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Vol. 55, Issue 2, 255-262, February 1999
Institut Cochin de Génétique Moléculaire,
Centre National de la Recherche Scientifique and Université Paris
VII, Laboratoire d'Immuno-Pharmacologie Moléculaire, Paris,
France
We present evidence that stimulation of the human beta-3
adrenergic receptor (AR), expressed in Chinese hamster
ovary/K1 cells, specifically activates the mitogen-activated
protein kinases extracellular signal-regulated kinase (ERK)1 and
2, but not JNK or p38. The extent and kinetics of the ERK
stimulation by the beta-3 AR are identical with those of
the endogenic insulin receptor. However, insulin augments cellular
proliferation, whereas beta-3 AR agonists inhibit
proliferation due to the production of cyclic AMP. The pharmacological
profile of the ERK activation by the beta-3 AR differs
significantly from its activation of adenylyl cyclase. The order of
potency and intrinsic activities of both natural ligands,
norepinephrine and epinephrine, is inversed between both signaling
pathways. In addition, BRL 37344 and propranolol, ligands that act as
agonists in the stimulation of cyclase, act as antagonists for ERK
activation. The activation of ERK1/2 is sensitive to pertussis toxin,
suggesting that the beta-3 AR, in addition to its
interaction with Gs, can couple to Gi/o.
Furthermore, the activation of ERK by the beta-3 AR is
sensitive to PD98059, wortmannin, and LY294002, indicating a crucial
role for mitogen-activated protein kinase kinase and
phosphatidylinositol-3 kinase (PI3K), respectively. A
beta-3 AR-mediated stimulation of PI3K is confirmed by
the observation that the selective agonist CGP 12177A specifically
activates protein kinase B. As was observed for the activation of ERK,
the activation of protein kinase B is inhibited by preincubation with
pertussis toxin and PI3K inhibitors, suggesting that both are a
consequence of a Gi/o-mediated activation of PI3K.
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