Increased sialylation of complex glycopeptides during differentiation of mouse embryonal carcinoma cells

Differentiation; Research in Biological Diversity
G CossuL Warren


High-molecular-weight, asparagine-linked glycopeptides--the lactosaminoglycans--are the major class of protein-bound carbohydrates synthesized by F9 cells; these cells synthesize only minor amounts of smaller glycopeptides. In contrast, F9ACC19, an endodermal cell line derived from F9 cells, synthesizes only minor amounts of lactosaminoglycans and a high proportion of smaller glycopeptides. Biochemical analysis of the small glycopeptides from F9ACC19 cells revealed that they are larger, bind less efficiently to concanavalin-A Sepharose and contain more sialic acid than their counterparts from F9 cells. Both cell types contain a small proportion of high-mannose glycopeptides. When synthesized by F9ACC19 cells, the glycopeptides of vesicular stomatitis virus show a high level of sialylation as compared to those synthesized by F9 cells, where few or no sialic-acid residues are present; this shows that the differences observed in total glycopeptides reflect differences in the glycosylation machinery of the cells. Consistent with this observation, sialyltransferase activity in vitro using a variety of acceptors was found to be markedly higher in F9ACC19 than in F9 cells, while galactosyltransferase activity was reduced several fold ...Continue Reading


May 1, 1978·Proceedings of the National Academy of Sciences of the United States of America·T MuramatsuF Jacob
Nov 1, 1978·Proceedings of the National Academy of Sciences of the United States of America·D Solter, B B Knowles
Oct 1, 1973·Proceedings of the National Academy of Sciences of the United States of America·K ArtztF Jacob
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