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Altered patterns of N-linked glycosylation of the Torpedo acetylcholine receptor expressed in Xenopus oocytes.
Buller AL
,
White MM
.
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The nicotinic acetylcholine receptor (AChR) from Torpedo electroplax is an oligomeric transmembrane glycoprotein made up of four highly homologous subunits in a stoichiometry of alpha 2 beta gamma delta. The role of N-linked glycosylation of the AChR has been studied in several cell lines and these studies have suggested that the addition of carbohydrate may be important for receptor expression. While Xenopus oocytes have proven to be an invaluable tool for studying the AChR, little is known about N-linked glycosylation of the oocyte-expressed receptor. The present report demonstrates that the oocyte-expressed AChR is glycosylated and contains the same number of oligosaccharide residues per subunit as the native receptor. However, unlike the native Torpedo receptor which contains both high mannose and complex oligosaccharides, the oocyte-expressed AChR contains only high mannose oligosaccharide modifications. However, as has been well documented, the Torpedo AChR expressed in oocytes is fully functional, demonstrating that the precise nature of the oligosaccharide modification is not critical for receptor function. The role of the oligosaccharide component of the AChR in receptor function was examined using tunicamycin (TM) to inhibit N-linked protein glycosylation. TM treatment resulted in a 70-80% inhibition of AChR expression in oocytes. Functional, unglycosylated receptors were not expressed; receptors expressed in TM-treated oocytes were functional wild-type, glycosylated AChR, formed only during the initial 12 hr of TM exposure. These data suggest that while glycosylation of the oocyte-expressed Torpedo AChR is required for assembly of subunits into a functional receptor, as has been demonstrated in other cells, oocyte modification of normal Torpedo glycosylation patterns does not affect receptor function or assembly.
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