Phosphorylation but not transport of sugars is enhanced in virus-transformed mouse 3T3 cells.
The transport and phosphorylation of 2-deoxy-D-glucose are separate and sequential events in both normal and virus-transformed 3T3 cells. The apparent enhancement of 2-dOG uptake by 3T3 cells accompanying virus transformation is not due to an effect on the transport process but to enhanced phosphorylation by intracellular kinases. Phosphorylation of 3-O-methyl-D-glucose does not occur in these cells. Both the rate and extent of transport of this glucose analog is the same in normal cells, SV40 virus-transformed cells and sarcoma virus-transformed cells. The appropriateness of using 3-O-MeG for studies of the glucose transport system of animal cells is examined and discussed.
D000818:Animals; D001693:Biological Transport, Active; D002250:Carbon Radioisotopes; D002460:Cell Line; D002471:Cell Transformation, Neoplastic; D003837:Deoxy Sugars / Q000378:metabolism*; D003847:Deoxyglucose / Q000378:metabolism*; D005347:Fibroblasts; D017988:Gammaretrovirus; D005947:Glucose / Q000031:analogs & derivatives / Q000378:metabolism; D006593:Hexokinase / Q000378:metabolism; D007700:Kinetics; D051379:Mice; D010758:Phosphorus / Q000378:metabolism*; D001357:Sarcoma, Avian; D012513:Sarcoma, Experimental; D013539:Simian virus 40; D013403:Sugar Phosphates / Q000096:biosynthesis; D014316:Tritium
D002250:Carbon Radioisotopes; D003837:Deoxy Sugars; D013403:Sugar Phosphates; D014316:Tritium; D010758:Phosphorus; D003847:Deoxyglucose; D006593:Hexokinase; D005947:Glucose