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J Biol Chem, Vol. 274, Issue 39, 27702-27710, September 24, 1999

Pituitary Adenylate Cyclase-activating Polypeptides Directly Stimulate Sympathetic Neuron Neuropeptide Y Release through PAC₁ Receptor Isoform Activation of Specific Intracellular Signaling Pathways

From the Department of Anatomy and Neurobiology, College of Medicine, University of Vermont, Burlington, Vermont 05405

Pituitary adenylate cyclase-activating polypeptides (PACAP) have potent regulatory and neurotrophic activities on superior cervical ganglion (SCG) sympathetic neurons with pharmacological profiles consistent for the PACAP-selective PAC₁ receptor. Multiple PAC₁ receptor isoforms are suggested to determine differential peptide potency and receptor coupling to multiple intracellular signaling pathways. The current studies examined rat SCG PAC₁ receptor splice variant expression and coupling to intracellular signaling pathways mediating PACAP-stimulated peptide release. PAC₁ receptor mRNA was localized in over 90% of SCG neurons, which correlated with the cells expressing receptor protein. The neurons expressed the PAC₁(short)HOP1 receptor but not VIP/PACAP-nonselective VPAC₁ receptors; low VPAC₂ receptor mRNA levels were restricted to ganglionic nonneuronal cells. PACAP27 and PACAP38 potently and efficaciously stimulated both cAMP and inositol phosphate production; inhibition of phospholipase C augmented PACAP-stimulated cAMP production, but inhibition of adenylyl cyclase did not alter stimulated inositol phosphate production. Phospholipase C inhibition blunted neuron peptide release, suggesting that the phosphatidylinositol pathway was a prominent component of the secretory response. These studies demonstrate preferential sympathetic neuron expression of PACAP-selective receptor variants contributing to regulation of autonomic function.

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