Phosphatidylcholine-specific phospholipase d activity is elevated in v-fps-transformed cells

Y. W. Jiang, J. G. Song, Q. Zang, D. A. Foster

Research output: Contribution to journalArticlepeer-review

26 Scopus citations


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 languageEnglish (US)
Pages (from-to)1195-1203
Number of pages9
JournalBiochemical and Biophysical Research Communications
Issue number2
StatePublished - Sep 15 1994

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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