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Volumn 1473, Issue 1, 1999, Pages 35-53

Identification and characterization of large galactosyltransferase gene families: Galactosyltransferases for all functions

Author keywords

Chromosome; Enzym e; Galactosyltransferase; Gene; Glycosylation; Glycosyltransferase

Indexed keywords

GALACTOSYLTRANSFERASE; GLYCOSYLTRANSFERASE;

EID: 0032759101     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0304-4165(99)00168-3     Document Type: Review
Times cited : (274)

References (112)
  • 1
    • 0345009059 scopus 로고
    • Bovine galactosyltransferase: Identification of a clone by direct immunological screening of a cDNA expression library
    • Shaper N.L., Shaper J.H., Meuth J.L., Fox J.L., Chang H., Kirsch I.R., Hollis G.F. Bovine galactosyltransferase: identification of a clone by direct immunological screening of a cDNA expression library. Proc. Natl. Acad. Sci. USA. 83:1986;1573-1577.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 1573-1577
    • Shaper, N.L.1    Shaper, J.H.2    Meuth, J.L.3    Fox, J.L.4    Chang, H.5    Kirsch, I.R.6    Hollis, G.F.7
  • 2
    • 0022542290 scopus 로고
    • Cloning and sequencing of cDNA of bovine N-acetylglucosamine (β1-4)galactosyltransferase
    • Narimatsu H., Sinha S., Brew K., Okayama H., Qasba P.K. Cloning and sequencing of cDNA of bovine N-acetylglucosamine (β1-4)galactosyltransferase. Proc. Natl. Acad. Sci. USA. 83:1986;4720-4724.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 4720-4724
    • Narimatsu, H.1    Sinha, S.2    Brew, K.3    Okayama, H.4    Qasba, P.K.5
  • 3
    • 0024312590 scopus 로고
    • Cloning of cDNA encoding the membrane-bound form of bovine β1,4-galactosyltransferase
    • D'Agostaro G., Bendiak B., Tropak M. Cloning of cDNA encoding the membrane-bound form of bovine β1,4-galactosyltransferase. Eur. J. Biochem. 183:1989;211-217.
    • (1989) Eur. J. Biochem. , vol.183 , pp. 211-217
    • D'Agostaro, G.1    Bendiak, B.2    Tropak, M.3
  • 4
    • 0023713645 scopus 로고
    • Characterization of the full length cDNA for murine β-1,4- galactosyltransferase. Novel features at the 5′-end predict two translational 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 β-1,4- galactosyltransferase. Novel features at the 5′-end predict two translational 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
  • 5
    • 0024431691 scopus 로고
    • Glycosyltransferases. Structure, localization, and control of cell type-specific glycosylation
    • Paulson J.C., Colley K.J. Glycosyltransferases. Structure, localization, and control of cell type-specific glycosylation. J. Biol. Chem. 264:1989;17615-17618.
    • (1989) J. Biol. Chem. , vol.264 , pp. 17615-17618
    • Paulson, J.C.1    Colley, K.J.2
  • 7
    • 0023623637 scopus 로고
    • Primary structure of β-galactoside α2,6- sialyltransferase. Conversion of membrane-bound enzyme to soluble forms by cleavage of the NH2-terminal signal anchor
    • Weinstein J., Lee E.U., McEntee K., Lai P.H., Paulson J.C. Primary structure of β-galactoside α2,6- sialyltransferase. Conversion of membrane-bound enzyme to soluble forms by cleavage of the NH2-terminal signal anchor. J. Biol. Chem. 262:1987;17735-17743.
    • (1987) J. Biol. Chem. , vol.262 , pp. 17735-17743
    • Weinstein, J.1    Lee, E.U.2    McEntee, K.3    Lai, P.H.4    Paulson, J.C.5
  • 8
    • 0025101066 scopus 로고
    • Cloning and characterization of DNA complementary to human UDP-GalNAc:Fuc α1-2Gal α1-3GalNAc transferase (histo-blood group A transferase) mRNA
    • Yamamoto F., Marken J., Tsuji T., White T., Clausen H., Hakomori S. Cloning and characterization of DNA complementary to human UDP-GalNAc:Fuc α1-2Gal α1-3GalNAc transferase (histo-blood group A transferase) mRNA. J. Biol. Chem. 265:1990;1146-1151.
    • (1990) J. Biol. Chem. , vol.265 , pp. 1146-1151
    • Yamamoto, F.1    Marken, J.2    Tsuji, T.3    White, T.4    Clausen, H.5    Hakomori, S.6
  • 9
    • 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-acetylglucosaminyltransferase I
    • Sarkar M., Hull E., Nishikawa Y., Simpson R.J., Moritz R.L., Dunn R., Schachter H. 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-acetylglucosaminyltransferase I. Proc. Natl. Acad. Sci. USA. 88:1991;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    Schachter, H.7
  • 10
    • 0024310039 scopus 로고
    • Bovine α1-3-galactosyltransferase: Isolation and characterization of a cDNA clone. Identification of homologous sequences in human genomic DNA
    • Joziasse D.H., Shaper J.H., Van den Eijnden D.H., Van Tunen A.J., Shaper N.L. Bovine α1-3-galactosyltransferase: isolation and characterization of a cDNA clone. Identification of homologous sequences in human genomic DNA. J. Biol. Chem. 264:1989;14290-14297.
    • (1989) J. Biol. Chem. , vol.264 , pp. 14290-14297
    • Joziasse, D.H.1    Shaper, J.H.2    Van Den Eijnden, D.H.3    Van Tunen, A.J.4    Shaper, N.L.5
  • 11
    • 0025017434 scopus 로고
    • Isolation to homogeneity and partial characterization of a histo-blood group A defined Fucα1-2Gal α1-3-N-acetylgalactosaminyltransferase from human lung tissue
    • Clausen H., White T., Takio K., Titani K., Stroud M., Holmes E., Karkov J., Thim L., Hakomori S. Isolation to homogeneity and partial characterization of a histo-blood group A defined Fucα1-2Gal α1-3-N-acetylgalactosaminyltransferase from human lung tissue. J. Biol. Chem. 265:1990;1139-1145.
    • (1990) J. Biol. Chem. , vol.265 , pp. 1139-1145
    • Clausen, H.1    White, T.2    Takio, K.3    Titani, K.4    Stroud, M.5    Holmes, E.6    Karkov, J.7    Thim, L.8    Hakomori, S.9
  • 12
    • 0024593480 scopus 로고
    • Stable expression of blood group H determinants and GDP-L-fucose:β-D-galactoside 2-α-L-fucosyltransferase in mouse cells after transfection with human DNA
    • Ernst L.K., Rajan V.P., Larsen R.D., Ruff M.M., Lowe J.B. Stable expression of blood group H determinants and GDP-L-fucose:β-D-galactoside 2-α-L-fucosyltransferase in mouse cells after transfection with human DNA. J. Biol. Chem. 264:1989;3436-3447.
    • (1989) J. Biol. Chem. , vol.264 , pp. 3436-3447
    • Ernst, L.K.1    Rajan, V.P.2    Larsen, R.D.3    Ruff, M.M.4    Lowe, J.B.5
  • 13
    • 0024375016 scopus 로고
    • A cloned human DNA restriction fragment determines expression of a GDP-L-fucose:β-D-galactoside 2-α-L-fucosyltransferase in transfected cells. Evidence for isolation and transfer of the human H blood group locus
    • Rajan V.P., Larsen R.D., Ajmera S., Ernst L.K., Lowe J.B. A cloned human DNA restriction fragment determines expression of a GDP-L-fucose:β-D-galactoside 2-α-L-fucosyltransferase in transfected cells. Evidence for isolation and transfer of the human H blood group locus. J. Biol. Chem. 264:1989;11158-11167.
    • (1989) J. Biol. Chem. , vol.264 , pp. 11158-11167
    • Rajan, V.P.1    Larsen, R.D.2    Ajmera, S.3    Ernst, L.K.4    Lowe, J.B.5
  • 14
    • 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., Stanley P. Cloning and expression of N-acetylglucosaminyltransferase I, the medial Golgi transferase that initiates complex N-linked carbohydrate formation. Proc. Natl. Acad. Sci. USA. 87:1990;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
  • 15
    • 0028041217 scopus 로고
    • Expression of a differentiation antigen and poly-N- acetyllactosaminyl O-glycans directed by a cloned core 2 β-1,6-N-acetylglucosaminyltransferase
    • Bierhuizen M.F., Maemura K., Fukuda M. Expression of a differentiation antigen and poly-N- acetyllactosaminyl O-glycans directed by a cloned core 2 β-1,6-N-acetylglucosaminyltransferase. J. Biol. Chem. 269:1994;4473-4479.
    • (1994) J. Biol. Chem. , vol.269 , pp. 4473-4479
    • Bierhuizen, M.F.1    Maemura, K.2    Fukuda, M.3
  • 16
    • 0031445110 scopus 로고    scopus 로고
    • Expression cloning of cDNA encoding a human β-1,3-N-acetylglucosaminyltransferase that is essential for poly-N-acetyllactosamine synthesis
    • Sasaki K., Kurata-Miura K., Ujita M., Angata K., Nakagawa S., Sekine S., Nishi T., Fukuda M. Expression cloning of cDNA encoding a human β-1,3-N-acetylglucosaminyltransferase that is essential for poly-N-acetyllactosamine synthesis. Proc. Natl. Acad. Sci. USA. 94:1997;14294-14299.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 14294-14299
    • Sasaki, K.1    Kurata-Miura, K.2    Ujita, M.3    Angata, K.4    Nakagawa, S.5    Sekine, S.6    Nishi, T.7    Fukuda, M.8
  • 17
    • 0026759584 scopus 로고
    • Isolation of a novel human α(1,3)fucosyltransferase gene and molecular comparison to the human Lewis blood group b (1,3/1,4)fucosyltransferase gene. Syntenic, homologous, nonallelic genes encoding enzymes with distinct acceptor substrate specificities
    • Weston B.W., Nair R.P., Larsen R.D., Lowe J.B. Isolation of a novel human α(1,3)fucosyltransferase gene and molecular comparison to the human Lewis blood group b (1,3/1,4)fucosyltransferase gene. Syntenic, homologous, nonallelic genes encoding enzymes with distinct acceptor substrate specificities. J. Biol. Chem. 267:1992;4152-4160.
    • (1992) J. Biol. Chem. , vol.267 , pp. 4152-4160
    • Weston, B.W.1    Nair, R.P.2    Larsen, R.D.3    Lowe, J.B.4
  • 18
    • 0025955701 scopus 로고
    • Molecular cloning of a human fucosyltransferase gene that determines expression of the Lewis x and VIM-2 epitopes but not ELAM-1-dependent cell adhesion
    • Lowe J.B., Kukowska-Latallo J.F., Nair R.P., Larsen R.D., Marks R.M., Macher B.A., Kelly R.J., Ernst L.K. Molecular cloning of a human fucosyltransferase gene that determines expression of the Lewis x and VIM-2 epitopes but not ELAM-1-dependent cell adhesion. J. Biol. Chem. 266:1991;17467-17477.
    • (1991) J. Biol. Chem. , vol.266 , pp. 17467-17477
    • Lowe, J.B.1    Kukowska-Latallo, J.F.2    Nair, R.P.3    Larsen, R.D.4    Marks, R.M.5    Macher, B.A.6    Kelly, R.J.7    Ernst, L.K.8
  • 20
    • 0028935724 scopus 로고
    • Molecular cloning of a human genomic region containing the H blood group α(1,2)fucosyltransferase gene and two H locus- related DNA restriction fragments. Isolation of a candidate for the human Secretor blood group locus
    • Rouquier S., Lowe J.B., Kelly R.J., Fertitta A.L., Lennon G.G., Giorgi D. Molecular cloning of a human genomic region containing the H blood group α(1,2)fucosyltransferase gene and two H locus- related DNA restriction fragments. Isolation of a candidate for the human Secretor blood group locus. J. Biol. Chem. 270:1995;4632-4639.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4632-4639
    • Rouquier, S.1    Lowe, J.B.2    Kelly, R.J.3    Fertitta, A.L.4    Lennon, G.G.5    Giorgi, D.6
  • 21
    • 0028965558 scopus 로고
    • Sequence and expression of a candidate for the human Secretor blood group α(1,2)fucosyltransferase gene (FUT2). Homozygosity for an enzyme-inactivating nonsense mutation commonly correlates with the non-secretor phenotype
    • Kelly R.J., Rouquier S., Giorgi D., Lennon G.G., Lowe J.B. Sequence and expression of a candidate for the human Secretor blood group α(1,2)fucosyltransferase gene (FUT2). Homozygosity for an enzyme-inactivating nonsense mutation commonly correlates with the non-secretor phenotype. J. Biol. Chem. 270:1995;4640-4649.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4640-4649
    • Kelly, R.J.1    Rouquier, S.2    Giorgi, D.3    Lennon, G.G.4    Lowe, J.B.5
  • 22
    • 0029874003 scopus 로고    scopus 로고
    • Organization of a human UDP-GalNAc:polypeptide, N- acetylgalactosaminyltransferase gene and a related processed pseudogene
    • Meurer J.A., Drong R.F., Homa F.L., Slightom J.L., Elhammer A.P. Organization of a human UDP-GalNAc:polypeptide, N- acetylgalactosaminyltransferase gene and a related processed pseudogene. Glycobiology. 6:1996;231-241.
    • (1996) Glycobiology , vol.6 , pp. 231-241
    • Meurer, J.A.1    Drong, R.F.2    Homa, F.L.3    Slightom, J.L.4    Elhammer, A.P.5
  • 23
    • 0028985664 scopus 로고
    • The sialyltransferase 'sialylmotif' participates in binding the donor substrate CMP-NeuAc
    • Datta A.K., Paulson J.C. The sialyltransferase 'sialylmotif' participates in binding the donor substrate CMP-NeuAc. J. Biol. Chem. 270:1995;1497-1500.
    • (1995) J. Biol. Chem. , vol.270 , pp. 1497-1500
    • Datta, A.K.1    Paulson, J.C.2
  • 24
    • 0027298677 scopus 로고
    • Polymerase chain reaction cloning of a developmentally regulated member of the sialyltransferase gene family
    • Livingston B.D., Paulson J.C. Polymerase chain reaction cloning of a developmentally regulated member of the sialyltransferase gene family. J. Biol. Chem. 268:1993;11504-11507.
    • (1993) J. Biol. Chem. , vol.268 , pp. 11504-11507
    • Livingston, B.D.1    Paulson, J.C.2
  • 25
    • 0029854379 scopus 로고    scopus 로고
    • Systematic nomenclature for sialyltransferases
    • Tsuji S., Datta A.K., Paulson J.C. Systematic nomenclature for sialyltransferases. Glycobiology. 6:1996;v-vii.
    • (1996) Glycobiology , vol.6
    • Tsuji, S.1    Datta, A.K.2    Paulson, J.C.3
  • 26
    • 0026666837 scopus 로고
    • Primary structure of Galβ1,3(4)GlcNAc α2,3- sialyltransferase determined by mass spectrometry sequence analysis and molecular cloning. Evidence for a protein motif in the sialyltransferase gene family
    • Wen D.X., Livingston B.D., Medzihradszky K.F., Kelm S., Burlingame A.L., Paulson J.C. Primary structure of Galβ1,3(4)GlcNAc α2,3- sialyltransferase determined by mass spectrometry sequence analysis and molecular cloning. Evidence for a protein motif in the sialyltransferase gene family. J. Biol. Chem. 267:1992;21011-21019.
    • (1992) J. Biol. Chem. , vol.267 , pp. 21011-21019
    • Wen, D.X.1    Livingston, B.D.2    Medzihradszky, K.F.3    Kelm, S.4    Burlingame, A.L.5    Paulson, J.C.6
  • 27
    • 0030035111 scopus 로고    scopus 로고
    • CDNA cloning and expression of a novel human UDP-N-acetyl-α-D-galactosamine. Polypeptide N-acetylgalactosaminyltransferase, GalNAc-T3
    • Bennett E.P., Hassan H., Clausen H. cDNA cloning and expression of a novel human UDP-N-acetyl-α-D-galactosamine. Polypeptide N-acetylgalactosaminyltransferase, GalNAc-T3. J. Biol. Chem. 271:1996;17006-17012.
    • (1996) J. Biol. Chem. , vol.271 , pp. 17006-17012
    • Bennett, E.P.1    Hassan, H.2    Clausen, H.3
  • 29
    • 0032538435 scopus 로고    scopus 로고
    • Cloning and expression of a novel, tissue specifically expressed member of the UDP-GalNAc:polypeptide n-acetylgalactosaminyltransferase family
    • Hagen T.K.G., Hagen F.K., Balys M.M., Beres T.M., Van Wuyckhuyse B., Tabak L.A. Cloning and expression of a novel, tissue specifically expressed member of the UDP-GalNAc:polypeptide n-acetylgalactosaminyltransferase family. J. Biol. Chem. 273:1998;27749-27754.
    • (1998) J. Biol. Chem. , vol.273 , pp. 27749-27754
    • Hagen, T.K.G.1    Hagen, F.K.2    Balys, M.M.3    Beres, T.M.4    Van Wuyckhuyse, B.5    Tabak, L.A.6
  • 31
    • 0029096634 scopus 로고
    • Toward a cDNA map of the human genome: Applications and statistics for multiple high-scoring segments in molecular sequences
    • Korenberg J.R., Chen X.N., Adams M.D., Venter J.C., Karlin S., Altschul S.F. Toward a cDNA map of the human genome: applications and statistics for multiple high-scoring segments in molecular sequences. Genomics. 29:1995;364-370.
    • (1995) Genomics , vol.29 , pp. 364-370
    • Korenberg, J.R.1    Chen, X.N.2    Adams, M.D.3    Venter, J.C.4    Karlin, S.5    Altschul, S.F.6
  • 35
    • 0029621863 scopus 로고
    • Cloning and sequence homology of a rat UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase
    • Hagen F.K., Gregoire C.A., Tabak L.A. Cloning and sequence homology of a rat UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase. Glycoconjugate J. 12:1995;901-909.
    • (1995) Glycoconjugate J. , vol.12 , pp. 901-909
    • Hagen, F.K.1    Gregoire, C.A.2    Tabak, L.A.3
  • 36
    • 0344706380 scopus 로고    scopus 로고
    • A Family of human β4-galactosyltransferases: Cloning and expression of two novel UDP-galactose:β-n-acetylglucosamine β1,4-galactosyltransferases, β4Gal-T2 and β4Gal-T3
    • Almeida R., Amado M., David L., Levery S.B., Holmes E.H., Merkx G., van Kessel A.G., Hassan H., Bennett E.P., Clausen H. A Family of human β4-galactosyltransferases: cloning and expression of two novel UDP-galactose:β-n-acetylglucosamine β1,4-galactosyltransferases, β4Gal-T2 and β4Gal-T3. J. Biol. Chem. 272:1997;31979-31992.
    • (1997) J. Biol. Chem. , vol.272 , pp. 31979-31992
    • 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    Hassan, H.8    Bennett, E.P.9    Clausen, H.10
  • 39
    • 0032491511 scopus 로고    scopus 로고
    • Cloning of a novel member of the UDP-galactose:β-N-acetylglucosamine β1,4-galactosyltransferase family, β4Gal-T4, involved in glycosphingolipid biosynthesis
    • Schwientek T., Almeida R., Levery S.B., Holmes E., Bennett E.P., Clausen H. Cloning of a novel member of the UDP-galactose:β-N-acetylglucosamine β1,4-galactosyltransferase family, β4Gal-T4, involved in glycosphingolipid biosynthesis. J. Biol. Chem. 273:1998;29295-29305.
    • (1998) J. Biol. Chem. , vol.273 , pp. 29295-29305
    • Schwientek, T.1    Almeida, R.2    Levery, S.B.3    Holmes, E.4    Bennett, E.P.5    Clausen, H.6
  • 40
    • 0033582478 scopus 로고    scopus 로고
    • Control of O-glycan branch formation. Molecular cloning of human cDNA encoding a novel β1,6-N-acetylglucosaminyltransferase forming core 2 and core 4
    • Schwientek T., Nomoto M., Levery S.B., Merkx G., van Kessel A.G., Bennett E.P., Hollingsworth M.A., Clausen H. Control of O-glycan branch formation. Molecular cloning of human cDNA encoding a novel β1,6-N-acetylglucosaminyltransferase forming core 2 and core 4. J. Biol. Chem. 274:1999;4504-4512.
    • (1999) J. Biol. Chem. , vol.274 , pp. 4504-4512
    • Schwientek, T.1    Nomoto, M.2    Levery, S.B.3    Merkx, G.4    Van Kessel, A.G.5    Bennett, E.P.6    Hollingsworth, M.A.7    Clausen, H.8
  • 41
    • 0033613934 scopus 로고    scopus 로고
    • Molecular cloning and expression of a novel β-1, 6-N-acetylglucosaminyltransferase that forms core 2, core 4, and I branches
    • Yeh J.C., Ong E., Fukuda M. Molecular cloning and expression of a novel β-1, 6-N-acetylglucosaminyltransferase that forms core 2, core 4, and I branches. J. Biol. Chem. 274:1999;3215-3221.
    • (1999) J. Biol. Chem. , vol.274 , pp. 3215-3221
    • Yeh, J.C.1    Ong, E.2    Fukuda, M.3
  • 42
    • 0033520457 scopus 로고    scopus 로고
    • Cloning and characterization of a close homologue of human UDP-N-acetyl-α-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase-T3, designated GalNAc-T6. Evidence for genetic but not functional redundancy
    • Bennett E.P., Hassan H., Mandel U., Hollingsworth M.A., Akisawa N., Ikematsu Y., Merkx G., van Kessel A.G., Olofsson S., Clausen H. Cloning and characterization of a close homologue of human UDP-N-acetyl-α-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase-T3, designated GalNAc-T6. Evidence for genetic but not functional redundancy. J. Biol. Chem. 274:1999;25362-25370.
    • (1999) J. Biol. Chem. , vol.274 , pp. 25362-25370
    • Bennett, E.P.1    Hassan, H.2    Mandel, U.3    Hollingsworth, M.A.4    Akisawa, N.5    Ikematsu, Y.6    Merkx, G.7    Van Kessel, A.G.8    Olofsson, S.9    Clausen, H.10
  • 43
    • 0033582505 scopus 로고    scopus 로고
    • Multiple isoforms of heparan sulfate D-glucosaminyl 3-O-sulfotransferase isolation, characterization, and expression of human cDNAs and identification of distinct genomic loci
    • Schworak N.W., Liu J., Petros L.M., Zhang L., Kobayashi M., Copeland N.G., Jenkins N.A., Rosenberg R.D. Multiple isoforms of heparan sulfate D-glucosaminyl 3-O-sulfotransferase isolation, characterization, and expression of human cDNAs and identification of distinct genomic loci. J. Biol. Chem. 274:1999;5170-5184.
    • (1999) J. Biol. Chem. , vol.274 , pp. 5170-5184
    • Schworak, N.W.1    Liu, J.2    Petros, L.M.3    Zhang, L.4    Kobayashi, M.5    Copeland, N.G.6    Jenkins, N.A.7    Rosenberg, R.D.8
  • 44
    • 0032478833 scopus 로고    scopus 로고
    • CDNA cloning and expression of a family of UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase sequence homologs from Caenorhabditis elegans
    • Hagen F.K., Nehrke K. cDNA cloning and expression of a family of UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase sequence homologs from Caenorhabditis elegans. J. Biol. Chem. 273:1998;8268-8277.
    • (1998) J. Biol. Chem. , vol.273 , pp. 8268-8277
    • Hagen, F.K.1    Nehrke, K.2
  • 45
    • 0032955846 scopus 로고    scopus 로고
    • Expression of three Caenorhabditis elegans N-acetylglucosaminyltransferase I genes during development
    • Chen S., Zhou S., Sarkar M., Spence A.M., Schachter H. Expression of three Caenorhabditis elegans N-acetylglucosaminyltransferase I genes during development. J. Biol. Chem. 274:1999;288-297.
    • (1999) J. Biol. Chem. , vol.274 , pp. 288-297
    • Chen, S.1    Zhou, S.2    Sarkar, M.3    Spence, A.M.4    Schachter, H.5
  • 46
    • 0030959555 scopus 로고    scopus 로고
    • Dynamic glycosylation of nuclear and cytosolic proteins. Cloning and characterization of a unique O-GlcNAc transferase with multiple tetratricopeptide repeats
    • Kreppel L.K., Blomberg M.A., Hart G.W. Dynamic glycosylation of nuclear and cytosolic proteins. Cloning and characterization of a unique O-GlcNAc transferase with multiple tetratricopeptide repeats. J. Biol. Chem. 272:1997;9308-9315.
    • (1997) J. Biol. Chem. , vol.272 , pp. 9308-9315
    • Kreppel, L.K.1    Blomberg, M.A.2    Hart, G.W.3
  • 48
    • 0031026624 scopus 로고    scopus 로고
    • Structures of sialylated O-linked oligosaccharides of bovine peripheral nerve α-dystroglycan. The role of a novel O-mannosyl-type oligosaccharide in the binding of α-dystroglycan with laminin
    • Chiba A., Matsumura K., Yamada H., Inazu T., Shimizu T., Kusunoki S., Kanazawa I., Kobata A., Endo T. Structures of sialylated O-linked oligosaccharides of bovine peripheral nerve α-dystroglycan. The role of a novel O-mannosyl-type oligosaccharide in the binding of α-dystroglycan with laminin. J. Biol. Chem. 272:1997;2156-2162.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2156-2162
    • Chiba, A.1    Matsumura, K.2    Yamada, H.3    Inazu, T.4    Shimizu, T.5    Kusunoki, S.6    Kanazawa, I.7    Kobata, A.8    Endo, T.9
  • 49
    • 0030851778 scopus 로고    scopus 로고
    • Lewis X biosynthesis in Helicobacter pylori. Molecular cloning of an α(1,3)-fucosyltransferase gene
    • Martin S.L., Edbrooke M.R., Hodgman T.C., Van den Eijnden D.H., Bird M.I. Lewis X biosynthesis in Helicobacter pylori. Molecular cloning of an α(1,3)-fucosyltransferase gene. J. Biol. Chem. 272:1997;21349-21356.
    • (1997) J. Biol. Chem. , vol.272 , pp. 21349-21356
    • Martin, S.L.1    Edbrooke, M.R.2    Hodgman, T.C.3    Van Den Eijnden, D.H.4    Bird, M.I.5
  • 50
    • 0031749203 scopus 로고    scopus 로고
    • Sequence-function relationships of prokaryotic and eukaryotic galactosyltransferases
    • Breton C., Bettler E., Joziasse D.H., Geremia R.A., Imberty A. Sequence-function relationships of prokaryotic and eukaryotic galactosyltransferases. J. Biochem. 123:1998;1000-1009.
    • (1998) J. Biochem. , vol.123 , pp. 1000-1009
    • Breton, C.1    Bettler, E.2    Joziasse, D.H.3    Geremia, R.A.4    Imberty, A.5
  • 51
    • 0027467841 scopus 로고
    • A conserved disulphide bond in sialyltransferases
    • Drickamer K. A conserved disulphide bond in sialyltransferases. Glycobiology. 3:1993;2-3.
    • (1993) Glycobiology , vol.3 , pp. 2-3
    • Drickamer, K.1
  • 52
    • 0029854393 scopus 로고    scopus 로고
    • A family of UDP-GalNAc:polypeptide N-acetylgalactosaminyl-transferases control the initiation of mucin-type O-linked glycosylation
    • Clausen H., Bennett E.P. A family of UDP-GalNAc:polypeptide N-acetylgalactosaminyl-transferases control the initiation of mucin-type O-linked glycosylation. Glycobiology. 6:1996;635-646.
    • (1996) Glycobiology , vol.6 , pp. 635-646
    • Clausen, H.1    Bennett, E.P.2
  • 53
    • 0033168184 scopus 로고    scopus 로고
    • Crystal structures of the bovine β4galactosyltransferase catalytic domain and its complex with uridine diphosphogalactose
    • Gastinel L.N., Cambillau C., Bourne Y. Crystal structures of the bovine β4galactosyltransferase 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
  • 54
    • 0032493440 scopus 로고    scopus 로고
    • Activity of the yeast MNN1 α-1,3-mannosyltransferase requires a motif conserved in many other families of glycosyltransferases
    • Wiggins C.A.R., Munro S. Activity of the yeast MNN1 α-1,3-mannosyltransferase requires a motif conserved in many other families of glycosyltransferases. Proc. Natl. Acad. Sci. USA. 95:1998;7945-7950.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 7945-7950
    • Wiggins, C.A.R.1    Munro, S.2
  • 55
    • 0031454414 scopus 로고    scopus 로고
    • The chicken genome contains two functional nonallelic β1,4-galactosyltransferase genes: Chromosomal assignment to syntenic regions tracks fate of the two gene lineages in the human genome
    • Shaper N.L., Meurer J.A., Joziasse D.H., Chou T.-D.D., Smith E.J., Schnaar R.A., Shaper J.H. The chicken genome contains two functional nonallelic β1,4-galactosyltransferase genes: chromosomal assignment to syntenic regions tracks fate of the two gene lineages in the human genome. J. Biol. Chem. 272:1997;31389-31399.
    • (1997) J. Biol. Chem. , vol.272 , pp. 31389-31399
    • Shaper, N.L.1    Meurer, J.A.2    Joziasse, D.H.3    Chou, T.-D.D.4    Smith, E.J.5    Schnaar, R.A.6    Shaper, J.H.7
  • 56
    • 0031469691 scopus 로고    scopus 로고
    • Identification of conserved amino acid motifs in members of the β1-4-galactosyltransferase gene family
    • Van Die I., Bakker H., Van den Eijnden D.H. Identification of conserved amino acid motifs in members of the β1-4-galactosyltransferase gene family. Glycobiology. 7:1997;v-ix.
    • (1997) Glycobiology , vol.7
    • Van Die, I.1    Bakker, H.2    Van Den Eijnden, D.H.3
  • 57
    • 0031777054 scopus 로고    scopus 로고
    • The expanding β4-galactosyltransferase gene family: Messages from the databanks
    • Lo N.-W., Shaper J.H., Pevsner J., Shaper N.L. The expanding β4-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
  • 58
    • 0031930477 scopus 로고    scopus 로고
    • Molecular cloning of a human cDNA encoding a novel β-1,4-galactosyltransferase with 37% identity to the mammalian UDP-Gal:GlcNAc β-1,4-galactosyltransferase
    • Sato T., Furukawa K., Bakker H., Van den Eijnden D.H., Van Die I. Molecular cloning of a human cDNA encoding a novel β-1,4-galactosyltransferase with 37% identity to the mammalian UDP-Gal:GlcNAc β-1,4-galactosyltransferase. Proc. Natl. Acad. Sci. USA. 95:1998;472-477.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 472-477
    • Sato, T.1    Furukawa, K.2    Bakker, H.3    Van Den Eijnden, D.H.4    Van Die, I.5
  • 60
    • 0033551690 scopus 로고    scopus 로고
    • Human homolog of Caenorhabditis elegans sqv-3 gene is galactosyltransferase I involved in the biosynthesis of the glycosaminoglycan-protein linkage region of proteoglycans
    • Okajima T., Yoshida K., Kondo T., Furukawa K. Human homolog of Caenorhabditis elegans sqv-3 gene is galactosyltransferase I involved in the biosynthesis of the glycosaminoglycan-protein linkage region of proteoglycans. J. Biol. Chem. 274:1999;22915-22918.
    • (1999) J. Biol. Chem. , vol.274 , pp. 22915-22918
    • Okajima, T.1    Yoshida, K.2    Kondo, T.3    Furukawa, K.4
  • 61
    • 0033543696 scopus 로고    scopus 로고
    • Cloning and expression of a proteoglycan UDP-galactose:β-xylose β1,4-galactosyltransferase I. A seventh member of the human β4-galactosyltransferase gene family
    • Almeida R., Levery S.B., Mandel U., Kresse H., Schwientek T., Bennett E.P., Clausen H. Cloning and expression of a proteoglycan UDP-galactose:β-xylose β1,4-galactosyltransferase I. A seventh member of the human β4-galactosyltransferase gene family. J. Biol. Chem. 274:1999;26165-26171.
    • (1999) J. Biol. Chem. , vol.274 , pp. 26165-26171
    • Almeida, R.1    Levery, S.B.2    Mandel, U.3    Kresse, H.4    Schwientek, T.5    Bennett, E.P.6    Clausen, H.7
  • 62
    • 0025190732 scopus 로고
    • Kinetic study of a galactosyltransferase in the B cells of patients with rheumatoid arthritis
    • Furukawa K., Matsuta K., Takeuchi F., Kosuge E., Miyamoto T., Kobata A. Kinetic study of a galactosyltransferase in the B cells of patients with rheumatoid arthritis. Int. Immunol. 2:1990;105-112.
    • (1990) Int. Immunol. , vol.2 , pp. 105-112
    • Furukawa, K.1    Matsuta, K.2    Takeuchi, F.3    Kosuge, E.4    Miyamoto, T.5    Kobata, A.6
  • 63
    • 0027161319 scopus 로고
    • Kinetic study of human β-1,4-galactosyltransferase expressed in E. coli
    • Nakazawa K., Furukawa K., Narimatsu H., Kobata A. Kinetic study of human β-1,4-galactosyltransferase expressed in E. coli. J. Biochem. 113:1993;747-753.
    • (1993) J. Biochem. , vol.113 , pp. 747-753
    • Nakazawa, K.1    Furukawa, K.2    Narimatsu, H.3    Kobata, A.4
  • 64
    • 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
  • 65
    • 0030977266 scopus 로고    scopus 로고
    • Growth retardation and early death of β-1,4-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 β-1,4-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
  • 69
    • 0030744591 scopus 로고    scopus 로고
    • Deletion of two exons from the Lymnaea stagnalis β1,4-N-acetylglucosaminyltransferase gene elevates the kinetic efficiency of the encoded enzyme for both UDP sugar donor and acceptor substrates
    • Bakker H., Vantering A., Agterberg M., Smit A.B., van de Eijnden D.H., Van Die I.R. Deletion of two exons from the Lymnaea stagnalis β1,4-N-acetylglucosaminyltransferase gene elevates the kinetic efficiency of the encoded enzyme for both UDP sugar donor and acceptor substrates. J. Biol. Chem. 272:1997;18580-18585.
    • (1997) J. Biol. Chem. , vol.272 , pp. 18580-18585
    • Bakker, H.1    Vantering, A.2    Agterberg, M.3    Smit, A.B.4    Van De Eijnden, D.H.5    Van Die, I.R.6
  • 70
    • 0344628712 scopus 로고    scopus 로고
    • Structure-function Analysis of the UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase. Essential residues lie in a predicted active site cleft resembling a lactose repressor fold
    • Hagen F.K., Hazes B., Raffo R., deSa D., Tabak L.A. Structure-function Analysis of the UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase. Essential residues lie in a predicted active site cleft resembling a lactose repressor fold. J. Biol. Chem. 274:1999;6797-6803.
    • (1999) J. Biol. Chem. , vol.274 , pp. 6797-6803
    • Hagen, F.K.1    Hazes, B.2    Raffo, R.3    Desa, D.4    Tabak, L.A.5
  • 72
    • 0028815836 scopus 로고
    • Use of site-directed mutagenesis to identify the galactosyltransferase binding sites for UDP-galactose
    • Zu H., Fukuda M.N., Wong S.S., Wang Y., Liu Z., Tang Q., Appert H.E. Use of site-directed mutagenesis to identify the galactosyltransferase binding sites for UDP-galactose. Biochem. Biophys. Res. Commun. 206:1995;362-369.
    • (1995) Biochem. Biophys. Res. Commun. , vol.206 , pp. 362-369
    • Zu, H.1    Fukuda, M.N.2    Wong, S.S.3    Wang, Y.4    Liu, Z.5    Tang, Q.6    Appert, H.E.7
  • 73
    • 0027942505 scopus 로고
    • A Lymnaea stagnalis gene, with sequence similarity to that of mammalian β1→4-galactosyltransferases, encodes a novel UDP- GlcNAc:GlcNAc β-R β1→4-N-acetylglucosaminyltransferase
    • Bakker H., Agterberg M., Van Tetering A., Koeleman C.A., Van den Eijnden D.H., Van Die I. A Lymnaea stagnalis gene, with sequence similarity to that of mammalian β1→4-galactosyltransferases, encodes a novel UDP- GlcNAc:GlcNAc β-R β1→4-N-acetylglucosaminyltransferase. J. Biol. Chem. 269:1994;30326-30333.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30326-30333
    • Bakker, H.1    Agterberg, M.2    Van Tetering, A.3    Koeleman, C.A.4    Van Den Eijnden, D.H.5    Van Die, I.6
  • 74
    • 33745144680 scopus 로고    scopus 로고
    • Novel pathways in complex-type oligosaccharide synthesis new vistas opened by studies on invertebrates
    • Van den Eijnden D.H. Novel pathways in complex-type oligosaccharide synthesis new vistas opened by studies on invertebrates. Biochem. Soc. Trans. 25:1997;887-893.
    • (1997) Biochem. Soc. Trans. , vol.25 , pp. 887-893
    • Van Den Eijnden, D.H.1
  • 75
    • 0032567431 scopus 로고    scopus 로고
    • Synthesis of poly-N-acetyllactosamine in core 2 branched O-glycans: The requirement of novel β-1,4-galactosyltransferase IV and β-1,3-N-acetylglucosaminyltransferase
    • Ujita M., McAuliffe J., Schwientek T., Almeida R., Hindsgaul O., Clausen H., Fukuda M. Synthesis of poly-N-acetyllactosamine in core 2 branched O-glycans: the requirement of novel β-1,4-galactosyltransferase IV and β-1,3-N-acetylglucosaminyltransferase. J. Biol. Chem. 273:1998;34843-34849.
    • (1998) J. Biol. Chem. , vol.273 , pp. 34843-34849
    • Ujita, M.1    McAuliffe, J.2    Schwientek, T.3    Almeida, R.4    Hindsgaul, O.5    Clausen, H.6    Fukuda, M.7
  • 76
    • 0033515687 scopus 로고    scopus 로고
    • Regulation of I-branched poly-N-acetyllactosamine synthesis. Concerted actions by I-extension enzyme, I-branching enzyme, and β1,4-galactosyltransferase I
    • Ujita M., McAuliffe J., Suzuki M., Hindsgaul O., Clausen H., Fukuda M.N., Fukuda M. Regulation of I-branched poly-N-acetyllactosamine synthesis. Concerted actions by I-extension enzyme, I-branching enzyme, and β1,4-galactosyltransferase I. J. Biol. Chem. 274:1999;9296-9304.
    • (1999) J. Biol. Chem. , vol.274 , pp. 9296-9304
    • Ujita, M.1    McAuliffe, J.2    Suzuki, M.3    Hindsgaul, O.4    Clausen, H.5    Fukuda, M.N.6    Fukuda, M.7
  • 77
    • 0033005637 scopus 로고    scopus 로고
    • The acceptor substrate specificity of human β4-galactosyltransferase V indicates its potential function in O-glycosylation
    • Van Die I., Van Tetering A., Schiphorst W.E., Sato T., Furukawa K., Van den Eijnden D.H. The acceptor substrate specificity of human β4-galactosyltransferase V indicates its potential function in O-glycosylation. FEBS Lett. 450:1999;52-56.
    • (1999) FEBS Lett. , vol.450 , pp. 52-56
    • Van Die, I.1    Van Tetering, A.2    Schiphorst, W.E.3    Sato, T.4    Furukawa, K.5    Van Den Eijnden, D.H.6
  • 78
    • 0032571136 scopus 로고    scopus 로고
    • Differential effect of α-lactalbumin on β-1,4-galactosyltransferase IV activities
    • Sato T., Aoki N., Matsuda T., Furukawa K. Differential effect of α-lactalbumin on β-1,4-galactosyltransferase IV activities. Biochem. Biophys. Res. Commun. 244:1998;637-641.
    • (1998) Biochem. Biophys. Res. Commun. , vol.244 , pp. 637-641
    • Sato, T.1    Aoki, N.2    Matsuda, T.3    Furukawa, K.4
  • 79
    • 0025098286 scopus 로고
    • A genetic defect in the biosynthesis of dermatan sulfate proteoglycan:galactosyltransferase I deficiency in fibroblasts from a patient with a progeroid syndrome
    • Quentin E., Gladen A., Roden L., Kresse H. A genetic defect in the biosynthesis of dermatan sulfate proteoglycan:galactosyltransferase I deficiency in fibroblasts from a patient with a progeroid syndrome. Proc. Natl. Acad. Sci. USA. 87:1990;1342-1346.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 1342-1346
    • Quentin, E.1    Gladen, A.2    Roden, L.3    Kresse, H.4
  • 80
    • 0026801166 scopus 로고
    • Effects of brefeldin A on the localization of chondroitin sulfate-synthesizing enzymes. Activities in subfractions of the Golgi from chick embryo epiphyseal cartilage
    • Sugumaran G., Katsman M., Silbert J.E. Effects of brefeldin A on the localization of chondroitin sulfate-synthesizing enzymes. Activities in subfractions of the Golgi from chick embryo epiphyseal cartilage. J. Biol. Chem. 267:1992;8802-8806.
    • (1992) J. Biol. Chem. , vol.267 , pp. 8802-8806
    • Sugumaran, G.1    Katsman, M.2    Silbert, J.E.3
  • 81
    • 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
  • 82
    • 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. USA. 95:1998;14805-14810.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 14805-14810
    • Charron, M.1    Shaper, J.H.2    Shaper, N.L.3
  • 83
    • 0032537932 scopus 로고    scopus 로고
    • Expression of β1,4-galactosyltransferase in the development of mouse brain
    • Zhou D., Chen C., Jiang S., Shen Z., Chi Z., Gu J. Expression of β1,4-galactosyltransferase in the development of mouse brain. Biochim. Biophys. Acta. 1425:1998;204-208.
    • (1998) Biochim. Biophys. Acta , vol.1425 , pp. 204-208
    • Zhou, D.1    Chen, C.2    Jiang, S.3    Shen, Z.4    Chi, Z.5    Gu, J.6
  • 84
    • 0028295681 scopus 로고
    • 2.2 Mbof contigous nucleotide sequence from chromosome III of C. elegans
    • Wilson R., Ainscough R., Anderson K., et al. 2.2 Mbof contigous nucleotide sequence from chromosome III of C. elegans. Nature. 368:1994;32-38.
    • (1994) Nature , vol.368 , pp. 32-38
    • Wilson, R.1    Ainscough, R.2    Anderson, K.3
  • 85
    • 0033514302 scopus 로고    scopus 로고
    • Three proteins involved in Caenorhabditis elegans vulval invagination are similar to components of a glycosylation pathway
    • Herman T., Horvitz R.H. Three proteins involved in Caenorhabditis elegans vulval invagination are similar to components of a glycosylation pathway. Proc. Natl. Acad. Sci. USA. 96:1999;974-979.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 974-979
    • Herman, T.1    Horvitz, R.H.2
  • 86
    • 0032549523 scopus 로고    scopus 로고
    • Molecular cloning and expression of glucuronyltransferase I involved in the biosynthesis of the glycosaminoglycan-protein linkage region of proteoglycans
    • Kitagawa H., Tone Y., Tamura J., Neumann K.W., Ogawa T., Oka S., Kawasaki T., Sugahara K. Molecular cloning and expression of glucuronyltransferase I involved in the biosynthesis of the glycosaminoglycan-protein linkage region of proteoglycans. J. Biol. Chem. 273:1998;6615-6618.
    • (1998) J. Biol. Chem. , vol.273 , pp. 6615-6618
    • Kitagawa, H.1    Tone, Y.2    Tamura, J.3    Neumann, K.W.4    Ogawa, T.5    Oka, S.6    Kawasaki, T.7    Sugahara, K.8
  • 87
    • 0028148991 scopus 로고
    • Genetic locus for the biosynthesis of the variable portion of Neisseria gonorrhoeae lipooligosaccharide
    • Gotschlich E.C. Genetic locus for the biosynthesis of the variable portion of Neisseria gonorrhoeae lipooligosaccharide. J. Exp. Med. 180:1994;2181-2190.
    • (1994) J. Exp. Med. , vol.180 , pp. 2181-2190
    • Gotschlich, E.C.1
  • 88
    • 0029741316 scopus 로고    scopus 로고
    • Functional relationships of the genetic locus encoding the glycosyltransferase enzymes involved in expression of the lacto-N-neotetraose terminal lipopolysaccharide structure in Neisseria meningitidis
    • Wakarchuk W., Martin A., Jennings M.P., Moxon E.R., Richards J.C. Functional relationships of the genetic locus encoding the glycosyltransferase enzymes involved in expression of the lacto-N-neotetraose terminal lipopolysaccharide structure in Neisseria meningitidis. J. Biol. Chem. 271:1996;19166-19173.
    • (1996) J. Biol. Chem. , vol.271 , pp. 19166-19173
    • Wakarchuk, W.1    Martin, A.2    Jennings, M.P.3    Moxon, E.R.4    Richards, J.C.5
  • 89
    • 0032423068 scopus 로고    scopus 로고
    • Identification and characterization of N-acetylglucosamine-6-O-sulfate-specific β1,4-galactosyltransferase in human colorectal mucosa
    • Seko A., Hara-Kuge S., Yonezawa S., Nagata K., Yamashita K. Identification and characterization of N-acetylglucosamine-6-O-sulfate-specific β1,4-galactosyltransferase in human colorectal mucosa. FEBS Lett. 440:1998;307-310.
    • (1998) FEBS Lett. , vol.440 , pp. 307-310
    • Seko, A.1    Hara-Kuge, S.2    Yonezawa, S.3    Nagata, K.4    Yamashita, K.5
  • 90
    • 0033043546 scopus 로고    scopus 로고
    • Bovine mammary gland UDP-GalNAc:GlcNAcβ-R β1→4-N-acetylgalactosaminyltransferase is glycoprotein hormone nonspecific and shows interaction with α-lactalbumin
    • Van den Nieuwenhof I.M., Schiphorst W.M., Van Die I., Van den Eijnden D.H. Bovine mammary gland UDP-GalNAc:GlcNAcβ-R β1→4-N-acetylgalactosaminyltransferase is glycoprotein hormone nonspecific and shows interaction with α-lactalbumin. Glycobiology. 9:1999;115-123.
    • (1999) Glycobiology , vol.9 , pp. 115-123
    • Van Den Nieuwenhof, I.M.1    Schiphorst, W.M.2    Van Die, I.3    Van Den Eijnden, D.H.4
  • 91
    • 0028869433 scopus 로고
    • A cluster of basic amino acids within an α-helix is essential for α-subunit recognition by the glycoprotein hormone N-acetylgalactosamine
    • Mengeling B.J., Manzella S.M., Baenziger J.U. A cluster of basic amino acids within an α-helix is essential for α-subunit recognition by the glycoprotein hormone N-acetylgalactosamine. Proc. Natl. Acad. Sci. USA. 92:1995;502-506.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 502-506
    • Mengeling, B.J.1    Manzella, S.M.2    Baenziger, J.U.3
  • 92
    • 0030972420 scopus 로고    scopus 로고
    • Molecular cloning and characterization of β-1,4-galactosylatransferase expressed in mouse testis
    • Uehara K., Muramatsu T. Molecular cloning and characterization of β-1,4-galactosylatransferase expressed in mouse testis. Eur. J. Biochem. 244:1997;706-712.
    • (1997) Eur. J. Biochem. , vol.244 , pp. 706-712
    • Uehara, K.1    Muramatsu, T.2
  • 93
    • 18344413924 scopus 로고    scopus 로고
    • Testis β-1,4-galactosyltransferase gene maps to mouse chromosome 5
    • Kaname T., Uehara K., Abe K., Muramatsu T., Yamamura K. Testis β-1,4-galactosyltransferase gene maps to mouse chromosome 5. Genomics. 53:1998;117-118.
    • (1998) Genomics , vol.53 , pp. 117-118
    • Kaname, T.1    Uehara, K.2    Abe, K.3    Muramatsu, T.4    Yamamura, K.5
  • 94
    • 0033582292 scopus 로고    scopus 로고
    • A β-1,3-N-acetylglucosaminyltransferase with poly-N-acetyllactosamine synthase activity is structurally related to β-1,3-galactosyltransferases
    • Zhou D., Dinter A., Gallego R.G., Kamerling J.P., Vliegenthart J.F.G., Berger E.G., Hennett T. A β-1,3-N-acetylglucosaminyltransferase with poly-N-acetyllactosamine synthase activity is structurally related to β-1,3-galactosyltransferases. Proc. Natl. Acad. Sci. USA. 96:1999;406-411.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 406-411
    • Zhou, D.1    Dinter, A.2    Gallego, R.G.3    Kamerling, J.P.4    Vliegenthart, J.F.G.5    Berger, E.G.6    Hennett, T.7
  • 95
    • 0025875756 scopus 로고
    • Proteoglycans: Structures and interactions
    • Kjellen L., Lindahl U. Proteoglycans: structures and interactions. Annu. Rev. Biochem. 60:1991;443-475.
    • (1991) Annu. Rev. Biochem. , vol.60 , pp. 443-475
    • Kjellen, L.1    Lindahl, U.2
  • 96
    • 0020490229 scopus 로고
    • Biosynthesis of galactosyl-β1,3-N-acetylglucosamine
    • Sheares B.T., Lau J.T., Carlson D.M. Biosynthesis of galactosyl-β1,3-N-acetylglucosamine. J. Biol. Chem. 257:1982;599-602.
    • (1982) J. Biol. Chem. , vol.257 , pp. 599-602
    • Sheares, B.T.1    Lau, J.T.2    Carlson, D.M.3
  • 97
    • 0024513407 scopus 로고
    • Characterization and membrane organization of β1-3- And β1-4-galactosyltransferases from human colonic adenocarcinoma cell lines Colo 205 and SW403: Basis for preferential synthesis of type 1 chain lacto-series carbohydrate structures
    • Holmes E.H. Characterization and membrane organization of β1-3- and β1-4-galactosyltransferases from human colonic adenocarcinoma cell lines Colo 205 and SW403: basis for preferential synthesis of type 1 chain lacto-series carbohydrate structures. Arch. Biochem. Biophys. 270:1989;630-646.
    • (1989) Arch. Biochem. Biophys. , vol.270 , pp. 630-646
    • Holmes, E.H.1
  • 98
    • 0031713428 scopus 로고    scopus 로고
    • Trinchera, β-1,3-galactosyltransferase and α-1,2-fucosyltransferase involved in the biosynthesis of type-1-chain carbohydrate antigens in human colon adenocarcinoma cell lines
    • Valli A., Gallanti S., Bozzaro M. Trinchera, β-1,3-galactosyltransferase and α-1,2-fucosyltransferase involved in the biosynthesis of type-1-chain carbohydrate antigens in human colon adenocarcinoma cell lines. Eur. J. Biochem. 256:1998;494-501.
    • (1998) Eur. J. Biochem. , vol.256 , pp. 494-501
    • Valli, A.1    Gallanti, S.2    Bozzaro, M.3
  • 99
    • 0030868544 scopus 로고    scopus 로고
    • Expression cloning of rat cDNA encoding UDP-galactose G(D2) β1,3 galactosyltransferase that determines the expression of G(D1b)/G(M1)/G(A1)
    • Miyaki H., Fukumoto S., Okada M., Hasegawa T., Furukawa K. Expression cloning of rat cDNA encoding UDP-galactose G(D2) β1,3 galactosyltransferase that determines the expression of G(D1b)/G(M1)/G(A1). J. Biol. Chem. 272:1997;24794-24799.
    • (1997) J. Biol. Chem. , vol.272 , pp. 24794-24799
    • Miyaki, H.1    Fukumoto, S.2    Okada, M.3    Hasegawa, T.4    Furukawa, K.5
  • 100
    • 0031972692 scopus 로고    scopus 로고
    • Cloning of a human UDP-galactose:2-acetamido-2-deoxy-D-glucose 3β-galactosyltransferase catalysing the formation of type 1 chains
    • Kolbinger F., Streiff M.B., Katopodis A.G. Cloning of a human UDP-galactose:2-acetamido-2-deoxy-D-glucose 3β-galactosyltransferase catalysing the formation of type 1 chains. J. Biol. Chem. 273:1998;433-440.
    • (1998) J. Biol. Chem. , vol.273 , pp. 433-440
    • Kolbinger, F.1    Streiff, M.B.2    Katopodis, A.G.3
  • 101
    • 0031983121 scopus 로고    scopus 로고
    • Genomic cloning and expression of three murine UDP-galactose:β-N-acetylglucosamine β1,3-galactosyltransferase genes
    • Hennett T., Dinter A., Kuhnert P., Mattu T.S., Rudd P.M., Berger E.G. Genomic cloning and expression of three murine UDP-galactose:β-N-acetylglucosamine β1,3-galactosyltransferase genes. J. Biol. Chem. 273:1998;58-65.
    • (1998) J. Biol. Chem. , vol.273 , pp. 58-65
    • Hennett, T.1    Dinter, A.2    Kuhnert, P.3    Mattu, T.S.4    Rudd, P.M.5    Berger, E.G.6
  • 102
    • 0033617363 scopus 로고    scopus 로고
    • Cloning, expression, and characterization of a novel UDP-galactose:β-N-acetylglucosamine β1,3-galactosyltransferase (β3Gal-T5) responsible for synthesis of type 1 chain in colorectal and pancreatic epithelia and tumor cells derived therefrom
    • Isshiki S., Togayachi A., Kudo T., Nishihara S., Watanabe M., Kubota T., Kitajima M., Shiraishi N., Sasaki K., Andoh T., Narimatsu H. Cloning, expression, and characterization of a novel UDP-galactose:β-N-acetylglucosamine β1,3-galactosyltransferase (β3Gal-T5) responsible for synthesis of type 1 chain in colorectal and pancreatic epithelia and tumor cells derived therefrom. J. Biol. Chem. 274:1999;12499-12507.
    • (1999) J. Biol. Chem. , vol.274 , pp. 12499-12507
    • Isshiki, S.1    Togayachi, A.2    Kudo, T.3    Nishihara, S.4    Watanabe, M.5    Kubota, T.6    Kitajima, M.7    Shiraishi, N.8    Sasaki, K.9    Andoh, T.10    Narimatsu, H.11
  • 103
    • 0001508998 scopus 로고    scopus 로고
    • Molecular cloning of a human UDP-galactose:GlcNAcβ1,3GalNAc β1,3 galactosyltransferase gene encoding an O-linked core3-elongation enzyme
    • Zhou D., Berger E.G., Hennett T. Molecular cloning of a human UDP-galactose:GlcNAcβ1,3GalNAc β1,3 galactosyltransferase gene encoding an O-linked core3-elongation enzyme. Eur. J. Biochem. 263:1999;571-576.
    • (1999) Eur. J. Biochem. , vol.263 , pp. 571-576
    • Zhou, D.1    Berger, E.G.2    Hennett, T.3
  • 104
    • 0032401616 scopus 로고    scopus 로고
    • Neutral core oligosaccharides of bovine submaxillary mucin. Use of lead tetraacetate in the cold for establishing branch positions
    • Mårtensson S., Levery S.B., Fang T., Bendiak B. Neutral core oligosaccharides of bovine submaxillary mucin. Use of lead tetraacetate in the cold for establishing branch positions. Eur. J. Biochem. 258:1998;603-622.
    • (1998) Eur. J. Biochem. , vol.258 , pp. 603-622
    • Mårtensson, S.1    Levery, S.B.2    Fang, T.3    Bendiak, B.4
  • 105
    • 0021112437 scopus 로고
    • Characterization of UDP-galactose:2-acetamido-2-deoxy-D-glucose 3β-galactosyltransferase from pig trachea
    • Sheares B.T., Carlson D.M. Characterization of UDP-galactose:2-acetamido-2-deoxy-D-glucose 3β-galactosyltransferase from pig trachea. J. Biol. Chem. 258:1983;9893-9898.
    • (1983) J. Biol. Chem. , vol.258 , pp. 9893-9898
    • Sheares, B.T.1    Carlson, D.M.2
  • 106
    • 0031561502 scopus 로고    scopus 로고
    • Secreted fringe-like signaling molecules may be glycosyltransferases
    • Yuan Y.P., Schultz J., Mlodzik M., Bork P. Secreted fringe-like signaling molecules may be glycosyltransferases. Cell. 88:1997;9-11.
    • (1997) Cell , vol.88 , pp. 9-11
    • Yuan, Y.P.1    Schultz, J.2    Mlodzik, M.3    Bork, P.4
  • 107
    • 0024585483 scopus 로고
    • Aberrant glycosylation in tumors and tumor-associated carbohydrate antigens
    • Hakomori S. Aberrant glycosylation in tumors and tumor-associated carbohydrate antigens. Adv. Cancer Res. 52:1989;257-331.
    • (1989) Adv. Cancer Res. , vol.52 , pp. 257-331
    • Hakomori, S.1
  • 108
    • 0030480250 scopus 로고    scopus 로고
    • Tumor malignancy defined by aberrant glycosylation and sphingo(glyco)lipid metabolism
    • Hakomori S. Tumor malignancy defined by aberrant glycosylation and sphingo(glyco)lipid metabolism. Cancer Res. 56:1996;5309-5318.
    • (1996) Cancer Res. , vol.56 , pp. 5309-5318
    • Hakomori, S.1
  • 109
    • 0023160889 scopus 로고
    • Oncofetal expression of Lex carbohydrate antigens in human colonic adenocarcinomas. Regulation through type 2 core chain synthesis rather than fucosylation
    • Holmes E.H., Ostrander G.K., Clausen H., Graem N. Oncofetal expression of Lex carbohydrate antigens in human colonic adenocarcinomas. Regulation through type 2 core chain synthesis rather than fucosylation. J. Biol. Chem. 262:1987;11331-11338.
    • (1987) J. Biol. Chem. , vol.262 , pp. 11331-11338
    • Holmes, E.H.1    Ostrander, G.K.2    Clausen, H.3    Graem, N.4
  • 110
    • 85044686082 scopus 로고
    • Synthesis of type 1 and 2 lacto series glycolipid antigens in human colonic adenocarcinoma and derived cell lines is due to activation of a normally unexpressed β1-3N-acetylglucosaminyltransferase Molecular changes in carbohydrate antigens associated with cancer
    • Holmes E.H., Hakomori S., Ostrander G.K., Singhal A. Synthesis of type 1 and 2 lacto series glycolipid antigens in human colonic adenocarcinoma and derived cell lines is due to activation of a normally unexpressed β1-3N-acetylglucosaminyltransferase Molecular changes in carbohydrate antigens associated with cancer. J. Biol. Chem. 262:1987;15649-15658.
    • (1987) J. Biol. Chem. , vol.262 , pp. 15649-15658
    • Holmes, E.H.1    Hakomori, S.2    Ostrander, G.K.3    Singhal, A.4
  • 111
    • 0024273824 scopus 로고
    • Identification of the full-length coding sequence for human galactosyltransferase (β-N-acetylglucosaminide:β1,4- galactosyltransferase)
    • Masri K.A., Appert H.E., Fukuda M.N. Identification of the full-length coding sequence for human galactosyltransferase (β-N-acetylglucosaminide:β1,4- galactosyltransferase). Biochem. Biophys. Res. Commun. 157:1988;657-663.
    • (1988) Biochem. Biophys. Res. Commun. , vol.157 , pp. 657-663
    • Masri, K.A.1    Appert, H.E.2    Fukuda, M.N.3
  • 112
    • 0032739349 scopus 로고    scopus 로고
    • β-1,4-Galactosylation of N-glycans is a complex process
    • Furukawa K., Sato T. β-1,4-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


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