Molecular Cloning of VIP and Distribution of VIP/VPACR System In
RESEARCH ARTICLE Molecular Cloning of VIP and Distribution of VIP/VPACR System in the Testis of Podarcis sicula MARISA AGNESE*, LUIGI ROSATI, FRANCESCA CORAGGIO, SALVATORE VALIANTE, AND MARINA PRISCO Department of Biology, University of Naples Federico II, Naples, Italy ABSTRACT Using molecular, biochemical, and cytological tools, we studied the nucleotide and the deduced amino acid sequence of PHI/VIP and the distribution of VIP/VPAC receptor system in the testis of the Italian wall lizard Podarcis sicula to evaluate the involvement of such a neuropeptide in the spermatogenesis control. We demonstrated that (1) Podarcis sicula VIP had a high identity with other vertebrate VIP sequences, (2) differently from mammals, VIP was synthesized directly in the testis, and (3) VIP and its receptor VPAC2 were widely distributed in germ and somatic cells, while the VPAC1R had a distribution limited to Leydig cells. Our results demonstrated that in Podarcis sicula the VIP sequence is highly preserved and that this neuropeptide is involved in lizard spermatogenesis and steroidogenesis. J. Exp. Zool. 321A:334–347, 2014. © 2014 Wiley Periodicals, Inc. J. Exp. Zool. How to cite this article: Agnese M, Rosati L, Coraggio F, Valiante S, Prisco M. 2014. Molecular 321AA:334–347, cloning of VIP and distribution of VIP/VPACR system in the testis of Podarcis sicula. J. Exp. Zool 2014 321A:334–347. Vasoactive Intestinal Peptide (VIP) is a 28 amino acid neuropeptide subtype 2), that are coupled in the adenylate cyclase pathway (Mutt and Said, '74), originally isolated from the porcine ileum (Dickson and Finlayson, 2009). The PACAP also binds to these (Said and Mutt, '70); it belongs to the glucagon/secretin receptors, in addition to a PACAP‐specific receptor (PAC1R).
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