc
    • Holt, G.D. and Hart, G.W. (1986) The subcellular distribution of terminal N-acetylglucosamine moieties. Localization of a novel protein-saccharide likage, O-linked GlcNAc. J. Biol. Chem., 261, 8049-8057.
    • (1986) J. Biol. Chem. , vol.261 , pp. 8049-8057
    • Holt, G.D.1    Hart, G.W.2
  • 18
    • 0032232959 scopus 로고    scopus 로고
    • Notch signalling pathway and human diseases
    • Joutel, A. and Tournier-Lasserve, E. (1998) Notch signalling pathway and human diseases. Sem. Cell Dev. Biol., 9, 619-625.
    • (1998) Sem. Cell Dev. Biol. , vol.9 , pp. 619-625
    • Joutel, A.1    Tournier-Lasserve, E.2
  • 20
    • 0025365591 scopus 로고
    • Lysosomal enzyme targeting
    • Kornfeld, S. (1990) Lysosomal enzyme targeting. Biochem. Soc. Trans, 18, 367-374.
    • (1990) Biochem. Soc. Trans. , vol.18 , pp. 367-374
    • Kornfeld, S.1
  • 21
    • 0031057323 scopus 로고    scopus 로고
    • Glycosylation analysis and protein structure determination of murine fetal antigen 1 (mFA1)-the circulating gene product of the delta-like protein (dlk), preadipocyte factor 1 (Pref-1) and stromal-cell-derived protein 1 (SCP-1) cDNAs
    • Krogh T.N., Bachmann, E., Teisner, B., Skjodt, K., and Hojrup, P. (1997) Glycosylation analysis and protein structure determination of murine fetal antigen 1 (mFA1)-the circulating gene product of the delta-like protein (dlk), preadipocyte factor 1 (Pref-1) and stromal-cell-derived protein 1 (SCP-1) cDNAs. Eur. J. Biochem., 244, 334-342.
    • (1997) Eur. J. Biochem. , vol.244 , pp. 334-342
    • Krogh, T.N.1    Bachmann, E.2    Teisner, B.3    Skjodt, K.4    Hojrup, P.5
  • 23
    • 0029799513 scopus 로고    scopus 로고
    • Detection of UDP-D-xylose: α-D-xyloside α1, 3xylosyltransferase activity in human hepatoma cell line HepG2
    • Minamida, S., Aoki, K., Natsuka, S., Omichi, K., Fukase, K., Kusumoto, S., and Hase, S. (1996) Detection of UDP-D-xylose: α-D-xyloside α1, 3xylosyltransferase activity in human hepatoma cell line HepG2. J. Biochem. (Tokyo), 120, 1002-1006.
    • (1996) J. Biochem. (Tokyo) , vol.120 , pp. 1002-1006
    • Minamida, S.1    Aoki, K.2    Natsuka, S.3    Omichi, K.4    Fukase, K.5    Kusumoto, S.6    Hase, S.7
  • 24
    • 0032805976 scopus 로고    scopus 로고
    • The O-linked fucose glycosylation pathway: Identification and characteriztion of a UDP-glucose: O-fucose β1, 3-glucosyltransferase
    • Moloney, D.J. and Haltiwanger, R.S. (1999) The O-linked fucose glycosylation pathway: Identification and characteriztion of a UDP-glucose: O-fucose β1, 3-glucosyltransferase. Glycobiology, 9, 679-687.
    • (1999) Glycobiology , vol.9 , pp. 679-687
    • Moloney, D.J.1    Haltiwanger, R.S.2
  • 25
    • 0030853960 scopus 로고    scopus 로고
    • The O-linked fucose glycosylation pathway: Evidence for protein specific elongation of O-linked fucose in Chinese hamster ovary cells
    • Moloney, D.J., Lin, A.I., and Haltiwanger, R.S. (1997) The O-linked fucose glycosylation pathway: evidence for protein specific elongation of O-linked fucose in Chinese hamster ovary cells. J. Biol. Chem., 272, 19046-19050.
    • (1997) J. Biol. Chem. , vol.272 , pp. 19046-19050
    • Moloney, D.J.1    Lin, A.I.2    Haltiwanger, R.S.3
  • 27
    • 0034737738 scopus 로고    scopus 로고
    • Mammalian Notch 1 is modified with two unusual forms of O-linked glycosylation found on epidermal growth factor-like modules
    • Moloney, D.J., Shair, L., Lu, F.M., Xia, J., Locke, R., Matta, K.L., and Haltiwanger, R.S. (2000b) Mammalian Notch 1 is modified with two unusual forms of O-linked glycosylation found on epidermal growth factor-like modules. J. Biol. Chem., 275, 9604-9611.
    • (2000) J. Biol. Chem. , vol.275 , pp. 9604-9611
    • Moloney, D.J.1    Shair, L.2    Lu, F.M.3    Xia, J.4    Locke, R.5    Matta, K.L.6    Haltiwanger, R.S.7
  • 28
    • 0034671686 scopus 로고    scopus 로고
    • Notch signaling: From the outside in
    • Mumm, J.S. and Kopan, R. (2000) Notch signaling: from the outside in. Dev. Biol., 228, 151-165.
    • (2000) Dev. Biol. , vol.228 , pp. 151-165
    • Mumm, J.S.1    Kopan, R.2
  • 29
    • 0024377258 scopus 로고
    • 2-Glc) O-glycosidically linked to a serine residue in the first epidermal growth factor-like domain of human factors VII and IX and protein Z and bovine protein Z
    • 2-Glc) O-glycosidically linked to a serine residue in the first epidermal growth factor-like domain of human factors VII and IX and protein Z and bovine protein Z. J. Biol. Chem., 264, 20320-20325.
    • (1989) J. Biol. Chem. , vol.264 , pp. 20320-20325
    • Nishimura, H.1    Kawabata, S.2    Kisiel, W.3    Hase, S.4    Ikenaka, T.5    Takao, T.6    Shimonishi, Y.7    Iwanaga, S.8
  • 30
    • 0026606075 scopus 로고
    • Evidence for the existence of O-linked sugar chains consisting of glucose and xylose in bovine thrombospondin
    • Nishimura, H., Yamashita, S., Zeng, Z., Walz, D.A., and Iwanaga, S. (1992) Evidence for the existence of O-linked sugar chains consisting of glucose and xylose in bovine thrombospondin. J. Biochem. (Tokyo), 111, 460-464.
    • (1992) J. Biochem. (Tokyo) , vol.111 , pp. 460-464
    • Nishimura, H.1    Yamashita, S.2    Zeng, Z.3    Walz, D.A.4    Iwanaga, S.5
  • 31
    • 0030901372 scopus 로고    scopus 로고
    • Presence of UDP-D-xylose: β-D-glucoside α-1, 3-D-xylosyltransferase involved in the biosynthesis of the Xylα1-3Glcβ-Ser structure of glycoproteins in the human hepatoma cell line HepG2
    • Omichi, K., Aoki, K., Minamida, S., and Hase, S. (1997) Presence of UDP-D-xylose: β-D-glucoside α-1, 3-D-xylosyltransferase involved in the biosynthesis of the Xylα1-3Glcβ-Ser structure of glycoproteins in the human hepatoma cell line HepG2. Eur. J. Biochem., 245, 143-146.
    • (1997) Eur. J. Biochem. , vol.245 , pp. 143-146
    • Omichi, K.1    Aoki, K.2    Minamida, S.3    Hase, S.4
  • 33
    • 0026643491 scopus 로고
    • Structural requirements for the growth factor activity of the amino-terminal domain of urokinase
    • Rabbani, S.A., Mazar, A.P., Bernier, S.M., Haq, M., Bolivar, I., Henkin, J., and Goltzman, D. (1992) Structural requirements for the growth factor activity of the amino-terminal domain of urokinase. J. Biol. Chem., 267, 14151-14156.
    • (1992) J. Biol. Chem. , vol.267 , pp. 14151-14156
    • Rabbani, S.A.1    Mazar, A.P.2    Bernier, S.M.3    Haq, M.4    Bolivar, I.5    Henkin, J.6    Goltzman, D.7
  • 34
    • 0026086474 scopus 로고
    • Specific EGF repeats of Notch mediate interactions with Delta and Serrate: Implications for Notch as a multifunctional receptor
    • Rebay, I., Fleming, R.J., Fehon, R.G., Cherbas, L., Cherbas, P., and Artavanis-Tsakonas, S. (1991) Specific EGF repeats of Notch mediate interactions with Delta and Serrate: implications for Notch as a multifunctional receptor. Cell, 67, 687-699.
    • (1991) Cell , vol.67 , pp. 687-699
    • Rebay, I.1    Fleming, R.J.2    Fehon, R.G.3    Cherbas, L.4    Cherbas, P.5    Artavanis-Tsakonas, S.6
  • 37
    • 0017398689 scopus 로고
    • Complementation between mutants of CHO cells resistant to a variety of plant lectins
    • Stanley, P. and Siminovitch, L. (1977) Complementation between mutants of CHO cells resistant to a variety of plant lectins. Som. Cell Genet., 3, 391-405.
    • (1977) Som. Cell Genet. , vol.3 , pp. 391-405
    • Stanley, P.1    Siminovitch, L.2
  • 38
    • 0026078476 scopus 로고
    • The SIT4 protein phosphatase functions in late G1 for progression into S phase
    • Sutton, A., Immanuel, D., and Arndt, K.T. (1991) The SIT4 protein phosphatase functions in late G1 for progression into S phase. Mol. Cell Biol., 11, 2133-2148.
    • (1991) Mol. Cell Biol. , vol.11 , pp. 2133-2148
    • Sutton, A.1    Immanuel, D.2    Arndt, K.T.3
  • 40
    • 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
  • 41
    • 0032478730 scopus 로고    scopus 로고
    • Purification and characterization of a GDP-fucose: Polypeptide fucosyltransferase from Chinese hamster ovary cells
    • Wang, Y. and Spellman, M.W. (1998) Purification and characterization of a GDP-fucose: polypeptide fucosyltransferase from Chinese hamster ovary cells. J. Biol. Chem., 273, 8112-8118.
    • (1998) J. Biol. Chem. , vol.273 , pp. 8112-8118
    • Wang, Y.1    Spellman, M.W.2
  • 42
    • 0030472840 scopus 로고    scopus 로고
    • Identification of a GDP-L-fucose: Polypeptide fucosyltransferase and enzymatic addition of O-linked fucose to EGF domains
    • Wang, Y., Lee, G.F., Kelley, R.F., and Spellman, M.W. (1996) Identification of a GDP-L-fucose: polypeptide fucosyltransferase and enzymatic addition of O-linked fucose to EGF domains. Glycobiology, 6, 837-842.
    • (1996) Glycobiology , vol.6 , pp. 837-842
    • Wang, Y.1    Lee, G.F.2    Kelley, R.F.3    Spellman, M.W.4
  • 43
    • 0035955684 scopus 로고    scopus 로고
    • Modification of epidermal growth factor-like repeats with O-fucose: Molecular cloning of a novel GDP-fucose: Protein O-fucosyltransferase
    • Wang, Y., Shao, L., Shi, S., Harris, R.J., Spellman, M.W., Stanley, P., and Haltiwanger, R.S. (2001) Modification of epidermal growth factor-like repeats with O-fucose: molecular cloning of a novel GDP-fucose: protein O-fucosyltransferase. J. Biol. Chem., 276, 40338-40345.
    • (2001) J. Biol. Chem. , vol.276 , pp. 40338-40345
    • Wang, Y.1    Shao, L.2    Shi, S.3    Harris, R.J.4    Spellman, M.W.5    Stanley, P.6    Haltiwanger, R.S.7
  • 44
    • 0036275653 scopus 로고    scopus 로고
    • Bi-functional activity of Cripto as a ligand and coreceptor in the Nodal signaling pathway
    • Yan, Y.T., Liu, J.J., Luo, Y.E.C., Haltiwanger, R.S., Abate-shen, C., and Shen, M.M. (2002) Bi-functional activity of Cripto as a ligand and coreceptor in the Nodal signaling pathway. Mol. Cell Biol., 22, 4439-4449.
    • (2002) Mol. Cell Biol. , vol.22 , pp. 4439-4449
    • Yan, Y.T.1    Liu, J.J.2    Luo, Y.E.C.3    Haltiwanger, R.S.4    Abate-shen, C.5    Shen, M.M.6


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