Abstract
The roles of Rac and p38 kinase in the activation of cPLA2 (cytosolic PLA2) in Rat-2 fibroblasts were investigated. In the present study, we found that PMA activates cPLA2 by a Rac-p38 kinase-dependent pathway. Consistent with this, Rac, if activated, was shown to stimulate cPLA2 in a p38 kinase-dependent manner. In another experiment to understand the signalling mechanism by which the Rac-p38 kinase cascade mediates cPLA2 activation in response to PMA, we observed that PMA-induced cPLA2 translocation to the perinuclear region is completely inhibited by the expression of Rac1N17 or treatment with SB203580 (inhibitor of p38 kinase), suggesting that Rac-p38 kinase cascade acts in this instance by mediating the translocation of cPLA2. The mediatory role of p38 kinase in cPLA2 activation was further demonstrated after a treatment with anisomycin, a very effective activator of p38 kinase. Consistent with the mediatory role of p38 kinase in stimulating cPLA2, anisomycin induced the translocation and activation of cPLA2 in a p38 kinase-dependent manner.
Original language | English |
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Pages (from-to) | 527-535 |
Number of pages | 9 |
Journal | Biochemical Journal |
Volume | 388 |
Issue number | 2 |
DOIs | |
Publication status | Published - 2005 Jun 1 |
Keywords
- Anisomycin
- Arachidonic acid
- PMA
- Rac
- cPLA
- p38 kinase
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Cell Biology