The Plant Journal · 1996 · 27 citations · 0 references
Life SciencesBiochemistryMolecular BiologyCarbohydrate BiochemistryCellular BiochemistryGlycobiologyGlycan AnalysisGlycan BiosynthesisGlycan StructureGlycosylation PathwaysN-linked GlycosylationGlycan Composition AnalysisGlycan Processing PathwaysGlycan Structure AnalysisN-glycan AnalysisN-glycan MaturationN-glycosylation In PlantsN-linked Glycan BiosynthesisOligosaccharide Processing
The role of N-glycans in the secretion of glycoproteins by suspension-cultured sycamore cells was studied. The transport of glycoproteins to the extracellular compartment was investigated in the presence of a glycan-processing inhibitor, castanospermine. Castanospermine has been selected because it inhibits homogeneously glycan maturation in sycamore cells and leads to the accumulation of a single immature N-glycan. The structure of this glycan has been identified as Glc3Man7GlcNAc2 by labeling experiments, affinity chromatography on concanavalin A-Sepharose and proton NMR. In contrast with previous results showing that N-glycosylation is a prerequisite for secretion of N-linked glycoproteins, this secretion is not affected by the presence of castanospermine. As a consequence, the presence of this unprocessed glycan is sufficient for an efficient secretion of glycoproteins in the extracellular compartment of suspension-cultured sycamore cells.