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Glycosylation causes an apparent block in translation of immunoglobulin heavy chain
Journal article   Open access   Peer reviewed

Glycosylation causes an apparent block in translation of immunoglobulin heavy chain

L W Bergman, E Harris and W M Kuehl
The Journal of biological chemistry, v 256(2), pp 701-706
25 Jan 1981
DOI: https://doi.org/10.1016/S0021-9258(19)70031-3
PMID: 6778872
Featured in Collection :   UN Sustainable Development Goals @ Drexel
url
https://doi.org/10.1016/S0021-9258(19)70031-3View
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Abstract

Animals Cell Line Cycloheximide - pharmacology Glycosides - metabolism Immunoglobulin Heavy Chains - biosynthesis Mice Molecular Weight Osmolar Concentration Plasmacytoma - metabolism Protein Biosynthesis - drug effects Tunicamycin - pharmacology
Analysis of nascent heavy chains isolated from MPC11 (gamma 2b heavy chains) and MOPC 21 (gamma 1 heavy chains) mouse myeloma cells demonstrates an accumulation of nascent heavy chains which are slightly smaller in mass (approximately 35,000 daltons) than nascent heavy chains which have just been glycosylated (approximately 38,000 daltons). The accumulation of 35,000-dalton nascent heavy chain appears to be a consequence of the glycosylation process since tunicamycin, an inhibitor of glycosylation, abolishes the apparent translational block manifested by the accumulation of 35,000-dalton nascent chains. Tunicamycin also causes a 15 to 25% increase n the relative rate of synthesis of heavy chain compared to the corresponding rate of synthesis of the nonglycosylated light chain synthesized by the same cell. These results suggest that the translation block, caused by the glycosylation process, of heavy chain synthesis contributes to the imbalance of heavy chain and light chain biosynthesis observed in malignant and normal lymphoid cells.

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Web of Science research areas
Biochemistry & Molecular Biology
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