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Volumn , Issue , 2008, Pages 71-85

Galectins as Regulators of Tumor Growth and Invasion by Targeting Distinct Cell Surface Glycans and Implications for Drug Design

Author keywords

Compound libraries and dendrimers; Drug design galectin growth invasion regulatory activity; Galectins tumor growth regulators

Indexed keywords


EID: 84887258429     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9780470378076.ch4     Document Type: Chapter
Times cited : (5)

References (44)
  • 1
    • 0034079042 scopus 로고    scopus 로고
    • Biological information transfer beyond the genetic code: the sugar code
    • Gabius H-J. Biological information transfer beyond the genetic code: the sugar code. Naturwissenschaften 2000;87:108-121.
    • (2000) Naturwissenschaften , vol.87 , pp. 108-121
    • Gabius, H.-J.1
  • 3
    • 0023187733 scopus 로고
    • Endogenous lectins in tumors and the immune system
    • Gabius H-J. Endogenous lectins in tumors and the immune system. Cancer Invest 1987;5:39-46.
    • (1987) Cancer Invest , vol.5 , pp. 39-46
    • Gabius, H.-J.1
  • 4
    • 0031029256 scopus 로고    scopus 로고
    • Animal lectins
    • Gabius H-J. Animal lectins. Eur J Biochem 1997;243:543-576.
    • (1997) Eur J Biochem , vol.243 , pp. 543-576
    • Gabius, H.-J.1
  • 5
    • 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. Cell surface glycans: the why and how of their functionality as biochemical signals in lectin-mediated information transfer. Crit Rev Immunol 2006;26:43-80.
    • (2006) Crit Rev Immunol , vol.26 , pp. 43-80
    • Gabius, H.-J.1
  • 6
    • 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, Nogales-Gonzalés A, Gabius H-J. A guide to signaling pathways connecting protein-glycan interaction with the emerging versatile effector functionality of mammalian lectins. Trends Glycosci Glycotechnol 2006;18:1-37.
    • (2006) Trends Glycosci Glycotechnol , vol.18 , pp. 1-37
    • Villalobo, A.1    Nogales-Gonzalés, A.2    Gabius, H.-J.3
  • 7
    • 0035070675 scopus 로고    scopus 로고
    • Evidence for stimulation of tumor proliferation in cell lines and histotypic cultures by clinically relevant low doses of the galactoside-binding mistletoe lectin, a component of proprietary extracts
    • Gabius H-J, Darro F, Remmelink M, André S, Kopitz J, Danguy A, Gabius S, Salmon I, Kiss R. Evidence for stimulation of tumor proliferation in cell lines and histotypic cultures by clinically relevant low doses of the galactoside-binding mistletoe lectin, a component of proprietary extracts. Cancer Invest 2001;19:114-126.
    • (2001) Cancer Invest , vol.19 , pp. 114-126
    • Gabius, H.-J.1    Darro, F.2    Remmelink, M.3    André, S.4    Kopitz, J.5    Danguy, A.6    Gabius, S.7    Salmon, I.8    Kiss, R.9
  • 9
    • 0022854422 scopus 로고
    • Specificity of binding of soluble rat lung lectins to substituted and unsubstituted mammalian b-galactosides
    • Leffler H, Barondes SH. Specificity of binding of soluble rat lung lectins to substituted and unsubstituted mammalian b-galactosides. J Biol Chem 1986;261:10119-10126.
    • (1986) J Biol Chem , vol.261 , pp. 10119-10126
    • Leffler, H.1    Barondes, S.H.2
  • 10
    • 0025076613 scopus 로고
    • Influence of type of linkage and spacer on the interaction of b-galactosidebinding proteins with immobilized affinity ligands
    • Gabius H-J. Influence of type of linkage and spacer on the interaction of b-galactosidebinding proteins with immobilized affinity ligands. Anal Biochem 1990;189:91-94.
    • (1990) Anal Biochem , vol.189 , pp. 91-94
    • Gabius, H.-J.1
  • 11
    • 0036436051 scopus 로고    scopus 로고
    • Thermodynamic binding studies of cell surface carbohydrate epitopes to galectins-1, -3 and -7. Evidence for differential binding specificities
    • Ahmad N, Gabius H-J, Kaltner H, André S, Kuwabara I, Liu F-T, Oscarson S, Norberg T, Brewer CF. Thermodynamic binding studies of cell surface carbohydrate epitopes to galectins-1, -3 and -7. Evidence for differential binding specificities. Can J Chem 2002;80:1096-1104.
    • (2002) Can J Chem , vol.80 , pp. 1096-1104
    • Ahmad, N.1    Gabius, H.-J.2    Kaltner, H.3    André, S.4    Kuwabara, I.5    Liu, F.-T.6    Oscarson, S.7    Norberg, T.8    Brewer, C.F.9
  • 12
    • 33846518464 scopus 로고    scopus 로고
    • Activity-structure correlations in divergent lectin evolution: fine specificity of chicken galectin CG-14 and computational analysis of flexible ligand docking for CG-14 and the closely related CG-16
    • Wu AM, Singh T, Liu J-H, Krzeminski M, Russwurm R, Siebert H-C, Bonvin AMJJ, André S, Gabius H-J. Activity-structure correlations in divergent lectin evolution: fine specificity of chicken galectin CG-14 and computational analysis of flexible ligand docking for CG-14 and the closely related CG-16. Glycobiology 2007;17:165-184.
    • (2007) Glycobiology , vol.17 , pp. 165-184
    • Wu, A.M.1    Singh, T.2    Liu, J.-H.3    Krzeminski, M.4    Russwurm, R.5    Siebert, H.-C.6    Bonvin, A.M.J.J.7    André, S.8    Gabius, H.-J.9
  • 13
    • 0037635976 scopus 로고    scopus 로고
    • Detection of ligandand solvent-induced shape alterations of cell-growth-regulatory human lectin galectin-1 in solution by small angle neutron and X-ray scattering
    • He L, André S, Siebert H-C, Helmholz H, Niemeyer B, Gabius H-J. Detection of ligandand solvent-induced shape alterations of cell-growth-regulatory human lectin galectin-1 in solution by small angle neutron and X-ray scattering. Biophys J 2003;85:511-524.
    • (2003) Biophys J , vol.85 , pp. 511-524
    • He, L.1    André, S.2    Siebert, H.-C.3    Helmholz, H.4    Niemeyer, B.5    Gabius, H.-J.6
  • 14
    • 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 MF, Solís D, André S, Hirabayashi J, Kasai K-i, Kaltner H, Gabius H-J, Romero A. 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 2004;343:957-970.
    • (2004) J Mol Biol , vol.343 , pp. 957-970
    • López-Lucendo, M.F.1    Solís, D.2    André, S.3    Hirabayashi, J.4    Kasai, K.-I.5    Kaltner, H.6    Gabius, H.-J.7    Romero, A.8
  • 15
    • 0035884413 scopus 로고    scopus 로고
    • Carbohydrate specificity of a galectin from chicken liver (CG-16)
    • Wu AM,Wu JH, Tsai M-S, Kaltner H, Gabius H-J. Carbohydrate specificity of a galectin from chicken liver (CG-16). Biochem J 2001;358:529-538.
    • (2001) Biochem J , vol.358 , pp. 529-538
    • Wu, A.M.1    Wu, J.H.2    Tsai, M.-S.3    Kaltner, H.4    Gabius, H.-J.5
  • 16
    • 0036846884 scopus 로고    scopus 로고
    • Fine specificity of domain-I of recombinant tandem-repeat-type galectin-4 from rat gastrointestinal tract (G4-N)
    • Wu AM, Wu JH, Tsai M-S, Liu J-H, André S, Wasano K, Kaltner H, Gabius H-J. Fine specificity of domain-I of recombinant tandem-repeat-type galectin-4 from rat gastrointestinal tract (G4-N). Biochem J 2002;367:653-664.
    • (2002) Biochem J , vol.367 , pp. 653-664
    • Wu, A.M.1    Wu, J.H.2    Tsai, M.-S.3    Liu, J.-H.4    André, S.5    Wasano, K.6    Kaltner, H.7    Gabius, H.-J.8
  • 17
    • 2942640032 scopus 로고    scopus 로고
    • Effects of polyvalency of glycotopes and natural modifications of human blood group ABH/Lewis sugars at the Galb1-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, Liu J-H, Singh T, André S, Kaltner H, Gabius H-J. Effects of polyvalency of glycotopes and natural modifications of human blood group ABH/Lewis sugars at the Galb1-terminated core saccharides on the binding of domain-I of recombinant tandem-repeat-type galectin-4 from rat gastrointestinal tract (G4-N) Biochimie 2004;86:317-326.
    • (2004) Biochimie , vol.86 , pp. 317-326
    • Wu, A.M.1    Wu, J.H.2    Liu, J.-H.3    Singh, T.4    André, S.5    Kaltner, H.6    Gabius, H.-J.7
  • 18
    • 33646863285 scopus 로고    scopus 로고
    • Interaction profile of galectin-5 with free saccharides and mammalian glycoproteins: probing its fine-specificity and the effect of naturally clustered ligand presentation
    • Wu AM, Singh T,Wu JH, Lensch M, André S, Gabius H-J. Interaction profile of galectin-5 with free saccharides and mammalian glycoproteins: probing its fine-specificity and the effect of naturally clustered ligand presentation. Glycobiology 2006;16:524-537.
    • (2006) Glycobiology , vol.16 , pp. 524-537
    • Wu, A.M.1    Singh, T.2    Wu, J.H.3    Lensch, M.4    André, S.5    Gabius, H.-J.6
  • 19
    • 1642499128 scopus 로고    scopus 로고
    • Determination of modulation of ligand properties of synthetic complex-type biantennary N-glycans by introduction of bisecting GlcNAc in silico, in vitro and in vivo
    • André S, Unverzagt C, Kojima S, Frank M, Seifert J, Fink C, Kayser K, von der Lieth C-W, Gabius H-J. Determination of modulation of ligand properties of synthetic complex-type biantennary N-glycans by introduction of bisecting GlcNAc in silico, in vitro and in vivo. Eur J Biochem 2004;271:118-134.
    • (2004) Eur J Biochem , vol.271 , pp. 118-134
    • André, S.1    Unverzagt, C.2    Kojima, S.3    Frank, M.4    Seifert, J.5    Fink, C.6    Kayser, K.7    Von Der Lieth, C.-W.8    Gabius, H.-J.9
  • 20
    • 17444365412 scopus 로고    scopus 로고
    • Introduction of extended LEC14-type branching into core-fucosylated biantennary N-glycan. Glycoengineering for enhanced cell binding and serum clearance of the neoglycoprotein
    • André S, Kojima S, Prahl I, Lensch M, Unverzagt C, Gabius H-J. Introduction of extended LEC14-type branching into core-fucosylated biantennary N-glycan. Glycoengineering for enhanced cell binding and serum clearance of the neoglycoprotein. FEBS J 2005; 272:1986-1998.
    • (2005) FEBS J , vol.272 , pp. 1986-1998
    • André, S.1    Kojima, S.2    Prahl, I.3    Lensch, M.4    Unverzagt, C.5    Gabius, H.-J.6
  • 21
    • 34250216008 scopus 로고    scopus 로고
    • Substitutions in the N-glycan core as regulators of biorecognition: the case of core-fucose and bisecting GlcNAc moieties
    • André S, Kozár T, Schuberth R, Unverzagt C, Kojima S, Gabius H-J. Substitutions in the N-glycan core as regulators of biorecognition: the case of core-fucose and bisecting GlcNAc moieties. Biochemistry 2007;46:6984-6995.
    • (2007) Biochemistry , vol.46 , pp. 6984-6995
    • André, S.1    Kozár, T.2    Schuberth, R.3    Unverzagt, C.4    Kojima, S.5    Gabius, H.-J.6
  • 22
    • 24944450621 scopus 로고    scopus 로고
    • Galectins bind to the multivalent glycoprotein asialofetuin with enhanced affinities and a gradient of decreasing binding constants
    • Dam TK, Gabius H-J, André S, Kaltner H, Lensch M, Brewer CF. Galectins bind to the multivalent glycoprotein asialofetuin with enhanced affinities and a gradient of decreasing binding constants. Biochemistry 2005;44:12564-12571.
    • (2005) Biochemistry , vol.44 , pp. 12564-12571
    • Dam, T.K.1    Gabius, H.-J.2    André, S.3    Kaltner, H.4    Lensch, M.5    Brewer, C.F.6
  • 26
    • 0034267915 scopus 로고    scopus 로고
    • CD7 delivers a pro-apoptotic signal during galectin-1-induced T cell death
    • Pace KE, Hahn HP, Pang M, Nguyen JT, Baum LG. CD7 delivers a pro-apoptotic signal during galectin-1-induced T cell death. J Immunol 2000;165:2331-2334.
    • (2000) J Immunol , vol.165 , pp. 2331-2334
    • Pace, K.E.1    Hahn, H.P.2    Pang, M.3    Nguyen, J.T.4    Baum, L.G.5
  • 28
    • 0032080122 scopus 로고    scopus 로고
    • Galectin-1 is a major receptor for gangliosideGM1, a product of the growth-controlling activity of a cell surface ganglioside sialidase, on human neuroblastoma cells in culture
    • Kopitz J, von Reitzenstein C, Burchert M, Cantz M, Gabius H-J. Galectin-1 is a major receptor for gangliosideGM1, a product of the growth-controlling activity of a cell surface ganglioside sialidase, on human neuroblastoma cells in culture. J Biol Chem 1998;273:11205-11211.
    • (1998) J Biol Chem , vol.273 , pp. 11205-11211
    • Kopitz, J.1    Von Reitzenstein, C.2    Burchert, M.3    Cantz, M.4    Gabius, H.-J.5
  • 29
    • 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, von Reitzenstein C, André S, Kaltner H, Uhl J, Ehemann V, Cantz M, Gabius H-J. Negative regulation of neuroblastoma cell growth by carbohydrate-dependent surface binding of galectin-1 and functional divergence from galectin-3. J Biol Chem 2001;276:35917-35923.
    • (2001) J Biol Chem , vol.276 , pp. 35917-35923
    • Kopitz, J.1    Von Reitzenstein, C.2    André, S.3    Kaltner, H.4    Uhl, J.5    Ehemann, V.6    Cantz, M.7    Gabius, H.-J.8
  • 30
    • 19944431311 scopus 로고    scopus 로고
    • Determination of structural and functional overlap/divergence of five prototype galectins by analysis of the growthregulatory interaction with gangliosideGM1in silico and in vitro on human neuroblastoma cells
    • André S, Kaltner H, Lensch M, Russwurm R, Siebert H-C, Fallsehr C, Tajkhorshid E, Heck AJR, von Knebel-Döberitz M, Gabius H-J, Kopitz J. Determination of structural and functional overlap/divergence of five prototype galectins by analysis of the growthregulatory interaction with gangliosideGM1in silico and in vitro on human neuroblastoma cells. Int J Cancer 2005;114:46-57.
    • (2005) Int J Cancer , vol.114 , pp. 46-57
    • André, S.1    Kaltner, H.2    Lensch, M.3    Russwurm, R.4    Siebert, H.-C.5    Fallsehr, C.6    Tajkhorshid, E.7    Heck, A.J.R.8    Von Knebel-Döberitz, M.9    Gabius, H.-J.10    Kopitz, J.11
  • 32
    • 0030045734 scopus 로고    scopus 로고
    • NMR-based, molecular dynamics- and random walk molecular mechanics-supported study of conformational aspects of a carbohydrate ligand (Galb1-2Galb1-R) for an animal galectin in the free and in the bound state
    • Siebert H-C, Gilleron M, Kaltner H, von der Lieth C-W, Kozár T, Bovin NV, Korchagina EY, Vliegenthart JFG, Gabius H-J. NMR-based, molecular dynamics- and random walk molecular mechanics-supported study of conformational aspects of a carbohydrate ligand (Galb1-2Galb1-R) for an animal galectin in the free and in the bound state. Biochem Biophys Res Commun 1996;219:205-212.
    • (1996) Biochem Biophys Res Commun , vol.219 , pp. 205-212
    • Siebert, H.-C.1    Gilleron, M.2    Kaltner, H.3    Von Der Lieth, C.-W.4    Kozár, T.5    Bovin, N.V.6    Korchagina, E.Y.7    Vliegenthart, J.F.G.8    Gabius, H.-J.9
  • 34
    • 29544439155 scopus 로고    scopus 로고
    • Carbohydrate chain of ganglioside GM1 as a ligand: identification of the binding strategies of three 15mer peptides and their divergence from the binding modes of growth-regulatory galectin-1 and cholera toxin
    • Siebert H-C, Born K, André S, Frank M, Kaltner H, von der Lieth C-W, Heck AJR, Jiménez-Barbero J, Kopitz J, Gabius H-J. Carbohydrate chain of ganglioside GM1 as a ligand: identification of the binding strategies of three 15mer peptides and their divergence from the binding modes of growth-regulatory galectin-1 and cholera toxin. Chem Eur J 2006;12:388-402.
    • (2006) Chem Eur J , vol.12 , pp. 388-402
    • Siebert, H.-C.1    Born, K.2    André, S.3    Frank, M.4    Kaltner, H.5    Von Der Lieth, C.-W.6    Heck, A.J.R.7    Jiménez-Barbero, J.8    Kopitz, J.9    Gabius, H.-J.10
  • 37
    • 33747134305 scopus 로고    scopus 로고
    • Glycosyldisulfides from dynamic combinatorial libraries as O-glycoside mimetics for plant and mammalian lectins: their reactivities in solid-phase and cell assays and conformational analysis by molecular dynamics simulations
    • André S, Pei Z, Siebert H-C, Ramstrm O, Gabius H-J. Glycosyldisulfides from dynamic combinatorial libraries as O-glycoside mimetics for plant and mammalian lectins: their reactivities in solid-phase and cell assays and conformational analysis by molecular dynamics simulations. Bioorg Med Chem 2006;14:6314-6323.
    • (2006) Bioorg Med Chem , vol.14 , pp. 6314-6323
    • André, S.1    Pei, Z.2    Siebert, H.-C.3    Ramstrm, O.4    Gabius, H.-J.5
  • 38
    • 33846241804 scopus 로고    scopus 로고
    • Discovery of galectin ligands in fully randomized combinatorial one-bead-one-compound (glyco)peptide libraries
    • André S, Maljaars CEP, Halkes KM, Gabius H-J, Kamerling JP. Discovery of galectin ligands in fully randomized combinatorial one-bead-one-compound (glyco)peptide libraries. Bioorg Med Chem Lett 2007;17:793-798.
    • (2007) Bioorg Med Chem Lett , vol.17 , pp. 793-798
    • André, S.1    Maljaars, C.E.P.2    Halkes, K.M.3    Gabius, H.-J.4    Kamerling, J.P.5
  • 39
    • 2342508517 scopus 로고    scopus 로고
    • Galectin-1(L11A) predicted from a computed galectin-1 farnesyl-binding pocket selectively inhibits Ras-GTP
    • Rotblat B, Niv H, André S, Kaltner H, Gabius H-J, Kloog Y. Galectin-1(L11A) predicted from a computed galectin-1 farnesyl-binding pocket selectively inhibits Ras-GTP. Cancer Res 2004;64:3112-3118.
    • (2004) Cancer Res , vol.64 , pp. 3112-3118
    • Rotblat, B.1    Niv, H.2    André, S.3    Kaltner, H.4    Gabius, H.-J.5    Kloog, Y.6
  • 40
    • 0012061680 scopus 로고    scopus 로고
    • Lactose-containing starburst dendrimers: influence of dendrimer generation and binding-site orientation of receptors (plant/animal lectins and immunoglobulins) on binding properties
    • André S, Cejas Ortega PJ, Alamino Perez M, Roy R, Gabius H-J. Lactose-containing starburst dendrimers: influence of dendrimer generation and binding-site orientation of receptors (plant/animal lectins and immunoglobulins) on binding properties. Glycobiology 1999;9:1253-1261.
    • (1999) Glycobiology , vol.9 , pp. 1253-1261
    • André, S.1    Cejas Ortega, P.J.2    Alamino Perez, M.3    Roy, R.4    Gabius, H.-J.5
  • 41
    • 0035814138 scopus 로고    scopus 로고
    • Wedgelike glycodendrimers as inhibitors of binding ofmammalian galectins to various glycoproteins, lactose maxiclusters and cell surface glycoconjugates
    • André S, Pieters RJ, Vrasidas I, Kaltner H, Kuwabara I, Liu F-T, Liskamp RMJ, Gabius H-J. Wedgelike glycodendrimers as inhibitors of binding ofmammalian galectins to various glycoproteins, lactose maxiclusters and cell surface glycoconjugates. Chem Bio Chem 2001;2:822-830.
    • (2001) Chem Bio Chem , vol.2 , pp. 822-830
    • André, S.1    Pieters, R.J.2    Vrasidas, I.3    Kaltner, H.4    Kuwabara, I.5    Liu, F.-T.6    Liskamp, R.M.J.7    Gabius, H.-J.8
  • 42
    • 0842328412 scopus 로고    scopus 로고
    • Persubstituted cyclodextrinbased glycoclusters as inhibitors of protein-carbohydrate recognition using purified plant and mammalian lectins and wild-type and lectin-gene-transfected tumor cells as targets
    • André S, Kaltner H, Furuike T, Nishimura S-I, Gabius H-J. Persubstituted cyclodextrinbased glycoclusters as inhibitors of protein-carbohydrate recognition using purified plant and mammalian lectins and wild-type and lectin-gene-transfected tumor cells as targets. Bioconjug Chem 2004;15:87-98.
    • (2004) Bioconjug Chem , vol.15 , pp. 87-98
    • André, S.1    Kaltner, H.2    Furuike, T.3    Nishimura, S.-I.4    Gabius, H.-J.5
  • 43
    • 0344515363 scopus 로고    scopus 로고
    • First demonstration of differential inhibition of lectin binding by synthetic tri- and tetravalent glycoclusters from cross-coupling of rigidified 2-propynyl lactoside
    • André S, Liu B, Gabius H-J, Roy R. First demonstration of differential inhibition of lectin binding by synthetic tri- and tetravalent glycoclusters from cross-coupling of rigidified 2-propynyl lactoside. Org Biomol Chem 2003;1:3909-3916.
    • (2003) Org Biomol Chem , vol.1 , pp. 3909-3916
    • André, S.1    Liu, B.2    Gabius, H.-J.3    Roy, R.4
  • 44
    • 1642483757 scopus 로고    scopus 로고
    • Galectin-3 precipitates as a pentamer with synthetic multivalent carbohydrates and forms heterogeneous cross-linked complexes
    • Ahmad N, Gabius H-J, André S, Kaltner H, Sabesan S, Roy R, Liu B, Macaluso F, Brewer CF. Galectin-3 precipitates as a pentamer with synthetic multivalent carbohydrates and forms heterogeneous cross-linked complexes. J Biol Chem 2004;279:10841-10847.
    • (2004) J Biol Chem , vol.279 , pp. 10841-10847
    • Ahmad, N.1    Gabius, H.-J.2    André, S.3    Kaltner, H.4    Sabesan, S.5    Roy, R.6    Liu, B.7    Macaluso, F.8    Brewer, C.F.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.