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

被引:27
作者
Onetti, R [1 ]
Baulida, J [1 ]
Bassols, A [1 ]
机构
[1] UNIV AUTONOMA BARCELONA,FAC VET,DEPT BIOQUIM & BIOL MOL,BELLATERRA 08193,SPAIN
关键词
glucose transport; ras transformation; GLUT1; N-glycosylation; rat fibroblast;
D O I
10.1016/S0014-5793(97)00340-2
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
2-Deoxyglucose uptake was enhanced in ts371 MiMuSV-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 imnunoblot 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. (C) 1997 Federation of European Biochemical Societies.
引用
收藏
页码:267 / 270
页数:4
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