TY - JOUR
T1 - Arachidonic acid, a principal product of Rac-activated phospholipase A2, stimulates c-fos serum response element via Rho-dependent mechanism
AU - Kim, Byung Chul
AU - Lim, Chang Jin
AU - Kim, Jae Hong
N1 - Funding Information:
This study was supported by the Korean Ministry of Education through Research Fund, 1996 (to J.H. Kim). We wish to thank Dr. Richard Treisman (Imperial Cancer Research Fund Laboratory, London, UK) for providing EF and EF-C3 plasmids.
PY - 1997/10/6
Y1 - 1997/10/6
N2 - Previously, we have reported that phospholipase A2 (PLA2) 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 PLA2, 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-PLA2-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 Rat-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.
AB - Previously, we have reported that phospholipase A2 (PLA2) 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 PLA2, 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-PLA2-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 Rat-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.
KW - Arachidonic acid
KW - Phospholipase A
KW - Rac
KW - Rho
KW - c-fos serum response element
UR - http://www.scopus.com/inward/record.url?scp=0030869541&partnerID=8YFLogxK
U2 - 10.1016/S0014-5793(97)01152-6
DO - 10.1016/S0014-5793(97)01152-6
M3 - Article
C2 - 9357993
AN - SCOPUS:0030869541
VL - 415
SP - 325
EP - 328
JO - FEBS Letters
JF - FEBS Letters
SN - 0014-5793
IS - 3
ER -