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Volumn 1022, Issue , 2013, Pages 283-298

N-acetylglucosaminyltransferase (GnT) assays using fluorescent oligosaccharide acceptor substrates: GnT-III, IV, V, and IX (GnT-Vb)

Author keywords

GnT III; GnT IV; GnT IX; GnT V; GnT Vb; N acetylglucosaminyltransferase; PA labeled oligosaccharide; Reversed phase HPLC

Indexed keywords

N ACETYLGLUCOSAMINYLTRANSFERASE; OLIGOSACCHARIDE;

EID: 84880469539     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-62703-465-4_21     Document Type: Article
Times cited : (9)

References (21)
  • 2
    • 84857692860 scopus 로고    scopus 로고
    • Branched N-glycans and their implications for cell adhesion, signaling and clinical applications for cancer biomarkers and in therapeutics
    • Taniguchi N, Korekane H (2011) Branched N-glycans and their implications for cell adhesion, signaling and clinical applications for cancer biomarkers and in therapeutics. BMB Rep 44:772-781
    • (2011) BMB Rep , vol.44 , pp. 772-781
    • Taniguchi, N.1    Korekane, H.2
  • 3
    • 0024117227 scopus 로고
    • The biosynthesis of highly branched N-glycans: Studies on the sequential pathway and functional role of N-Acetylglucosaminyltransferases I, II, III, IV, v and VI
    • Brockhausen I, Narasimhan S, Schachter H (1988) The biosynthesis of highly branched N-glycans: Studies on the sequential pathway and functional role of N-Acetylglucosaminyltransferases I, II, III, IV, V and VI. Biochimie 70:1521-1533
    • (1988) Biochimie , vol.70 , pp. 1521-1533
    • Brockhausen, I.1    Narasimhan, S.2    Schachter, H.3
  • 4
    • 0242322005 scopus 로고    scopus 로고
    • Molecular cloning and characterization of human GnT-IX, a novel β1,6-N-Acetylglucosaminyltransferase that is specifi cally expressed in the brain
    • Inamori K, Endo T, Ide Y, Fujii S, Gu J, Honke K, Taniguchi N (2003) Molecular cloning and characterization of human GnT-IX, a novel β1,6-N-Acetylglucosaminyltransferase that is specifi cally expressed in the brain. J Biol Chem 278:43102-43109
    • (2003) J Biol Chem , vol.278 , pp. 43102-43109
    • Inamori, K.1    Endo, T.2    Ide, Y.3    Fujii, S.4    Gu, J.5    Honke, K.6    Taniguchi, N.7
  • 6
    • 0030884451 scopus 로고    scopus 로고
    • Purifi cation and characterization of UDP-N-Acetylglucosamine: Alpha1,3-D-mannoside beta 1,4-N-Acetylglucosaminyltransferase (N-Acetylglucosaminyltransferase-IV) from bovine small intestine
    • Oguri S, Minowa MT, Ihara Y, Taniguchi N, Ikenaga H, Takeuchi M (1997) Purifi cation and characterization of UDP-N-Acetylglucosamine: Alpha1,3-D-mannoside beta 1,4-N-Acetylglucosaminyltransferase (N-Acetylglucosaminyltransferase-IV) from bovine small intestine. J Biol Chem 272:22721-22727
    • (1997) J Biol Chem , vol.272 , pp. 22721-22727
    • Oguri, S.1    Minowa, M.T.2    Ihara, Y.3    Taniguchi, N.4    Ikenaga, H.5    Takeuchi, M.6
  • 7
    • 0027196125 scopus 로고
    • Purifi cation and characterization of UDP-Nacetylglucosamine: Alpha-6-D-mannoside beta 1-6 N-Acetylglucosaminyltransferase (N-Acetylglucosaminyltransferase V) from a human lung cancer cell line
    • Gu J, Nishikawa A, Tsuruoka N, Ohno M, Yamaguchi N, Kangawa K, Taniguchi N (1993) Purifi cation and characterization of UDP-Nacetylglucosamine: Alpha-6-D-mannoside beta 1-6 N-Acetylglucosaminyltransferase (N-Acetylglucosaminyltransferase V) from a human lung cancer cell line. J Biochem 113:614-619
    • (1993) J Biochem , vol.113 , pp. 614-619
    • Gu, J.1    Nishikawa, A.2    Tsuruoka, N.3    Ohno, M.4    Yamaguchi, N.5    Kangawa, K.6    Taniguchi, N.7
  • 8
    • 33749166219 scopus 로고    scopus 로고
    • Kinetic properties and substrate specifi cities of two recombinant human N-Acetylglucosaminyltransferase-IV isozymes
    • Oguri S, Yoshida A, Minowa MT, Takeuchi M (2006) Kinetic properties and substrate specifi cities of two recombinant human N- Acetylglucosaminyltransferase-IV isozymes. Glycoconj J 23:473-480
    • (2006) Glycoconj J , vol.23 , pp. 473-480
    • Oguri, S.1    Yoshida, A.2    Minowa, M.T.3    Takeuchi, M.4
  • 9
    • 29244449332 scopus 로고    scopus 로고
    • Dietary and genetic control of glucose transporter-2 glycosylation promotes insulin secretion in suppressing diabetes
    • Ohtsubo K, Takamatsu S, Minowa MT, Yoshida A, Takeuchi M, Marth JD (2005) Dietary and genetic control of glucose transporter-2 glycosylation promotes insulin secretion in suppressing diabetes. Cell 123: 1307-1321
    • (2005) Cell , vol.123 , pp. 1307-1321
    • Ohtsubo, K.1    Takamatsu, S.2    Minowa, M.T.3    Yoshida, A.4    Takeuchi, M.5    Marth, J.D.6
  • 10
    • 80052433997 scopus 로고    scopus 로고
    • Pathway to diabetes through attenuation of pancreatic beta cell glycosylation and glucose transport
    • Ohtsubo K, Chen MZ, Olefsky JM, Marth JD (2011) Pathway to diabetes through attenuation of pancreatic beta cell glycosylation and glucose transport. Nat Med 17:1067-1075
    • (2011) Nat Med , vol.17 , pp. 1067-1075
    • Ohtsubo, K.1    Chen, M.Z.2    Olefsky, J.M.3    Marth, J.D.4
  • 11
    • 9144252532 scopus 로고    scopus 로고
    • N-Acetylglucosaminyltransferase IX acts on the GlcNAcß1,2- Manα1-Ser/Thr moiety, forming a 2,6-branched structure in brain O-mannosyl glycan
    • Inamori K, Endo T, Gu J, Matsuo I, Ito Y, Fujii S, Iwasaki H, Narimatsu H, Miyoshi E, Honke K, Taniguchi N (2004) N-Acetylglucosaminyltransferase IX acts on the GlcNAcß1,2-Manα1-Ser/Thr moiety, forming a 2,6-branched structure in brain O-mannosyl glycan. J Biol Chem 279:2337-2340
    • (2004) J Biol Chem , vol.279 , pp. 2337-2340
    • Inamori, K.1    Endo, T.2    Gu, J.3    Matsuo, I.4    Ito, Y.5    Fujii, S.6    Iwasaki, H.7    Narimatsu, H.8    Miyoshi, E.9    Honke, K.10    Taniguchi, N.11
  • 12
    • 57749114758 scopus 로고    scopus 로고
    • Receptor tyrosine phosphatase β (RPTPβ) activity and signaling are attenuated by glycosylation and subsequent cell surface galectin-1 binding
    • Abbott KL, Matthews RT, Pierce M (2008) Receptor tyrosine phosphatase β (RPTPβ) activity and signaling are attenuated by glycosylation and subsequent cell surface galectin-1 binding. J Biol Chem 283: 33026-33035
    • (2008) J Biol Chem , vol.283 , pp. 33026-33035
    • Abbott, K.L.1    Matthews, R.T.2    Pierce, M.3
  • 13
    • 0018163581 scopus 로고
    • Structure analyses of oligosaccharides by tagging of the reducing end sugars with a fluorescent compound
    • Hase S, Ikenaka T, Matsushima Y (1978) Structure analyses of oligosaccharides by tagging of the reducing end sugars with a fl uorescent compound. Biochem Biophys Res Commun 85:257-263
    • (1978) Biochem Biophys Res Commun , vol.85 , pp. 257-263
    • Hase, S.1    Ikenaka, T.2    Matsushima, Y.3
  • 14
    • 0021308647 scopus 로고
    • Reexamination of the pyridylamination used for fl uorescence labeling of oligosaccharides and its application to glycoproteins
    • Hase S, Ibuki T, Ikenaka T (1984) Reexamination of the pyridylamination used for fl uorescence labeling of oligosaccharides and its application to glycoproteins. J Biochem 95:197-203
    • (1984) J Biochem , vol.95 , pp. 197-203
    • Hase, S.1    Ibuki, T.2    Ikenaka, T.3
  • 15
    • 0024840851 scopus 로고
    • Glycosyltransferase assays using pyridylaminated acceptors: N-Acetylglucosaminyltransferase III, IV, and -Rfvn1
    • Taniguchi N, Nishikawa A, Fujii S, Gu JG (1989) Glycosyltransferase assays using pyridylaminated acceptors: N-Acetylglucosaminyltransferase III, IV, and V. Methods Enzymol 179:397-408
    • (1989) Methods Enzymol , vol.179 , pp. 397-408
    • Taniguchi, N.1    Nishikawa, A.2    Fujii, S.3    Gu, J.G.4
  • 16
    • 0031975312 scopus 로고    scopus 로고
    • A method for determination of UDP-GlcNAc:GlcNAcß1-6(GlcNAcß1- 2)Manα1-R [GlcNAc to Man β1-4 N-Acetylglucosaminyltransferase VI activity using a pyridylaminated tetraantennary oligosaccharide as an acceptor substrate
    • Taguchi T, Ogawa T, Kitajima K, Inoue S, Inoue Y, Ihara Y, Sakamoto Y, Nagai K, Taniguchi N (1998) A method for determination of UDP-GlcNAc: GlcNAcß1-6(GlcNAcß1-2)Manα1-R [GlcNAc to Man] β1-4 N-Acetylglucosaminyltransferase VI activity using a pyridylaminated tetraantennary oligosaccharide as an acceptor substrate. Anal Biochem 255:155-157
    • (1998) Anal Biochem , vol.255 , pp. 155-157
    • Taguchi, T.1    Ogawa, T.2    Kitajima, K.3    Inoue, S.4    Inoue, Y.5    Ihara, Y.6    Sakamoto, Y.7    Nagai, K.8    Taniguchi, N.9
  • 17
    • 0029927882 scopus 로고    scopus 로고
    • Large scale preparation of PA-oligosaccharides from glycoproteins using an improved extraction method
    • Tokugawa K, Oguri S, Takeuchi M (1996) Large scale preparation of PA-oligosaccharides from glycoproteins using an improved extraction method. Glycoconj J 13:53-56
    • (1996) Glycoconj J. , vol.13 , pp. 53-56
    • Tokugawa, K.1    Oguri, S.2    Takeuchi, M.3
  • 19
    • 33749946901 scopus 로고
    • Colorimetric method for determination of sugars and related substances
    • Dubois M, Gilles K, Hamilton JK, Rebers PA, Smith F (1956) Colorimetric method for determination of sugars and related substances. Anal Chem 28:350-356
    • (1956) Anal Chem , vol.28 , pp. 350-356
    • Dubois, M.1    Gilles, K.2    Hamilton, J.K.3    Rebers, P.A.4    Smith, F.5
  • 20
    • 0031616461 scopus 로고    scopus 로고
    • Analysis of N-And O-glycans by pyridylamination
    • Natsuka S, Hase S (1998) Analysis of N-And O-glycans by pyridylamination. Methods Mol Biol 76:101-113
    • (1998) Methods Mol Biol , vol.76 , pp. 101-113
    • Natsuka, S.1    Hase, S.2
  • 21
    • 0032486374 scopus 로고    scopus 로고
    • Gain-of-function Chinese hamster ovary mutants Lec18 and Lec14 each express a novel N-Acetylglucosaminyltransferase activity
    • Raju TS, Stanley P (1998) Gain-of-function Chinese hamster ovary mutants Lec18 and Lec14 each express a novel N-Acetylglucosaminyltransferase activity. J Biol Chem 273:14090-14098 Japan
    • (1998) J Biol Chem , vol.273 , pp. 14090-14098
    • Raju, T.S.1    Stanley, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.