Translocation across Golgi vesicle membranes: a CHO glycosylation mutant deficient in CMP-sialic acid transport.
Golgi vesicle membranes from the Lec2 CHO glycosylation mutant translocate CMP-sialic acid at only 2% the rate of vesicles from wild-type CHO cells. The deficiency is specific, because vesicles from Lec2 cells can translocate UDP-N-acetylglucosamine, adenosine 3'-phosphate 5'-phosphosulfate, and UDP-galactose at rates comparable to those of vesicles from wild-type cells. Complementation analyses show that Lec2 mutants belong to the same genetic complementation group as clone 1021, a CHO mutant of similar phenotype. Both mutants have previously been shown to have a 90% reduction in the sialylation of glycoproteins and gangliosides compared with wild-type cells. However, 1021 cells appear to have normal levels of CMP-sialic acid, sialyltransferase activity, and endogenous acceptors for sialylation. It seems likely that the primary defect in Lec2 and 1021 cells is their inability to translocate CMP-sialic acid across Golgi vesicle membranes.
D000818:Animals; D001692:Biological Transport; D002458:Cell Fractionation; D002460:Cell Line; D006224:Cricetinae; D003412:Cricetulus; D003569:Cytidine Monophosphate N-Acetylneuraminic Acid / Q000378:metabolism; D005260:Female; D006056:Golgi Apparatus / Q000378:metabolism* / Q000648:ultrastructure; D007425:Intracellular Membranes / Q000378:metabolism*; D007700:Kinetics; D009154:Mutation; D010053:Ovary
D003569:Cytidine Monophosphate N-Acetylneuraminic Acid