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

Rafael Onetti, Josep Baulida, Anna Bassols

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26 Citations (Scopus)

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 languageEnglish
Pages (from-to)267-270
JournalFEBS Letters
Volume407
DOIs
Publication statusPublished - 5 May 1997

Keywords

  • GLUT1
  • Glucose transport
  • N-Glycosylation
  • Rat fibroblast
  • ras Transformation

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