Publication | Open Access
Structure of β-Glucan Oligomer from Laminarin and Its Effect on Human Monocytes to Inhibit the Proliferation of U937 Cells
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Citations
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References
2005
Year
GlycobiologyPolysaccharideCellular PhysiologyOriginal LaminarinBioanalysisInhibitory ActivityGlycosylationBiochemistryPharmacologyCell BiologyU937 CellsHuman MonocytesNatural SciencesCellular BiochemistryMedicineCetraria IslandicaHemicelluloseCarbohydrate-protein InteractionExtracellular Matrixβ-Glucan Oligomer
We analyzed the human monocyte-stimulating ability of laminarin from Eisenia bicyclis, lichenan from Cetraria islandica, and their oligomers depolymerized with endo-1,3-beta-glucanase from Arthrobacter sp. The respective beta-glucan oligomers with different degrees of polymerization (DP) were fractionated from hydrolytic products of laminarin and lichenan using gel-filtration chromatography. The monocyte-conditioned medium pre-cultured in the presence of a fraction of beta-glucan oligomer (DP>/=8) from laminarin exhibited inhibitory activity against the proliferation of human myeloid leukemia U937 cells, while those pre-cultured with other beta-glucan oligomers and the original laminarin and lichenan showed little or no activity. NMR analysis indicated that the beta-glucan oligomer (DP>/=8) has an average DP value of 13, and its ratio of beta-1,3- to beta-1,6-linkages in glucopyranose units was estimated to be 1.3:1. These results indicate that the beta-1,3-glucan oligomer with a higher content of beta-1,6-linkage stimulates monocytes to inhibit the proliferation of U937 cells.
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