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(Received for publication, December 26, 1995, and in revised form, March 7, 1996)
From the Department of Physiology, College of Medicine, University
of Florida, Gainesville, Florida 32610
Neurons cultured from neonatal rat hypothalamus
and brainstem contain many angiotensin II (Ang II) type 2 (AT2) receptors, and we previously determined that
activation of these sites elicited a stimulation of serine/threonine
phosphatase 2A (PP2A). Here, we have investigated the effects of Ang II
on neuronal mitogen-activated protein (MAP) kinases, potential targets
for PP2A. Using in-gel kinase assays and immunoprecipitation analyses
we have shown that Ang II (10 nM-1 µM)
elicits significant increases in p44MAPK (Erk1) and
p42MAPK (Erk2) activities in cultured neurons, mediated via
Ang II type 1 (AT1) receptors. This stimulatory effect of
Ang II on Erk1 and Erk2 activities was potentiated by blockade of
AT2 receptors with
(S)-1-[4-(dimethylamino)-3-methylphenyl]methyl-5-(diphenylacetyl)-4,5,6,7-tetrahydro-1H-imidazo[4,5-C]pyridine-6-carboxylic
acid (PD 123319, 1 µM). Furthermore, the
AT2 receptor agonist
N-
Volume 271, Number 26,
Issue of June 28, 1996
pp. 15635-15641
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
-nicotinoyl-Tyr-Lys-(N-CBZ-Arg)-His-Pro-Ile-OH
(CGP42112A) (10-50 nM) caused significant decreases
in neuronal Erk1 and Erk2 activities, which were abolished by PD 123319 (1 µM) and by the PP2A inhibitor okadaic acid (3 nM). This indicates that AT1 and
AT2 receptors have opposite actions on Erk1 and Erk2
activities in neonatal neurons. Since MAP kinases are involved in the
regulation of growth/differentiation and apoptosis, our data may
provide an intracellular basis for modulatory effects of Ang II
receptors on these processes.
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