Lerouge P, Fichette-Lainé A C, Chekkafi A, Avidgor V, Faye L
Centre Régional Universitaire de Spectroscopie, CNRS-URA 464, Mont Saint Aignan, France.
Plant J. 1996 Oct;10(4):713-9. doi: 10.1046/j.1365-313x.1996.10040713.x.
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.
研究了N-聚糖在悬浮培养的悬铃木细胞分泌糖蛋白过程中的作用。在聚糖加工抑制剂栗精胺存在的情况下，研究了糖蛋白向细胞外区室的转运。选择栗精胺是因为它能均匀抑制悬铃木细胞中的聚糖成熟，并导致单一未成熟N-聚糖的积累。通过标记实验、伴刀豆球蛋白A-琼脂糖亲和层析和质子核磁共振，已确定该聚糖的结构为Glc3Man7GlcNAc2。与之前表明N-糖基化是N-连接糖蛋白分泌的先决条件的结果相反，这种分泌不受栗精胺存在的影响。因此，这种未加工聚糖的存在足以使糖蛋白在悬浮培养的悬铃木细胞的细胞外区室中有效分泌。
