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

doi:10.1006/bbrc.1998.8855

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 journal › Article › peer-review

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 language	English
Pages (from-to)	630-635
Number of pages	6
Journal	Biochemical and biophysical research communications
Volume	247
Issue number	3
DOIs	https://doi.org/10.1006/bbrc.1998.8855
Publication status	Published - 1998 Jun 29
Externally published	Yes

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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

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.",

author = "Kim, {Byung Chul} and Ha, {Kwon Soo} and Park, {Jae Bong} and Kim, {Jae Hong}",

note = "Funding Information: This work was supported by fund from Hallym Academy of Sciences, Hallym University (to J. H. Kim).",

year = "1998",

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doi = "10.1006/bbrc.1998.8855",

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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

N1 - Funding Information: This work was supported by fund from Hallym Academy of Sciences, Hallym University (to J. H. Kim).

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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DO - 10.1006/bbrc.1998.8855

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JO - Biochemical and Biophysical Research Communications

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

Abstract

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