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Carbohydrate Requirement for Expression and Stability of Acetylcholine Receptor on the Surface of Embryonic Muscle Cells in Culture
Joav M. Prives and Kenneth Olden
Proceedings of the National Academy of Sciences of the United States of America
Vol. 77, No. 9, [Part 2: Biological Sciences] (Sep., 1980), pp. 5263-5267
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/9311
Page Count: 5
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We have investigated the significance of protein glycosylation for metabolism of acetylcholine receptors (AcChoR) in primary cultures of embryonic chicken muscle cells. Tunicamycin, a specific inhibitor of the glycosylation of asparagine residues on glycoproteins, decreased AnChoR accumulation and accelerated its degradation. In contrast, there was no evidence that tunicamycin treatment affected AcChoR biosynthesis, intracellular transport, or incorporation into surface membranes. Leupeptin, an inhibitor of intracellular proteases, markedly increased accumulation of AcChoR on the external surface of muscle cells treated with tunicamycin. Our findings indicate that impairment of protein glycosylation prevents accumulation of AcChoR by increasing its susceptibility to degradation by cellular proteases.
Proceedings of the National Academy of Sciences of the United States of America © 1980 National Academy of Sciences