TY - JOUR
T1 - Alterations on glucose metabolism in chick embryo cells transformed by rous sarcoma virus
T2 - intracellular levels of glycolytic intermediates
AU - Nath Singh, V.
AU - Singh, M.
AU - August, J. T.
AU - Horecker, B. L.
PY - 1974
Y1 - 1974
N2 - Chick embryo cells, transformed with Rous sarcoma virus, show enhanced rates of sugar transport and glycolysis. Determination of intracellular concentrations of glycolytic intermediates suggests that the enhanced glycolytic flux is due to increased activities of hexokinase (ATP:D hexose 6 phosphotransferase, EC 2.7.1.1), phosphofructokinase, (ATP:D fructose 1 phosphate 6 phosphotransferase, EC 2.7.1.56), and pyruvate kinase (ATP: pyruvate 2 O phosphotransferase, EC 2.7.1.40), and not directly to the increased glucose transport. This conclusion is supported by the finding that the intracellular concentration of free glucose is decreased, rather than increased, in the transformed cells. The present observations suggest that the increased glycolytic flux is related to an increased rate of phosphorylation of glucose, and that hexokinase in the transformed cells is at least partly released from its normal control mechanism involving feedback inhibition by glucose 6 P.
AB - Chick embryo cells, transformed with Rous sarcoma virus, show enhanced rates of sugar transport and glycolysis. Determination of intracellular concentrations of glycolytic intermediates suggests that the enhanced glycolytic flux is due to increased activities of hexokinase (ATP:D hexose 6 phosphotransferase, EC 2.7.1.1), phosphofructokinase, (ATP:D fructose 1 phosphate 6 phosphotransferase, EC 2.7.1.56), and pyruvate kinase (ATP: pyruvate 2 O phosphotransferase, EC 2.7.1.40), and not directly to the increased glucose transport. This conclusion is supported by the finding that the intracellular concentration of free glucose is decreased, rather than increased, in the transformed cells. The present observations suggest that the increased glycolytic flux is related to an increased rate of phosphorylation of glucose, and that hexokinase in the transformed cells is at least partly released from its normal control mechanism involving feedback inhibition by glucose 6 P.
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U2 - 10.1073/pnas.71.10.4129
DO - 10.1073/pnas.71.10.4129
M3 - Article
C2 - 4372608
AN - SCOPUS:0005162157
SN - 0027-8424
VL - 71
SP - 4129
EP - 4132
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
IS - 10
ER -