Arachidonic acid, a principal product of Rac-activated phospholipase A2, stimulates c-fos serum response element via Rho-dependent mechanism
摘要:
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.
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DOI:
10.1016/S0014-5793(97)01152-6
被引量:
年份:
1997
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