Abstract
In the present study, we investigated whether hydrogen peroxide activates c-fos serum response element (SRE) in Rat-2 fibroblast cells. By transient transfection analysis, exogenous H2O2 stimulated SRE-dependent reporter gene activity in a dose and time-dependent manner. Also, we examined the role of Rac GTPase and phospholipase A2 (PLA2) in the H2O2-induced SRE activation. Either transfection of a dominant negative Rac mutant, RacN17, plasmid or pretreatment of mepacrine, a potent inhibitor of PLA2, blocked H2O2-induced SRE activation dramatically. Together, these findings suggest a critical role of 'Rac and subsequent activation of phospholipase A2' in the signaling pathway of H2O2 to SRE.
Original language | English |
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Pages (from-to) | 93-96 |
Number of pages | 4 |
Journal | FEBS Letters |
Volume | 406 |
Issue number | 1-2 |
DOIs | |
Publication status | Published - 1997 Apr 7 |
Externally published | Yes |
Keywords
- Arachidonic acid
- Hydrogen peroxide
- Phospholipase A
- Rac GTPase
- Serum response element
- c-fos
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology