Ganglioside structure in solution

Hirai, Mitsuhiro; Yabuki, Sadato; Takizawa, Toshiharu; Nakata, Yoshiro; Mitomo, Hiroshi; Hirai, Toshihiro; Shimizu, Shigeru; Kobayashi, Kazuo; Furusaka, M.; Hayashi, Kyozo

doi:10.1016/0921-4526(95)00268-e

Cited by 14 publications

(14 citation statements)

References 5 publications

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“…To compare with the previous results on the interaction of crude mixture (G M /G D ) with met-albumin, we focused the present neutron scattering experiments to observe the complexation of the ganglioside mixture (G M1 /G D1a ) with albumin at low protein concentrations, below the albumin/ganglioside ratio of 0.5/1, by using 41% (v/v) D 2 O/H 2 O solvent. This value mostly agrees with that obtained in our previous study (Hirai et al, 1995b). Then the scattering curve only reflected the change of the ganglioside aggregate structure, because the 41% (v/v) D 2 O/H 2 O solvent is the contrast matching point of albumin (Hirai et al, 1995a).…”

Section: Complexation Of Type III Gangliosides With Albumins Measured By Neutron Scatteringsupporting

confidence: 91%

Interaction of Gangliosides with Proteins Depending on Oligosaccharide Chain and Protein Surface Modification

Hirai

Iwase

Arai

et al. 1998

Biophysical Journal

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By using neutron and synchrotron x-ray small-angle scattering techniques, we investigated the process of the complexation of gangliosides with proteins. We treated monosialoganglioside (G(M1)), disialoganglioside (G(D1a)), and a mixture of G(M1)/G(D1a). Proteins used were bovine serum albumins whose surfaces were modified with different sugars (deoxy-D-galactose, deoxy-L-fucose, deoxymaltitol, and deoxycellobiitol), which were used as model glycoproteins in a membrane. We found that the complexation of gangliosides with albumins greatly depends on the combination of ganglioside species and protein surface modification. With a varying protein/ganglioside ratio in a buffer solution at pH 7, the complexation of G(M1) or G(D1a) with albumins modified by monosaccharides appears to be less destructive for ganglioside aggregate structures in forming large complexes; the complexation of G(D1a) with the albumins modified by disaccharides induces the formation of complexes with a dimeric structure; and the complexation of G(M1) with albumins modified by disaccharides, to form small complexes, is very destructive. The present results show a strong dependence of the interaction between ganglioside and protein on the characteristics of the ganglioside and protein surface, which would relate to a physiological function of gangliosides, such as a function regulating the receptor activity of glycoproteins in a cell membrane.

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Section: Complexation Of Type III Gangliosides With Albumins Measured By Neutron Scatteringsupporting

confidence: 91%

Interaction of Gangliosides with Proteins Depending on Oligosaccharide Chain and Protein Surface Modification

Hirai

Iwase

Arai

et al. 1998

Biophysical Journal

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“…By using neutron and X-ray scattering techniques and calorimetry, we have been studying the structural phase behavior of ganglioside aggregates depending on temperature, − pH, and concentration . We have also clarified the binding specificity of gangliosides with proteins depending on both oligosaccharide chain and protein surface modification. − We have shown the following results on the thermal structural stability of ganglioside micelles.…”

Section: Introductionmentioning

confidence: 99%

Thermal Induced Modulation of Surface Charge of Sialoglycosphingolipid Micelles

1999

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In the present study, by using a shell-modeling method under a rescaled mean spherical approximation (RMSA) for charged particle dispersions, we have found that the thermal structural change of sialoglycosphingolipid micelles accompanies a change of the micellar surface charge, which greatly depends on the oligosaccharide chains. Here, we treat three different types of glycosphingolipids (monosialoganglioside, disialoganglioside, and trisialoganglioside). This phenomenon is induced by a variation of temperature in the physiological temperature range 20−40 °C, which is in agreement with our recent reports showing that the thermal induced shrinkage of the hydrophilic portion of the ganglioside micelles accompanies extrusion of water. The present and previous results strongly suggest that ganglioside molecules localized in outer cell membranes are able to modulate locally both electrostatic charge potential and hydrophilicity of cell surfaces through ganglioside-rich microdomains. These functional properties of gangliosides would play an important role in regulation of various physiological cell surface events such as an adhesion between cells or protein binding to the cell surface.

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“…Many intensive studies have been carried out to clarify the aggregative characteristics of gangliosides (Tettamanti et al, 1985;Maggio et al, 1985;Corti and Cantù, 1990;Corti et al, 1996;Sonnion et al, 1994). Using neutron and x-ray-scattering techniques, we have been studying the structural phase behavior of ganglioside aggregates with regard to temperature, pH, and concentration (Hirai et al, 1995b(Hirai et al, , 1996a, and the complexation of gangliosides with proteins (Hirai et al, 1995a(Hirai et al, , 1998Takizawa et al, 1995).…”

Section: Introductionmentioning

confidence: 99%

Intensive Extrusion and Occlusion of Water in Ganglioside Micelles with Thermal Reversibility

Hirai

Takizawa

1998

Biophysical Journal

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By using a shell-modeling analysis for small-angle scattering data of ganglioside micellar dispersion, we recently reported that the elevation of temperature induces a significant shrinkage of the hydrophilic region of the ganglioside micelle, suggesting that the oligosaccharide chains with sialic acid residues of ganglioside molecules change the conformation, sensitively responding to a change in temperature (Hirai et al., 1996. Biophys. J. 70:1761-1768; J. Phys. Chem. 100:11675-11680). We have carried out further analyses of the temperature dependence of the structural parameters reported previously, and we have found clear evidence of reversible extrusion and occlusion of a large amount of water in the hydrophilic region of the ganglioside micelle in the physiological temperature range of 6-60 degrees C. The present results suggest a remarkable function of ganglioside molecules: they change the hydrophilicity of the cell surface locally as a response to variations in temperature. This phenomenon might be involved in various surface events, such as cell-cell interaction and cell surface-protein interaction.

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Ganglioside structure in solution

Cited by 14 publications

References 5 publications

Interaction of Gangliosides with Proteins Depending on Oligosaccharide Chain and Protein Surface Modification

Interaction of Gangliosides with Proteins Depending on Oligosaccharide Chain and Protein Surface Modification

Thermal Induced Modulation of Surface Charge of Sialoglycosphingolipid Micelles

Intensive Extrusion and Occlusion of Water in Ganglioside Micelles with Thermal Reversibility

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