Altered protein glycosylation of rat 3Y1 cells induced by activated c-myc gene.
N-linked sugar chains of rat 3Y1 cells and tumorigenic cells derived by transfection with activated c-myc gene were quantitatively released as oligosaccharides from membrane preparations by hydrazinolysis. Structural analyses revealed that cells of both types contain bi-, tri- and tetra-antennary complex-type oligosaccharides as well as high-mannose-type oligosaccharides. However, the c-myc-transfected cells showed an increase in tri- and tetra-antennary oligosaccharides having the GlcNAc beta 1----4Man alpha 1----and/or the GlcNAc beta 1----6Man alpha 1----linkages with a decrease in biantennary oligosaccharides compared to control 3Y1 cells. The data suggest that c-myc gene has a potential role in the regulation of cellular protein glycosylation and that an elevated expression of c-myc gene in the cells leads to increased branch formation of outer chains in N-linked oligosaccharides concomitant with the acquisition of tumorigenicity.
Hiraizumi
S
S
Department of Biochemistry, University of Tokyo, Japan.
Takakasaki
S
S
Shiroki
K
K
Kobata
A
A
D000818:Animals; D002240:Carbohydrate Sequence; D002461:Cell Line, Transformed; D016259:Genes, myc / Q000502:physiology*; D006031:Glycosylation; D008562:Membrane Glycoproteins / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics*; D008969:Molecular Sequence Data; D009844:Oligosaccharides / Q000032:analysis; D051381:Rats; D014162:Transfection
D008562:Membrane Glycoproteins; D009844:Oligosaccharides