메뉴 건너뛰기




Volumn 1253, Issue 1, 2012, Pages 206-221

Beyond glycoproteins as galectin counterreceptors: Effector T cell growth control of tumors via ganglioside GM1

Author keywords

Anoikis; Carcinoma; Diabetes; Galectin 1; Glycosphingolipid; GM1 ganglioside; Immune suppression; T cells

Indexed keywords

ALPHA5 INTEGRIN; BETA GALACTOSIDASE; CYCLIN DEPENDENT KINASE INHIBITOR 2A; GALECTIN 1; GALECTIN 4; GANGLIOSIDE GM1; GLUCOSYLCERAMIDE; GLYCOPROTEIN; SIALIC ACID; TRANSIENT RECEPTOR POTENTIAL CHANNEL 5;

EID: 84860251714     PISSN: 00778923     EISSN: 17496632     Source Type: Book Series    
DOI: 10.1111/j.1749-6632.2012.06479.x     Document Type: Review
Times cited : (52)

References (122)
  • 2
    • 0001810168 scopus 로고    scopus 로고
    • The information-storing potential of the sugar code
    • H.-J. Gabius & S. Gabius, Eds.:. Chapman & Hall. London/Weinheim.
    • Laine, R.A. 1997. The information-storing potential of the sugar code. In Glycosciences: Status and Perspectives. H.-J. Gabius & S. Gabius, Eds.: 1-14. Chapman & Hall. London/Weinheim.
    • (1997) Glycosciences: Status and Perspectives , pp. 1-14
    • Laine, R.A.1
  • 3
  • 4
    • 0030219388 scopus 로고    scopus 로고
    • Why mammalian cell surface proteins are glycoproteins
    • Gahmberg, C.G. & M. Tolvanen. 1996. Why mammalian cell surface proteins are glycoproteins. Trends Biochem. Sci. 21: 308-311.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 308-311
    • Gahmberg, C.G.1    Tolvanen, M.2
  • 5
    • 77953240454 scopus 로고    scopus 로고
    • Precision mapping of an in vivo N-glycoproteome reveals rigid topological and sequence constraints
    • Zielinska, D.F., F. Gnad, J.R. Wisniewski & M. Mann. 2010. Precision mapping of an in vivo N-glycoproteome reveals rigid topological and sequence constraints. Cell 141: 897-907.
    • (2010) Cell , vol.141 , pp. 897-907
    • Zielinska, D.F.1    Gnad, F.2    Wisniewski, J.R.3    Mann, M.4
  • 6
    • 77953778927 scopus 로고    scopus 로고
    • O-Glycosylation: structural diversity and function
    • H.-J. Gabius, Ed.:. Wiley-VCH. Weinheim, Germany.
    • Patsos, G. & A. Corfield. 2009. O-Glycosylation: structural diversity and function. In The Sugar Code. Fundamentals of Glycosciences. H.-J. Gabius, Ed.: 111-137. Wiley-VCH. Weinheim, Germany.
    • (2009) The Sugar Code. Fundamentals of Glycosciences , pp. 111-137
    • Patsos, G.1    Corfield, A.2
  • 7
  • 8
    • 66249106029 scopus 로고    scopus 로고
    • Compensation of loss of protein function in microsatellite-unstable colon cancer cells (HCT116): a gene-dependent effect on the cell surface glycan profile
    • Patsos, G., S. André, N. Roeckel, et al. 2009. Compensation of loss of protein function in microsatellite-unstable colon cancer cells (HCT116): a gene-dependent effect on the cell surface glycan profile. Glycobiology 19: 726-734.
    • (2009) Glycobiology , vol.19 , pp. 726-734
    • Patsos, G.1    André, S.2    Roeckel, N.3
  • 9
    • 79951677328 scopus 로고    scopus 로고
    • Nitric oxide changes distinct aspects of the glycophenotype of human neuroblastoma NB69 cells
    • van de Wouwer, M., S. André, H.-J. Gabius & A. Villalobo. 2011. Nitric oxide changes distinct aspects of the glycophenotype of human neuroblastoma NB69 cells. Nitric Oxide 24: 91-101.
    • (2011) Nitric Oxide , vol.24 , pp. 91-101
    • van de Wouwer, M.1    André, S.2    Gabius, H.-J.3    Villalobo, A.4
  • 10
    • 68149131940 scopus 로고    scopus 로고
    • From structural to functional glycomics: core substitutions as molecular switches for shape and lectin affinity of N-glycans
    • André, S., T. Kozár, S. Kojima, C. Unverzagt & H.-J. Gabius. 2009. From structural to functional glycomics: core substitutions as molecular switches for shape and lectin affinity of N-glycans. Biol. Chem. 390: 557-565.
    • (2009) Biol. Chem. , vol.390 , pp. 557-565
    • André, S.1    Kozár, T.2    Kojima, S.3    Unverzagt, C.4    Gabius, H.-J.5
  • 11
    • 70349326274 scopus 로고    scopus 로고
    • The repertoire of glycan determinants in the human glycome
    • Cummings, R.D. 2009. The repertoire of glycan determinants in the human glycome. Mol. BioSyst. 5: 1087-1104.
    • (2009) Mol. BioSyst. , vol.5 , pp. 1087-1104
    • Cummings, R.D.1
  • 12
    • 75749084864 scopus 로고    scopus 로고
    • Regulation of intracellular signaling by extracellular glycan remodeling
    • Parker, R.B. & J.J. Kohler. 2010. Regulation of intracellular signaling by extracellular glycan remodeling. ACS Chem. Biol. 5: 35-46.
    • (2010) ACS Chem. Biol. , vol.5 , pp. 35-46
    • Parker, R.B.1    Kohler, J.J.2
  • 14
    • 0036816147 scopus 로고    scopus 로고
    • Clusters, bundles, arrays and lattices: novel mechanisms for lectin-saccharide-mediated cellular interactions
    • Brewer, C.F., M.C. Miceli & L.G. Baum. 2002. Clusters, bundles, arrays and lattices: novel mechanisms for lectin-saccharide-mediated cellular interactions. Curr. Opin. Struct. Biol. 12: 616-623.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 616-623
    • Brewer, C.F.1    Miceli, M.C.2    Baum, L.G.3
  • 16
  • 17
    • 84857738686 scopus 로고    scopus 로고
    • A toolbox of lectins for translating the sugar code: the galectin network in phylogenesis and tumors
    • Kaltner, H. & H.-J. Gabius. 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
  • 18
    • 5144232009 scopus 로고    scopus 로고
    • Growth-regulatory human galectin-1: crystallographic characterisation of the structural changes induced by single-site mutations and their impact on the thermodynamics of ligand binding
    • López-Lucendo, M.F., D. Solís, S. André, et al. 2004. Growth-regulatory human galectin-1: crystallographic characterisation of the structural changes induced by single-site mutations and their impact on the thermodynamics of ligand binding. J. Mol. Biol. 343: 957-970.
    • (2004) J. Mol. Biol. , vol.343 , pp. 957-970
    • López-Lucendo, M.F.1    Solís, D.2    André, S.3
  • 19
    • 27744552971 scopus 로고    scopus 로고
    • 1 fibronectin receptor to restrict carcinoma cell growth via induction of p21 and p27
    • 1 fibronectin receptor to restrict carcinoma cell growth via induction of p21 and p27. J. Biol. Chem. 280: 37266-37277.
    • (2005) J. Biol. Chem. , vol.280 , pp. 37266-37277
    • Fischer, C.1    Sanchez-Ruderisch, H.2    Welzel, M.3
  • 21
    • 0037470066 scopus 로고    scopus 로고
    • The ST6Gal1 sialyltransferase selectively modifies N-glycans on CD45 to negatively regulate galectin-1-induced CD45 clustering, phosphatase modulation, and T cell death
    • Amano, M., M. Galvan, J. He & L.G. Baum. 2003. The ST6Gal1 sialyltransferase selectively modifies N-glycans on CD45 to negatively regulate galectin-1-induced CD45 clustering, phosphatase modulation, and T cell death. J. Biol. Chem. 278: 7469-7475.
    • (2003) J. Biol. Chem. , vol.278 , pp. 7469-7475
    • Amano, M.1    Galvan, M.2    He, J.3    Baum, L.G.4
  • 23
    • 34447097387 scopus 로고    scopus 로고
    • INK4a: modulator of glycomic profile and galectin-1 expression to increase susceptibility to carbohydrate-dependent induction of anoikis in pancreatic carcinoma cells
    • INK4a: modulator of glycomic profile and galectin-1 expression to increase susceptibility to carbohydrate-dependent induction of anoikis in pancreatic carcinoma cells. FEBS J. 274: 3233-3256.
    • (2007) FEBS J. , vol.274 , pp. 3233-3256
    • André, S.1    Sanchez-Ruderisch, H.2    Nakagawa, H.3
  • 25
    • 77955778590 scopus 로고    scopus 로고
    • INK4a: downregulation of galectin-3, an endogenous competitor of the pro-anoikis effector galectin-1, in a pancreatic carcinoma model
    • INK4a: downregulation of galectin-3, an endogenous competitor of the pro-anoikis effector galectin-1, in a pancreatic carcinoma model. FEBS J. 277: 3552-3563.
    • (2010) FEBS J. , vol.277 , pp. 3552-3563
    • Sanchez-Ruderisch, H.1    Fischer, C.2    Detjen, K.M.3
  • 26
    • 33646554216 scopus 로고    scopus 로고
    • A guide to signaling pathways connecting protein-glycan interaction with the emerging versatile effector functionality of mammalian lectins
    • Villalobo, A., A. Nogales-Gonzáles & H.-J. Gabius. 2006. A guide to signaling pathways connecting protein-glycan interaction with the emerging versatile effector functionality of mammalian lectins. Trends Glycosci. Glycotechnol. 18: 1-37.
    • (2006) Trends Glycosci. Glycotechnol. , vol.18 , pp. 1-37
    • Villalobo, A.1    Nogales-Gonzáles, A.2    Gabius, H.-J.3
  • 27
    • 59149097542 scopus 로고    scopus 로고
    • Galectin-glycan lattices regulate cell-surface glycoprotein organization and signalling
    • Garner, O.B. & L.G. Baum. 2008. Galectin-glycan lattices regulate cell-surface glycoprotein organization and signalling. Biochem. Soc. Trans. 36: 1472-1477.
    • (2008) Biochem. Soc. Trans. , vol.36 , pp. 1472-1477
    • Garner, O.B.1    Baum, L.G.2
  • 28
    • 71649106024 scopus 로고    scopus 로고
    • Sialic acids in T cell development and function
    • Bi, S. & L.G. Baum. 2009. Sialic acids in T cell development and function. Biochim. Biophys. Acta 1790: 1599-1610.
    • (2009) Biochim. Biophys. Acta , vol.1790 , pp. 1599-1610
    • Bi, S.1    Baum, L.G.2
  • 29
    • 79952561576 scopus 로고    scopus 로고
    • How does it act when soluble? Critical evaluation of mechanism of galectin-1 induced T-cell apoptosis
    • Blasko, A., R. Fajka-Boja, G. Ion & E. Monostori. 2011. How does it act when soluble? Critical evaluation of mechanism of galectin-1 induced T-cell apoptosis. Acta Biol. Hung. 62: 106-111.
    • (2011) Acta Biol. Hung. , vol.62 , pp. 106-111
    • Blasko, A.1    Fajka-Boja, R.2    Ion, G.3    Monostori, E.4
  • 30
    • 35348871278 scopus 로고    scopus 로고
    • (Glyco)sphingolipidology: an amazing challenge and opportunity for systems biology
    • Merrill, A.H., Jr., M.D. Wang, M. Park & M.C. Sullards. 2007. (Glyco)sphingolipidology: an amazing challenge and opportunity for systems biology. Trends Biochem. Sci. 32: 457-468.
    • (2007) Trends Biochem. Sci. , vol.32 , pp. 457-468
    • Merrill Jr., A.H.1    Wang, M.D.2    Park, M.3    Sullards, M.C.4
  • 31
    • 77953755681 scopus 로고    scopus 로고
    • Glycolipids
    • H.-J. Gabius, Ed.:. Wiley-VCH. Weinheim, Germany.
    • Kopitz, J. 2009. Glycolipids. In The Sugar Code. Fundamentals of Glycosciences. H.-J. Gabius, Ed.: 177-198. Wiley-VCH. Weinheim, Germany.
    • (2009) The Sugar Code. Fundamentals of Glycosciences , pp. 177-198
    • Kopitz, J.1
  • 32
    • 72249098524 scopus 로고    scopus 로고
    • Neurobiology meets glycosciences
    • H.-J. Gabius, Ed.:. Wiley-VCH. Weinheim, Germany.
    • Ledeen, R.W. & G. Wu. 2009. Neurobiology meets glycosciences. In The Sugar Code. Fundamentals of Glycosciences. H.-J. Gabius, Ed.: 495-516. Wiley-VCH. Weinheim, Germany.
    • (2009) The Sugar Code. Fundamentals of Glycosciences , pp. 495-516
    • Ledeen, R.W.1    Wu, G.2
  • 33
    • 70349871692 scopus 로고    scopus 로고
    • Gangliosides in cell recognition and membrane protein regulation
    • Lopez, P.H. & R.L. Schnaar. 2009. Gangliosides in cell recognition and membrane protein regulation. Curr. Opin. Struct. Biol. 19: 549-557.
    • (2009) Curr. Opin. Struct. Biol. , vol.19 , pp. 549-557
    • Lopez, P.H.1    Schnaar, R.L.2
  • 34
    • 85014129365 scopus 로고    scopus 로고
    • Glycosphingolipid structures
    • J.P. Kamerling, Ed.:. Elsevier. Oxford, UK.
    • Yu, R.K., M. Yanagisawa & T. Ariga. 2007. Glycosphingolipid structures. In Comprehensive Glycoscience. J.P. Kamerling, Ed.: 73-122. Elsevier. Oxford, UK.
    • (2007) Comprehensive Glycoscience , pp. 73-122
    • Yu, R.K.1    Yanagisawa, M.2    Ariga, T.3
  • 35
    • 0016911427 scopus 로고
    • Interaction of cholera toxin and ganglioside G(M1)
    • Svennerholm, L. 1976. Interaction of cholera toxin and ganglioside G(M1). Adv. Exp. Med. Biol. 71: 191-204.
    • (1976) Adv. Exp. Med. Biol. , vol.71 , pp. 191-204
    • Svennerholm, L.1
  • 36
    • 78651313573 scopus 로고    scopus 로고
    • In search of a solution to the Sphinx-like riddle of GM1
    • Ledeen, R.W. & G. Wu. 2010. In search of a solution to the Sphinx-like riddle of GM1. Neurochem. Res. 35: 1867-1874.
    • (2010) Neurochem. Res. , vol.35 , pp. 1867-1874
    • Ledeen, R.W.1    Wu, G.2
  • 37
    • 0033582517 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a plasma membrane-associated sialidase specific for gangliosides
    • Miyagi, T., T. Wada, A. Iwamatsu, et al. 1999. Molecular cloning and characterization of a plasma membrane-associated sialidase specific for gangliosides. J. Biol. Chem. 274: 5004-5011.
    • (1999) J. Biol. Chem. , vol.274 , pp. 5004-5011
    • Miyagi, T.1    Wada, T.2    Iwamatsu, A.3
  • 38
    • 0023951018 scopus 로고
    • Endogenous glycosphingolipid acceptor specificity of sialosyltransferase systems in intact Golgi membranes, synaptosomes, and synaptic plasma membranes from rat brain
    • Durrie, R., M. Saito & A. Rosenberg. 1988. Endogenous glycosphingolipid acceptor specificity of sialosyltransferase systems in intact Golgi membranes, synaptosomes, and synaptic plasma membranes from rat brain. Biochemistry 27: 3759-3764.
    • (1988) Biochemistry , vol.27 , pp. 3759-3764
    • Durrie, R.1    Saito, M.2    Rosenberg, A.3
  • 39
    • 38449090335 scopus 로고    scopus 로고
    • Modulation of cell functions by glycosphingolipid metabolic remodeling in the plasma membrane
    • Prinetti, A., V. Chigorno, L. Mauri, et al. 2007. Modulation of cell functions by glycosphingolipid metabolic remodeling in the plasma membrane. J. Neurochem. 103(Suppl 1): 113-125.
    • (2007) J. Neurochem. , vol.103 , Issue.SUPPL. 1 , pp. 113-125
    • Prinetti, A.1    Chigorno, V.2    Mauri, L.3
  • 40
    • 84870678616 scopus 로고    scopus 로고
    • Nomenclature of Glycolipids. International Union of Pure and Applied Chemistry. Available at:.
    • Nomenclature of Glycolipids. International Union of Pure and Applied Chemistry. Available at:.
  • 41
    • 0036694862 scopus 로고    scopus 로고
    • Stable transfection of GM1 synthase gene into GM1-deficient NG108-15 cells, CR-72 cells, rescues the responsiveness of Trk-neurotrophin receptor to its ligand, NGF
    • Mutoh, T., T. Hamano, S. Yano, et al. 2002. Stable transfection of GM1 synthase gene into GM1-deficient NG108-15 cells, CR-72 cells, rescues the responsiveness of Trk-neurotrophin receptor to its ligand, NGF. Neurochem. Res. 27: 801-806.
    • (2002) Neurochem. Res. , vol.27 , pp. 801-806
    • Mutoh, T.1    Hamano, T.2    Yano, S.3
  • 42
    • 0036316409 scopus 로고    scopus 로고
    • Potentiation of a sodium-calcium exchanger in the nuclear envelope by nuclear GM1 ganglioside
    • Xie, X., G. Wu, Z.H. Lu & R.W. Ledeen. 2002. Potentiation of a sodium-calcium exchanger in the nuclear envelope by nuclear GM1 ganglioside. J. Neurochem. 81: 1185-1195.
    • (2002) J. Neurochem. , vol.81 , pp. 1185-1195
    • Xie, X.1    Wu, G.2    Lu, Z.H.3    Ledeen, R.W.4
  • 43
    • 0031039056 scopus 로고    scopus 로고
    • Interaction of the {eth}-opioid receptor with GM1 ganglioside: conversion from inhibitory to excitatory mode
    • Wu, G., Z.H. Lu & R.W. Ledeen. 1997. Interaction of the {eth}-opioid receptor with GM1 ganglioside: conversion from inhibitory to excitatory mode. Mol. Brain Res. 44: 341-346.
    • (1997) Mol. Brain Res. , vol.44 , pp. 341-346
    • Wu, G.1    Lu, Z.H.2    Ledeen, R.W.3
  • 44
    • 0021327310 scopus 로고
    • Promotion of neuritogenesis in mouse neuroblastoma cells by exogenous gangliosides. Relationship between the effect and the cell association of ganglioside GM1
    • Facci, L., A. Leon, G. Toffano, et al. 1984. Promotion of neuritogenesis in mouse neuroblastoma cells by exogenous gangliosides. Relationship between the effect and the cell association of ganglioside GM1. J. Neurochem. 42: 299-305.
    • (1984) J. Neurochem. , vol.42 , pp. 299-305
    • Facci, L.1    Leon, A.2    Toffano, G.3
  • 45
    • 0021133012 scopus 로고
    • Biology of gangliosides: neuritogenic and neuronotrophic properties
    • Ledeen, R.W. 1984. Biology of gangliosides: neuritogenic and neuronotrophic properties. J. Neurosci. Res. 12: 147-159.
    • (1984) J. Neurosci. Res. , vol.12 , pp. 147-159
    • Ledeen, R.W.1
  • 46
    • 0031949027 scopus 로고    scopus 로고
    • The role of GM1 and other gangliosides in neuronal differentiation - overview and new findings
    • Ledeen, R.W., G.S. Wu, Z.H. Lu, D. Kozireski-Chubak & Y. Fang. 1998. The role of GM1 and other gangliosides in neuronal differentiation - overview and new findings. Ann. NY Acad. Sci. 845: 341-348.
    • (1998) Ann. NY Acad. Sci. , vol.845 , pp. 341-348
    • Ledeen, R.W.1    Wu, G.S.2    Lu, Z.H.3    Kozireski-Chubak, D.4    Fang, Y.5
  • 47
    • 38449110060 scopus 로고    scopus 로고
    • Regulation of axonal development by plasma membrane gangliosides
    • Abad-Rodriguez, J. & A. Robotti. 2007. Regulation of axonal development by plasma membrane gangliosides. J. Neurochem. 103(Suppl 1): 47-55.
    • (2007) J. Neurochem. , vol.103 , Issue.SUPPL. 1 , pp. 47-55
    • Abad-Rodriguez, J.1    Robotti, A.2
  • 48
    • 0020364635 scopus 로고
    • Density-dependent changes in gangliosides and sialidase activity of murine neuroblastoma cells
    • Schengrund, C.L. & M.A. Repman. 1982. Density-dependent changes in gangliosides and sialidase activity of murine neuroblastoma cells. J. Neurochem. 39: 940-947.
    • (1982) J. Neurochem. , vol.39 , pp. 940-947
    • Schengrund, C.L.1    Repman, M.A.2
  • 49
    • 0028200352 scopus 로고
    • Role of plasma membrane ganglioside sialidase of human neuroblastoma cells in growth control and differentiation
    • Kopitz, J., C. von Reitzenstein, C. Mühl & M. Cantz. 1994. Role of plasma membrane ganglioside sialidase of human neuroblastoma cells in growth control and differentiation. Biochem. Biophys. Res. Comm. 199: 1188-1193.
    • (1994) Biochem. Biophys. Res. Comm. , vol.199 , pp. 1188-1193
    • Kopitz, J.1    von Reitzenstein, C.2    Mühl, C.3    Cantz, M.4
  • 50
    • 0029666071 scopus 로고    scopus 로고
    • Selective ganglioside desialylation in the plasma membrane of human neuroblastoma cells
    • Kopitz, J., C. von Reitzenstein, K. Sinz & M. Cantz. 1996. Selective ganglioside desialylation in the plasma membrane of human neuroblastoma cells. Glycobiology 6: 367-376.
    • (1996) Glycobiology , vol.6 , pp. 367-376
    • Kopitz, J.1    von Reitzenstein, C.2    Sinz, K.3    Cantz, M.4
  • 51
    • 0343487873 scopus 로고    scopus 로고
    • Effects of cell surface ganglioside sialidase inhibition on growth control and differentiation of human neuroblastoma cells
    • Kopitz, J., C. Mühl, V. Ehemann, et al. 1997. Effects of cell surface ganglioside sialidase inhibition on growth control and differentiation of human neuroblastoma cells. Eur. J. Cell Biol. 73: 1-7.
    • (1997) Eur. J. Cell Biol. , vol.73 , pp. 1-7
    • Kopitz, J.1    Mühl, C.2    Ehemann, V.3
  • 52
    • 0025375708 scopus 로고
    • 1 is a ligand for specific binding sites in various human tumor cell types and peripheral blood lymphocytes and monocytes
    • 1 is a ligand for specific binding sites in various human tumor cell types and peripheral blood lymphocytes and monocytes. Biochem. Biophys. Res. Commun. 169: 239-244.
    • (1990) Biochem. Biophys. Res. Commun. , vol.169 , pp. 239-244
    • Gabius, S.1    Kayser, K.2    Hellmann, K.P.3
  • 53
    • 0029907861 scopus 로고    scopus 로고
    • 1) glycoligands in nasal polyps and other human lesions including neoplasms
    • 1) glycoligands in nasal polyps and other human lesions including neoplasms. Histol. Histopathol. 11: 985-992.
    • (1996) Histol. Histopathol. , vol.11 , pp. 985-992
    • Hassid, S.1    Salmon, I.2    Bovin, N.V.3
  • 54
    • 0027184431 scopus 로고
    • Study of lectin-ganglioside interactions by high-performance liquid affinity chromatography
    • Caron, M., R. Joubert-Caron, J.R. Cartier, et al. 1993. Study of lectin-ganglioside interactions by high-performance liquid affinity chromatography. J. Chromatography 646: 327-333.
    • (1993) J. Chromatography , vol.646 , pp. 327-333
    • Caron, M.1    Joubert-Caron, R.2    Cartier, J.R.3
  • 55
    • 0032080122 scopus 로고    scopus 로고
    • 1, a product of the growth-controlling activity of a cell surface ganglioside sialidase, on human neuroblastoma cells in culture
    • 1, a product of the growth-controlling activity of a cell surface ganglioside sialidase, on human neuroblastoma cells in culture. J. Biol. Chem. 273: 11205-11211.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11205-11211
    • Kopitz, J.1    von Reitzenstein, C.2    Burchert, M.3
  • 56
    • 0035929631 scopus 로고    scopus 로고
    • Negative regulation of neuroblastoma cell growth by carbohydrate-dependent surface binding of galectin-1 and functional divergence from galectin-3
    • Kopitz, J., C. von Reitzenstein, S. André, et al. 2001. Negative regulation of neuroblastoma cell growth by carbohydrate-dependent surface binding of galectin-1 and functional divergence from galectin-3. J. Biol. Chem. 276: 35917-35923.
    • (2001) J. Biol. Chem. , vol.276 , pp. 35917-35923
    • Kopitz, J.1    von Reitzenstein, C.2    André, S.3
  • 57
    • 77955873679 scopus 로고    scopus 로고
    • How adhesion/growth-regulatory galectins-1 and -3 attain cell specificity: case study defining their target on neuroblastoma cells (SK-N-MC) and marked affinity regulation by affecting microdomain organization of the membrane
    • Kopitz, J., M. Bergmann & H.-J. Gabius. 2010. How adhesion/growth-regulatory galectins-1 and -3 attain cell specificity: case study defining their target on neuroblastoma cells (SK-N-MC) and marked affinity regulation by affecting microdomain organization of the membrane. IUBMB Life 62: 624-628.
    • (2010) IUBMB Life , vol.62 , pp. 624-628
    • Kopitz, J.1    Bergmann, M.2    Gabius, H.-J.3
  • 60
    • 77249139404 scopus 로고    scopus 로고
    • Protein-carbohydrate interactions: basic concepts and methods for analysis
    • H.-J. Gabius, Ed.:. Wiley-VCH. Weinheim, Germany.
    • Solís, D., A. Romero, M. Menéndez & J. Jiménez-Barbero. 2009. Protein-carbohydrate interactions: basic concepts and methods for analysis. In The Sugar Code. Fundamentals of Glycosciences. H.-J. Gabius, Ed.: 233-245. Wiley-VCH. Weinheim, Germany.
    • (2009) The Sugar Code. Fundamentals of Glycosciences , pp. 233-245
    • Solís, D.1    Romero, A.2    Menéndez, M.3    Jiménez-Barbero, J.4
  • 61
    • 0034805645 scopus 로고    scopus 로고
    • The plasma membrane ganglioside sialidase cofractionates with markers of lipid rafts
    • Kalka, D., C. von Reitzenstein, J. Kopitz & M. Cantz. 2001. The plasma membrane ganglioside sialidase cofractionates with markers of lipid rafts. Biochem. Biophys. Res. Commun. 283: 989-993.
    • (2001) Biochem. Biophys. Res. Commun. , vol.283 , pp. 989-993
    • Kalka, D.1    von Reitzenstein, C.2    Kopitz, J.3    Cantz, M.4
  • 62
    • 0037136406 scopus 로고    scopus 로고
    • Oligosaccharide specificity of galectins: a search by frontal affinity chromatography
    • Hirabayashi, J., T. Hashidate, Y. Arata, et al. 2002. Oligosaccharide specificity of galectins: a search by frontal affinity chromatography. Biochim. Biophys. Acta 1572: 232-254.
    • (2002) Biochim. Biophys. Acta , vol.1572 , pp. 232-254
    • Hirabayashi, J.1    Hashidate, T.2    Arata, Y.3
  • 63
    • 60849094468 scopus 로고    scopus 로고
    • Modulation of growth factors receptors in membrane microdomains
    • Inokuchi, J.-I. & K. Kabayama. 2008. Modulation of growth factors receptors in membrane microdomains. Trends Glycosci. Glycotechnol. 20: 353-371.
    • (2008) Trends Glycosci. Glycotechnol. , vol.20 , pp. 353-371
    • Inokuchi, J.-I.1    Kabayama, K.2
  • 64
    • 61949107641 scopus 로고    scopus 로고
    • Binding of laminin-1 to monosialoganglioside GM1 in lipid rafts is crucial for neurite outgrowth
    • Ichikawa, N., K. Iwabuchi, H. Kurihara, et al. 2009. Binding of laminin-1 to monosialoganglioside GM1 in lipid rafts is crucial for neurite outgrowth. J. Cell Sci. 122: 289-299.
    • (2009) J. Cell Sci. , vol.122 , pp. 289-299
    • Ichikawa, N.1    Iwabuchi, K.2    Kurihara, H.3
  • 65
    • 50249138175 scopus 로고    scopus 로고
    • Co-localization of galectin-1 with GM1 ganglioside in the course of its clathrin- and raft-dependent endocytosis
    • Fajka-Boja, R., A. Blasko, F. Kovacs-Solyom, et al. 2008. Co-localization of galectin-1 with GM1 ganglioside in the course of its clathrin- and raft-dependent endocytosis. Cell. Mol. Life Sci. 65: 2586-2593.
    • (2008) Cell. Mol. Life Sci. , vol.65 , pp. 2586-2593
    • Fajka-Boja, R.1    Blasko, A.2    Kovacs-Solyom, F.3
  • 66
    • 33748460087 scopus 로고    scopus 로고
    • + natural regulatory T cells revealed by DNA microarray analysis
    • + natural regulatory T cells revealed by DNA microarray analysis. Int. Immunol. 18: 1197-1209.
    • (2006) Int. Immunol. , vol.18 , pp. 1197-1209
    • Sugimoto, N.1    Oida, T.2    Hirota, K.3
  • 68
    • 64249146003 scopus 로고    scopus 로고
    • Cross-linking of GM1 ganglioside by galectin-1 mediates regulatory T cell activity involving TRPC5 channel activation: possible role in suppressing experimental autoimmune encephalomyelitis
    • Wang, J., Z.H. Lu, H.-J. Gabius, et al. 2009. Cross-linking of GM1 ganglioside by galectin-1 mediates regulatory T cell activity involving TRPC5 channel activation: possible role in suppressing experimental autoimmune encephalomyelitis. J. Immunol. 182: 4036-4045.
    • (2009) J. Immunol. , vol.182 , pp. 4036-4045
    • Wang, J.1    Lu, Z.H.2    Gabius, H.-J.3
  • 69
    • 0035104202 scopus 로고    scopus 로고
    • Organization of plasma membrane functional rafts upon T cell activation
    • Tuosto, L., I. Parolini, S. Schroder, et al. 2001. Organization of plasma membrane functional rafts upon T cell activation. Eur. J. Immunol. 31: 345-349.
    • (2001) Eur. J. Immunol. , vol.31 , pp. 345-349
    • Tuosto, L.1    Parolini, I.2    Schroder, S.3
  • 70
    • 33747813547 scopus 로고    scopus 로고
    • Differential partitioning and trafficking of GM gangliosides and cholesterol-rich lipid rafts in thymic and splenic CD4 T cells
    • Brumeanu, T.D., A. Preda-Pais, C. Stoica, et al. 2007. Differential partitioning and trafficking of GM gangliosides and cholesterol-rich lipid rafts in thymic and splenic CD4 T cells. Mol. Immunol. 44: 530-540.
    • (2007) Mol. Immunol. , vol.44 , pp. 530-540
    • Brumeanu, T.D.1    Preda-Pais, A.2    Stoica, C.3
  • 71
    • 2942751956 scopus 로고    scopus 로고
    • Induction of lysosomal and plasma membrane-bound sialidases in human T-cells via T-cell receptor
    • Wang, P., J. Zhang, H. Bian, et al. 2004. Induction of lysosomal and plasma membrane-bound sialidases in human T-cells via T-cell receptor. Biochem. J. 380: 425-433.
    • (2004) Biochem. J. , vol.380 , pp. 425-433
    • Wang, P.1    Zhang, J.2    Bian, H.3
  • 72
    • 0031914013 scopus 로고    scopus 로고
    • The B-subunit of cholera toxin induces immunoregulatory cells and prevents diabetes in the NOD mouse
    • Sobel, D.O., B. Yankelevich, D. Goyal, et al. 1998. The B-subunit of cholera toxin induces immunoregulatory cells and prevents diabetes in the NOD mouse. Diabetes 47: 186-191.
    • (1998) Diabetes , vol.47 , pp. 186-191
    • Sobel, D.O.1    Yankelevich, B.2    Goyal, D.3
  • 73
    • 0033083188 scopus 로고    scopus 로고
    • Immune modulation by the cholera-like enterotoxins: from adjuvant to therapeutic
    • Williams, N.A., T.R. Hirst & T.O. Nashar. 1999. Immune modulation by the cholera-like enterotoxins: from adjuvant to therapeutic. Immunol. Today 20: 95-101.
    • (1999) Immunol. Today , vol.20 , pp. 95-101
    • Williams, N.A.1    Hirst, T.R.2    Nashar, T.O.3
  • 75
    • 63149170012 scopus 로고    scopus 로고
    • Galectin-1 is a novel functional receptor for tissue plasminogen activator in pancratic cancer
    • Roda, O., E. Ortiz-Zapater, N. Martín-Bosch, et al. 2009. Galectin-1 is a novel functional receptor for tissue plasminogen activator in pancratic cancer. Gastroenterology 136: 1379-1390.
    • (2009) Gastroenterology , vol.136 , pp. 1379-1390
    • Roda, O.1    Ortiz-Zapater, E.2    Martín-Bosch, N.3
  • 76
    • 0023631214 scopus 로고
    • Transmembrane signaling by the B subunit of cholera toxin: increased cytoplasmic free calcium in rat lymphocytes
    • Dixon, S.J., D. Stewart, S. Grinstein & S. Spiegel. 1987. Transmembrane signaling by the B subunit of cholera toxin: increased cytoplasmic free calcium in rat lymphocytes. J. Cell Biol. 105: 1153-1161.
    • (1987) J. Cell Biol. , vol.105 , pp. 1153-1161
    • Dixon, S.J.1    Stewart, D.2    Grinstein, S.3    Spiegel, S.4
  • 77
    • 0028278702 scopus 로고
    • Cell calcium signaling via GM1 cell surface gangliosides in the human Jurkat T cell line
    • Gouy, H., P. Deterre, P. Debre & G. Bismuth. 1994. Cell calcium signaling via GM1 cell surface gangliosides in the human Jurkat T cell line. J. Immunol. 152: 3271-3281.
    • (1994) J. Immunol. , vol.152 , pp. 3271-3281
    • Gouy, H.1    Deterre, P.2    Debre, P.3    Bismuth, G.4
  • 78
    • 0034077257 scopus 로고    scopus 로고
    • Involvement of CD2 and CD3 in galectin-1 induced signaling in human Jurkat T-cells
    • Walzel, H., M. Blach, J. Hirabayashi, et al. 2000. Involvement of CD2 and CD3 in galectin-1 induced signaling in human Jurkat T-cells. Glycobiology 10: 131-140.
    • (2000) Glycobiology , vol.10 , pp. 131-140
    • Walzel, H.1    Blach, M.2    Hirabayashi, J.3
  • 82
    • 17644361955 scopus 로고    scopus 로고
    • The NOD mouse: a model of immune dysregulation
    • Anderson, M.S. & J.A. Bluestone. 2005. The NOD mouse: a model of immune dysregulation. Annu. Rev. Immunol. 23: 447-485.
    • (2005) Annu. Rev. Immunol. , vol.23 , pp. 447-485
    • Anderson, M.S.1    Bluestone, J.A.2
  • 84
    • 58149386381 scopus 로고    scopus 로고
    • The defect in T-cell regulation in NOD mice is an effect on the T-cell effectors
    • D'Alise, A.M., V. Auyeung, M. Feuerer, et al. 2008. The defect in T-cell regulation in NOD mice is an effect on the T-cell effectors. Proc. Natl. Acad. Sci. USA 105: 19857-19862.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 19857-19862
    • D'Alise, A.M.1    Auyeung, V.2    Feuerer, M.3
  • 85
    • 80052906797 scopus 로고    scopus 로고
    • Ganglioside GM1 deficiency in effector T cells from NOD mice induces resistance to regulatory T cell suppression
    • Wu, G., Z.H. Lu, H.-J. Gabius, et al. 2011. Ganglioside GM1 deficiency in effector T cells from NOD mice induces resistance to regulatory T cell suppression. Diabetes 60: 2341-2349.
    • (2011) Diabetes , vol.60 , pp. 2341-2349
    • Wu, G.1    Lu, Z.H.2    Gabius, H.-J.3
  • 89
    • 0028280099 scopus 로고
    • Gangliosides as modulators of neuronal calcium
    • Wu, G. & R.W. Ledeen. 1994. Gangliosides as modulators of neuronal calcium. Progr. Brain Res. 101: 101-112.
    • (1994) Progr. Brain Res. , vol.101 , pp. 101-112
    • Wu, G.1    Ledeen, R.W.2
  • 90
    • 41149168525 scopus 로고    scopus 로고
    • Ganglioside GM1 effects on the expression of nerve growth factor (NGF), Trk-A receptor, proinflammatory cytokines and on autoimmune diabetes onset in non-obese diabetic (NOD) mice
    • Vieira, K.P., A.R. de Almeida e Silva Lima Zollner, C. Malaguti, et al. 2008. Ganglioside GM1 effects on the expression of nerve growth factor (NGF), Trk-A receptor, proinflammatory cytokines and on autoimmune diabetes onset in non-obese diabetic (NOD) mice. Cytokine 42: 92-104.
    • (2008) Cytokine , vol.42 , pp. 92-104
    • Vieira, K.P.1    de Almeida e Silva Lima Zollner, A.R.2    Malaguti, C.3
  • 91
    • 0028215213 scopus 로고
    • Suppression of experimental allergic encephalomyelitis in Lewis rats by administration of gangliosides
    • Shimada, K., C.S. Koh, K. Uemura & N. Yanagisawa. 1994. Suppression of experimental allergic encephalomyelitis in Lewis rats by administration of gangliosides. Cell. Immunol. 154: 231-239.
    • (1994) Cell. Immunol. , vol.154 , pp. 231-239
    • Shimada, K.1    Koh, C.S.2    Uemura, K.3    Yanagisawa, N.4
  • 92
    • 0035365092 scopus 로고    scopus 로고
    • Brain-derived gangliosides suppress the chronic relapsing-remitting experimental autoimmune encephalomyelitis in NOD mice induced with myelin oligodendrocyte glycoprotein peptide
    • Sekiguchi, Y., M. Ichikawa, A. Inoue, et al. 2001. Brain-derived gangliosides suppress the chronic relapsing-remitting experimental autoimmune encephalomyelitis in NOD mice induced with myelin oligodendrocyte glycoprotein peptide. J. Neuroimmunol. 116: 196-205.
    • (2001) J. Neuroimmunol. , vol.116 , pp. 196-205
    • Sekiguchi, Y.1    Ichikawa, M.2    Inoue, A.3
  • 93
    • 2442593609 scopus 로고    scopus 로고
    • Th1 and Th2 cytokine immunomodulation by gangliosides in experimental autoimmune encephalomyelitis
    • Monteiro de Castro, G., M. Eduarda Zanin, D. Ventura-Oliveira, et al. 2004. Th1 and Th2 cytokine immunomodulation by gangliosides in experimental autoimmune encephalomyelitis. Cytokine 26: 155-163.
    • (2004) Cytokine , vol.26 , pp. 155-163
    • Monteiro de Castro, G.1    Eduarda Zanin, M.2    Ventura-Oliveira, D.3
  • 94
    • 0025944068 scopus 로고
    • Effects of gangliosides on the expression of autoimmune demyelination in the peripheral nervous system
    • Ponzin, D., A.M. Menegus, G. Kirschner, et al. 1991. Effects of gangliosides on the expression of autoimmune demyelination in the peripheral nervous system. Ann. Neurol. 30: 678-685.
    • (1991) Ann. Neurol. , vol.30 , pp. 678-685
    • Ponzin, D.1    Menegus, A.M.2    Kirschner, G.3
  • 95
    • 0025332968 scopus 로고
    • Gangliosides offer partial protection in experimental allergic neuritis
    • Ledeen, R.W., B. Oderfeld-Nowak, C.F. Brosnan & A. Cervone. 1990. Gangliosides offer partial protection in experimental allergic neuritis. Ann. Neurol. 27(Suppl): S69-S74.
    • (1990) Ann. Neurol. , vol.27 , Issue.SUPPL.
    • Ledeen, R.W.1    Oderfeld-Nowak, B.2    Brosnan, C.F.3    Cervone, A.4
  • 96
    • 47749148805 scopus 로고    scopus 로고
    • Removal of sialic acid involving Klotho causes cell-surface retention of TRPV5 channel via binding to galectin-1
    • Cha, S.K., B. Ortega, H. Kurosu, et al. 2008. Removal of sialic acid involving Klotho causes cell-surface retention of TRPV5 channel via binding to galectin-1. Proc. Natl. Acad. Sci. USA 105: 9805-9810.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 9805-9810
    • Cha, S.K.1    Ortega, B.2    Kurosu, H.3
  • 97
    • 36849040950 scopus 로고    scopus 로고
    • Lateral compartmentalization of T cell receptor versus CD45 by galectin-N-glycan binding and microfilaments coordinate basal and activation signaling
    • Chen, I.-J., H.-L. Chen & M. Demetriou. 2007. Lateral compartmentalization of T cell receptor versus CD45 by galectin-N-glycan binding and microfilaments coordinate basal and activation signaling. J. Biol. Chem. 282: 35361-35372.
    • (2007) J. Biol. Chem. , vol.282 , pp. 35361-35372
    • Chen, I.-J.1    Chen, H.-L.2    Demetriou, M.3
  • 98
    • 33947724303 scopus 로고    scopus 로고
    • Complex N-glycan number and degree of branching cooperate to regulate cell proliferation and differentiation
    • Lau, K.S., E.A. Partridge, A. Grigorian, et al. 2007. Complex N-glycan number and degree of branching cooperate to regulate cell proliferation and differentiation. Cell 129: 123-134.
    • (2007) Cell , vol.129 , pp. 123-134
    • Lau, K.S.1    Partridge, E.A.2    Grigorian, A.3
  • 99
    • 0035825644 scopus 로고    scopus 로고
    • Negative regulation of T-cell activation and autoimmunity by Mgat5 N-glycosylation
    • Demetriou, M., M. Granovsky, S. Quaggin & J.W. Dennis. 2001. Negative regulation of T-cell activation and autoimmunity by Mgat5 N-glycosylation. Nature 409: 733-739.
    • (2001) Nature , vol.409 , pp. 733-739
    • Demetriou, M.1    Granovsky, M.2    Quaggin, S.3    Dennis, J.W.4
  • 100
    • 33646879955 scopus 로고    scopus 로고
    • Cell surface glycans: the why and how of their functionality as biochemical signals in lectin-mediated information transfer
    • Gabius, H.-J. 2006. Cell surface glycans: the why and how of their functionality as biochemical signals in lectin-mediated information transfer. Crit. Rev. Immunol. 26: 43-79.
    • (2006) Crit. Rev. Immunol. , vol.26 , pp. 43-79
    • Gabius, H.-J.1
  • 101
    • 4644305974 scopus 로고    scopus 로고
    • Human galectin-2: novel inducer of T cell apoptosis with distinct profile of caspase activation
    • Sturm, A., M. Lensch, S. André, et al. 2004. Human galectin-2: novel inducer of T cell apoptosis with distinct profile of caspase activation. J. Immunol. 173: 3825-3837.
    • (2004) J. Immunol. , vol.173 , pp. 3825-3837
    • Sturm, A.1    Lensch, M.2    André, S.3
  • 102
    • 0142057134 scopus 로고    scopus 로고
    • Homodimeric galectin-7 (p53-induced gene 1) is a negative growth regulator for human neuroblastoma cells
    • Kopitz, J., S. André, C. von Reitzenstein, et al. 2003. Homodimeric galectin-7 (p53-induced gene 1) is a negative growth regulator for human neuroblastoma cells. Oncogene 22: 6277-6288.
    • (2003) Oncogene , vol.22 , pp. 6277-6288
    • Kopitz, J.1    André, S.2    von Reitzenstein, C.3
  • 103
    • 0030785340 scopus 로고    scopus 로고
    • Galectin-4 and small intestinal brush border enzymes form clusters
    • Danielsen, E.M. & B. van Deurs. 1997. Galectin-4 and small intestinal brush border enzymes form clusters. Mol. Biol. Cell 8: 2241-2251.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 2241-2251
    • Danielsen, E.M.1    van Deurs, B.2
  • 104
    • 33645311204 scopus 로고    scopus 로고
    • Lipid raft organization and function in brush borders of epithelial cells
    • Danielsen, E.M. & G.H. Hansen. 2006. Lipid raft organization and function in brush borders of epithelial cells. Mol. Membr. Biol. 23: 71-79.
    • (2006) Mol. Membr. Biol. , vol.23 , pp. 71-79
    • Danielsen, E.M.1    Hansen, G.H.2
  • 105
    • 21044458257 scopus 로고    scopus 로고
    • Galectin-4 and sulfatides in apical membrane trafficking in enterocyte-like cells
    • Delacour, D., V. Gouyer, J.-P. Zanetta, et al. 2005. Galectin-4 and sulfatides in apical membrane trafficking in enterocyte-like cells. J. Cell Biol. 169: 491-501.
    • (2005) J. Cell Biol. , vol.169 , pp. 491-501
    • Delacour, D.1    Gouyer, V.2    Zanetta, J.-P.3
  • 106
    • 63049124765 scopus 로고    scopus 로고
    • Galectin-4-regulated delivery of glycoproteins to the brush border membrane of enterocyte-like cells
    • Stechly, L., W. Morelle, A.F. Dessein, et al. 2009. Galectin-4-regulated delivery of glycoproteins to the brush border membrane of enterocyte-like cells. Traffic 10: 438-450.
    • (2009) Traffic , vol.10 , pp. 438-450
    • Stechly, L.1    Morelle, W.2    Dessein, A.F.3
  • 107
    • 2942640032 scopus 로고    scopus 로고
    • Effects of polyvalency of glycotopes and natural modifications of human blood group ABH/Lewis sugars at the β-terminated core saccharides on the binding of domain-I of recombinant tandem-repeat-type galectin-4 from rat gastrointestinal tract (G4-N)
    • Wu, A.M., J.H. Wu, J.-H. Liu, et al. 2004. Effects of polyvalency of glycotopes and natural modifications of human blood group ABH/Lewis sugars at the β-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    Liu, J.-H.3
  • 108
    • 24944450621 scopus 로고    scopus 로고
    • Galectins bind to the multivalent glycoprotein asialofetuin with enhanced affinities and a gradient of decreasing binding constants
    • Dam, T.K., H.-J. Gabius, S. André, et al. 2005. Galectins bind to the multivalent glycoprotein asialofetuin with enhanced affinities and a gradient of decreasing binding constants. Biochemistry 44: 12564-12571.
    • (2005) Biochemistry , vol.44 , pp. 12564-12571
    • Dam, T.K.1    Gabius, H.-J.2    André, S.3
  • 109
    • 14244257721 scopus 로고    scopus 로고
    • Galectin-4 binds to sulfated glycosphingolipids and carcinoembryonic antigen in patches on the cell surface of human colon adenocarcinoma cells
    • Ideo, H., A. Seko & K. Yamashita. 2005. Galectin-4 binds to sulfated glycosphingolipids and carcinoembryonic antigen in patches on the cell surface of human colon adenocarcinoma cells. J. Biol. Chem. 280: 4730-4737.
    • (2005) J. Biol. Chem. , vol.280 , pp. 4730-4737
    • Ideo, H.1    Seko, A.2    Yamashita, K.3
  • 110
    • 68149158650 scopus 로고    scopus 로고
    • Glycosylation pattern of brush border-associated glycoproteins in enterocyte-like cells: involvement of complex-type N-glycans in apical trafficking
    • Morelle, W., L. Stechly, S. André, et al. 2009. Glycosylation pattern of brush border-associated glycoproteins in enterocyte-like cells: involvement of complex-type 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
  • 111
    • 0032714092 scopus 로고    scopus 로고
    • Secretion of the galectin family of mammalian carbohydrate-binding proteins
    • Hughes, R.C. 1999. Secretion of the galectin family of mammalian carbohydrate-binding proteins. Biochim. Biophys. Acta 1473: 172-185.
    • (1999) Biochim. Biophys. Acta , vol.1473 , pp. 172-185
    • Hughes, R.C.1
  • 112
    • 0025925260 scopus 로고
    • CD62/P-selectin recognition of myeloid and tumor cell sulfatides
    • Aruffo, A., W. Kolanus, G. Walz, et al. 1991. CD62/P-selectin recognition of myeloid and tumor cell sulfatides. Cell 67: 35-44.
    • (1991) Cell , vol.67 , pp. 35-44
    • Aruffo, A.1    Kolanus, W.2    Walz, G.3
  • 113
    • 0027183774 scopus 로고
    • Sulfated glycolipids are ligands for a lymphocyte homing receptor, L-selectin (LECAM-1), binding epitope in sulfated sugar chain
    • Suzuki, Y., Y. Toda, T. Tamatani, et al. 1993. Sulfated glycolipids are ligands for a lymphocyte homing receptor, L-selectin (LECAM-1), binding epitope in sulfated sugar chain. Biochem. Biophys. Res. Commun. 190: 426-434.
    • (1993) Biochem. Biophys. Res. Commun. , vol.190 , pp. 426-434
    • Suzuki, Y.1    Toda, Y.2    Tamatani, T.3
  • 114
    • 33846499817 scopus 로고    scopus 로고
    • P-selectin mediates metastatic progression through binding to sulfatides on tumor cells
    • Garcia, J., N. Callewaert & L. Borsig. 2007. P-selectin mediates metastatic progression through binding to sulfatides on tumor cells. Glycobiology 17: 185-196.
    • (2007) Glycobiology , vol.17 , pp. 185-196
    • Garcia, J.1    Callewaert, N.2    Borsig, L.3
  • 115
    • 71949094540 scopus 로고    scopus 로고
    • Sulfatide, a major lipid component of myelin sheath, activates inflammatory responses as an endogenous stimulator in brain-resident immune cells.
    • Jeon, S.-B., H.J. Yoon, S.-H. Park, et al. 2008. Sulfatide, a major lipid component of myelin sheath, activates inflammatory responses as an endogenous stimulator in brain-resident immune cells. J. Immunol. 181: 8077-8087.
    • (2008) J. Immunol. , vol.181 , pp. 8077-8087
    • Jeon, S.-B.1    Yoon, H.J.2    Park, S.-H.3
  • 116
    • 0345329271 scopus 로고    scopus 로고
    • New aspects of galectin functionality in nuclei of cultured bone marrow stromal and epidermal cells: biotinylated galectins as tool to detect specific binding sites
    • Purkrábková, T., K. Smetana Jr., B. Dvoránková, et al. 2003. New aspects of galectin functionality in nuclei of cultured bone marrow stromal and epidermal cells: biotinylated galectins as tool to detect specific binding sites. Biol. Cell 95: 535-545.
    • (2003) Biol. Cell , vol.95 , pp. 535-545
    • Purkrábková, T.1    Smetana Jr., K.2    Dvoránková, B.3
  • 117
    • 30044443669 scopus 로고    scopus 로고
    • Nuclear presence of adhesion/growth-regulatory galectins in normal/malignant cells of squamous epithelial origin
    • Smetana Jr., K., B. Dvoránková, M. Chovanec, et al. 2006. Nuclear presence of adhesion/growth-regulatory galectins in normal/malignant cells of squamous epithelial origin. Histochem. Cell Biol. 125: 171-182.
    • (2006) Histochem. Cell Biol. , vol.125 , pp. 171-182
    • Smetana Jr., K.1    Dvoránková, B.2    Chovanec, M.3
  • 118
    • 38449087709 scopus 로고    scopus 로고
    • GM1 in the nuclear envelope regulates nuclear calcium through association with a nuclear sodium-calcium exchanger
    • Ledeen, R.W. & G. Wu. 2007. GM1 in the nuclear envelope regulates nuclear calcium through association with a nuclear sodium-calcium exchanger. J. Neurochem. 103(Suppl 1): 126-134.
    • (2007) J. Neurochem. , vol.103 , Issue.SUPPL. 1 , pp. 126-134
    • Ledeen, R.W.1    Wu, G.2
  • 119
    • 77949293368 scopus 로고    scopus 로고
    • Dynamics of galectin-3 in the nucleus and cytoplasm
    • Haudek, K.C., K.J. Spronk, P.G. Voss, et al. 2010. Dynamics of galectin-3 in the nucleus and cytoplasm. Biochim. Biophys. Acta 1800: 181-189.
    • (2010) Biochim. Biophys. Acta , vol.1800 , pp. 181-189
    • Haudek, K.C.1    Spronk, K.J.2    Voss, P.G.3
  • 120
    • 84855380062 scopus 로고    scopus 로고
    • Comparative analysis of nuclear presence of adhesion/growth-regulatory galectins and galectin reactivity in interphasic and mitotic cells
    • Kodet, O., B. Dvoránková, L. Lacina, et al. 2011. Comparative analysis of nuclear presence of adhesion/growth-regulatory galectins and galectin reactivity in interphasic and mitotic cells. Folia Biol. (Praha) 57: 125-132.
    • (2011) Folia Biol. (Praha) , vol.57 , pp. 125-132
    • Kodet, O.1    Dvoránková, B.2    Lacina, L.3
  • 121
    • 79851492113 scopus 로고    scopus 로고
    • New findings on nuclear gangliosides: overview on metabolism and function
    • Ledeen, R.W. & G. Wu. 2011. New findings on nuclear gangliosides: overview on metabolism and function. J. Neurochem. 116: 714-720.
    • (2011) J. Neurochem. , vol.116 , pp. 714-720
    • Ledeen, R.W.1    Wu, G.2
  • 122
    • 77955902749 scopus 로고    scopus 로고
    • Animal and human lectins
    • H.-J. Gabius, Ed.:. Wiley-VCH. Weinheim, Germany.
    • Gabius, H.-J. 2009. Animal and human lectins. In The Sugar Code. Fundamentals of Glycosciences. H.-J. Gabius, Ed.: 317-328. Wiley-VCH. Weinheim, Germany.
    • (2009) The Sugar Code. Fundamentals of Glycosciences , pp. 317-328
    • Gabius, H.-J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.