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Volumn 1573, Issue 3, 2002, Pages 258-270

Targeted mutations in β1,4-galactosyltransferase I reveal its multiple cellular functions

Author keywords

1,4 Galactosyltransferase I; Fertilization; Glycosylation; Golgi complex; Mammary gland; Plasma membrane

Indexed keywords

GALACTOSYLTRANSFERASE; GLYCOLIPID; GLYCOPROTEIN; OLIGOSACCHARIDE; ISOENZYME; N ACETYLLACTOSAMINE SYNTHASE;

EID: 0037137455     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0304-4165(02)00392-6     Document Type: Review
Times cited : (37)

References (84)
  • 1
    • 0015150656 scopus 로고
    • The purification and properties of the A protein of lactose synthetase
    • Trayer I.P., Hill R.L. The purification and properties of the A protein of lactose synthetase. J. Biol. Chem. 246:1971;6666-6675.
    • (1971) J. Biol. Chem. , vol.246 , pp. 6666-6675
    • Trayer, I.P.1    Hill, R.L.2
  • 3
  • 5
    • 0033168184 scopus 로고    scopus 로고
    • Crystal structures of the bovine β1,4-galactosyltransferase catalytic domain and its complex with uridine diphosphogalactose
    • Gastinel L.N., Cambillau C., Bourne Y. Crystal structures of the bovine β1,4-galactosyltransferase catalytic domain and its complex with uridine diphosphogalactose. EMBO J. 18:1999;3546-3557.
    • (1999) EMBO J. , vol.18 , pp. 3546-3557
    • Gastinel, L.N.1    Cambillau, C.2    Bourne, Y.3
  • 6
    • 0035813137 scopus 로고    scopus 로고
    • α-Lactalbumin (LA) stimulates milk β1,4-galactosyltransferase I (β4Gal-T1) to transfer glucose from UDP-glucose to N-acetylglucosamine: Crystal structure of β4Gal-T1·LA complex with UDP-Glc
    • Ramakrishnan B., Shah P.S., Qasba P.K. α-Lactalbumin (LA) stimulates milk β1,4-galactosyltransferase I (β4Gal-T1) to transfer glucose from UDP-glucose to N-acetylglucosamine: crystal structure of β4Gal-T1·LA complex with UDP-Glc. J. Biol. Chem. 276:2001;37665-37671.
    • (2001) J. Biol. Chem. , vol.276 , pp. 37665-37671
    • Ramakrishnan, B.1    Shah, P.S.2    Qasba, P.K.3
  • 7
    • 0024402457 scopus 로고
    • Cell surface and Golgi pools of β1,4-galactosyltransferase are differentially regulated during embryonal carcinoma cell differentiation
    • Lopez L.C., Maillet C.M., Oleszkowicz K., Shur B.D. Cell surface and Golgi pools of β1,4-galactosyltransferase are differentially regulated during embryonal carcinoma cell differentiation. Mol. Cell. Biol. 9:1989;2370-2377.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 2370-2377
    • Lopez, L.C.1    Maillet, C.M.2    Oleszkowicz, K.3    Shur, B.D.4
  • 8
    • 0034067636 scopus 로고    scopus 로고
    • Insulin-induced redistribution of the insulin-like growth factor II/mannose 6-phosphate receptor in intact rat liver
    • Villevalois-Cam L., Tahiri K., Chauvet G., Desbuquois B. Insulin-induced redistribution of the insulin-like growth factor II/mannose 6-phosphate receptor in intact rat liver. J. Cell. Biochem. 77:2000;310-322.
    • (2000) J. Cell. Biochem. , vol.77 , pp. 310-322
    • Villevalois-Cam, L.1    Tahiri, K.2    Chauvet, G.3    Desbuquois, B.4
  • 9
    • 0028123669 scopus 로고
    • A protein-specific monoclonal antibody to rat liver β1,4-galactosyltransferase and its application to immunohistochemistry
    • Kawano J., Ide S., Oinuma T., Suganuma T. A protein-specific monoclonal antibody to rat liver β1,4-galactosyltransferase and its application to immunohistochemistry. J. Histochem. Cytochem. 42:1994;363-369.
    • (1994) J. Histochem. Cytochem. , vol.42 , pp. 363-369
    • Kawano, J.1    Ide, S.2    Oinuma, T.3    Suganuma, T.4
  • 10
    • 0016743158 scopus 로고
    • Cell surface glycosyltransferases
    • Shur B.D., Roth S. Cell surface glycosyltransferases. Biochim. Biophys. Acta. 415:1975;473-512.
    • (1975) Biochim. Biophys. Acta , vol.415 , pp. 473-512
    • Shur, B.D.1    Roth, S.2
  • 11
    • 0031854370 scopus 로고    scopus 로고
    • Cell surface galactosyltransferase: Current issues
    • Shur B.D., Evans S., Lu Q. Cell surface galactosyltransferase: current issues. Glycoconj. J. 15:1998;537-548.
    • (1998) Glycoconj. J. , vol.15 , pp. 537-548
    • Shur, B.D.1    Evans, S.2    Lu, Q.3
  • 12
    • 0014867207 scopus 로고
    • The synthesis of complex carbohydrates by multiglycosyltransferase systems and their potential function in intercellular adhesion
    • Roseman S. The synthesis of complex carbohydrates by multiglycosyltransferase systems and their potential function in intercellular adhesion. Chem. Phys. Lipids. 5:1970;270-297.
    • (1970) Chem. Phys. Lipids , vol.5 , pp. 270-297
    • Roseman, S.1
  • 13
    • 0015159047 scopus 로고
    • Evidence for cell surface glycosyltransferases: Their potential role in cellular recognition
    • Roth S., McGuire E.J., Roseman S. Evidence for cell surface glycosyltransferases: their potential role in cellular recognition. J. Cell Biol. 51:1971;536-547.
    • (1971) J. Cell Biol. , vol.51 , pp. 536-547
    • Roth, S.1    McGuire, E.J.2    Roseman, S.3
  • 14
    • 0027682606 scopus 로고
    • Glycosyltransferases as cell adhesion molecules
    • Shur B.D. Glycosyltransferases as cell adhesion molecules. Curr. Opin. Cell Biol. 5:1993;854-863.
    • (1993) Curr. Opin. Cell Biol. , vol.5 , pp. 854-863
    • Shur, B.D.1
  • 15
    • 0024281351 scopus 로고
    • Temporally specific involvement of cell surface β1,4-galactosyltransferase during mouse embryo morula compaction
    • Bayna E.M., Shaper J.H., Shur B.D. Temporally specific involvement of cell surface β1,4-galactosyltransferase during mouse embryo morula compaction. Cell. 53:1988;145-157.
    • (1988) Cell , vol.53 , pp. 145-157
    • Bayna, E.M.1    Shaper, J.H.2    Shur, B.D.3
  • 16
    • 0020037889 scopus 로고
    • Immunocytochemical localization of galactosyltransferase in HeLa cells: Codistribution with thiamine pyrophosphatase in trans-Golgi cisternae
    • Roth J., Berger E.G. Immunocytochemical localization of galactosyltransferase in HeLa cells: codistribution with thiamine pyrophosphatase in trans-Golgi cisternae. J. Cell Biol. 93:1982;223-229.
    • (1982) J. Cell Biol. , vol.93 , pp. 223-229
    • Roth, J.1    Berger, E.G.2
  • 17
    • 0028171413 scopus 로고
    • Expressing murine β1,4-galactosyltransferase in HeLa cells produces a cell surface galactosyltransferase-dependent phenotype
    • Nguyen T.T., Hinton D.A., Shur B.D. Expressing murine β1,4-galactosyltransferase in HeLa cells produces a cell surface galactosyltransferase-dependent phenotype. J. Biol. Chem. 269:1994;28000-28009.
    • (1994) J. Biol. Chem. , vol.269 , pp. 28000-28009
    • Nguyen, T.T.1    Hinton, D.A.2    Shur, B.D.3
  • 18
    • 0024297290 scopus 로고
    • Plasma membrane association, purification, and partial characterization of mouse sperm β1,4-galactosyltransferase
    • (published erratum appears in J. Biol. Chem. 1989 Mar 5;264(7):4264)
    • Shur B.D., Neely C.A. Plasma membrane association, purification, and partial characterization of mouse sperm β1,4-galactosyltransferase. (published erratum appears in J. Biol. Chem. 1989 Mar 5;264(7):4264) J. Biol. Chem. 263:1988;17706-17714.
    • (1988) J. Biol. Chem. , vol.263 , pp. 17706-17714
    • Shur, B.D.1    Neely, C.A.2
  • 19
    • 0026677271 scopus 로고
    • Immunocytochemical localization of β1,4galactosyltransferase in epithelial cells from bovine tissues using monoclonal antibodies
    • Taatjes D.J., Roth J., Shaper N.L., Shaper J.H. Immunocytochemical localization of β1,4galactosyltransferase in epithelial cells from bovine tissues using monoclonal antibodies. Glycobiology. 2:1992;579-589.
    • (1992) Glycobiology , vol.2 , pp. 579-589
    • Taatjes, D.J.1    Roth, J.2    Shaper, N.L.3    Shaper, J.H.4
  • 20
    • 0025981404 scopus 로고
    • Subcellular localization of N-acetylglucosaminide β1,4-galactosyltransferase revealed by immunoelectron microscopy
    • Suganuma T., Muramatsu H., Muramatsu T., Ihida K., Kawano J., Murata F. Subcellular localization of N-acetylglucosaminide β1,4-galactosyltransferase revealed by immunoelectron microscopy. J. Histochem. Cytochem. 39:1991;299-309.
    • (1991) J. Histochem. Cytochem. , vol.39 , pp. 299-309
    • Suganuma, T.1    Muramatsu, H.2    Muramatsu, T.3    Ihida, K.4    Kawano, J.5    Murata, F.6
  • 21
    • 0028016498 scopus 로고
    • Overexpressing sperm surface β1,4-galactosyltransferase in transgenic mice affects multiple aspects of sperm-egg interactions
    • Youakim A., Hathaway H.J., Miller D.J., Gong X., Shur B.D. Overexpressing sperm surface β1,4-galactosyltransferase in transgenic mice affects multiple aspects of sperm-egg interactions. J. Cell Biol. 126:1994;1573-1583.
    • (1994) J. Cell Biol. , vol.126 , pp. 1573-1583
    • Youakim, A.1    Hathaway, H.J.2    Miller, D.J.3    Gong, X.4    Shur, B.D.5
  • 22
    • 0032545370 scopus 로고    scopus 로고
    • In vivo autopolysialylation and localization of the polysialyltransferases PST and STX
    • Close B.E., Colley K.J. In vivo autopolysialylation and localization of the polysialyltransferases PST and STX. J. Biol. Chem. 273:1998;34586-34593.
    • (1998) J. Biol. Chem. , vol.273 , pp. 34586-34593
    • Close, B.E.1    Colley, K.J.2
  • 23
    • 0035339119 scopus 로고    scopus 로고
    • Fucosyltransferase I and H-type complex carbohydrates modulate epithelial cell proliferation during prostatic branching morphogenesis
    • Marker P.C., Stephan J.P., Lee J., Bald L., Mather J.P., Cunha G.R. Fucosyltransferase I and H-type complex carbohydrates modulate epithelial cell proliferation during prostatic branching morphogenesis. Dev. Biol. 233:2001;95-108.
    • (2001) Dev. Biol. , vol.233 , pp. 95-108
    • Marker, P.C.1    Stephan, J.P.2    Lee, J.3    Bald, L.4    Mather, J.P.5    Cunha, G.R.6
  • 25
    • 0032939863 scopus 로고    scopus 로고
    • Expression of polypeptide GalNAc-transferases in stratified epithelia and squamous cell carcinomas: Immunohistological evaluation using monoclonal antibodies to three members of the GalNAc-transferase family
    • Mandel U., Hassan H., Therkildsen M.H., Rygaard J., Jakobsen M.H., Juhl B.R., Dabelsteen E., Clausen H. Expression of polypeptide GalNAc-transferases in stratified epithelia and squamous cell carcinomas: immunohistological evaluation using monoclonal antibodies to three members of the GalNAc-transferase family. Glycobiology. 9:1999;43-52.
    • (1999) Glycobiology , vol.9 , pp. 43-52
    • Mandel, U.1    Hassan, H.2    Therkildsen, M.H.3    Rygaard, J.4    Jakobsen, M.H.5    Juhl, B.R.6    Dabelsteen, E.7    Clausen, H.8
  • 26
    • 0027082203 scopus 로고
    • Cadherin-mediated adhesion in pancreatic islet cells is modulated by a cell surface N-acetylgalactosaminylphosphotransferase
    • Bauer G.E., Balsamo J., Lilien J. Cadherin-mediated adhesion in pancreatic islet cells is modulated by a cell surface N-acetylgalactosaminylphosphotransferase. J. Cell Sci. 103:1992;1235-1241.
    • (1992) J. Cell Sci. , vol.103 , pp. 1235-1241
    • Bauer, G.E.1    Balsamo, J.2    Lilien, J.3
  • 27
    • 0023713645 scopus 로고
    • Characterization of the full length cDNA for murine β1,4-galactosyltransferase: Novel features at the 5′-end predict two translation start sites at two in-frame AUGs
    • Shaper N.L., Hollis G.F., Douglas J.G., Kirsch I.R., Shaper J.H. Characterization of the full length cDNA for murine β1,4-galactosyltransferase: novel features at the 5′-end predict two translation start sites at two in-frame AUGs. J. Biol. Chem. 263:1988;10420-10428.
    • (1988) J. Biol. Chem. , vol.263 , pp. 10420-10428
    • Shaper, N.L.1    Hollis, G.F.2    Douglas, J.G.3    Kirsch, I.R.4    Shaper, J.H.5
  • 28
    • 0025254311 scopus 로고
    • Bovine β1,4-galactosyltransferase: Two sets of mRNA transcripts encode two forms of the protein with different amino-terminal domains: In vitro translation experiments demonstrate that both the short and the long forms of the enzyme are type II membrane-bound glycoproteins
    • Russo R.N., Shaper N.L., Shaper J.H. Bovine β1,4-galactosyltransferase: two sets of mRNA transcripts encode two forms of the protein with different amino-terminal domains: in vitro translation experiments demonstrate that both the short and the long forms of the enzyme are type II membrane-bound glycoproteins. J. Biol. Chem. 265:1990;3324-3331.
    • (1990) J. Biol. Chem. , vol.265 , pp. 3324-3331
    • Russo, R.N.1    Shaper, N.L.2    Shaper, J.H.3
  • 30
    • 0026687937 scopus 로고
    • Mammalian glycosyltransferases: Genomic organization and protein structure
    • Joziasse D.H. Mammalian glycosyltransferases: genomic organization and protein structure. Glycobiology. 2:1992;271-277.
    • (1992) Glycobiology , vol.2 , pp. 271-277
    • Joziasse, D.H.1
  • 31
    • 0027157541 scopus 로고
    • Characterization of two cis-regulatory regions in the murine β1,4-galactosyltransferase gene: Evidence for a negative regulatory element that controls initiation at the proximal site
    • Harduin-Lepers A., Shaper J.H., Shaper N.L. Characterization of two cis-regulatory regions in the murine β1,4-galactosyltransferase gene: evidence for a negative regulatory element that controls initiation at the proximal site. J. Biol. Chem. 268:1993;14348-14359.
    • (1993) J. Biol. Chem. , vol.268 , pp. 14348-14359
    • Harduin-Lepers, A.1    Shaper, J.H.2    Shaper, N.L.3
  • 32
    • 0029865115 scopus 로고    scopus 로고
    • Transcriptional regulation of murine β1,4-galactosyltransferase in somatic cells: Analysis of a gene that serves both a housekeeping and a mammary gland-specific function
    • Rajput B., Shaper N.L., Shaper J.H. Transcriptional regulation of murine β1,4-galactosyltransferase in somatic cells: analysis of a gene that serves both a housekeeping and a mammary gland-specific function. J. Biol. Chem. 271:1996;5131-5142.
    • (1996) J. Biol. Chem. , vol.271 , pp. 5131-5142
    • Rajput, B.1    Shaper, N.L.2    Shaper, J.H.3
  • 33
    • 0032217083 scopus 로고    scopus 로고
    • The increased level of β1,4-galactosyltransferase required for lactose biosynthesis is achieved in part by translational control
    • Charron M., Shaper J.H., Shaper N.L. The increased level of β1,4-galactosyltransferase required for lactose biosynthesis is achieved in part by translational control. Proc. Natl. Acad. Sci. U. S. A. 95:1998;14805-14810.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 14805-14810
    • Charron, M.1    Shaper, J.H.2    Shaper, N.L.3
  • 34
    • 0029257319 scopus 로고
    • Biological consequences of targeting β1,4-galactosyltransferase to two different subcellular compartments
    • Evans S.C., Youakim A., Shur B.D. Biological consequences of targeting β1,4-galactosyltransferase to two different subcellular compartments. BioEssays. 17:1995;261-268.
    • (1995) BioEssays , vol.17 , pp. 261-268
    • Evans, S.C.1    Youakim, A.2    Shur, B.D.3
  • 35
    • 0035094452 scopus 로고    scopus 로고
    • Cell surface β1,4-galactosyltransferase-I activates G-protein-dependent exocytotic signaling
    • Shi X., Amindari S., Paruchuru K., Skalla D., Burkin H., Shur B.D., Miller D.J. Cell surface β1,4-galactosyltransferase-I activates G-protein-dependent exocytotic signaling. Development. 128:2001;645-654.
    • (2001) Development , vol.128 , pp. 645-654
    • Shi, X.1    Amindari, S.2    Paruchuru, K.3    Skalla, D.4    Burkin, H.5    Shur, B.D.6    Miller, D.J.7
  • 36
    • 0030728461 scopus 로고    scopus 로고
    • Sperm from β1,4-galactosyltransferase-null mice are refractory to ZP3-induced acrosome reactions and penetrate the zona pellucida poorly
    • Lu Q., Shur B.D. Sperm from β1,4-galactosyltransferase-null mice are refractory to ZP3-induced acrosome reactions and penetrate the zona pellucida poorly. Development. 124:1997;4121-4131.
    • (1997) Development , vol.124 , pp. 4121-4131
    • Lu, Q.1    Shur, B.D.2
  • 37
    • 0026072695 scopus 로고
    • The membrane spanning domain of β1,4-galactosyltransferase specifies trans Golgi localization
    • Nilsson T., Lucocq J.M., Mackay D., Warren G. The membrane spanning domain of β1,4-galactosyltransferase specifies trans Golgi localization. EMBO J. 10:1991;3567-3575.
    • (1991) EMBO J. , vol.10 , pp. 3567-3575
    • Nilsson, T.1    Lucocq, J.M.2    Mackay, D.3    Warren, G.4
  • 38
    • 0026784536 scopus 로고
    • The signal for Golgi retention of bovine β1,4-galactosyltransferase is in the transmembrane domain
    • Teasdale R.D., D'Agostaro G., Gleeson P.A. The signal for Golgi retention of bovine β1,4-galactosyltransferase is in the transmembrane domain. J. Biol. Chem. 267:1992;4084-4096.
    • (1992) J. Biol. Chem. , vol.267 , pp. 4084-4096
    • Teasdale, R.D.1    D'Agostaro, G.2    Gleeson, P.A.3
  • 39
    • 0027172770 scopus 로고
    • Mutational analysis of the Golgi retention signal of bovine β1,4-galactosyltransferase
    • Masibay A.S., Balaji P.V., Boeggeman E.E., Qasba P.K. Mutational analysis of the Golgi retention signal of bovine β1,4-galactosyltransferase. J. Biol. Chem. 268:1993;9908-9916.
    • (1993) J. Biol. Chem. , vol.268 , pp. 9908-9916
    • Masibay, A.S.1    Balaji, P.V.2    Boeggeman, E.E.3    Qasba, P.K.4
  • 40
    • 0026793378 scopus 로고
    • β1,4-Galactosyltransferase: A short NH2-terminal fragment that includes the cytoplasmic and transmembrane domain is sufficient for Golgi retention
    • Russo R.N., Shaper N.L., Taatjes D.J., Shaper J.H. β1,4-Galactosyltransferase: a short NH2-terminal fragment that includes the cytoplasmic and transmembrane domain is sufficient for Golgi retention. J. Biol. Chem. 267:1992;9241-9247.
    • (1992) J. Biol. Chem. , vol.267 , pp. 9241-9247
    • Russo, R.N.1    Shaper, N.L.2    Taatjes, D.J.3    Shaper, J.H.4
  • 41
    • 0029067675 scopus 로고
    • Golgi retention mechanism of β1,4-galactosyltransferase. Membrane-spanning domain-dependent homodimerization and association with α- and β-tubulins
    • Yamaguchi N., Fukuda M.N. Golgi retention mechanism of β1,4-galactosyltransferase. Membrane-spanning domain-dependent homodimerization and association with α- and β-tubulins. J. Biol. Chem. 270:1995;12170-12176.
    • (1995) J. Biol. Chem. , vol.270 , pp. 12170-12176
    • Yamaguchi, N.1    Fukuda, M.N.2
  • 42
    • 0031040995 scopus 로고    scopus 로고
    • Golgi localization of glycosyltransferases: More questions than answers
    • Colley K.J. Golgi localization of glycosyltransferases: more questions than answers. Glycobiology. 7:1997;1-13.
    • (1997) Glycobiology , vol.7 , pp. 1-13
    • Colley, K.J.1
  • 44
    • 0031567823 scopus 로고    scopus 로고
    • Targeted mutation in β1,4-galactosyltransferase leads to pituitary insufficiency and neonatal lethality
    • Lu Q., Hasty P., Shur B.D. Targeted mutation in β1,4-galactosyltransferase leads to pituitary insufficiency and neonatal lethality. Dev. Biol. 181:1997;257-267.
    • (1997) Dev. Biol. , vol.181 , pp. 257-267
    • Lu, Q.1    Hasty, P.2    Shur, B.D.3
  • 45
    • 0030977266 scopus 로고    scopus 로고
    • Growth retardation and early death of β1,4-galactosyltransferase knockout mice with augmented proliferation and abnormal differentiation of epithelial cells
    • Asano M., Furukawa K., Kido M., Matsumoto S., Umesaki Y., Kochibe N., Iwakura Y. Growth retardation and early death of β1,4-galactosyltransferase knockout mice with augmented proliferation and abnormal differentiation of epithelial cells. EMBO J. 16:1997;1850-1857.
    • (1997) EMBO J. , vol.16 , pp. 1850-1857
    • Asano, M.1    Furukawa, K.2    Kido, M.3    Matsumoto, S.4    Umesaki, Y.5    Kochibe, N.6    Iwakura, Y.7
  • 46
    • 0032576979 scopus 로고    scopus 로고
    • Presence of polysialic acid and HNK-1 carbohydrate on brain glycoproteins from β1,4-galactosyltransferase-knockout mice
    • Kido M., Asano M., Iwakura Y., Ichinose M., Miki K., Furukawa K. Presence of polysialic acid and HNK-1 carbohydrate on brain glycoproteins from β1,4-galactosyltransferase-knockout mice. Biochem. Biophys. Res. Commun. 245:1998;860-864.
    • (1998) Biochem. Biophys. Res. Commun. , vol.245 , pp. 860-864
    • Kido, M.1    Asano, M.2    Iwakura, Y.3    Ichinose, M.4    Miki, K.5    Furukawa, K.6
  • 47
    • 0035158267 scopus 로고    scopus 로고
    • Differential gene expression of β1,4-galactosyltransferases I, II and V during mouse brain development
    • Nakamura N., Yamakawa N., Sato T., Tojo H., Tachi C., Furukawa K. Differential gene expression of β1,4-galactosyltransferases I, II and V during mouse brain development. J. Neurochem. 76:2001;29-38.
    • (2001) J. Neurochem. , vol.76 , pp. 29-38
    • Nakamura, N.1    Yamakawa, N.2    Sato, T.3    Tojo, H.4    Tachi, C.5    Furukawa, K.6
  • 48
    • 0033408505 scopus 로고    scopus 로고
    • Normal levels of serum glycoproteins maintained in β1,4-galactosyltransferase I-knockout mice
    • Kido M., Asano M., Iwakura Y., Ichinose M., Miki K., Furukawa K. Normal levels of serum glycoproteins maintained in β1,4-galactosyltransferase I-knockout mice. FEBS Lett. 464:1999;75-79.
    • (1999) FEBS Lett. , vol.464 , pp. 75-79
    • Kido, M.1    Asano, M.2    Iwakura, Y.3    Ichinose, M.4    Miki, K.5    Furukawa, K.6
  • 49
    • 0032881550 scopus 로고    scopus 로고
    • Glycosylation and rheumatic disease
    • Axford J.S. Glycosylation and rheumatic disease. Biochim. Biophys. Acta. 1455:1999;219-229.
    • (1999) Biochim. Biophys. Acta , vol.1455 , pp. 219-229
    • Axford, J.S.1
  • 50
    • 0027531961 scopus 로고
    • Immunoglobulin heavy chain constant region determines the pathogenicity and the antigen-binding activity of rheumatoid factor
    • Fulpius T., Spertini F., Reininger L., Izui S. Immunoglobulin heavy chain constant region determines the pathogenicity and the antigen-binding activity of rheumatoid factor. Proc. Natl. Acad. Sci. U. S. A. 90:1993;2345-2349.
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 2345-2349
    • Fulpius, T.1    Spertini, F.2    Reininger, L.3    Izui, S.4
  • 51
    • 0033600155 scopus 로고    scopus 로고
    • Impaired glactosylation of core 2 O-glycans in erythrocytes of β1,4-galactosyltransferase knockout mice
    • Kotani N., Asano M., Iwakura Y., Takasaki S. Impaired glactosylation of core 2 O-glycans in erythrocytes of β1,4-galactosyltransferase knockout mice. Biochem. Biophys. Res. Commun. 260:1999;94-98.
    • (1999) Biochem. Biophys. Res. Commun. , vol.260 , pp. 94-98
    • Kotani, N.1    Asano, M.2    Iwakura, Y.3    Takasaki, S.4
  • 52
    • 0024282581 scopus 로고
    • Pituitary glycoprotein hormone oligosaccharides: Structure, synthesis and function of the asparagine-linked oligosaccharides on lutropin, follitropin and thyrotropin
    • Baenziger J.U., Green E.D. Pituitary glycoprotein hormone oligosaccharides: structure, synthesis and function of the asparagine-linked oligosaccharides on lutropin, follitropin and thyrotropin. Biochim. Biophys. Acta. 947:1988;287-306.
    • (1988) Biochim. Biophys. Acta , vol.947 , pp. 287-306
    • Baenziger, J.U.1    Green, E.D.2
  • 53
    • 0028890259 scopus 로고
    • Glycoprotein hormones: Glycobiology of gonadotrophins, thyrotrophin and free alpha subunit
    • Thotakura N.R., Blithe D.L. Glycoprotein hormones: glycobiology of gonadotrophins, thyrotrophin and free alpha subunit. Glycobiology. 5:1995;3-10.
    • (1995) Glycobiology , vol.5 , pp. 3-10
    • Thotakura, N.R.1    Blithe, D.L.2
  • 54
    • 0036535136 scopus 로고    scopus 로고
    • Enhanced branching morphogenesis in mammary glands of mice lacking cell surface β1,4-galactosyltransferase
    • Steffgen K., Dufraux K., Hathaway H. Enhanced branching morphogenesis in mammary glands of mice lacking cell surface β1,4-galactosyltransferase. Dev. Biol. 224:2002;114-133.
    • (2002) Dev. Biol. , vol.224 , pp. 114-133
    • Steffgen, K.1    Dufraux, K.2    Hathaway, H.3
  • 55
    • 0018831516 scopus 로고
    • Mammalian sperm-egg interaction: Identification of a glycoprotein in mouse egg zonae pellucidae possessing receptor activity for sperm
    • Bleil J.D., Wassarman P.M. Mammalian sperm-egg interaction: identification of a glycoprotein in mouse egg zonae pellucidae possessing receptor activity for sperm. Cell. 20:1980;873-882.
    • (1980) Cell , vol.20 , pp. 873-882
    • Bleil, J.D.1    Wassarman, P.M.2
  • 56
    • 0021874149 scopus 로고
    • O-linked oligosaccharides of mouse egg ZP3 account for its sperm receptor activity
    • Florman H.M., Wassarman P.M. O-linked oligosaccharides of mouse egg ZP3 account for its sperm receptor activity. Cell. 41:1985;313-324.
    • (1985) Cell , vol.41 , pp. 313-324
    • Florman, H.M.1    Wassarman, P.M.2
  • 57
    • 0022351299 scopus 로고
    • Receptor function of mouse sperm surface galactosyltransferase during fertilization
    • Lopez L.C., Bayna E.M., Litoff D., Shaper N.L., Shaper J.H., Shur B.D. Receptor function of mouse sperm surface galactosyltransferase during fertilization. J. Cell Biol. 101:1985;1501-1510.
    • (1985) J. Cell Biol. , vol.101 , pp. 1501-1510
    • Lopez, L.C.1    Bayna, E.M.2    Litoff, D.3    Shaper, N.L.4    Shaper, J.H.5    Shur, B.D.6
  • 58
    • 0023445560 scopus 로고
    • Spatial and temporal expression of cell surface galactosyltransferase during mouse spermatogenesis and epididymal maturation
    • Scully N.F., Shaper J.H., Shur B.D. Spatial and temporal expression of cell surface galactosyltransferase during mouse spermatogenesis and epididymal maturation. Dev. Biol. 124:1987;111-124.
    • (1987) Dev. Biol. , vol.124 , pp. 111-124
    • Scully, N.F.1    Shaper, J.H.2    Shur, B.D.3
  • 59
    • 0020410869 scopus 로고
    • A role for mouse sperm surface galactosyltransferase in sperm binding to the egg zona pellucida
    • Shur B.D., Hall N.G. A role for mouse sperm surface galactosyltransferase in sperm binding to the egg zona pellucida. J. Cell Biol. 95:1982;574-579.
    • (1982) J. Cell Biol. , vol.95 , pp. 574-579
    • Shur, B.D.1    Hall, N.G.2
  • 60
    • 0026611050 scopus 로고
    • Complementarity between sperm surface β1,4-galactosyltransferase and egg-coat ZP3 mediates sperm-egg binding
    • Miller D.J., Macek M.B., Shur B.D. Complementarity between sperm surface β1,4-galactosyltransferase and egg-coat ZP3 mediates sperm-egg binding. Nature. 357:1992;589-593.
    • (1992) Nature , vol.357 , pp. 589-593
    • Miller, D.J.1    Macek, M.B.2    Shur, B.D.3
  • 61
    • 0026052068 scopus 로고
    • Aggregation of β1,4-galactosyltransferase on mouse sperm induces the acrosome reaction
    • Macek M.B., Lopez L.C., Shur B.D. Aggregation of β1,4-galactosyltransferase on mouse sperm induces the acrosome reaction. Dev. Biol. 147:1991;440-444.
    • (1991) Dev. Biol. , vol.147 , pp. 440-444
    • Macek, M.B.1    Lopez, L.C.2    Shur, B.D.3
  • 62
    • 0029094342 scopus 로고
    • Activation of a G protein complex by aggregation of β1,4-galactosyltransferase on the surface of sperm
    • Gong X., Dubois D.H., Miller D.J., Shur B.D. Activation of a G protein complex by aggregation of β1,4-galactosyltransferase on the surface of sperm. Science. 269:1995;1718-1721.
    • (1995) Science , vol.269 , pp. 1718-1721
    • Gong, X.1    Dubois, D.H.2    Miller, D.J.3    Shur, B.D.4
  • 63
    • 0026078645 scopus 로고
    • Galactosyltransferase activity is restricted to the plasma membranes of equine and bovine sperm
    • Fayrer-Hosken R.A., Caudle A.B., Shur B.D. Galactosyltransferase activity is restricted to the plasma membranes of equine and bovine sperm. Mol. Reprod. Dev. 28:1991;74-78.
    • (1991) Mol. Reprod. Dev. , vol.28 , pp. 74-78
    • Fayrer-Hosken, R.A.1    Caudle, A.B.2    Shur, B.D.3
  • 64
    • 0030759615 scopus 로고    scopus 로고
    • Sperm from a variety of mammalian species express β1,4-galactosyltransferase on their surface
    • Larson J.L., Miller D.J. Sperm from a variety of mammalian species express β1,4-galactosyltransferase on their surface. Biol. Reprod. 57:1997;442-453.
    • (1997) Biol. Reprod. , vol.57 , pp. 442-453
    • Larson, J.L.1    Miller, D.J.2
  • 65
    • 0030978645 scopus 로고    scopus 로고
    • Sperm plasma membrane remodeling during spermiogenetic maturation in men: Relationship among plasma membrane β1,4-galactosyltransferase, cytoplasmic creatine phosphokinase, and creatine phosphokinase isoform ratios
    • Huszar G., Sbracia M., Vigue L., Miller D.J., Shur B.D. Sperm plasma membrane remodeling during spermiogenetic maturation in men: relationship among plasma membrane β1,4-galactosyltransferase, cytoplasmic creatine phosphokinase, and creatine phosphokinase isoform ratios. Biol. Reprod. 56:1997;1020-1024.
    • (1997) Biol. Reprod. , vol.56 , pp. 1020-1024
    • Huszar, G.1    Sbracia, M.2    Vigue, L.3    Miller, D.J.4    Shur, B.D.5
  • 66
    • 0034746758 scopus 로고    scopus 로고
    • Subcellular localization of β1,4-galactosyltransferase on bull sperm and its function during sperm-egg interactions
    • Tengowski M.W., Wassler M.J., Shur B.D., Schatten G. Subcellular localization of β1,4-galactosyltransferase on bull sperm and its function during sperm-egg interactions. Mol. Reprod. Dev. 58:2001;236-244.
    • (2001) Mol. Reprod. Dev. , vol.58 , pp. 236-244
    • Tengowski, M.W.1    Wassler, M.J.2    Shur, B.D.3    Schatten, G.4
  • 67
    • 0026445723 scopus 로고
    • Selectins: Interpreters of cell-specific carbohydrate information during inflammation
    • Lasky L.A. Selectins: interpreters of cell-specific carbohydrate information during inflammation. Science. 258:1992;964-969.
    • (1992) Science , vol.258 , pp. 964-969
    • Lasky, L.A.1
  • 68
    • 0014251737 scopus 로고
    • The role of α-lactalbumin and the A protein in lactose synthetase: A unique mechanism for the control of a biological reaction
    • Brew K., Vanaman T.C., Hill R.L. The role of α-lactalbumin and the A protein in lactose synthetase: a unique mechanism for the control of a biological reaction. Proc. Natl. Acad. Sci. U. S. A. 59:1968;491-497.
    • (1968) Proc. Natl. Acad. Sci. U. S. A. , vol.59 , pp. 491-497
    • Brew, K.1    Vanaman, T.C.2    Hill, R.L.3
  • 69
    • 0035863007 scopus 로고    scopus 로고
    • Postnatal mammary gland morphogenesis
    • Silberstein G.B. Postnatal mammary gland morphogenesis. Microsc. Res. Tech. 52:2001;155-162.
    • (2001) Microsc. Res. Tech. , vol.52 , pp. 155-162
    • Silberstein, G.B.1
  • 70
    • 0029835647 scopus 로고    scopus 로고
    • Mammary gland morphogenesis is inhibited in transgenic mice that overexpress cell surface β1,4-galactosyltransferase
    • Hathaway H.J., Shur B.D. Mammary gland morphogenesis is inhibited in transgenic mice that overexpress cell surface β1,4-galactosyltransferase. Development. 122:1996;2859-2872.
    • (1996) Development , vol.122 , pp. 2859-2872
    • Hathaway, H.J.1    Shur, B.D.2
  • 71
    • 0026632465 scopus 로고
    • Mammary epithelial reorganization on extracellular matrix is mediated by cell surface galactosyltransferase
    • Barcellos-Hoff M.H. Mammary epithelial reorganization on extracellular matrix is mediated by cell surface galactosyltransferase. Exp. Cell Res. 201:1992;225-234.
    • (1992) Exp. Cell Res. , vol.201 , pp. 225-234
    • Barcellos-Hoff, M.H.1
  • 72
    • 0031777054 scopus 로고    scopus 로고
    • The expanding β1,4-galactosyltransferase gene family: Messages from the databanks
    • Lo N.W., Shaper J.H., Pevsner J., Shaper N.L. The expanding β1,4-galactosyltransferase gene family: messages from the databanks. Glycobiology. 8:1998;517-526.
    • (1998) Glycobiology , vol.8 , pp. 517-526
    • Lo, N.W.1    Shaper, J.H.2    Pevsner, J.3    Shaper, N.L.4
  • 73
    • 0031930477 scopus 로고    scopus 로고
    • Molecular cloning of a human cDNA encoding β1,4-galactosyltransferase with 37% identity to mammalian UDP-Gal:GlcNAc β1,4-galactosyltransferase
    • Sato T., Furukawa K., Bakker H., Van den Eijnden D.H., Van Die I. Molecular cloning of a human cDNA encoding β1,4-galactosyltransferase with 37% identity to mammalian UDP-Gal:GlcNAc β1,4-galactosyltransferase. Proc. Natl. Acad. Sci. U. S. A. 95:1998;472-477.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 472-477
    • Sato, T.1    Furukawa, K.2    Bakker, H.3    Van den Eijnden, D.H.4    Van Die, I.5
  • 74
    • 0344706380 scopus 로고    scopus 로고
    • A family of β4-galactosyltransferases: Cloning and expression of two novel UDP-galactose:β-N-acetylglucosamine β1,4-galactosyltransferases, β4GalT2 and β4GalT3
    • Almeida R., Amado M., David L., Levery S.B., Holmes E.H., Merkx G., van Kessel A.G., Rygaard E., Hassan H., Bennett E., Clausen H. A family of β4-galactosyltransferases: cloning and expression of two novel UDP-galactose:β-N-acetylglucosamine β1,4-galactosyltransferases, β4GalT2 and β4GalT3. J. Biol. Chem. 272:1997;31979-31991.
    • (1997) J. Biol. Chem. , vol.272 , pp. 31979-31991
    • Almeida, R.1    Amado, M.2    David, L.3    Levery, S.B.4    Holmes, E.H.5    Merkx, G.6    Van Kessel, A.G.7    Rygaard, E.8    Hassan, H.9    Bennett, E.10    Clausen, H.11
  • 75
    • 0032759101 scopus 로고    scopus 로고
    • Identification and characterization of large galactosyltransferase gene families: Galactosyltransferases for all functions
    • Amado M., Almeida R., Schwientek T., Clausen H. Identification and characterization of large galactosyltransferase gene families: galactosyltransferases for all functions. Biochim. Biophys. Acta. 1473:1999;35-53.
    • (1999) Biochim. Biophys. Acta , vol.1473 , pp. 35-53
    • Amado, M.1    Almeida, R.2    Schwientek, T.3    Clausen, H.4
  • 76
    • 0032739349 scopus 로고    scopus 로고
    • β1,4-galactosylation of N-glycans is a complex process
    • Furukawa K., Sato T. β1,4-galactosylation of N-glycans is a complex process. Biochim. Biophys. Acta. 1473:1999;54-66.
    • (1999) Biochim. Biophys. Acta , vol.1473 , pp. 54-66
    • Furukawa, K.1    Sato, T.2
  • 77
    • 0034768391 scopus 로고    scopus 로고
    • Galactosylation of N-linked oligosaccharides by human β1,4-galactosyltransferases I, II, II, IV, V and VI expressed in Sf-9 cells
    • Guo S., Sato T., Shirane K., Furukawa K. Galactosylation of N-linked oligosaccharides by human β1,4-galactosyltransferases I, II, II, IV, V and VI expressed in Sf-9 cells. Glycobiology. 11:2001;813-820.
    • (2001) Glycobiology , vol.11 , pp. 813-820
    • Guo, S.1    Sato, T.2    Shirane, K.3    Furukawa, K.4
  • 78
    • 0027738464 scopus 로고
    • The MyoD family and myogenesis: Redundancy, networks, and thresholds
    • Weintraub H. The MyoD family and myogenesis: redundancy, networks, and thresholds. Cell. 75:1993;1241-1244.
    • (1993) Cell , vol.75 , pp. 1241-1244
    • Weintraub, H.1
  • 79
    • 0029894277 scopus 로고    scopus 로고
    • Deletion of integrin α1 by homologous recombination permits normal murine development but gives rise to a specific deficit in cell adhesion
    • Gardner H., Kreidberg J., Koteliansky V., Jaenisch R. Deletion of integrin α1 by homologous recombination permits normal murine development but gives rise to a specific deficit in cell adhesion. Dev. Biol. 175:1996;301-313.
    • (1996) Dev. Biol. , vol.175 , pp. 301-313
    • Gardner, H.1    Kreidberg, J.2    Koteliansky, V.3    Jaenisch, R.4
  • 80
    • 0033593481 scopus 로고    scopus 로고
    • Normal development of mice and unimpaired cell adhesion/cell motility/actin-based cytoskeleton without compensatory upregulation of ezrin or radixin in moesin gene knockout
    • Doi Y., Itoh M., Yonemura S., Ishihara S., Takano H., Noda T., Tsukita S. Normal development of mice and unimpaired cell adhesion/cell motility/actin-based cytoskeleton without compensatory upregulation of ezrin or radixin in moesin gene knockout. J. Biol. Chem. 274:1999;2315-2321.
    • (1999) J. Biol. Chem. , vol.274 , pp. 2315-2321
    • Doi, Y.1    Itoh, M.2    Yonemura, S.3    Ishihara, S.4    Takano, H.5    Noda, T.6    Tsukita, S.7
  • 84
    • 0035923524 scopus 로고    scopus 로고
    • Fringe modulation of Jagged1-induced Notch signaling requires the action of β4galactosyltransferase-1
    • Chen J., Moloney D.J., Stanley P. Fringe modulation of Jagged1-induced Notch signaling requires the action of β4galactosyltransferase-1. Proc. Natl. Acad. Sci. U. S. A. 98:2001;13716-13721.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 13716-13721
    • Chen, J.1    Moloney, D.J.2    Stanley, P.3


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