N‐linked oligosaccharide changes with oncogenic transformation require sialylation of multiantennae

Abstract

Glycopeptides derived from NIH 3T3 fibroblasts and these cells transformed by transfection with human DNA containing oncogene H‐ras were analyzed by 500‐MHz 1H‐NMR spectroscopy and binding to immobilized lectins. The cells were metabolically labeled with D‐[3H]glucosamine or L‐[3H]fucose and the glycopeptides included in Bio‐Gel P‐10 (Mr 5000–3500) were separated into neutral and charged fractions on DEAE‐cellulose. The major portion (80%) of these [3H]fucose glycopeptides from the non‐transformed NIH 3T3 fibroblasts were neutral or contained one or two charged residues, whereas 90% of the glycopeptides from the transformed cells contained two or more charged residues. Copyright © 1989, Wiley Blackwell. All rights reserved