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Volumn 22, Issue 9, 2012, Pages 1207-1217

Comparative study of the glycan specificities of cell-bound human tandem-repeat-type galectin-4,-8 and-9

Author keywords

blood group antigens; cell adhesion; galectins; glycan; glycomics

Indexed keywords

BLOOD GROUP ABH ANTIGEN; DISACCHARIDE; ECALECTIN; GALECTIN 4; GALECTIN 8; GLYCAN; LIGAND;

EID: 84864477387     PISSN: 09596658     EISSN: 14602423     Source Type: Journal    
DOI: 10.1093/glycob/cws079     Document Type: Article
Times cited : (50)

References (40)
  • 1
    • 48649102319 scopus 로고    scopus 로고
    • Calixnarene-based glycoclusters: Bioactivity of thiourea-linked galactose/lactose moieties as inhibitors of binding of medically relevant lectins to a glycoprotein and cell-surface glycoconjugates and selectivity among human adhesion/growth-regulatory galectins
    • André S, Sansone F, Kaltner H, Casnati A, Kopitz J, Gabius H-J, Ungaro R. 2008. Calixnarene-based glycoclusters: Bioactivity of thiourea-linked galactose/lactose moieties as inhibitors of binding of medically relevant lectins to a glycoprotein and cell-surface glycoconjugates and selectivity among human adhesion/growth-regulatory galectins. ChemBioChem. 9:1649-1661.
    • (2008) ChemBioChem , vol.9 , pp. 1649-1661
    • André, S.1    Sansone, F.2    Kaltner, H.3    Casnati, A.4    Kopitz, J.5    Gabius, H.-J.6    Ungaro, R.7
  • 3
    • 45549107987 scopus 로고    scopus 로고
    • Structural features of galectin-9 and galectin-1 that determine distinct T cell death pathways
    • Bi S, Earl LA, Jacobs L, Baum LG. 2008. Structural features of galectin-9 and galectin-1 that determine distinct T cell death pathways. J Biol Chem. 283:12248-12258.
    • (2008) J Biol Chem , vol.283 , pp. 12248-12258
    • Bi, S.1    Earl, L.A.2    Jacobs, L.3    Baum, L.G.4
  • 5
    • 0037136416 scopus 로고    scopus 로고
    • Galectinomics: Finding themes in complexity
    • Cooper DNW. 2002. Galectinomics: Finding themes in complexity. Biochim Biophys Acta. 1572:209-231.
    • (2002) Biochim Biophys Acta , vol.1572 , pp. 209-231
    • Cooper, D.N.W.1
  • 6
    • 67349234088 scopus 로고    scopus 로고
    • Galectin-8 interacts with podoplanin and modulates lymphatic endothelial cell functions
    • Cueni LN, Detmar M. 2009. Galectin-8 interacts with podoplanin and modulates lymphatic endothelial cell functions. Exp Cell Res. 315:1715-1723.
    • (2009) Exp Cell Res , vol.315 , pp. 1715-1723
    • Cueni, L.N.1    Detmar, M.2
  • 8
    • 0025076613 scopus 로고
    • Influence of type of linkage and spacer on the interaction of β-galactoside-binding proteins with immobilized affinity ligands
    • Gabius H-J. 1990. Influence of type of linkage and spacer on the interaction of β-galactoside-binding proteins with immobilized affinity ligands. Anal Biochem. 189:91-94.
    • (1990) Anal Biochem , vol.189 , pp. 91-94
    • Gabius, H.-J.1
  • 11
    • 77953572271 scopus 로고    scopus 로고
    • Hydrodynamic properties of human adhesion/growth-regulatory galectins studied by fluorescence correlation spectroscopy
    • Göhler A, André S, Kaltner H, Sauer M, Gabius H-J, Doose S. 2010. Hydrodynamic properties of human adhesion/growth-regulatory galectins studied by fluorescence correlation spectroscopy. Biophys J. 98:3044-3053.
    • (2010) Biophys J , vol.98 , pp. 3044-3053
    • Göhler, A.1    André, S.2    Kaltner, H.3    Sauer, M.4    Gabius, H.-J.5    Doose, S.6
  • 12
    • 79955915952 scopus 로고    scopus 로고
    • Routes in lectin evolution: Case study on the C-type lectin-like domains
    • Gabius H-J, editor Weinheim (Germany): Wiley, VCH
    • Gready JN, Zelensky AN. 2009. Routes in lectin evolution: case study on the C-type lectin-like domains. In: Gabius H-J, editor. The Sugar Code. Fundamentals of Glycosciences. Weinheim (Germany): Wiley-VCH. p. 329-346.
    • (2009) The Sugar Code. Fundamentals of Glycosciences , pp. 329-346
    • Gready, J.N.1    Zelensky, A.N.2
  • 16
    • 4143128862 scopus 로고    scopus 로고
    • Galectin-4 in normal tissue and cancer
    • Huflejt M, Leffler H. 2004. Galectin-4 in normal tissue and cancer. Glycoconj J. 20:247-255.
    • (2004) Glycoconj J , vol.20 , pp. 247-255
    • Huflejt, M.1    Leffler, H.2
  • 17
    • 0242287981 scopus 로고    scopus 로고
    • The N-terminal carbohydrate recognition domain of galectin-8 recognizes specific glycosphingolipids with high affinity
    • Ideo H, Seko A, Ishizuka I, Yamashita K. 2003. The N-terminal carbohydrate recognition domain of galectin-8 recognizes specific glycosphingolipids with high affinity. Glycobiology. 13:713-723.
    • (2003) Glycobiology , vol.13 , pp. 713-723
    • Ideo, H.1    Seko, A.2    Ishizuka, I.3    Yamashita, K.4
  • 18
    • 0036262673 scopus 로고    scopus 로고
    • High-affinity binding of recombinant human galectin-4 to SO(3)(-)→3Galß1→3GalNAc pyranoside
    • Ideo H, Seko A, Ohkura T, Matta KL, Yamashita K. 2002. High-affinity binding of recombinant human galectin-4 to SO(3)(-) →3Galß1→3GalNAc pyranoside. Glycobiology. 12:199-208.
    • (2002) Glycobiology , vol.12 , pp. 199-208
    • Ideo, H.1    Seko, A.2    Ohkura, T.3    Matta, K.L.4    Yamashita, K.5
  • 19
    • 84857738686 scopus 로고    scopus 로고
    • A toolbox of lectins for translating the sugar code: The galectin network in phylogenesis and tumors
    • Kaltner H, Gabius H-J. 2012. A toolbox of lectins for translating the sugar code: The galectin network in phylogenesis and tumors. Histol Histopathol. 27:397-416.
    • (2012) Histol Histopathol , vol.27 , pp. 397-416
    • Kaltner, H.1    Gabius, H.-J.2
  • 20
    • 66149166021 scopus 로고    scopus 로고
    • Unique chicken tandem repeat-type galectin: Implications of alternative splicing and a distinct expression profile compared to those of the three proto-type proteins
    • Kaltner H, Solís D, André S, Lensch M, Manning JC, Mürnseer M, Saiz JL, Gabius H-J. 2009. Unique chicken tandem repeat-type galectin: Implications of alternative splicing and a distinct expression profile compared to those of the three proto-type proteins. Biochemistry. 48:4403-4416.
    • (2009) Biochemistry , vol.48 , pp. 4403-4416
    • Kaltner, H.1    Solís, D.2    André, S.3    Lensch, M.4    Manning, J.C.5    Mürnseer, M.6    Saiz, J.L.7    Gabius, H.-J.8
  • 21
    • 0030064027 scopus 로고    scopus 로고
    • Galectins: A family of animal lectins that decipher glycocodes
    • Kasai K-i, Hirabayashi J. 1996. Galectins: A family of animal lectins that decipher glycocodes. J Biochem. 119:1-8.
    • (1996) J Biochem , vol.119 , pp. 1-8
    • Kasai, K.-I.1    Hirabayashi, J.2
  • 22
    • 0028225392 scopus 로고
    • Correlation of expression of binding sites for synthetic blood group A-, B-and H-trisaccharides and for sarcolectin with survival of patients with bronchial carcinoma
    • Kayser K, Bovin NV, Korchagina EY, Zeilinger C, Zeng FY, Gabius H-J. 1994. Correlation of expression of binding sites for synthetic blood group A-, B-and H-trisaccharides and for sarcolectin with survival of patients with bronchial carcinoma. Eur J Cancer. 30A:653-657.
    • (1994) Eur J Cancer , vol.30 A , pp. 653-657
    • Kayser, K.1    Bovin, N.V.2    Korchagina, E.Y.3    Zeilinger, C.4    Zeng, F.Y.5    Gabius, H.-J.6
  • 23
    • 84862876828 scopus 로고    scopus 로고
    • Ganglioside GM1/galectindependent growth regulation in human neuroblastoma cells: Special properties of bivalent galectin-4 and significance of linker length for ligand selection
    • Kopitz J, Ballikaya S, André S, Gabius H-J. 2012. Ganglioside GM1/galectindependent growth regulation in human neuroblastoma cells: Special properties of bivalent galectin-4 and significance of linker length for ligand selection. Neurochem Res. 37:1267-1276.
    • (2012) Neurochem Res , vol.37 , pp. 1267-1276
    • Kopitz, J.1    Ballikaya, S.2    André, S.3    Gabius, H.-J.4
  • 24
    • 78649773993 scopus 로고    scopus 로고
    • Human galectin-3 (Mac-2 antigen): Defining molecular switches of affinity to natural glycoproteins, structural and dynamic aspects of glycan binding by flexible ligand docking and putative regulatory sequences in the proximal promoter region
    • Krzeminski M, Singh T, André S, Lensch M, Wu A M, Bonvin AM, Gabius H-J. 2011. Human galectin-3 (Mac-2 antigen): Defining molecular switches of affinity to natural glycoproteins, structural and dynamic aspects of glycan binding by flexible ligand docking and putative regulatory sequences in the proximal promoter region. Biochim Biophys Acta. 1810:150-161.
    • (2011) Biochim Biophys Acta , vol.1810 , pp. 150-161
    • Krzeminski, M.1    Singh, T.2    André, S.3    Lensch, M.4    Wu, A.M.5    Bonvin, A.M.6    Gabius, H.-J.7
  • 26
    • 33745371936 scopus 로고    scopus 로고
    • Unique sequence and expression profiles of rat galectins-5 and-9 as a result of species-specific gene divergence
    • Lensch M, Lohr M, Russwurm R, Vidal M, Kaltner H, André S, Gabius H-J. 2006. Unique sequence and expression profiles of rat galectins-5 and-9 as a result of species-specific gene divergence. Int J Biochem Cell Biol. 38:1741-1758.
    • (2006) Int J Biochem Cell Biol , vol.38 , pp. 1741-1758
    • Lensch, M.1    Lohr, M.2    Russwurm, R.3    Vidal, M.4    Kaltner, H.5    André, S.6    Gabius, H.-J.7
  • 28
    • 68149158650 scopus 로고    scopus 로고
    • Glycosylation pattern of brush borderassociated glycoproteins in enterocyte-like cells: Involvement of complextype N-glycans in apical trafficking
    • Morelle W, Stechly L, André S, van Seuningen I, Porchet N, Gabius H-J, Michalski JC, Huet G. 2009. Glycosylation pattern of brush borderassociated glycoproteins in enterocyte-like cells: Involvement of complextype N-glycans in apical trafficking. Biol Chem. 390:529-544.
    • (2009) Biol Chem , vol.390 , pp. 529-544
    • Morelle, W.1    Stechly, L.2    André, S.3    Van Seuningen, I.4    Porchet, N.5    Gabius, H.-J.6    Michalski, J.C.7    Huet, G.8
  • 29
    • 58149352519 scopus 로고    scopus 로고
    • Structural analysis of the recognition mechanism of poly-N- acetyllactosamine by the human galectin-9 N-terminal carbohydrate recognition domain
    • Nagae M, Nishi N, Murata T, Usui T, Nakamura T, Wakatsuki S, Kato R. 2009. Structural analysis of the recognition mechanism of poly-N- acetyllactosamine by the human galectin-9 N-terminal carbohydrate recognition domain. Glycobiology. 19:112-117.
    • (2009) Glycobiology , vol.19 , pp. 112-117
    • Nagae, M.1    Nishi, N.2    Murata, T.3    Usui, T.4    Nakamura, T.5    Wakatsuki, S.6    Kato, R.7
  • 31
    • 0027457991 scopus 로고
    • Soluble lactose-binding lectin from rat intestine with two different carbohydrate-binding domains in the same peptide chain
    • Oda Y, Herrmann J, Gitt MA, Turck CW, Burlingame AL, Barondes SH, Leffler H. 1993. Soluble lactose-binding lectin from rat intestine with two different carbohydrate-binding domains in the same peptide chain. J Biol Chem. 268:5929-5939.
    • (1993) J Biol Chem , vol.268 , pp. 5929-5939
    • Oda, Y.1    Herrmann, J.2    Gitt, M.A.3    Turck, C.W.4    Burlingame, A.L.5    Barondes, S.H.6    Leffler, H.7
  • 32
    • 41549129317 scopus 로고    scopus 로고
    • Galectin-loaded cells as platform for profiling of lectin specificity by fluorescent neoglycoconjugates: Case study on galectins-1 and-3 and the impact of assay setting
    • Rapoport EM, André S, Kurmyshkina OV, Pochechueva TV, Severov VV, Pazynina GV, Gabius H-J, Bovin NV. 2008. Galectin-loaded cells as platform for profiling of lectin specificity by fluorescent neoglycoconjugates: Case study on galectins-1 and-3 and the impact of assay setting. Glycobiology. 18:315-324.
    • (2008) Glycobiology , vol.18 , pp. 315-324
    • Rapoport, E.M.1    André, S.2    Kurmyshkina, O.V.3    Pochechueva, T.V.4    Severov, V.V.5    Pazynina, G.V.6    Gabius, H.-J.7    Bovin, N.V.8
  • 34
    • 77953741266 scopus 로고    scopus 로고
    • N-domain of human adhesion/growth-regulatory galectin-9: Preference for distinct conformers and non-sialylated N-glycans and detection of ligand-induced structural changes in crystal and solution
    • Solís D, Mate MJ, Lohr M, Ribeiro JP, Lopez-Merino L, André S, Buzamet E, Canada J, Kaltner H, Lensch M, et al. 2010. N-domain of human adhesion/growth-regulatory galectin-9: Preference for distinct conformers and non-sialylated N-glycans and detection of ligand-induced structural changes in crystal and solution. Int J Biochem Cell Biol. 42:1019-1029.
    • (2010) Int J Biochem Cell Biol , vol.42 , pp. 1019-1029
    • Solís, D.1    Mate, M.J.2    Lohr, M.3    Ribeiro, J.P.4    Lopez-Merino, L.5    André, S.6    Buzamet, E.7    Canada, J.8    Kaltner, H.9    Lensch, M.10
  • 37
    • 50649125265 scopus 로고    scopus 로고
    • Dimeric galectin-8 induces phosphatidylserine exposure in leukocytes through polylactosamine recognition by the C-terminal domain
    • Stowell SR, Arthur CM, Slanina KA, Horton JR, Smith DF, Cummings RD. 2008. Dimeric galectin-8 induces phosphatidylserine exposure in leukocytes through polylactosamine recognition by the C-terminal domain. J Biol Chem. 283:20547-20559.
    • (2008) J Biol Chem , vol.283 , pp. 20547-20559
    • Stowell, S.R.1    Arthur, C.M.2    Slanina, K.A.3    Horton, J.R.4    Smith, D.F.5    Cummings, R.D.6
  • 39
    • 2942640032 scopus 로고    scopus 로고
    • Effects of polyvalency of glycotopes and natural modifications of human blood group ABH/lewis sugars at the galß-terminated core saccharides on the binding of domain-i of recombinant tandem repeat-type galectin-4 from rat gastrointestinal tract (G4-N)
    • Wu AM, Wu JH, Singh T, André S, Kaltner H, Gabius H-J. 2004. Effects of polyvalency of glycotopes and natural modifications of human blood group ABH/Lewis sugars at the Galß-terminated core saccharides on the binding of domain-I of recombinant tandem repeat-type galectin-4 from rat gastrointestinal tract (G4-N). Biochimie. 86:317-326.
    • (2004) Biochimie , vol.86 , pp. 317-326
    • Wu, A.M.1    Wu, J.H.2    Singh, T.3    André, S.4    Kaltner, H.5    Gabius, H.-J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.