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(Received for publication, April 24, 1996, and in revised form, September 6, 1996)
From the We have investigated the contribution
of Ca2+/calmodulin-dependent protein kinase II (CaM kinase
II) and mitogen-activated protein kinase (MAP kinase) in norepinephrine
(NE)-induced arachidonic acid (AA) release in rabbit aortic vascular
smooth muscle cells (VSMC). NE enhanced release of AA via activation of
cytosolic phospholipase A2 (cPLA2) but not
secretory PLA2 in VSMC prelabeled with
[3H]AA. NE (10 µM) enhanced CaM
kinase II and MAP kinase activity. In cells transiently transfected
with antisense oligonucleotides complementary to the translation
initiation sites of CaM kinase II and MAP kinase, NE-induced AA release
was inhibited by 100 and 35% respectively. Treatment of cells with
PD-098059, a MAP kinase kinase inhibitor, or with MAP kinase antisense
oligonucleotide reduced NE-induced activation of MAP kinase and
cPLA2. NE-induced MAP kinase and cPLA2
activation was also inhibited in cells treated with a CaM kinase II
inhibitor, KN-93, or with CaM kinase II antisense oligonucleotide. On
the other hand, inhibition of MAP kinase kinase with PD-098059 or of
MAP kinase with antisense oligonucleotides did not alter the NE-induced
increase in CaM kinase II activity. Phosphorylation of MAP kinase and
CaM kinase II by NE, studied by 32P incorporation and
immune complex kinase assays, was inhibited by KN-93. Collectively,
these data suggest that CaM kinase II can activate MAP kinase, which in
turn activates cPLA2 to release AA for prostacyclin
synthesis in the rabbit VSMC. This novel pathway for activation of MAP
kinase by CaM kinase II appears to be mediated through stimulation of
MAP kinase kinase. Activation of adrenergic receptors with NE in VSMC
caused translocation of CaM kinase II, MAP kinase, and
cPLA2 to the nuclear envelope only in the presence of
extracellular Ca2+. Okadaic acid, which increased
phosphorylation and activity, did not translocate these enzymes.
Therefore, it appears that in rabbit VSMC, NE, by promoting
extracellular Ca2+ influx, increases CaM kinase II
activity, leading to activation of MAP kinase and cPLA2 and
translocation to the nuclear envelope, resulting in release of AA from
the nuclear envelope for prostacyclin synthesis.
Volume 271, Number 47,
Issue of November 22, 1996
pp. 30149-30157
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
Mediates Activation of Mitogen-activated Protein Kinase and Cytosolic
Phospholipase A2 in Norepinephrine-induced Arachidonic Acid
Release in Rabbit Aortic Smooth Muscle Cells
,
Department of Pharmacology, College of
Medicine, The University of Tennessee Center for Health Sciences,
Memphis, Tennessee 38163, § Southern College of Optometry,
Memphis, Tennessee 38104, and ¶ LeMoyne Owen College, Memphis,
Tennessee 38126
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