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To characterize the potential role of cAMP in pheromone transduction, we  have examined the occurrence of cyclic nucleotide phosphodiesterases (PDEs) in  the mouse vomeronasal organ (VNO). We show that the cAMP-specific isoforms  PDE4A and PDE4D are found preferentially in the apical and basal layers,  respectively, of the VNO neuroepithelium and in the rostral (PDE4A) and caudal  (PDE4D) portions of the accessory olfactory bulb glomerular layer. Assays for  cAMP hydrolysis showed that PDE activity in VNO homogenates was about half  that measured in the cerebral cortex and olfactory epithelium, and the  proportion of total activity inhibited by rolipram, a PDE4-specific inhibitor,  was ∼40%. Activity in the VNO was enhanced 60% by Ca 2+  and  calmodulin (CaM), implicating the presence of Ca 2+ /CaM-dependent  PDE1. Zaprinast, which is known to inhibit PDE1C isoforms, completely  suppressed Ca 2+ /CaM-stimulated activity and, together, zaprinast  and rolipram inhibited cAMP hydrolysis by ∼70%. Our results suggest that  PDE1 and PDE4 isoforms are the primary source of cAMP degradation in the  VNO.

Characterization of cAMP Degradation by Phosphodiesterases in the Accessory Olfactory System