Altered protein glycosylation of rat 3Y1 cells induced by activated c-myc gene

✍ Scribed by Sen Hiraizumi; Seiichi Takakasaki; Kazuko Shiroki; Akira Kobata

• Book ID: 102868770
• Publisher: John Wiley and Sons
• Year: 1991
• Tongue: French
• Weight: 697 KB
• Volume: 48
• Category: Article
• ISSN: 0020-7136
• DOI: 10.1002/ijc.2910480225

✦ Synopsis

Abstract

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 GIcNAcβI→4Manαl→ and/or the GlcNAcβl→ 6Manαl→ 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 tumorigeniclty.