Ras (proto)oncogene induces N‐linked carbohydrate modification: temporal relationship with induction of invasive potential

• Published in: The EMBO journal 1988-11, Vol.7 (11), p.3361-3368
• Main Authors: Bolscher, J. G., Bijl, M. M., Neefjes, J. J., Hall, A., Smets, L. A., Ploegh, H. L.
• Format: Article
• Language: English
• Subjects: Animals; Biological and medical sciences; Carbohydrate Metabolism; Cell Line; Cell Line, Transformed; Cell physiology; Cell transformation and carcinogenesis. Action of oncogenes and antioncogenes; Cell Transformation, Neoplastic; Chromatography, Gel; Electrophoresis, Polyacrylamide Gel; Fundamental and applied biological sciences. Psychology; Gene Expression Regulation; Genes, ras; Glycopeptides - metabolism; Glycosylation; Histocompatibility Antigens Class I - metabolism; Isoelectric Focusing; Kinetics; Membrane Glycoproteins; Molecular and cellular biology; Proteins - metabolism; Proto-Oncogene Proteins - biosynthesis; Proto-Oncogene Proteins p21(ras); Transfection; Viral Envelope Proteins - metabolism
• ISSN: 0261-4189; 1460-2075
• DOI: 10.1002/j.1460-2075.1988.tb03208.x

The effect of expression of the ras oncogene on protein glycosylation was studied. VSV G‐protein and class I histocompatibility antigens were analysed to monitor ras‐mediated changes in glycosylation. Transient expression of the c‐Ha‐ras oncogene, introduced into NIH 3T3 cells by the DEAE‐dextran method, altered protein glycosylation within 25 h of transfection. The same result was obtained after dexamethasone‐induced expression of p21‐ras in stable NIH 3T3 transfectants containing either an activated Ha‐ras oncogene or a normal N‐ras proto‐oncogene under control of the glucocorticoid‐inducible MMTV promoter. The alteration of cell surface carbohydrates, induced by the ras (proto)oncogene and the subsequent acquisition of invasive potential, occurred prior to morphological transformation.