Isolation and structural characterization of fucosylated gangliosides with linear poly-N-acetyllactosaminyl chains from human granulocytes

Müthing J, Spanbroek R, PeterKatalinic J, Hanisch FG, Hanski C, Hasegawa A, Unland F, Lehmann J, Tschesche H, Egge H (1996)
GLYCOBIOLOGY 6(2): 147-156.

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The isolation and structural characterization of fucosylated neolacto-series gangliosides with linear poly-N-acetyllactosaminyl chains from normal human granulocytes is described. Gangliosides were purified by consecutive use of anion exchange HPLC on Fractogel TMAE-650(S), adsorption and reversed phase HPLC on Nucleosil 50-7 and Nucleosil 7C(18) columns, respectively, TLC immunostaining with carbohydrate specific monoclonal antibodies, fast atom bombardment-mass spectrometry (FAB-MS) of the permethylated derivatives and gas chromatography-electron impact mass spectrometry (GC-EIMS) of partially methylated alditol acetates were used for structure elucidations, One ganglioside was identified as sialyl Lewis(x) antigen with nLcOse(6)Cer core, Neu5-Ac alpha 2-3Gal beta 1-4(Fuc alpha 1-3)GlcNAc beta 1-3Gal beta 1-4Glc NAc beta 1-3Gal beta 1-4Glc beta 1-1Cer. Furthermore, monosialylated ceramide: deca-, undeca-, dodeca- and tridecasaccharides with three (nLcOse(8)Cer) and four (nLcOse(10)Cer) linear lactosaminyl repeats were identified, carrying one to three fucoses. The ceramide portions were found to contain C-18 sphingosine and predominantly C-16:0 fatty acids, All monosialogangliosides were homogenous concerning their terminal alpha 2-3Neu5Ac-sialylation, but different in their fucosylation status, Beside VI(3)Neu5Ac, V(3)Fuc-nLcOse(6)Cer, in two of the fucosylated polylactosaminyl ganglioside fractions the sialyl Lewis(x) epitope was found, whereas five species expressed the terminal VIM-2 motif. The role of protein linked sialyl Lewis(x) epitope of human granulocytes as a ligand for endothelial leukocyte adhesion molecule-1 (ELAM-1; E-selectin) and platelet activation-dependent granule external membrane protein (PADGEM; P-selectin) is well documented, However, the involvement of endothelial cells E- and/or P-selectin mediated cell-cell adhesion via lipid bound sialyl Lewis(x) and/or VIM-2 epitopes on human granulocytes has to be proved in further investigations.
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Müthing J, Spanbroek R, PeterKatalinic J, et al. Isolation and structural characterization of fucosylated gangliosides with linear poly-N-acetyllactosaminyl chains from human granulocytes. GLYCOBIOLOGY. 1996;6(2):147-156.
Müthing, J., Spanbroek, R., PeterKatalinic, J., Hanisch, F. G., Hanski, C., Hasegawa, A., Unland, F., et al. (1996). Isolation and structural characterization of fucosylated gangliosides with linear poly-N-acetyllactosaminyl chains from human granulocytes. GLYCOBIOLOGY, 6(2), 147-156.
Müthing, J., Spanbroek, R., PeterKatalinic, J., Hanisch, F. G., Hanski, C., Hasegawa, A., Unland, F., Lehmann, J., Tschesche, H., and Egge, H. (1996). Isolation and structural characterization of fucosylated gangliosides with linear poly-N-acetyllactosaminyl chains from human granulocytes. GLYCOBIOLOGY 6, 147-156.
Müthing, J., et al., 1996. Isolation and structural characterization of fucosylated gangliosides with linear poly-N-acetyllactosaminyl chains from human granulocytes. GLYCOBIOLOGY, 6(2), p 147-156.
J. Müthing, et al., “Isolation and structural characterization of fucosylated gangliosides with linear poly-N-acetyllactosaminyl chains from human granulocytes”, GLYCOBIOLOGY, vol. 6, 1996, pp. 147-156.
Müthing, J., Spanbroek, R., PeterKatalinic, J., Hanisch, F.G., Hanski, C., Hasegawa, A., Unland, F., Lehmann, J., Tschesche, H., Egge, H.: Isolation and structural characterization of fucosylated gangliosides with linear poly-N-acetyllactosaminyl chains from human granulocytes. GLYCOBIOLOGY. 6, 147-156 (1996).
Müthing, Johannes, Spanbroek, R, PeterKatalinic, J, Hanisch, FG, Hanski, C, Hasegawa, A, Unland, F, Lehmann, J, Tschesche, Harald, and Egge, H. “Isolation and structural characterization of fucosylated gangliosides with linear poly-N-acetyllactosaminyl chains from human granulocytes”. GLYCOBIOLOGY 6.2 (1996): 147-156.
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