The γ-subunit of the rod photoreceptor cGMP-binding cGMP-specific PDE is expressed in mouse lung

The type 6 phosphodiesterase (PDE-6) from retinal rod photoreceptors is an αβγ[in2] heterotetramer. The α-and β-subunits contain catalytic sites for cGMP hydrolysis, whereas the γ-subunits (Pγ) serve as a protein inhibitor of the enzyme. Pγ is believed to be expressed only in photoreceptors. Using RT-PCR, we have amplified the complete coding sequence for Pγ from mouse lung RNA. The expression of Pγ in this tissue may be related to its ability to interact the type 5 phosphodiesterase (PDE-5), which is the predominant cGMP binding protein in lung. We therefore suggest that Pγ may have a wider signaling role in mammalian cells than previousl y appreciated.     

10-nonacosanol,sitosterol and nonacosanediols in Juniperus pinchotii

GC of juniper leaf non-saponifiables gave three peaks of sterol-triterpenes which were identified as 10-nonacosanol, sitosterol and a mixture of nonacosanediols.