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Arachidonic acid, a principal product of Rac‐activated phospholipase A 2 , stimulates c‐ fos serum response element via Rho‐dependent mechanism
Author(s) -
Kim Byung-Chul,
Lim Chang-Jin,
Kim Jae-Hong
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)01152-6
Subject(s) - serum response element , rhoa , signal transduction , arachidonic acid , chemistry , microbiology and biotechnology , phospholipase c , rac gtp binding proteins , serum response factor , mediator , phospholipase a2 , gtpase , biology , biochemistry , rac1 , transcription factor , enzyme , gene
Previously, we have reported that phospholipase A 2 (PLA 2 ) is one of the major downstream targets by which Rac GTPase mediates the activation of c‐ fos serum response element (SRE) in response to agonists such as EGF [FEBS Lett. 407 (1997) 7–12]. Thus, the potential activity of arachidonic acid (AA), a principal product of Rac‐activated PLA 2 , on c‐ fos SRE stimulation has been suggested. Here, we provide evidence about the biological activity of AA on c‐ fos SRE activation. Further, we observed that co‐transfection with expression plasmid of either RhoN19, a dominant negative RhoA mutant, or botulinum C3 transferase which inhibits Rho via ADP ribosylation, selectively repressed AA‐ or Rac‐induced SRE activation, suggesting that Rho activity is critical for the signaling cascade of `Rac‐PLA 2 ‐AA' to c‐ fos SRE. Thus, Rac signaling to the nucleus appears to be, at least partly, mediated by a Rho‐linked pathway and this Rac‐Rho signaling connection is mediated by AA. In accordance with the role of Rho as a potential mediator of AA signaling to the nucleus, AA induces a rapid translocation of RhoA.