Ras (proto)oncogene induces N-linked carbohydrate modification: temporal relationship with induction of invasive potential.
AUTOR(ES)
Bolscher, J G
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=454833Documentos Relacionados
- Oncogenicity of human N-ras oncogene and proto-oncogene introduced into retroviral vectors.
- An intrinsic membrane glycoprotein with cytosolically oriented n-linked sugars.
- Cloning and expression of N-acetylglucosaminyltransferase I, the medial Golgi transferase that initiates complex N-linked carbohydrate formation.
- Loss of the amino-terminal helix-loop-helix domain of the vav proto-oncogene activates its transforming potential.
- Carbohydrate-deficient glycoprotein syndrome: not an N-linked oligosaccharide processing defect, but an abnormality in lipid-linked oligosaccharide biosynthesis?
