Evidence for role of phospholipase A2 in phosphatidic acid-induced signaling to c-fos serum response element activation

Byung Chul Kim, Kwon Soo Ha, Jae Bong Park, Jae-Hong Kim

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

The activity of exogenous phosphatidic acid (PA) to transactivate c-fos serum response element (SRE) was investigated by transient transfection analysis. Incubation of Rat-2 fibroblast cells with exogenous PA caused a stimulation of c-fos SRE-linked luciferase activity in a dose- and time-dependent manner. The SRE stimulation by PA was dramatically reduced by either pre-treatment with mepacrine, an inhibitor of phospholipase A2 (PLA2), or co-transfection with antisense cytosolic phospholipase A2 (cPLA2) oligonucleotide, whereas lysophosphatidic acid (LPA)-induced SRE activation was not affected. Consistent with this specific requirement for PLA2 by PA, the translocation of cPLA2 protein was rapidly induced followed by PA treatment. Together, these results suggest that PLA2, especially cPLA2, plays a critical role in the nuclear signaling cascade of PA in Rat-2 fibroblast cells.

Original languageEnglish
Pages (from-to)630-635
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume247
Issue number3
DOIs
Publication statusPublished - 1998 Jun 29
Externally publishedYes

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Serum Response Element
Phosphatidic Acids
Phospholipases A2
Chemical activation
Cytosolic Phospholipases A2
Fibroblasts
Transfection
Rats
Cells
Quinacrine
Luciferases
Oligonucleotides
Transient analysis

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Evidence for role of phospholipase A2 in phosphatidic acid-induced signaling to c-fos serum response element activation. / Kim, Byung Chul; Ha, Kwon Soo; Park, Jae Bong; Kim, Jae-Hong.

In: Biochemical and Biophysical Research Communications, Vol. 247, No. 3, 29.06.1998, p. 630-635.

Research output: Contribution to journalArticle

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