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• W4248332605 startingPage "4197" @default.
• W4248332605 abstract "The importance of carbohydrate in the secretion of immunoglobulin A (IgA) has previously been suggested by results of studies with tunicamycin, which prevents N-linked glycosylation of all cell glycoproteins. To directly evaluate the role of individual oligosaccharides in the secretion of IgA, we have used site-directed mutagenesis to selectively eliminate the two N-linked attachment sites reported to be glycosylated in alpha heavy chains. Transfected wild-type and mutant alpha genes were expressed in kappa light-chain-producing MPC-11 variant myeloma cells, and secretion kinetics of the IgAs were compared. Removal of either or both glycosylation sites led to intracellular alpha heavy-chain degradation and a 90 to 95% inhibition of IgA secretion. These results reveal that both N-linked oligosaccharides of the alpha heavy chain are essential for intracellular stability and normal secretion of IgA. This suggests that the key function of carbohydrate here is to maintain proper conformation of the glycoprotein. We also found that when expressed in the MPC-11 variant cells, alpha heavy chains were glycosylated at a third, normally unused site." @default.
• W4248332605 created "2022-05-12" @default.
• W4248332605 creator A5047327659 @default.
• W4248332605 creator A5090085505 @default.
• W4248332605 date "1988-10-01" @default.
• W4248332605 modified "2023-09-24" @default.
• W4248332605 title "Selective removal of alpha heavy-chain glycosylation sites causes immunoglobulin A degradation and reduced secretion" @default.
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• W4248332605 doi "https://doi.org/10.1128/mcb.8.10.4197-4203.1988" @default.
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