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J. Biol. Chem., Vol. 265, Issue 11, 6042-6047, Apr, 1990
D Teegarden, EJ Taparowsky and C Kent
The effect of expression of the Harvey-ras oncogene on phosphatidylcholine
metabolism in C3H10T1/2 mouse fibroblast cells was examined. There were
multiple changes in the CDP-choline pathway for phosphatidylcholine
biosynthesis in the ras-expressing cells. The activity of the first enzyme
in the pathway, choline kinase, was stimulated 1.9-fold, while the activity
of the second enzyme, CTP:phosphocholine cytidylyltransferase, was
decreased by one-half. High levels of intracellular phosphocholine measured
in the ras cells were consistent with the altered activities of choline
kinase and cytidylyltransferase. The overall rate of phosphatidylcholine
synthesis appeared to be increased because the turnover rate of
phosphocholine from the intracellular pool was higher in the
ras-transfected cells. There also appeared to be an increased rate of
phosphatidylcholine degradation in ras-expressing C3H10T1/2 cells. Very
high levels of glycerophosphocholine (6-fold increased over control cells)
suggested that phospholipase A was activated in these cells. These results
indicate that the ras oncogene product directly or indirectly causes an
increased turnover of phosphatidylcholine in C3H10T1/2 cells.
Altered phosphatidylcholine metabolism in C3H10T1/2 cells transfected with the Harvey-ras oncogene
Department of Biochemistry, Purdue University, West Lafayette, Indiana 47907.
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