Increased glucose transport in ras-transformed fibroblasts: a possible role for N-glycosylation of GLUT1

FEBS Letters
R OnettiA Bassols

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.

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Citations

Mar 2, 1999·Microvascular Research·P Dore-DuffyJ C LaManna
Feb 9, 2016·Cell Metabolism·Shawn M DavidsonMatthew G Vander Heiden
Dec 8, 2017·Biomolecules & Therapeutics·Hye-Young Min, Ho-Young Lee
Mar 17, 2001·Medicine and Science in Sports and Exercise·T W Balon, K K Yerneni
Apr 4, 2021·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·Marta BaczewskaPaweł Knapp

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