INCREASED GLUCOSE-TRANSPORT IN RAS-TRANSFORMED FIBROBLASTS - A POSSIBLE ROLE FOR N-GLYCOSYLATION OF GLUT1

Citation
R. Onetti et al., INCREASED GLUCOSE-TRANSPORT IN RAS-TRANSFORMED FIBROBLASTS - A POSSIBLE ROLE FOR N-GLYCOSYLATION OF GLUT1, FEBS letters, 407(3), 1997, pp. 267-270
Citations number
36
Categorie Soggetti
Biophysics,Biology
Journal title
ISSN journal
00145793
Volume
407
Issue
3
Year of publication
1997
Pages
267 - 270
Database
ISI
SICI code
0014-5793(1997)407:3<267:IGIRF->2.0.ZU;2-B
Abstract
2-Deoxyglucose uptake was enhanced in ts371 MiMuSV-NRK cells when grow ing at the permissive temperature to allow the expression of a transfo rming p21 ras protein. This change is due to a decrease in the K-m by approximately 2.5-fold without affecting the V-max of the transporter. The amount of the GLUT1 glucose transporter dit not increase as deduc ed from imnunoblot experiments on total membranes. Nevertheless, ras-t ransformed GLUT1 displays a higher molecular mass due to an increased N-glycosylation of the protein. Experiments made in tunicamycin-treate d cells indicates that a higher glycosylation is responsible for the i ncrease in 2-deoxyglucose uptake in ras-transformed cells. (C) 1997 Fe deration of European Biochemical Societies.