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- W2094543128 abstract "Fucose binding protein (FBP) from Lotus tetragonolobus seed was studied by fluorescencemicroscopy for its binding characteristics to various guinea pig peritoneal macrophage populations. Fluoresceinated FBP (FITC-FBP) was bound optimally at 22°C in a punctate distribution and was internalized at 37°C. Binding of FBP to macrophages was reversed specifically by the competitive sugar L-fucose, and not by D-fucose, L-rhamnose, or D-galactose. FBP was bound with greater frequency and intensity to 3-day oil-elicited peritoneal macrophages which are responsive to migration inhibition by FBP and migration inhibitory factor (MIF) than to resident or 7-day inflammatory macrophages which are unresponsive to activation by the same effectors. Competition for visual binding of FITC-FBP to macrophages was demonstrated by preincubation of cells with unlabeled FBP or MIF. Competition of FITC-FBP binding by MIF was reversed by L-fucose. These results indicate that FBP binds preferentially, with greater frequency and intensity, to macrophage subpopulations which are responsive to MIF than to MIF-refractory macrophages. The data further supports the existence of a common receptor site for MIF and FBP on the macrophage membrane which involves fucosyl determinants." @default.
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- W2094543128 title "Binding characteristics of fluoresceinated lotustetragonolobus fucolectin to macrophage populations which are either responsive or refractory to activation by lymphokine" @default.
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- W2094543128 doi "https://doi.org/10.1016/s0171-2985(85)80039-5" @default.
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