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and MAP kinase in bradykinin-induced
arachidonic acid release in rabbit CCD cells
1 Departments of Cellular and Molecular Medicine, 2 Biochemistry, and 3 Medicine, Faculty of Medicine, University of Ottawa, Ottawa, Ontario, Canada K1H 8M5
Arachidonic acid
(AA) release is the rate-limiting step in the production of
prostaglandins, an important class of autocrine/paracrine factors that
modulate collecting duct function. Previous results from this
laboratory have established cytosolic phospholipase A2
(cPLA2) as the enzyme
responsible for bradykinin (BK)-stimulated AA mobilization in rabbit
cortical collecting duct (RCCD) cells, and the present study pursues
the intracellular signaling mechanisms responsible for its activation.
Pretreatment of cells with Ro-31-8220, an inhibitor of protein kinase C
(PKC), or PD-98059, an inhibitor of the mitogen-activated protein
kinase (MAPK) cascade, resulted in a 50-60% reduction in
BK-stimulated AA release. Incubation of RCCD cells with a combination
of both Ro-31-8220 and PD-98059 did not achieve a greater inhibition of
either BK-stimulated AA release or
cPLA2 activity, possibly
indicating that MAPK activation was dependent upon prior activation of
PKC. This was supported by the observation that BK-induced MAPK
activation could be reversed by either inhibitor. Additional
experiments dealing with immunoblots for PKC isozymes revealed that
RCCD cells express PKC species 
, 
, 
, and 
. Following BK
stimulation, only PKC translocated to the particulate fraction.
Based on these results, it appears that PKC is activated and involved
in the sequential activation of MAPK and
cPLA2 following BK treatment. The
results also suggest that PKC may be the isozyme implicated in the
process.
cytosolic phospholipase A2; mitogen-activated protein kinase; protein kinase C isozymes
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