메뉴 건너뛰기




Volumn 48, Issue 4, 2009, Pages 786-791

Critical role of the solvent environment in galectin-1 binding to the disaccharide lactose

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEINS; CARBOHYDRATE LIGANDS; CARBOHYDRATE-RECOGNITION DOMAINS; DISACCHARIDE LACTOSE; GALECTIN-1; GLYCOCONJUGATES; IMMUNE CELLS; INFLAMMATORY RESPONSE; LIGAND BINDINGS; MOLECULAR DYNAMIC SIMULATIONS; PHYSICO-CHEMICAL PROPERTIES; RADIAL DISTRIBUTION FUNCTIONS; ROLE OF WATERS; SOLVENT ENVIRONMENTS; SOLVENT REORGANIZATIONS; STRUCTURAL CHANGES; SYNTHETIC INHIBITORS; TUMOR PROGRESSIONS; UV-RAMAN SPECTRUM; UV-RESONANCE RAMAN SPECTROSCOPIES;

EID: 60749084683     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi801855g     Document Type: Article
Times cited : (22)

References (38)
  • 1
    • 0032875554 scopus 로고    scopus 로고
    • God must love galectins; he made so many of them
    • Cooper, D. N. W., and Barondes, S. H. (1999) God must love galectins; he made so many of them. Glycobiology 9, 979-984.
    • (1999) Glycobiology , vol.9 , pp. 979-984
    • Cooper, D.N.W.1    Barondes, S.H.2
  • 2
    • 0028986609 scopus 로고
    • Galectin-1, a β-galactoside- binding lectin in Chinese hamster ovary cells. I. Physical and chemical characterization
    • Cho, M., and Cummings, R. D. (1995) Galectin-1, a β-galactoside- binding lectin in Chinese hamster ovary cells. I. Physical and chemical characterization. J. Biol. Chem. 270, 5198-5206.
    • (1995) J. Biol. Chem , vol.270 , pp. 5198-5206
    • Cho, M.1    Cummings, R.D.2
  • 6
    • 18044374479 scopus 로고    scopus 로고
    • Galectin-1 as a potential cancer target
    • Rabinovich, G. A. (2005) Galectin-1 as a potential cancer target. Br. J. Cancer 92, 1188-1192.
    • (2005) Br. J. Cancer , vol.92 , pp. 1188-1192
    • Rabinovich, G.A.1
  • 7
    • 34447301574 scopus 로고    scopus 로고
    • An emerging role for lectins in tuning the immune response: Lessons from experimental models of inflammatory disease, autoimmunity and cancer
    • Rabinovich, G. A., Liu, F. T., Hirashima, M., and Anderson, A. (2007) An emerging role for lectins in tuning the immune response: Lessons from experimental models of inflammatory disease, autoimmunity and cancer. Scand. J. Immunol. 66, 143-158.
    • (2007) Scand. J. Immunol , vol.66 , pp. 143-158
    • Rabinovich, G.A.1    Liu, F.T.2    Hirashima, M.3    Anderson, A.4
  • 8
    • 34447136940 scopus 로고    scopus 로고
    • Galectins: Matricellular glycan-binding proteins linking cell adhesion, migration and survival
    • Elola, M. T., Wolfenstein-Todel, Ç., Troncoso, M. F., Vasta, G. R., and Rabinovich, G. A. (2007) Galectins: Matricellular glycan-binding proteins linking cell adhesion, migration and survival. Cell. Mol. Life Sci. 64, 1679-1700.
    • (2007) Cell. Mol. Life Sci , vol.64 , pp. 1679-1700
    • Elola, M.T.1    Wolfenstein-Todel, C.2    Troncoso, M.F.3    Vasta, G.R.4    Rabinovich, G.A.5
  • 9
    • 0032823402 scopus 로고    scopus 로고
    • Galectins-1 and -3 and their ligands in tumor biology. Non-uniform properties in cell-surface presentation and modulation of adhesion to matrix glycoproteins for various tumor cell lines, in biodistribution of free and liposome-bound galectins and in their expression by breast and colorectal carcinomas with/without metastatic propensity
    • Andre, S., Kojima, S., Yamazaki, N., Fink, C., Kaltner, H., Kayser, K., and Gabius, H. J. (1999) Galectins-1 and -3 and their ligands in tumor biology. Non-uniform properties in cell-surface presentation and modulation of adhesion to matrix glycoproteins for various tumor cell lines, in biodistribution of free and liposome-bound galectins and in their expression by breast and colorectal carcinomas with/without metastatic propensity. J. Cancer Res. Clin. Oncol. 125, 461-474.
    • (1999) J. Cancer Res. Clin. Oncol , vol.125 , pp. 461-474
    • Andre, S.1    Kojima, S.2    Yamazaki, N.3    Fink, C.4    Kaltner, H.5    Kayser, K.6    Gabius, H.J.7
  • 10
    • 0033561213 scopus 로고    scopus 로고
    • Galectin-1, a natural ligand for the receptor-type protein tyrosine phosphatase CD45
    • Walzel, H., Schulz, U., Neels, P., and Brock, J. (1999) Galectin-1, a natural ligand for the receptor-type protein tyrosine phosphatase CD45. Immunol. Lett. 67, 193-202.
    • (1999) Immunol. Lett , vol.67 , pp. 193-202
    • Walzel, H.1    Schulz, U.2    Neels, P.3    Brock, J.4
  • 11
    • 0028053242 scopus 로고
    • Selective modulation of the interaction of α 7β1 integrin with fibronectin and laminin by L-14 lectin during skeletal muscle differentiation
    • Gu, M., Wang, W., Song, W. K., Cooper, D. N., and Kaufman, S. J. (1994) Selective modulation of the interaction of α 7β1 integrin with fibronectin and laminin by L-14 lectin during skeletal muscle differentiation. J. Cell Sci. 107, 175-181.
    • (1994) J. Cell Sci , vol.107 , pp. 175-181
    • Gu, M.1    Wang, W.2    Song, W.K.3    Cooper, D.N.4    Kaufman, S.J.5
  • 12
    • 0032080122 scopus 로고    scopus 로고
    • Galectin-1 is a major receptor for ganglioside GM1, 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., and Gabius, H. J. (1998) Galectin-1 is a major receptor for ganglioside GM1, 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    Cantz, M.4    Gabius, H.J.5
  • 13
    • 0141704154 scopus 로고    scopus 로고
    • Molecular Dynamics Simulations of Galectin-1-oligosaccharides Complexes Reveal the Molecular Basis of Ligand Diversity
    • Ford, M. G., Weimar, T, Kölhi, T., and Woods, R. J. (2003) Molecular Dynamics Simulations of Galectin-1-oligosaccharides Complexes Reveal the Molecular Basis of Ligand Diversity. Proteins: Struct., Funct., Genet. 53, 229-240.
    • (2003) Proteins: Struct., Funct., Genet , vol.53 , pp. 229-240
    • Ford, M.G.1    Weimar, T.2    Kölhi, T.3    Woods, R.J.4
  • 14
    • 4444329794 scopus 로고    scopus 로고
    • Thermodynamic binding studies of bivalent oligosaccharides to galectin-1, galectin-3, and the carbohydrate recognition domain of galectin-3
    • Ahmad, N., Gabius, H., Sabesan, S., Oscarson, S., and Brewer, C. F. (2004) Thermodynamic binding studies of bivalent oligosaccharides to galectin-1, galectin-3, and the carbohydrate recognition domain of galectin-3. Glycobiology 14, 817-825.
    • (2004) Glycobiology , vol.14 , pp. 817-825
    • Ahmad, N.1    Gabius, H.2    Sabesan, S.3    Oscarson, S.4    Brewer, C.F.5
  • 15
    • 0034257212 scopus 로고    scopus 로고
    • Asensio, J. L., Siebert, H.-C., von der Lieth, C.-W., Laynez, J., Bruix, M., Soedjanaamadja, U. M., Beintema, J. J., Canada, F. J., Gabius, H., and Jiménez-Barbero, J. (2000) NMR Investigations of Protein-Carbohydrate Interactions: Studies on the Relevance of Trp/Tyr Variations in Lectin Binding Sites as Deduced from Titration Microcalorimetry and NMR Studies on Hevein Domains. Determination of the NMR Structure of the Complex Between Pseudohevein and N,N′,N′-Triacetylchitotriose. Proteins: Struct., Funct., Genet. 40, 218-236.
    • Asensio, J. L., Siebert, H.-C., von der Lieth, C.-W., Laynez, J., Bruix, M., Soedjanaamadja, U. M., Beintema, J. J., Canada, F. J., Gabius, H., and Jiménez-Barbero, J. (2000) NMR Investigations of Protein-Carbohydrate Interactions: Studies on the Relevance of Trp/Tyr Variations in Lectin Binding Sites as Deduced from Titration Microcalorimetry and NMR Studies on Hevein Domains. Determination of the NMR Structure of the Complex Between Pseudohevein and N,N′,N′-Triacetylchitotriose. Proteins: Struct., Funct., Genet. 40, 218-236.
  • 17
    • 13644272606 scopus 로고    scopus 로고
    • Structural and Thermodynamic Studies on Cation-π interactions in Lectin-Ligand Complexes: High-Affinity Galectin-3 Inhibitors through Fine-Tuning of an Arginine-Arene Interaction
    • Sörme, P., Arnoux, P., Kahl-Knutsson, B., Leffler, H., Rini, J. M., and Nilsson, U. J. (2005) Structural and Thermodynamic Studies on Cation-π interactions in Lectin-Ligand Complexes: High-Affinity Galectin-3 Inhibitors through Fine-Tuning of an Arginine-Arene Interaction. J. Am. Chem. Soc. 127, 1737-1743.
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 1737-1743
    • Sörme, P.1    Arnoux, P.2    Kahl-Knutsson, B.3    Leffler, H.4    Rini, J.M.5    Nilsson, U.J.6
  • 18
    • 33144454670 scopus 로고    scopus 로고
    • Synthetic lactulose amines: Novel class of anticancer agents that induce tumor-cell apoptosis and inhibit galectin-mediated homotypic cell aggregation and endothelial cell morphogenesis
    • Rabinovich, G A., Cumashi, A., Bianco, G. A., Ciavardelli, D., Iurisci, I., D'Egidio, M., Piccolo, E., Tinari, N., Nifantiev, N., and Iacobelli, S. (2005) Synthetic lactulose amines: Novel class of anticancer agents that induce tumor-cell apoptosis and inhibit galectin-mediated homotypic cell aggregation and endothelial cell morphogenesis. Glycobiology 16, 210-220.
    • (2005) Glycobiology , vol.16 , pp. 210-220
    • Rabinovich, G.A.1    Cumashi, A.2    Bianco, G.A.3    Ciavardelli, D.4    Iurisci, I.5    D'Egidio, M.6    Piccolo, E.7    Tinari, N.8    Nifantiev, N.9    Iacobelli, S.10
  • 19
    • 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
    • Lopez-Lucendo, M. F., Solis, D., Andre, S., Hirabayashi, J., Kasai, K., Kaltner, H., Gabius, H. J., and Romero, A. (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
    • Lopez-Lucendo, M.F.1    Solis, D.2    Andre, S.3    Hirabayashi, J.4    Kasai, K.5    Kaltner, H.6    Gabius, H.J.7    Romero, A.8
  • 20
    • 34547294822 scopus 로고    scopus 로고
    • Characterization of the Carbohydrate Recognition Domain of Galectin-1 in Terms of Solvent Occupancy
    • Di Lella, S., Marti, M. A., Alvarez, R. M. S., Estrin, D. A., and Díaz Ricci, J. C. (2007) Characterization of the Carbohydrate Recognition Domain of Galectin-1 in Terms of Solvent Occupancy. J. Phys. Chem. B 111, 7360-7366.
    • (2007) J. Phys. Chem. B , vol.111 , pp. 7360-7366
    • Di Lella, S.1    Marti, M.A.2    Alvarez, R.M.S.3    Estrin, D.A.4    Díaz Ricci, J.C.5
  • 21
    • 0027916874 scopus 로고
    • UV Resonance Raman spectroscopy for analytical, physical, and biophysical chemistry
    • Asher, S. (1993) UV Resonance Raman spectroscopy for analytical, physical, and biophysical chemistry. Anal. Chem. 65, 201-210.
    • (1993) Anal. Chem , vol.65 , pp. 201-210
    • Asher, S.1
  • 22
    • 0032477947 scopus 로고    scopus 로고
    • UV resonance Raman determination of protein acid denaturation: Selective unfolding of helical segments of horse myoglobin
    • Chi, Z., and Asher, S. (1998) UV resonance Raman determination of protein acid denaturation: Selective unfolding of helical segments of horse myoglobin. Biochemistry 37, 2865-2872.
    • (1998) Biochemistry , vol.37 , pp. 2865-2872
    • Chi, Z.1    Asher, S.2
  • 23
    • 23744503388 scopus 로고    scopus 로고
    • UV-Resonance Raman Thermal Unfolding Study of Trp-Cage Shows That It Is Not a Simple Two-State Miniprotein
    • Ahmed, Z., Beta, I. A., Mikhonin, A. V., and Asher, S. (2005) UV-Resonance Raman Thermal Unfolding Study of Trp-Cage Shows That It Is Not a Simple Two-State Miniprotein. J. Am. Chem. Soc. 127, 10943-10950.
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 10943-10950
    • Ahmed, Z.1    Beta, I.A.2    Mikhonin, A.V.3    Asher, S.4
  • 24
    • 0000281676 scopus 로고    scopus 로고
    • UV Raman Determination of the Environment and Solvent Exposure of Tyr and Trp Residues
    • Chi, Z., and Asher, S. (1998) UV Raman Determination of the Environment and Solvent Exposure of Tyr and Trp Residues. J. Phys. Chem. B 102, 9595-9602.
    • (1998) J. Phys. Chem. B , vol.102 , pp. 9595-9602
    • Chi, Z.1    Asher, S.2
  • 25
    • 84983085435 scopus 로고
    • An examination of linear solvation energy relationships
    • Kamlet, M. J., Abbound, J.-L. M., and Taft, R. W. (1981) An examination of linear solvation energy relationships. Prog. Phys. Org. Chem. 13, 485-630.
    • (1981) Prog. Phys. Org. Chem , vol.13 , pp. 485-630
    • Kamlet, M.J.1    Abbound, J.-L.M.2    Taft, R.W.3
  • 26
    • 0037495483 scopus 로고
    • Effect of hydrophobic environment on the resonance Raman spectra of tryptophan residues in proteins
    • Efremov, R. G., Feofanov, A. V., and Nabiev, I. R. (1992) Effect of hydrophobic environment on the resonance Raman spectra of tryptophan residues in proteins. J. Raman Spectrosc. 23, 69-73.
    • (1992) J. Raman Spectrosc , vol.23 , pp. 69-73
    • Efremov, R.G.1    Feofanov, A.V.2    Nabiev, I.R.3
  • 27
    • 0001579281 scopus 로고
    • Normal Coordinate Analysis of the Indole Ring
    • Takeuchi, H., and Harada, I. (1986) Normal Coordinate Analysis of the Indole Ring. Spectrochim. Acta 42, 1067-1078.
    • (1986) Spectrochim. Acta , vol.42 , pp. 1067-1078
    • Takeuchi, H.1    Harada, I.2
  • 29
    • 33845958124 scopus 로고    scopus 로고
    • A novel function for galectin-1 a the crossroad of innate and a adaptive immunity: Galectin-1 regulates monocyte/macrophage physiology through a nonapoptotic ERK-dependent pathway
    • Barrionuevo, P., Beigier-Bompadre, M., Ilarregui, J. M., Toscano, M., Bianco, G. A., Isturiz, M. A., and Rabinovich, G. A. (2007) A novel function for galectin-1 a the crossroad of innate and a adaptive immunity: Galectin-1 regulates monocyte/macrophage physiology through a nonapoptotic ERK-dependent pathway. J. Immunol. 178, 436-445.
    • (2007) J. Immunol , vol.178 , pp. 436-445
    • Barrionuevo, P.1    Beigier-Bompadre, M.2    Ilarregui, J.M.3    Toscano, M.4    Bianco, G.A.5    Isturiz, M.A.6    Rabinovich, G.A.7
  • 30
    • 0142075256 scopus 로고    scopus 로고
    • Preparation of recombinant human galectin-1 and use in T cell death assays
    • Pace, K E., Hahn, H. P., and Baum, L. G. (2003) Preparation of recombinant human galectin-1 and use in T cell death assays. Methods Enzymol. 363, 499-518.
    • (2003) Methods Enzymol , vol.363 , pp. 499-518
    • Pace, K.E.1    Hahn, H.P.2    Baum, L.G.3
  • 35
    • 33845379542 scopus 로고
    • UV Resonance Raman studies of acetone, acetamide, and N-methylacetamide: Models for the peptide bond
    • Dudik, J. M., Johnson, C. R., and Asher, S. A. (1985) UV Resonance Raman studies of acetone, acetamide, and N-methylacetamide: Models for the peptide bond. J. Phys. Chem. 89, 3805-3814.
    • (1985) J. Phys. Chem , vol.89 , pp. 3805-3814
    • Dudik, J.M.1    Johnson, C.R.2    Asher, S.A.3
  • 36
    • 0042737808 scopus 로고    scopus 로고
    • Raman Structural Markers of Tryptophan and Histidine Side Chains in Proteins
    • Takeuchi, H. (2003) Raman Structural Markers of Tryptophan and Histidine Side Chains in Proteins. Biopolymers 72, 305-317.
    • (2003) Biopolymers , vol.72 , pp. 305-317
    • Takeuchi, H.1
  • 37
    • 0024284778 scopus 로고
    • Characterization of individual tryptophan side chains in proteins using Raman spectroscopy and hydrogen-deuterium exchange kinetics
    • Miura, T., Takeuchi, H., and Harada, I. (1988) Characterization of individual tryptophan side chains in proteins using Raman spectroscopy and hydrogen-deuterium exchange kinetics. Biochemistry 27, 88-94.
    • (1988) Biochemistry , vol.27 , pp. 88-94
    • Miura, T.1    Takeuchi, H.2    Harada, I.3
  • 38


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.