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 journalArticle

24 Citations (Scopus)

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 languageEnglish (US)
Pages (from-to)1195-1203
Number of pages9
JournalBiochemical and Biophysical Research Communications
Volume203
Issue number2
DOIs
StatePublished - Sep 15 1994

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Phospholipase D
Diglycerides
Phosphatidylcholines
Phosphatidic Acids
Myristic Acid
Phosphatidate Phosphatase
Fibroblasts
Metabolites
Phosphoric Monoester Hydrolases
Protein-Tyrosine Kinases
Rats
Phospholipids
Phosphotransferases
1-dodecylpyridoxal

ASJC Scopus subject areas

  • Molecular Biology
  • Biophysics
  • Biochemistry

Cite this

Phosphatidylcholine-Specific Phospholipase D Activity Is Elevated in v-Fps-Transformed Cells. / Jiang, Y. W.; Song, J. G.; Zang, Q.; Foster, D. A.

In: Biochemical and Biophysical Research Communications, Vol. 203, No. 2, 15.09.1994, p. 1195-1203.

Research output: Contribution to journalArticle

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