Glycosylation changes in membrane glycoproteins after transfection of NIH 3T3 with human tumor DNA.
Glycoproteins from NIH 3T3 transformed by transfection with human tumor DNA had altered glycosylation. That is, the glycoproteins have a decrease in biantennary oligosaccharides with a concomitant increase in tri- and tetraantennary oligosaccharides. After swainsonine treatment, glycosylation of oncogene transfected NIH 3T3 was more similar to the normal counterpart. Thus, this inhibitor of glycoprotein processing is able to reverse at least one phenotypic expression of transformation, the formation of more highly branched oligosaccharides. The mechanism may be by inhibition of a specific glycosyl transferase.
D000818:Animals; D002236:Carbohydrate Conformation; D002471:Cell Transformation, Neoplastic / Q000378:metabolism*; D004273:DNA, Neoplasm / Q000235:genetics*; D006023:Glycoproteins / Q000378:metabolism*; D006801:Humans; D008565:Membrane Proteins / Q000378:metabolism; D051379:Mice; D009447:Neuroblastoma / Q000235:genetics; D009844:Oligosaccharides / Q000378:metabolism; D009857:Oncogenes
D004273:DNA, Neoplasm; D006023:Glycoproteins; D008565:Membrane Proteins; D009844:Oligosaccharides