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N‐linked oligosaccharide processing is not necessary for glycoprotein secretion in plants
Author(s) -
Lerouge Patrice,
FitchetteLainé AnneCatherine,
Chekkafi Aïcha,
Avidgor Véronique,
Faye Loïc
Publication year - 1996
Publication title -
the plant journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.058
H-Index - 269
eISSN - 1365-313X
pISSN - 0960-7412
DOI - 10.1046/j.1365-313x.1996.10040713.x
Subject(s) - castanospermine , glycan , glycoprotein , secretion , glycosylation , extracellular , concanavalin a , biochemistry , swainsonine , oligosaccharide , chemistry , biology , in vitro
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 Glc 3 Man 7 GlcNAc 2 by labeling experiments, affinity chromatography on concanavalin A‐Sepharose and proton NMR. In contrast with previous results showing that N‐glycosylation is a pre‐requisite 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.