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 language | English |
|---|---|
| Pages (from-to) | 630-635 |
| Number of pages | 6 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 247 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - 1998 Jun 29 |
| Externally published | Yes |
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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 journal › Article
}
TY - JOUR
T1 - Evidence for role of phospholipase A2 in phosphatidic acid-induced signaling to c-fos serum response element activation
AU - Kim, Byung Chul
AU - Ha, Kwon Soo
AU - Park, Jae Bong
AU - Kim, Jae-Hong
PY - 1998/6/29
Y1 - 1998/6/29
N2 - 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.
AB - 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.
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UR - http://www.scopus.com/inward/citedby.url?scp=0032577914&partnerID=8YFLogxK
U2 - 10.1006/bbrc.1998.8855
DO - 10.1006/bbrc.1998.8855
M3 - Article
VL - 247
SP - 630
EP - 635
JO - The BMJ
JF - The BMJ
SN - 0730-6512
IS - 3
ER -