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- W2040558859 abstract "Peroxidases are secreted into the culture medium of BY2 suspension cells. In order to determine the role of glycosylation and glycan processing for peroxidase secretion, inhibition studies were performed. When glycosylation was inhibited by tunicamycin, secretion of peroxidases into the medium ceased totally. When glycan processing was inhibited by castanospermine, the molecular size of the peroxidases was increased concomitant with their decreased secretion into the medium. Upon inhibition treatment, pulse-labeled total secreted protein behaved similarly to the peroxidases, indicating that for secretion, glycosylation is generally essential, while glycan processing is not prerequisite but none the less necessary. These studies are supported by the observation that inhibitor treatment also induced transcript accumulation for the molecular chaperon, BiP, and for calnexin, which recognizes immature glycans. Taken together, these results strongly suggest that correct N-glycan structure is critical for protein secretion in plant cells." @default.
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- W2040558859 date "1999-05-01" @default.
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- W2040558859 title "Glycosylation and its Adequate Processing is Critical for Protein Secretion in Tobacco BY2 Cells" @default.
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- W2040558859 doi "https://doi.org/10.1016/s0176-1617(99)80236-3" @default.
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