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Plant J ; 10(4): 713-9, 1996 Oct.
Article in English | MEDLINE | ID: mdl-8998501

ABSTRACT

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.


Subject(s)
Glycoproteins/metabolism , Oligosaccharides/metabolism , Plant Proteins/metabolism , Protein Processing, Post-Translational , Carbohydrate Sequence , Cells, Cultured , Chromatography, Affinity , Chromatography, Ion Exchange/methods , Enzyme Inhibitors/pharmacology , Indolizines/pharmacology , Magnetic Resonance Spectroscopy , Molecular Sequence Data , Oligosaccharides/chemistry , Protein Processing, Post-Translational/drug effects , Sequence Analysis , Trees/cytology , Trees/drug effects , Trees/metabolism
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