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Volumn 391, Issue 1, 2005, Pages 77-85

Porcine, mouse and human galactose 3-O-sulphotransferase-2 enzymes have different substrate specificities; the porcine enzyme requires basic compounds for its catalytic activity

Author keywords

Colonic mucosa; Mucin; Spermine; Sphingosine; Sulphotransferase

Indexed keywords

CATALYST ACTIVITY; DNA; HYDROXYAPATITE; LIPIDS; SUBSTRATES;

EID: 26844444532     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20050362     Document Type: Article
Times cited : (7)

References (36)
  • 1
    • 0023221836 scopus 로고
    • Structural studies of the carbohydrate moieties of carcinoembryonic antigens
    • Yamashita, K., Totani, K., Kuroki, M., Matsuoka, Y., Ueda, I. and Kobata, A. (1987) Structural studies of the carbohydrate moieties of carcinoembryonic antigens. Cancer Res. 47, 3451-3459
    • (1987) Cancer Res. , vol.47 , pp. 3451-3459
    • Yamashita, K.1    Totani, K.2    Kuroki, M.3    Matsuoka, Y.4    Ueda, I.5    Kobata, A.6
  • 3
    • 0028819437 scopus 로고
    • Carbohydrate structures of a normal counterpart of the carcinoembryonic antigen produced by colon epithelial cells of normal adults
    • Fukushima, K., Ohkura, T., Kanai, M., Kuroki, M., Matsuoka, Y., Kobata, A. and Yamashita, K. (1995) Carbohydrate structures of a normal counterpart of the carcinoembryonic antigen produced by colon epithelial cells of normal adults. Glycobiology 5, 105-115
    • (1995) Glycobiology , vol.5 , pp. 105-115
    • Fukushima, K.1    Ohkura, T.2    Kanai, M.3    Kuroki, M.4    Matsuoka, Y.5    Kobata, A.6    Yamashita, K.7
  • 4
    • 0031449971 scopus 로고    scopus 로고
    • Sulfated Lewis X determinants as a major structural motif in glycans from LS174T-HM7 human colon carcinoma mucin
    • Capon, C., Wieruszeski, J.-M., Lemoine, J., Byrd, J. C., Leffler, H. and Kim, Y. S. (1997) Sulfated Lewis X determinants as a major structural motif in glycans from LS174T-HM7 human colon carcinoma mucin. J. Biol. Chem. 272, 31957-31968
    • (1997) J. Biol. Chem. , vol.272 , pp. 31957-31968
    • Capon, C.1    Wieruszeski, J.-M.2    Lemoine, J.3    Byrd, J.C.4    Leffler, H.5    Kim, Y.S.6
  • 6
    • 0031040255 scopus 로고    scopus 로고
    • Molecular cloning and expression of cDNA encoding human 3′-phosphoadenylylsulfate: Galactosylceramide 3′-sulfotransferase
    • Honke, K., Tsuda, M., Hirahara, Y., Ishii, A., Makita, A. and Wada, Y. (1997) Molecular cloning and expression of cDNA encoding human 3′-phosphoadenylylsulfate: galactosylceramide 3′-sulfotransferase. J. Biol. Chem. 272, 4864-4868
    • (1997) J. Biol. Chem. , vol.272 , pp. 4864-4868
    • Honke, K.1    Tsuda, M.2    Hirahara, Y.3    Ishii, A.4    Makita, A.5    Wada, Y.6
  • 7
    • 0029966104 scopus 로고    scopus 로고
    • Purification and characterization of 3′-phosphoadenosine-5′- phosphosulfate:GalCer sulfotransferase from human renal cancer cells
    • Honke, K., Yamane, M., Ishii, A., Kobayashi, T. and Makita, A. (1996) Purification and characterization of 3′-phosphoadenosine-5′- phosphosulfate:GalCer sulfotransferase from human renal cancer cells. J. Biochem. (Tokyo) 119, 421-427
    • (1996) J. Biochem. (Tokyo) , vol.119 , pp. 421-427
    • Honke, K.1    Yamane, M.2    Ishii, A.3    Kobayashi, T.4    Makita, A.5
  • 8
    • 0035808299 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a human β-Gal-3′- sulfotransferase that acts on both type 1 and type 2 (Galβ1-3/1-4GlcNAc-R) oligosaccharides
    • Honke, K., Tsuda, M., Koyota, S., Wada, Y., Iida-Tanaka, N., Ishizuka, I., Nakayama, J. and Taniguchi, N. (2001) Molecular cloning and characterization of a human β-Gal-3′-sulfotransferase that acts on both type 1 and type 2 (Galβ1-3/1-4GlcNAc-R) oligosaccharides. J. Biol. Chem. 276, 267-274
    • (2001) J. Biol. Chem. , vol.276 , pp. 267-274
    • Honke, K.1    Tsuda, M.2    Koyota, S.3    Wada, Y.4    Iida-Tanaka, N.5    Ishizuka, I.6    Nakayama, J.7    Taniguchi, N.8
  • 9
    • 0035968263 scopus 로고    scopus 로고
    • Molecular cloning and expression of a novel human β-Gal-3-O- sulfotransferase that acts preferentially on N-acetyllactosamine in N- and O-glycans
    • Suzuki, A., Hiraoka, N., Suzuki, M., Angata, K., Misra, A. K., McAuliffe, J., Hindsgaul, O. and Fukuda, M. (2001) Molecular cloning and expression of a novel human β-Gal-3-O-sulfotransferase that acts preferentially on N-acetyllactosamine in N- and O-glycans. J. Biol. Chem. 276, 24388-24395
    • (2001) J. Biol. Chem. , vol.276 , pp. 24388-24395
    • Suzuki, A.1    Hiraoka, N.2    Suzuki, M.3    Angata, K.4    Misra, A.K.5    McAuliffe, J.6    Hindsgaul, O.7    Fukuda, M.8
  • 11
    • 0035854793 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a novel human galactose 3-O-sulfotransferase that transfers sulfate to Galβ1 → 3GalNAc residue in O-glycans
    • Seko, A., Hara-Kuge, S. and Yamashita, K. (2001) Molecular cloning and characterization of a novel human galactose 3-O-sulfotransferase that transfers sulfate to Galβ1 → 3GalNAc residue in O-glycans. J. Biol. Chem. 276, 25697-25704
    • (2001) J. Biol. Chem. , vol.276 , pp. 25697-25704
    • Seko, A.1    Hara-Kuge, S.2    Yamashita, K.3
  • 12
    • 0036317303 scopus 로고    scopus 로고
    • Down-regulation of Gal 3-O-sulfotransferase-2(Gal3ST-2) expression in human colonic non-mucinous adenocarcinoma
    • Seko, A., Nagata, K., Yonezawa, S. and Yamashita, K. (2002) Down-regulation of Gal 3-O-sulfotransferase-2(Gal3ST-2) expression in human colonic non-mucinous adenocarcinoma. Jpn. J. Cancer Res. 93, 507-515
    • (2002) Jpn. J. Cancer Res. , vol.93 , pp. 507-515
    • Seko, A.1    Nagata, K.2    Yonezawa, S.3    Yamashita, K.4
  • 13
    • 0028803521 scopus 로고
    • Characterization of a novel mucin sulphotransferase activity synthesizing sulphated O-glycan core 1,3-sulphate-Galβ1 → 3GalNAcα-R
    • Kuhns, W., Jain, R. K., Matta, K. L., Paulsen, H., Baker, M. A., Geyer, R. and Brockhausen, I. (1995) Characterization of a novel mucin sulphotransferase activity synthesizing sulphated O-glycan core 1,3-sulphate-Galβ1 → 3GalNAcα-R. Glycobiology 5, 689-697
    • (1995) Glycobiology , vol.5 , pp. 689-697
    • Kuhns, W.1    Jain, R.K.2    Matta, K.L.3    Paulsen, H.4    Baker, M.A.5    Geyer, R.6    Brockhausen, I.7
  • 14
    • 77956990690 scopus 로고
    • Isolation of oligosaccharides from human milk
    • Kobata, A. (1972) Isolation of oligosaccharides from human milk. Methods Enzymol. 28, 262-271
    • (1972) Methods Enzymol. , vol.28 , pp. 262-271
    • Kobata, A.1
  • 15
    • 0019732831 scopus 로고
    • Urinary oligosaccharides of Gm1-gangliosidosis: Different excretion patterns of oligosaccharides in the urine of type 1 and type 2 subgroups
    • Yamashita, K., Ohkura, T., Okada, S., Yabuuchi, H. and Kobata, A. (1981) Urinary oligosaccharides of Gm1-gangliosidosis: different excretion patterns of oligosaccharides in the urine of type 1 and type 2 subgroups. J. Biol. Chem. 256, 4789-4798
    • (1981) J. Biol. Chem. , vol.256 , pp. 4789-4798
    • Yamashita, K.1    Ohkura, T.2    Okada, S.3    Yabuuchi, H.4    Kobata, A.5
  • 17
    • 0003541870 scopus 로고
    • The covalent binding of nucleotides, polynucleotides, and nucleic acids to cellulose
    • Gilham, P. T. (1971) The covalent binding of nucleotides, polynucleotides, and nucleic acids to cellulose. Methods Enzymol. 21, 191-197
    • (1971) Methods Enzymol. , vol.21 , pp. 191-197
    • Gilham, P.T.1
  • 18
    • 77956996948 scopus 로고
    • Characterization of carbohydrate units of glycoproteins
    • Spiro, R. G. (1966) Characterization of carbohydrate units of glycoproteins. Methods Enzymol. 8, 26-52
    • (1966) Methods Enzymol. , vol.8 , pp. 26-52
    • Spiro, R.G.1
  • 19
    • 0016702060 scopus 로고
    • The purification, composition, and specificity of the anti-T lectin from peanut (Arachis hypogaea)
    • Lotan, R., Skutelsky, E., Danon, D. and Sharon, N. (1975) The purification, composition, and specificity of the anti-T lectin from peanut (Arachis hypogaea). J. Biol. Chem. 250, 8518-8523
    • (1975) J. Biol. Chem. , vol.250 , pp. 8518-8523
    • Lotan, R.1    Skutelsky, E.2    Danon, D.3    Sharon, N.4
  • 20
    • 0033848568 scopus 로고    scopus 로고
    • Biochemical differences between two types of N-acetylglucosamine: → 6sulfotransferases in human colonic adenocarcinomas and the adjacent normal mucosa: Specific expression of a GlcNAc: → 6sulfotransferase in mucinous adenocarcinoma
    • Seko, A., Sumiya, J., Yonezawa, S., Nagata, K. and Yamashita, K. (2000) Biochemical differences between two types of N-acetylglucosamine: → 6sulfotransferases in human colonic adenocarcinomas and the adjacent normal mucosa: specific expression of a GlcNAc: → 6sulfotransferase in mucinous adenocarcinoma. Glycobiology 10, 919-929
    • (2000) Glycobiology , vol.10 , pp. 919-929
    • Seko, A.1    Sumiya, J.2    Yonezawa, S.3    Nagata, K.4    Yamashita, K.5
  • 21
    • 0032514894 scopus 로고    scopus 로고
    • Purification and characterization of a glucuronyltransferase involved in the biosynthesis of the HNK-1 epitope on glycoproteins from rat brain
    • Terayama, K., Seiki, T., Nakamura, A., Matsumori, K., Ohta, S., Oka, S., Sugita, M. and Kawasaki, T. (1998) Purification and characterization of a glucuronyltransferase involved in the biosynthesis of the HNK-1 epitope on glycoproteins from rat brain. J. Biol. Chem. 273, 30295-30300
    • (1998) J. Biol. Chem. , vol.273 , pp. 30295-30300
    • Terayama, K.1    Seiki, T.2    Nakamura, A.3    Matsumori, K.4    Ohta, S.5    Oka, S.6    Sugita, M.7    Kawasaki, T.8
  • 22
    • 0037984379 scopus 로고    scopus 로고
    • β1,4-galactosyltransferase (β4GalT)-IV is specific for GlcNAc 6-0-sulfate: β4GalT-IV acts on keratan sulfate-related glycans and a precursor glycan of 6-sulfosialyl-Lewis X
    • Seko, A., Dohmae, N., Takio, K. and Yamashita, K. (2003) β1,4-galactosyltransferase (β4GalT)-IV is specific for GlcNAc 6-0-sulfate: β4GalT-IV acts on keratan sulfate-related glycans and a precursor glycan of 6-sulfosialyl-Lewis X. J. Biol. Chem. 278, 9150-9158
    • (2003) J. Biol. Chem. , vol.278 , pp. 9150-9158
    • Seko, A.1    Dohmae, N.2    Takio, K.3    Yamashita, K.4
  • 25
    • 0037044826 scopus 로고    scopus 로고
    • Enzymatic synthesis in vitro of the disulfated disaccharide unit of corneal keratan sulfate
    • Akama, T. O., Misra, A. K., Hindsgaul, O. and Fukuda, M. N. (2002) Enzymatic synthesis in vitro of the disulfated disaccharide unit of corneal keratan sulfate. J. Biol. Chem. 277, 42505-42513
    • (2002) J. Biol. Chem. , vol.277 , pp. 42505-42513
    • Akama, T.O.1    Misra, A.K.2    Hindsgaul, O.3    Fukuda, M.N.4
  • 26
    • 0020457314 scopus 로고
    • Separation and characterization of chondroitin 6-sulfotransferase and chondroitin 4-sultotransferase from chick embryo cartilage
    • Habuchi, O. and Miyashita, N. (1982) Separation and characterization of chondroitin 6-sulfotransferase and chondroitin 4-sultotransferase from chick embryo cartilage. Biochim. Biophys. Acta 717, 414-421
    • (1982) Biochim. Biophys. Acta , vol.717 , pp. 414-421
    • Habuchi, O.1    Miyashita, N.2
  • 27
    • 0024807517 scopus 로고
    • Regulation of serum glycosaminoglycan sulfotransferase activities: Inhibition by sulfated glycosaminoglycans and activation by polyamines and basic peptides including a polylysine-containing segment of the c-Ki-ras 2 protein
    • Sugahara, K., Nakamura, M., Nagisa, J., Masuda, M., Nunokawa, Y., Fujii, N. and Yamashina, I. (1989) Regulation of serum glycosaminoglycan sulfotransferase activities: inhibition by sulfated glycosaminoglycans and activation by polyamines and basic peptides including a polylysine-containing segment of the c-Ki-ras 2 protein. J. Biochem. (Tokyo) 106, 910-919
    • (1989) J. Biochem. (Tokyo) , vol.106 , pp. 910-919
    • Sugahara, K.1    Nakamura, M.2    Nagisa, J.3    Masuda, M.4    Nunokawa, Y.5    Fujii, N.6    Yamashina, I.7
  • 28
    • 0029301072 scopus 로고
    • Effect of lipids on glycoprotein sulphotransferase activity in rat submandibular salivary glands
    • Kasinathan, C., William, S., Vaidyanathan, S. and Leventhal, J. (1995) Effect of lipids on glycoprotein sulphotransferase activity in rat submandibular salivary glands. Arch. Oral Biol. 40, 433-438
    • (1995) Arch. Oral Biol. , vol.40 , pp. 433-438
    • Kasinathan, C.1    William, S.2    Vaidyanathan, S.3    Leventhal, J.4
  • 29
    • 0027398828 scopus 로고
    • Inhibition of tyrosylprotein sulfotransferase by sphingosine and its reversal by acidic phospholipids
    • Kasinathan, C., Sundaram, P., Slomiany, B. L. and Slomiany, A. (1993) Inhibition of tyrosylprotein sulfotransferase by sphingosine and its reversal by acidic phospholipids. Biochemistry 32, 1194-1198
    • (1993) Biochemistry , vol.32 , pp. 1194-1198
    • Kasinathan, C.1    Sundaram, P.2    Slomiany, B.L.3    Slomiany, A.4
  • 30
    • 0016372387 scopus 로고
    • Enhancement of UDP-galactose:mucin galactosyltransferase activity by spermine
    • Baker, A. P. and Hillegass, L. M. (1974) Enhancement of UDP-galactose:mucin galactosyltransferase activity by spermine. Arch. Biochem. Biophys. 165, 597-603
    • (1974) Arch. Biochem. Biophys. , vol.165 , pp. 597-603
    • Baker, A.P.1    Hillegass, L.M.2
  • 31
    • 0019943552 scopus 로고
    • Mucin biosynthesis. Characterization of UDP-galactose:α-N- acetylgalactosaminide β3galactosyltransferase from human tracheal epithelium
    • Cheng, P.-W. and Bona, J. (1982) Mucin biosynthesis. Characterization of UDP-galactose:α-N-acetylgalactosaminide β3galactosyltransferase from human tracheal epithelium. J. Biol. Chem. 257, 6251-6258
    • (1982) J. Biol. Chem. , vol.257 , pp. 6251-6258
    • Cheng, P.-W.1    Bona, J.2
  • 33
    • 0022445298 scopus 로고
    • Cationic activation of galactosyltransferase from rat mammary Golgi membranes by polyamines and by basic peptides and proteins
    • Navaratnam, N., Virk, S. S., Ward, S. and Kuhn, N. J. (1986) Cationic activation of galactosyltransferase from rat mammary Golgi membranes by polyamines and by basic peptides and proteins. Biochem. J. 239, 423-433
    • (1986) Biochem. J. , vol.239 , pp. 423-433
    • Navaratnam, N.1    Virk, S.S.2    Ward, S.3    Kuhn, N.J.4
  • 34
    • 0025655435 scopus 로고
    • Characterization of solubilized GlcAT-1 (UDP-GlcA: NLcOse4Cer β1-3glucuronyltransferase) activity from embryonic chicken grain and its inhibition by D-erythro-sphingosine
    • Das, K. K., Basu, M., Li, Z., Basu, S. and Jungalwala, F. (1990) Characterization of solubilized GlcAT-1 (UDP-GlcA: nLcOse4Cer β1-3glucuronyltransferase) activity from embryonic chicken grain and its inhibition by D-erythro-sphingosine. Indian J. Biochem. Biophys. 27, 396-401
    • (1990) Indian J. Biochem. Biophys. , vol.27 , pp. 396-401
    • Das, K.K.1    Basu, M.2    Li, Z.3    Basu, S.4    Jungalwala, F.5
  • 35
    • 0024556966 scopus 로고
    • Swelling of the Golgi apparatus and decrease of galactosyltransferase in polyamine-deficient bovine lymphocytes and epithelium of mouse small intestine
    • Sakamaki, Y., Terao, K., Ito, E., Kashiwagi, K. and Igarashi, K. (1989) Swelling of the Golgi apparatus and decrease of galactosyltransferase in polyamine-deficient bovine lymphocytes and epithelium of mouse small intestine. Biochem. Pharmacol. 38, 1083-1089
    • (1989) Biochem. Pharmacol. , vol.38 , pp. 1083-1089
    • Sakamaki, Y.1    Terao, K.2    Ito, E.3    Kashiwagi, K.4    Igarashi, K.5
  • 36
    • 0004139057 scopus 로고    scopus 로고
    • Oxford University Press, Oxford
    • Cohen, S. S. (1998) in A Guide to the Polyamines, pp. 185-230, Oxford University Press, Oxford
    • (1998) A Guide to the Polyamines , pp. 185-230
    • Cohen, S.S.1


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