Membrane biogenesis in embryonal carcinomas: glycoproteins destined for the cell surface are delayed in a pre-Golgi compartment.
Embryonal carcinoma and early embryonic cells assemble a family of unusually large and complex carbohydrates. These glycans are highly branched, repeating copolymers of the sugars galactose and N-acetylglucosamine, referred to as polylactosamines, and are frequently decorated with fucose, sulfate, and sialic acid. We have previously shown that in teratocarcinoma cells these glycans are part of a large spectrum of glycans assembled on mannose cores derived from a common precursor glycan. Metabolic studies revealed a large excess of high-mannose glycans at a time when complex-type glycans cease to accumulate. The present studies demonstrate that these high-Man glycans are not degraded internally or secreted directly but are on glycoproteins destined for the cell surface. These unprocessed glycoproteins replace material lost during the extensive membrane turnover that occurs in these cells. Their export to the cell surface is delayed in a pre-Golgi compartment.
D000818:Animals; D002460:Cell Line; D002462:Cell Membrane / Q000378:metabolism; D006020:Glycopeptides / Q000032:analysis; D006023:Glycoproteins / Q000096:biosynthesis*; D007700:Kinetics; D008565:Membrane Proteins / Q000096:biosynthesis*; D051379:Mice; D013347:Subcellular Fractions / Q000378:metabolism; D013724:Teratoma / Q000378:metabolism*
D006020:Glycopeptides; D006023:Glycoproteins; D008565:Membrane Proteins