메뉴 건너뛰기




Volumn 12, Issue 9, 2013, Pages 2468-2480

Mass isotopomer analysis of metabolically labeled nucleotide sugars and N-and O-glycans for tracing nucleotide sugar metabolisms

Author keywords

[No Author keywords available]

Indexed keywords

CARBON 13; CELL PROTEIN; GLUCOSAMINE; GLUCOSE; GLYCAN; GLYCOSYLTRANSFERASE; HYALURONIC ACID; ISOTOPE; N ACETYLGALACTOSAMINE; N ACETYLGLUCOSAMINE; NUCLEOTIDE; SUGAR; URIDINE DIPHOSPHATE;

EID: 84884382622     PISSN: 15359476     EISSN: 15359484     Source Type: Journal    
DOI: 10.1074/mcp.M112.027151     Document Type: Article
Times cited : (30)

References (40)
  • 1
    • 33748195979 scopus 로고    scopus 로고
    • Glycosylation in Cellular Mechanisms of Health and Disease
    • DOI 10.1016/j.cell.2006.08.019, PII S0092867406010865
    • Ohtsubo, K., and Marth, J. D. (2006) Glycosylation in cellular mechanisms of health and disease. Cell 126, 855-867 (Pubitemid 44310784)
    • (2006) Cell , vol.126 , Issue.5 , pp. 855-867
    • Ohtsubo, K.1    Marth, J.D.2
  • 2
    • 0036677372 scopus 로고    scopus 로고
    • Glycosylation defining cancer malignancy: New wine in an old bottle
    • Hakomori, S. (2002) Glycosylation defining cancer malignancy: new wine in an old bottle. Proc. Natl. Acad. Sci. U.S.A. 99, 10231-10233
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 10231-10233
    • Hakomori, S.1
  • 3
    • 71749098786 scopus 로고    scopus 로고
    • From the gamma-glutamyl cycle to the glycan cycle: A road with many turns and pleasant surprises
    • Taniguchi, N. (2009) From the gamma-glutamyl cycle to the glycan cycle: a road with many turns and pleasant surprises. J. Biol. Chem. 284, 34469-34478
    • (2009) J. Biol. Chem. , vol.284 , pp. 34469-34478
    • Taniguchi, N.1
  • 5
    • 77956396629 scopus 로고    scopus 로고
    • O-glcnac signaling: A metabolic link between diabetes and cancer?
    • Slawson, C., Copeland, R. J., and Hart, G. W. (2010) O-GlcNAc signaling: a metabolic link between diabetes and cancer? Trends Biochem. Sci. 35, 547-555
    • (2010) Trends Biochem. Sci. , vol.35 , pp. 547-555
    • Slawson, C.1    Copeland, R.J.2    Hart, G.W.3
  • 6
    • 0030884451 scopus 로고    scopus 로고
    • Purification and characterization of UDP-N-acetylglucosamine: α1,3-D- mannoside β1,4-N-acetylglucosaminyltransferase (N- acetylglucosaminyltransferase-IV) from bovine small intestine
    • DOI 10.1074/jbc.272.36.22721
    • Oguri, S., Minowa, M. T., Ihara, Y., Taniguchi, N., Ikenaga, H., and Takeuchi, M. (1997) Purification and characterization of UDP-N- Acetylglucosamine: alpha1,3-D-mannoside beta1,4-N-Acetylglucosaminyltransferase (N-Acetylglucosaminyltransferase-IV) from bovine small intestine. J. Biol. Chem. 272, 22721-22727 (Pubitemid 27386089)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.36 , pp. 22721-22727
    • Oguri, S.1    Minowa, M.T.2    Ihara, Y.3    Taniguchi, N.4    Ikenaga, H.5    Takeuchi, M.6
  • 7
    • 0036233290 scopus 로고    scopus 로고
    • UDP-GlcNAc concentration is an important factor in the biosynthesis of β1,6-branched oligosaccharides: Regulation based on the kinetic properties of N-acetylglucosaminyltransferase V
    • Sasai, K., Ikeda, Y., Fujii, T., Tsuda, T., and Taniguchi, N. (2002) UDPGlcNAc concentration is an important factor in the biosynthesis of beta1,6-branched oligosaccharides: regulation based on the kinetic properties of N-Acetylglucosaminyltransferase V. Glycobiology 12, 119-127 (Pubitemid 34428935)
    • (2002) Glycobiology , vol.12 , Issue.2 , pp. 119-127
    • Sasai, K.1    Ikeda, Y.2    Fujii, T.3    Tsuda, T.4    Taniguchi, N.5
  • 9
    • 0033591388 scopus 로고    scopus 로고
    • UDP-GlcNAc 2-Epimerase: A regulator of cell surface sialylation
    • DOI 10.1126/science.284.5418.1372
    • Keppler, O. T., Hinderlich, S., Langner, J., Schwartz-Albiez, R., Reutter, W., and Pawlita, M. (1999) UDP-GlcNAc 2-epimerase: a regulator of cell surface sialylation. Science 284, 1372-1376 (Pubitemid 29289666)
    • (1999) Science , vol.284 , Issue.5418 , pp. 1372-1376
    • Keppler, O.T.1    Hinderlich, S.2    Langner, J.3    Schwartz-Albiez, R.4    Reutter, W.5    Pawlita, M.6
  • 10
    • 0015503856 scopus 로고
    • Uridine diphosphate n-Acetyl-dglucosamine-2-epimerase from rat liver. I. Catalytic and regulatory properties
    • Sommar, K. M., and Ellis, D. B. (1972) Uridine diphosphate N-Acetyl-Dglucosamine-2-epimerase from rat liver. I. Catalytic and regulatory properties. Biochim. Biophys. Acta 268, 581-589
    • (1972) Biochim. Biophys. Acta , vol.268 , pp. 581-589
    • Sommar, K.M.1    Ellis, D.B.2
  • 12
    • 34447276204 scopus 로고    scopus 로고
    • Direct measurement of isotopomer of intracellular metabolites using capillary electrophoresis time-of-flight mass spectrometry for efficient metabolic flux analysis
    • DOI 10.1016/j.chroma.2007.04.011, PII S0021967307006760
    • Toya, Y., Ishii, N., Hirasawa, T., Naba, M., Hirai, K., Sugawara, K., Igarashi, S., Shimizu, K., Tomita, M., and Soga, T (2007) Direct measurement of isotopomer of intracellular metabolites using capillary electrophoresis time-of-flight mass spectrometry for efficient metabolic flux analysis. J. Chromatogr. A. 1159, 134-141 (Pubitemid 47048250)
    • (2007) Journal of Chromatography A , vol.1159 , Issue.1-2 , pp. 134-141
    • Toya, Y.1    Ishii, N.2    Hirasawa, T.3    Naba, M.4    Hirai, K.5    Sugawara, K.6    Igarashi, S.7    Shimizu, K.8    Tomita, M.9    Soga, T.10
  • 13
    • 82455175716 scopus 로고    scopus 로고
    • Insights into neuronal cell metabolism using nmr spectroscopy: Uridyl diphosphate n-Acetylglucosamine as a unique metabolic marker
    • Gallinger, A., Biet, T., Pellerin, L., and Peters, T (2011) Insights into neuronal cell metabolism using NMR Spectroscopy: Uridyl diphosphate N-Acetylglucosamine as a unique metabolic marker. Angew. Chem. Int. Ed. 50, 1-4
    • (2011) Angew. Chem. Int. Ed. , vol.50 , pp. 1-4
    • Gallinger, A.1    Biet, T.2    Pellerin, L.3    Peters, T.4
  • 15
    • 79957630849 scopus 로고    scopus 로고
    • A novel deconvolution method for modeling udp-n-Acetyl-dglucosamine biosynthetic pathways based on 13c mass isotopologue profiles under non-steady-state conditions
    • Moseley, H. N., Lane, A. N., Belshoff, A. C., Higashi, R. M., and Fan, T. W. (2011) A novel deconvolution method for modeling UDP-N-Acetyl-Dglucosamine biosynthetic pathways based on 13C mass isotopologue profiles under non-steady-state conditions. BMC Biol. 9, 37
    • (2011) BMC Biol. , vol.9 , pp. 37
    • Moseley, H.N.1    Lane, A.N.2    Belshoff, A.C.3    Higashi, R.M.4    Fan, T.W.5
  • 16
    • 69249113498 scopus 로고    scopus 로고
    • Metabolic radiolabeling of animal cell glycoconjugates
    • Diaz. S., and Varki. A. (2009) Metabolic radiolabeling of animal cell glycoconjugates. Curr. Protoc. Protein Sci. 12, 1-55
    • (2009) Curr. Protoc. Protein Sci. , vol.12 , pp. 1-55
    • Diaz, S.1    Varki, A.2
  • 19
    • 0025281303 scopus 로고
    • Establishment of a pancreatic β cell line that retains glucose-inducible insulin secretion: Special reference to expression of glucose transporter isoforms
    • Miyazaki, J., Araki, K., Yamato, E., Ikegami, H., Asano, T., Shibasaki, Y., Oka, Y., and Yamamura, K. (1990) Establishment of a pancreatic beta cell line that retains glucose-inducible insulin secretion: special reference to expression of glucose transporter isoforms. Endocrinology 127, 126-132 (Pubitemid 20228111)
    • (1990) Endocrinology , vol.127 , Issue.1 , pp. 126-132
    • Miyazaki, J.-I.1    Araki, K.2    Yamato, E.3    Ikegami, H.4    Asano, T.5    Shibasaki, Y.6    Oka, Y.7    Yamamura, K.-I.8
  • 20
    • 34547911022 scopus 로고    scopus 로고
    • Sugar nucleotide pools of Trypanosoma brucei, Trypanosoma cruzi, and Leishmania major
    • DOI 10.1128/EC.00175-07
    • Turnock, D. C., and Ferguson, M. A. (2007) Sugar nucleotide pools of Trypanosoma brucei, Trypanosoma cruzi, and Leishmania major. Eukaryot. Cell 8, 1450-1463 (Pubitemid 47257714)
    • (2007) Eukaryotic Cell , vol.6 , Issue.8 , pp. 1450-1463
    • Turnock, D.C.1    Ferguson, M.A.J.2
  • 21
    • 61849124194 scopus 로고    scopus 로고
    • Comparative studies on the structural features of o-glycans between leukemia and epithelial cell lines
    • Yamada, K., Kinoshita, M., Hayakawa, T., Nakaya, S., and Kakehi, K. (2009) Comparative studies on the structural features of O-Glycans between leukemia and epithelial cell lines. J. Proteome Res. 8, 521-537
    • (2009) J. Proteome Res. , vol.8 , pp. 521-537
    • Yamada, K.1    Kinoshita, M.2    Hayakawa, T.3    Nakaya, S.4    Kakehi, K.5
  • 22
    • 0036874367 scopus 로고    scopus 로고
    • Sequential analysis of N- and O-linked glycosylation of 2D-PAGE separated glycoproteins
    • DOI 10.1021/pr025538d
    • Wilson, N. L., Schulz, B. L., Karlsson, N. G., and Packer, N. H. (2002) Sequential analysis of N-And O-linked glycosylation of 2D-PAGE separated glycoproteins. J. Proteome Res. 1, 521-529 (Pubitemid 36395851)
    • (2002) Journal of Proteome Research , vol.1 , Issue.6 , pp. 521-529
    • Wilson, N.L.1    Schulz, B.L.2    Karlsson, N.G.3    Packer, N.H.4
  • 23
    • 80555136756 scopus 로고    scopus 로고
    • Identification of glycan structure alterations on cell membrane proteins in desoxyepothilone b resistant leukemia cells
    • Nakano, M., Saldanha, R., Gobel, A., Kavallaris, M., and Packer, N. H. (2011) Identification of glycan structure alterations on cell membrane proteins in desoxyepothilone B resistant leukemia cells. Mol. Cell. Proteomics 10, 11, M111009001
    • (2011) Mol. Cell. Proteomics , vol.10 , Issue.11
    • Nakano, M.1    Saldanha, R.2    Gobel, A.3    Kavallaris, M.4    Packer, N.H.5
  • 25
    • 0018163581 scopus 로고
    • Structure analyses of oligosaccharides by tagging of the reducing end sugars with a fluorescent compound
    • Hase, S., Ikenaka, T., and Matsushima, Y. (1978) Structure analyses of oligosaccharides by tagging of the reducing end sugars with a fluorescent compound. Biochem. Biophys. Res. Commun., 85, 257-263 (Pubitemid 9073177)
    • (1978) Biochemical and Biophysical Research Communications , vol.85 , Issue.1 , pp. 257-263
    • Hase, S.1    Ikenaka, T.2    Matsushima, Y.3
  • 26
    • 0029927882 scopus 로고    scopus 로고
    • Large scale preparation of PA-oligosaccharides from glycoproteins using an improved extraction method
    • DOI 10.1007/BF01049679
    • Tokugawa, K., Oguri, S., and Takeuchi, M. (1996) Large scale preparation of PA-oligosaccharides from glycoproteins using an improved extraction method. Glycoconj. J. 13, 53-56 (Pubitemid 26074301)
    • (1996) Glycoconjugate Journal , vol.13 , Issue.1 , pp. 53-56
    • Tokugawa, K.1    Oguri, S.2    Takeuchi, M.3
  • 27
    • 0028207949 scopus 로고
    • High-performance liquid chromatography of pyridylaminated saccharides
    • Hase, S. (1994) High-performance liquid chromatography of pyridylaminated saccharides. Methods Enzymol. 230, 225-237
    • (1994) Methods Enzymol. , vol.230 , pp. 225-237
    • Hase, S.1
  • 29
    • 77951531555 scopus 로고    scopus 로고
    • Dynamics and control of the central carbon metabolism in hepatoma cells
    • Maier, K., Hofmann, U., Reuss, M., and Mauch, K. (2010) Dynamics and control of the central carbon metabolism in hepatoma cells. BMC Syst. Biol. 4, 54
    • (2010) BMC Syst. Biol. , vol.4 , pp. 54
    • Maier, K.1    Hofmann, U.2    Reuss, M.3    Mauch, K.4
  • 31
    • 29244449332 scopus 로고    scopus 로고
    • Dietary and genetic control of glucose transporter 2 glycosylation promotes insulin secretion in suppressing diabetes
    • DOI 10.1016/j.cell.2005.09.041, PII S0092867405011712
    • Ohtsubo, K., Takamatsu, S., Minowa, M. T., Yoshida, A., Takeuchi, M., and Marth, J. D. (2005) Dietary and genetic control of glucose transporter 2 glycosylation promotes insulin secretion in suppressing diabetes. Cell 123, 1307-1321 (Pubitemid 41821787)
    • (2005) Cell , vol.123 , Issue.7 , pp. 1307-1321
    • Ohtsubo, K.1    Takamatsu, S.2    Minowa, M.T.3    Yoshida, A.4    Takeuchi, M.5    Marth, J.D.6
  • 32
    • 80052433997 scopus 로고    scopus 로고
    • Pathway to diabetes through attenuation of pancreatic beta cell glycosylation and glucose transport
    • Ohtsubo, K., Chen, M. Z., Olefsky, J. M., and Marth, J. D. (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
  • 34
    • 0025827497 scopus 로고
    • 3H]thymidine incorporations and staining of hyaluronan on mitotic keratinocytes
    • Tammi, R., and Tammi, M. (1991) Correlations between hyaluronan and epidermal proliferation as studied by [3H]glucosamine and [3H]thymidine incorporations and staining of hyaluronan on mitotic keratinocytes. Exp. Cell Res. 195, 524-527 (Pubitemid 121006355)
    • (1991) Experimental Cell Research , vol.195 , Issue.2 , pp. 524-527
    • Tammi, R.1    Tammi, M.2
  • 36
    • 44949083699 scopus 로고    scopus 로고
    • Detection and analysis of proteins modified by o-linked n-Acetylglucosamine
    • Zachara, N. E., Vosseller, K., Hart, G. W., and Gao, Y. (2001) Detection and analysis of proteins modified by O-linked N-Acetylglucosamine. Curr. Protoc. Protein Sci. 12, 8
    • (2001) Curr. Protoc. Protein Sci. , vol.12 , pp. 8
    • Zachara, N.E.1    Vosseller, K.2    Hart, G.W.3    Gao, Y.4
  • 37
    • 0032584299 scopus 로고    scopus 로고
    • Fundamental metabolic differences between hepatocytes and islet β- cells revealed by glucokinase overexpression
    • DOI 10.1021/bi9726133
    • Berman, H. K., and Newgard, C. B. (1998) Fundamental metabolic differences between hepatocytes and islet beta-cells revealed by glucokinase overexpression. Biochemistry 37, 4543-4552 (Pubitemid 28217173)
    • (1998) Biochemistry , vol.37 , Issue.13 , pp. 4543-4552
    • Berman, H.K.1    Newgard, C.B.2
  • 38
    • 80054092824 scopus 로고    scopus 로고
    • Synergizing metabolic flux analysis and nucleotide sugar metabolism to understand the control of glycosylation of recombinant protein in cho cells
    • Burleigh, S. C., van de Laar, T., Stroop, C. J., van Grunsven, W. M., O'Donoghue, N., Rudd, P. M., and Davey, G. P. (2011) Synergizing metabolic flux analysis and nucleotide sugar metabolism to understand the control of glycosylation of recombinant protein in CHO cells. BMC Biotechnol. 11, 95
    • (2011) BMC Biotechnol. , vol.11 , pp. 95
    • Burleigh, S.C.1    Van De Laar, T.2    Stroop, C.J.3    Van Grunsven, W.M.4    O'Donoghue, N.5    Rudd, P.M.6    Davey, G.P.7
  • 39
    • 24144491568 scopus 로고    scopus 로고
    • The intracellular concentration of sialic acid regulates the polysialylation of the neural cell adhesion molecule
    • DOI 10.1016/j.febslet.2005.08.013, PII S0014579305009919
    • Bork, K., Reutter, W., Gerardy-Schahn, R., and Horstkorte, R. (2005) The intracellular concentration of sialic acid regulates the polysialylation of the neural cell adhesion molecule. FEBS Lett. 579, 22, 5079-5083 (Pubitemid 41242856)
    • (2005) FEBS Letters , vol.579 , Issue.22 , pp. 5079-5083
    • Bork, K.1    Reutter, W.2    Gerardy-Schahn, R.3    Horstkorte, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.