Acute Effects of Ethanol on Biosynthesis and Glycosylation of IgGl(k) Antibody Molecules in Cultured P3/X63‐Ag8 Myeloma Cells

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Abstract
Protein synthesis in cultured P3/X63-Ag8 mouse myeloma cells was inhibited by acute exposure to ethanol. The synthesis of IgGl antigbody, as a percentage of total protein synthesis, increased slightly. Experiments using actinomycin D suggested that the overall inhibition of protein synthesis by ethanol occurred at the translational level. Following an L-[35S]Met pulse, cultured P3/X63-Ag8 cells contained 1 light antibody polypeptide and 2 heavy antibody polypeptides. One heavy chain was the unglycosylated precursor of the other, mature molecule. Only the glycosylated polypeptide was a normal constituent of secreted IgGl antibody. The glycosylation of the immature heavy chains occurred more rapidly during a 1 h isotopic pulse in cells exposed to ethanol (.gtoreq. 0.1 vol/vol%), than in unexposed control cells. The effects of ethanol on antibody glycosylation may have been related to the increased susceptibility of alcoholic patients to infections. Ethanol may also affect the synthesis of other glycoproteins in myeloma cells and other tissues.