메뉴 건너뛰기




Volumn 5, Issue 3, 2015, Pages 1810-1831

A panel of recombinant mucins carrying a repertoire of sialylated O-glycans based on different core chains for studies of glycan binding proteins

Author keywords

CHO; Core saccharide; Glycosyltransferase; Mucin; O glycans; Sialic acid

Indexed keywords

AGGLUTININ; COMPLEMENTARY DNA; GLYCAN; GLYCAN BINDING PROTEIN; GLYCOSYLTRANSFERASE; IMMUNOGLOBULIN G2B; MUCIN; P SELECTIN GLYCOPROTEIN LIGAND 1; PROTEIN; RECOMBINANT PROTEIN; SIALOPROTEIN; UNCLASSIFIED DRUG; HYBRID PROTEIN; MEMBRANE PROTEIN; N ACETYLNEURAMINIC ACID; P-SELECTIN LIGAND PROTEIN; POLYSACCHARIDE;

EID: 85012092914     PISSN: None     EISSN: 2218273X     Source Type: Journal    
DOI: 10.3390/biom5031810     Document Type: Article
Times cited : (14)

References (41)
  • 2
    • 0022973880 scopus 로고
    • Purification and characterization of UDP-N-acetylgalactosamine: Polypeptide N-acetylgalactosaminyltransferase from bovine colostrum and murine lymphoma BW5147 cells
    • Elhammer, A.; Kornfeld, S. Purification and characterization of UDP-N-acetylgalactosamine: Polypeptide N-acetylgalactosaminyltransferase from bovine colostrum and murine lymphoma BW5147 cells. J. Biol. Chem. 1986, 261, 5249-5255.
    • (1986) J. Biol. Chem , vol.261 , pp. 5249-5255
    • Elhammer, A.1    Kornfeld, S.2
  • 3
    • 22844433667 scopus 로고    scopus 로고
    • The chemistry and biology of mucin-type O-linked glycosylation
    • Hang, H.C.; Bertozzi, C.R. The chemistry and biology of mucin-type O-linked glycosylation. Bioorg. Med. Chem. 2005, 13, 5021-5034.
    • (2005) Bioorg. Med. Chem , vol.13 , pp. 5021-5034
    • Hang, H.C.1    Bertozzi, C.R.2
  • 4
    • 0030006293 scopus 로고    scopus 로고
    • O-linked protein glycosylation structure and function
    • Hounsell, E.F.; Davies, M.J.; Renouf, D.V. O-linked protein glycosylation structure and function. Glycoconj. J. 1996, 13, 19-26.
    • (1996) Glycoconj. J , vol.13 , pp. 19-26
    • Hounsell, E.F.1    Davies, M.J.2    Renouf, D.V.3
  • 5
    • 62449106207 scopus 로고    scopus 로고
    • Recent insights into the biological roles of mucin-type O-glycosylation
    • Tian, E.; Ten Hagen, K.G. Recent insights into the biological roles of mucin-type O-glycosylation. Glycoconj. J. 2009, 26, 325-334.
    • (2009) Glycoconj. J , vol.26 , pp. 325-334
    • Tian, E.1    Ten Hagen, K.G.2
  • 6
    • 0032759101 scopus 로고    scopus 로고
    • Identification and characterization of large galactosyltransferase gene families: Galactosyltransferases for all functions
    • Amado, M.; Almeida, R.; Schwientek, T.; Clausen, H. Identification and characterization of large galactosyltransferase gene families: Galactosyltransferases for all functions. Biochim. Biophys. Acta 1999, 1473, 35-53.
    • (1999) Biochim. Biophys. Acta , vol.1473 , pp. 35-53
    • Amado, M.1    Almeida, R.2    Schwientek, T.3    Clausen, H.4
  • 7
    • 77649206380 scopus 로고    scopus 로고
    • Structure and biological roles of mucin-type O-glycans at the ocular surface
    • Guzman-Aranguez, A.; Argueso, P. Structure and biological roles of mucin-type O-glycans at the ocular surface. Ocul. Surf. 2010, 8, 8-17.
    • (2010) Ocul. Surf , vol.8 , pp. 8-17
    • Guzman-Aranguez, A.1    Argueso, P.2
  • 8
    • 48149090000 scopus 로고    scopus 로고
    • Sialic acids in human health and disease
    • Varki, A. Sialic acids in human health and disease. Trends Mol. Med. 2008, 14, 351-360.
    • (2008) Trends Mol. Med , vol.14 , pp. 351-360
    • Varki, A.1
  • 9
    • 0030993576 scopus 로고    scopus 로고
    • Sialic acids as ligands in recognition phenomena
    • Varki, A. Sialic acids as ligands in recognition phenomena. FASEB J. 1997, 11, 248-255.
    • (1997) FASEB J , vol.11 , pp. 248-255
    • Varki, A.1
  • 10
    • 15244351686 scopus 로고    scopus 로고
    • Receptor specificity of influenza viruses from birds and mammals: New data on involvement of the inner fragments of the carbohydrate chain
    • Gambaryan, A.; Yamnikova, S.; Lvov, D.; Tuzikov, A.; Chinarev, A.; Pazynina, G.; Webster, R.; Matrosovich, M.; Bovin, N. Receptor specificity of influenza viruses from birds and mammals: New data on involvement of the inner fragments of the carbohydrate chain. Virology 2005, 334, 276-283.
    • (2005) Virology , vol.334 , pp. 276-283
    • Gambaryan, A.1    Yamnikova, S.2    Lvov, D.3    Tuzikov, A.4    Chinarev, A.5    Pazynina, G.6    Webster, R.7    Matrosovich, M.8    Bovin, N.9
  • 12
    • 29444433087 scopus 로고    scopus 로고
    • Glycan microarray analysis of the hemagglutinins from modern and pandemic influenza viruses reveals different receptor specificities
    • Stevens, J.; Blixt, O.; Glaser, L.; Taubenberger, J.K.; Palese, P.; Paulson, J.C.; Wilson, I.A. Glycan microarray analysis of the hemagglutinins from modern and pandemic influenza viruses reveals different receptor specificities. J. Mol. Biol. 2006, 355, 1143-1155.
    • (2006) J. Mol. Biol , vol.355 , pp. 1143-1155
    • Stevens, J.1    Blixt, O.2    Glaser, L.3    Taubenberger, J.K.4    Palese, P.5    Paulson, J.C.6    Wilson, I.A.7
  • 15
    • 18744365774 scopus 로고    scopus 로고
    • Enterovirus 70 binds to different glycoconjugates containing α2,3-linked sialic acid on different cell lines
    • Nokhbeh, M.R.; Hazra, S.; Alexander, D.A.; Khan, A.; McAllister, M.; Suuronen, E.J.; Griffith, M.; Dimock, K. Enterovirus 70 binds to different glycoconjugates containing α2,3-linked sialic acid on different cell lines. J. Virol. 2005, 79, 7087-7094.
    • (2005) J. Virol , vol.79 , pp. 7087-7094
    • Nokhbeh, M.R.1    Hazra, S.2    Alexander, D.A.3    Khan, A.4    McAllister, M.5    Suuronen, E.J.6    Griffith, M.7    Dimock, K.8
  • 16
    • 0026062477 scopus 로고
    • Detection and functions of mammalian lectins-With emphasis on membrane lectins
    • Gabius, H.-J. Detection and functions of mammalian lectins-With emphasis on membrane lectins. Biochim. Biophys. Acta 1991, 1071, 1-18.
    • (1991) Biochim. Biophys. Acta , vol.1071 , pp. 1-18
    • Gabius, H.-J.1
  • 17
    • 84875978675 scopus 로고    scopus 로고
    • Global comparisons of lectin-glycan interactions using a database of analyzed glycan array data
    • Kletter, D.; Singh, S.; Bern, M.; Haab, B.B. Global comparisons of lectin-glycan interactions using a database of analyzed glycan array data. Mol. Cell. Proteomics 2013, 12, 1026-1035.
    • (2013) Mol. Cell. Proteomics , vol.12 , pp. 1026-1035
    • Kletter, D.1    Singh, S.2    Bern, M.3    Haab, B.B.4
  • 18
    • 84924081123 scopus 로고    scopus 로고
    • O-glycan repertoires on a mucin-type reporter protein expressed in CHO cell pools transiently transfected with O-glycan core enzyme cDNAs
    • Liu, J.; Jin, C.; Cherian, R.M.; Karlsson, N.G.; Holgersson, J. O-glycan repertoires on a mucin-type reporter protein expressed in CHO cell pools transiently transfected with O-glycan core enzyme cDNAs. J. Biotechnol. 2015, 199, 77-89.
    • (2015) J. Biotechnol , vol.199 , pp. 77-89
    • Liu, J.1    Jin, C.2    Cherian, R.M.3    Karlsson, N.G.4    Holgersson, J.5
  • 19
    • 0033127471 scopus 로고    scopus 로고
    • Structure and function of the selectin ligand PSGL-1
    • Cummings, R.D. Structure and function of the selectin ligand PSGL-1. Braz. J. Med. Biol. Res. 1999, 32, 519-528.
    • (1999) Braz. J. Med. Biol. Res , vol.32 , pp. 519-528
    • Cummings, R.D.1
  • 20
    • 0030916762 scopus 로고    scopus 로고
    • Removal of xenoreactive human anti-pig antibodies by absorption on recombinant mucin-containing glycoproteins carrying the Gal alpha1,3Gal epitope
    • Liu, J.; Qian, Y.; Holgersson, J. Removal of xenoreactive human anti-pig antibodies by absorption on recombinant mucin-containing glycoproteins carrying the Gal alpha1,3Gal epitope. Transplantation 1997, 63, 1673-1682.
    • (1997) Transplantation , vol.63 , pp. 1673-1682
    • Liu, J.1    Qian, Y.2    Holgersson, J.3
  • 22
    • 33745613801 scopus 로고    scopus 로고
    • Glycosyltransferases involved in type 1 chain and Lewis antigen biosynthesis exhibit glycan and core chain specificity
    • Holgersson, J.; Löfling, J. Glycosyltransferases involved in type 1 chain and Lewis antigen biosynthesis exhibit glycan and core chain specificity. Glycobiology 2006, 16, 584-593.
    • (2006) Glycobiology , vol.16 , pp. 584-593
    • Holgersson, J.1    Löfling, J.2
  • 23
    • 45749135061 scopus 로고    scopus 로고
    • Studies of Lewis antigens and H. pylori adhesion in CHO cell lines engineered to express Lewis b determinants
    • Löfling, J.; Diswall, M.; Eriksson, S.; Borén, T.; Breimer, M.E.; Holgersson, J. Studies of Lewis antigens and H. pylori adhesion in CHO cell lines engineered to express Lewis b determinants. Glycobiology 2008, 18, 494-501.
    • (2008) Glycobiology , vol.18 , pp. 494-501
    • Löfling, J.1    Diswall, M.2    Eriksson, S.3    Borén, T.4    Breimer, M.E.5    Holgersson, J.6
  • 24
    • 59449101143 scopus 로고    scopus 로고
    • Core saccharide dependence of sialyl Lewis X biosynthesis
    • Lofling, J.; Holgersson, J. Core saccharide dependence of sialyl Lewis X biosynthesis. Glycoconj. J. 2009, 26, 33-40.
    • (2009) Glycoconj. J , vol.26 , pp. 33-40
    • Lofling, J.1    Holgersson, J.2
  • 25
    • 24044514683 scopus 로고    scopus 로고
    • Anti-pig antibody adsorption efficacy of α-Gal carrying recombinant P-selectin glycoprotein ligand-1/immunoglobulin chimeras increases with core 2 α1, 6-N-acetylglucosaminyltransferase expression
    • Liu, J.; Gustafsson, A.; Breimer, M.E.; Kussak, A.; Holgersson, J. Anti-pig antibody adsorption efficacy of α-Gal carrying recombinant P-selectin glycoprotein ligand-1/immunoglobulin chimeras increases with core 2 α1, 6-N-acetylglucosaminyltransferase expression. Glycobiology 2005, 15, 571-583.
    • (2005) Glycobiology , vol.15 , pp. 571-583
    • Liu, J.1    Gustafsson, A.2    Breimer, M.E.3    Kussak, A.4    Holgersson, J.5
  • 26
    • 84890419928 scopus 로고    scopus 로고
    • Shiga-like toxin binds with high avidity to multivalent O-linked blood group P1 determinants on mucin-type fusion proteins
    • Cherian, R.M.; Gaunitz, S.; Nilsson, A.; Liu, J.; Karlsson, N.G.; Holgersson, J. Shiga-like toxin binds with high avidity to multivalent O-linked blood group P1 determinants on mucin-type fusion proteins. Glycobiology 2014, 24, 26-38.
    • (2014) Glycobiology , vol.24 , pp. 26-38
    • Cherian, R.M.1    Gaunitz, S.2    Nilsson, A.3    Liu, J.4    Karlsson, N.G.5    Holgersson, J.6
  • 30
    • 0032848329 scopus 로고    scopus 로고
    • Genetic engineering of recombinant glycoproteins and the glycosylation pathway in mammalian host cells
    • Grabenhorst, E.; Schlenke, P.; Pohl, S.; Nimtz, M.; Conradt, H.S. Genetic engineering of recombinant glycoproteins and the glycosylation pathway in mammalian host cells. Glycoconj. J. 1999, 16, 81-97.
    • (1999) Glycoconj. J , vol.16 , pp. 81-97
    • Grabenhorst, E.1    Schlenke, P.2    Pohl, S.3    Nimtz, M.4    Conradt, H.S.5
  • 32
    • 33749044817 scopus 로고    scopus 로고
    • Human glycogene cloning: Focus on β3-glycosyltransferase and β4-glycosyltransferase families
    • Narimatsu, H. Human glycogene cloning: focus on β3-glycosyltransferase and β4-glycosyltransferase families. Curr. Opin. Struct. Biol. 2006, 16, 567-575.
    • (2006) Curr. Opin. Struct. Biol , vol.16 , pp. 567-575
    • Narimatsu, H.1
  • 33
    • 0021074339 scopus 로고
    • Regulatory mutations in CHO cells induce expression of the mouse embryonic antigen SSEA-1
    • Campbell, C.; Stanley, P. Regulatory mutations in CHO cells induce expression of the mouse embryonic antigen SSEA-1. Cell 1983, 35, 303-309.
    • (1983) Cell , vol.35 , pp. 303-309
    • Campbell, C.1    Stanley, P.2
  • 34
    • 0027457979 scopus 로고
    • Regulation of UDP-GlcNAc:Galβ1-3GalNAc-R β1-6-N-acetylglucosaminyltransferase (GlcNAc to GalNAc) in Chinese hamster ovary cells
    • Datti, A.; Dennis, J.W. Regulation of UDP-GlcNAc:Galβ1-3GalNAc-R β1-6-N-acetylglucosaminyltransferase (GlcNAc to GalNAc) in Chinese hamster ovary cells. J. Biol. Chem. 1993, 268, 5409-5416.
    • (1993) J. Biol. Chem , vol.268 , pp. 5409-5416
    • Datti, A.1    Dennis, J.W.2
  • 35
    • 0038920413 scopus 로고    scopus 로고
    • A family of human β3-galactosyltransferases: Characterization of four members of a UDP-galactose: β-N-acetyl-glucosamine/β-N-acetyl -galactosamine β-1,3-galactosyltransferase family
    • Amado, M.; Almeida, R.; Carneiro, F.; Levery, S.B.; Holmes, E.H.; Nomoto, M.; Hollingsworth, M.A.; Hassan, H.; Schwientek, T.; Nielsen, P.A.; et al. A family of human β3-galactosyltransferases: Characterization of four members of a UDP-galactose: β-N-acetyl-glucosamine/β-N-acetyl -galactosamine β-1,3-galactosyltransferase family. J. Biol. Chem. 1998, 273, 12770-12778.
    • (1998) J. Biol. Chem , vol.273 , pp. 12770-12778
    • Amado, M.1    Almeida, R.2    Carneiro, F.3    Levery, S.B.4    Holmes, E.H.5    Nomoto, M.6    Hollingsworth, M.A.7    Hassan, H.8    Schwientek, T.9    Nielsen, P.A.10
  • 36
    • 0034637408 scopus 로고    scopus 로고
    • Recombinant Galα1,3Gal-substituted mucin/immunoglobulin chimeras: A superior absorber of anti-pig antibodies
    • Liu, J.; Holgersson, J. Recombinant Galα1,3Gal-substituted mucin/immunoglobulin chimeras: A superior absorber of anti-pig antibodies. Transplant. Proc. 2000, doi:10.1016/S0041-1345(00)01010-1.
    • (2000) Transplant. Proc
    • Liu, J.1    Holgersson, J.2
  • 37
    • 0024206786 scopus 로고
    • A systematic nomenclature for carbohydrate fragmentations in FAB-MS/MS spectra of glycoconjugates
    • Domon, B.; Costello, C.E. A systematic nomenclature for carbohydrate fragmentations in FAB-MS/MS spectra of glycoconjugates. Glycoconj. J. 1988, 5, 397-409.
    • (1988) Glycoconj. J , vol.5 , pp. 397-409
    • Domon, B.1    Costello, C.E.2
  • 38
    • 84863197183 scopus 로고    scopus 로고
    • Detailed O-glycomics of the Muc2 mucin from colon of wild-type, core 1- and core 3-transferase -deficient mice highlights differences compared with human MUC2
    • Thomsson, K.A.; Holmén-Larsson, J.M.; Ångström, J.; Johansson, M.E.V.; Xia, L.; Hansson, G.C. Detailed O-glycomics of the Muc2 mucin from colon of wild-type, core 1- and core 3-transferase -deficient mice highlights differences compared with human MUC2. Glycobiology 2012, 22, 1128-1139.
    • (2012) Glycobiology , vol.22 , pp. 1128-1139
    • Thomsson, K.A.1    Holmén-Larsson, J.M.2    Ångström, J.3    Johansson, M.E.V.4    Xia, L.5    Hansson, G.C.6
  • 39
    • 0020491372 scopus 로고
    • Purification of a Gal α 1 to 4GlcNAc α 2 to 6 sialyltransferase and a Gal α 1 to 3(4)GlcNAc α 2 to 3 sialyltransferase to homogeneity from rat liver
    • Weinstein, J.; de Souza-e-Silva, U.; Paulson, J.C. Purification of a Gal α 1 to 4GlcNAc α 2 to 6 sialyltransferase and a Gal α 1 to 3(4)GlcNAc α 2 to 3 sialyltransferase to homogeneity from rat liver. J. Biol. Chem. 1982, 257, 13835-13844.
    • (1982) J. Biol. Chem , vol.257 , pp. 13835-13844
    • Weinstein, J.1    de Souza-e-Silva, U.2    Paulson, J.C.3
  • 41
    • 0036894272 scopus 로고    scopus 로고
    • Small-scale analysis of O-linked oligosaccharides from glycoproteins and mucins separated by gel electrophoresis
    • Schulz, B.L.; Packer, N.H.; Karlsson, N.G. Small-scale analysis of O-linked oligosaccharides from glycoproteins and mucins separated by gel electrophoresis. Anal. Chem. 2002, 74, 6088-6097.
    • (2002) Anal. Chem , vol.74 , pp. 6088-6097
    • Schulz, B.L.1    Packer, N.H.2    Karlsson, N.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.