Erythroglycan biosynthesis in K-562 cells. Inhibition of synthesis by tunicamycin and lack of attachment to the G-protein of vesicular-stomatitis virus.
K-562 cells, which express foetal erythroglycan, are shown to synthesize the lipid-linked oligosaccharide intermediates commonly found in tissues and cultured fibroblasts. The addition of tunicamycin, which blocks the formation of these intermediates and thus of asparagine-linked oligosaccharides, inhibits the synthesis of erythroglycan (Mr 7000-11 000). Vesicular-stomatitis-virus infection of K-562 cells results in the glycosylation of the G-protein with the transferrin-type oligosaccharide (Mr 3000), but not with the larger erythroglycan. These results suggest that, in K-562 cells, the early stages of erythroglycan biosynthesis are the same as those of the transferrin-type oligosaccharides. However, maturation of the oligosaccharide is influenced by protein structure such that erythroglycan is only expressed on specific glycoproteins.
D001457:Anion Exchange Protein 1, Erythrocyte; D002460:Cell Line; D002478:Cells, Cultured; D055598:Chemical Phenomena; D002621:Chemistry; D002850:Chromatography, Gel; D005944:Glucosamine / Q000031:analogs & derivatives*; D006020:Glycopeptides / Q000096:biosynthesis*; D006801:Humans; D007951:Leukemia, Myeloid; D008562:Membrane Glycoproteins; D008565:Membrane Proteins / Q000096:biosynthesis*; D014415:Tunicamycin / Q000494:pharmacology*; D014721:Vesicular stomatitis Indiana virus / Q000378:metabolism; D014759:Viral Envelope Proteins; D014764:Viral Proteins / Q000378:metabolism*
D001457:Anion Exchange Protein 1, Erythrocyte; C028391:G protein, vesicular stomatitis virus; D006020:Glycopeptides; D008562:Membrane Glycoproteins; D008565:Membrane Proteins; D014759:Viral Envelope Proteins; D014764:Viral Proteins; C018059:erythroglycan; D014415:Tunicamycin; D005944:Glucosamine