Abstract
Activating the protein-tyrosine kinase of v-Fps results in a rapid increase in diglyceride (DG) in rat fibroblasts. The v-Fps-induced increases in DG were detected only when phospholipids were prelabeled with [3H]-myristate, which is incorporated primarily into phosphatidylcholine (PC). Inhibition of phosphatidic acid (PA) phosphatase (PAP), which converts PA to DG, blocked v-Fps-induced DG production. PA is a primary metabolite of type D phospholipases (PLD). Consistent with these observations, PLD activity was activated in response to the kinase activity of v-Fps. The increased PLD activity was detected only when the cells were prelabeled with the PC-specific [3H]-myristate. These data support the hypothesis that v-fps-induced DG is derived from PC via the PLD/PAP pathway.
Original language | English (US) |
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Pages (from-to) | 1195-1203 |
Number of pages | 9 |
Journal | Biochemical and Biophysical Research Communications |
Volume | 203 |
Issue number | 2 |
DOIs | |
State | Published - Sep 15 1994 |
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology