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J Biol Chem, Vol. 274, Issue 37, 26337-26343, September 10, 1999

Nitric Oxide Modulates beta 2-Adrenergic Receptor Palmitoylation and Signaling

Lynda Adam, Michel Bouvier, and Teresa L. Z. Jones

From the Département de Biochimie and Le Groupe de Recherche sur le Système Nerveux Autonome, Université de Montréal, Montréal, Quebec H3T 1J4, Canada and  Metabolic Diseases Branch, NIDDK, National Institutes of Health, Bethesda, Maryland 20892

To determine whether nitric oxide (NO) modulates the beta -adrenergic signaling pathway, we treated cells expressing beta 2-adrenergic receptors (beta 2AR) with the NO donors, 3-morpholinosydnonimine (SIN-1) and 1,2,3,4-oxatriazolium,5-amino-3-(3-chloro-2-methylphenyl)chloride and determined the intracellular production of cAMP after exposure to beta -adrenergic receptor agonists, cholera toxin and forskolin. NO significantly decreased the potency of the beta -adrenergic agonist, isoproterenol, to stimulate cAMP production without affecting the stimulatory action of forskolin and cholera toxin, which directly activate adenylyl cyclase and Gs, respectively. Treatment with the NO donor increased the guanyl nucleotide-sensitive high affinity constant for the agonist, isoproterenol, thus suggesting that it reduced functional coupling between the receptor and Gs. Stimulation of endogenous NO production by lipopolysaccharide in RAW 264.7 macrophages also caused a significant increase in the EC50 for isoproterenol-stimulated cAMP production. SIN-1 treatment also led to a reduction in both basal and isoproterenol-stimulated incorporation of [3H]palmitate into the beta 2AR. Signaling through the nonpalmitoylated, Gly341beta 2AR mutant was unchanged by SIN-1 treatment. Given the link between beta 2AR palmitoylation and its responsiveness to agonist, these results suggest that the primary action of NO was depalmitoylation of the beta 2AR resulting in decreased signaling through the beta 2AR.

Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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