Abstract
2-Deoxyglucose uptake was enhanced in ts371 KiMuSV-NRK cells when growing at the permissive temperature to allow the expression of a transforming 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 deduced from immunoblot experiments on total membranes. Nevertheless, ras-transformed GLUT1 displays a higher molecular mass due to an increased N-glycosylation of the protein. Experiments made in tunicamycin-treated cells indicates that a higher glycosylation is responsible for the increase in 2-deoxyglucose uptake in ras-transformed cells.
Original language | English |
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Pages (from-to) | 267-270 |
Journal | FEBS Letters |
Volume | 407 |
DOIs | |
Publication status | Published - 5 May 1997 |
Keywords
- GLUT1
- Glucose transport
- N-Glycosylation
- Rat fibroblast
- ras Transformation