Salvatore Valiante

Publications (53) View all

• Article: Expression of orexin A and its receptor 1 in the human prostate.

  Salvatore Valiante, Giovanna Liguori, Simona Tafuri, Roberto Campese, Roberto Monaco, Salvatore Paino, Vincenza Laforgia, Norma Staiano, Alfredo Vittoria
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  ABSTRACT: The peptides orexin A (OXA) and orexin B, deriving from the cleavage of the precursor molecule prepro-orexin, bind two G-coupled transmembrane receptors, named as receptor 1 (OX1R) and receptor 2 for orexin, showing different affinity-binding properties. First discovered in the rat hypothalamus, orexins and their receptors have been also found in many peripheral tissues where they exert neuroendocrine, autocrine and paracrine functions. Because inconclusive data on their localization in the mammalian prostate are reported, the aim of this study was to investigate the presence of prepro-orexin, OXA and OX1R in the human normal and hyperplastic gland. Immunohistochemistry revealed the localization of both OXA and OX1R in the cytoplasm of the follicular exocrine epithelium of all tested normal and hyperplastic prostates. Positive immunostaining was mainly observed in the basal cells of the stratified epithelium, and only rarely in the apical cells. The expression of mRNAs coding for prepro-orexin and OX1R and of proteins in the tissues was also ascertained by polymerase chain reaction and Western blotting analysis, respectively. In order to gain insights into the functional activity of OXA in the prostate, we administered different concentrations of OXA to cultured prostatic epithelial cells PNT1A. We first demonstrated that PNT1A cells express OX1R. The addition of OXA did not affect PNT1A cell proliferation, while it enhanced cAMP synthesis and Ca(2+) release from intracellular storage. Overall, our results definitely demonstrate the expression of OXA and OX1R in the human prostate, and suggest an active role for them in the metabolism of the gland.
  Journal of Anatomy 02/2013; · 2.37 Impact Factor
• Article: Cellular Localization of PACAP and Its Receptors in the Ovary of the Spotted Ray Torpedo marmorata Risso 1880 (Elasmobranchii: Torpediniformes).

  Marisa Agnese, Salvatore Valiante, Vincenza Laforgia, Piero Andreuccetti, Marina Prisco
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  ABSTRACT: The pituitary adenylate cyclase-activating polypeptide (PACAP) is a member of the glucagon-related family and occurs in two amidated forms, PACAP38 and PACAP27, with 38 and 27 amino acids, respectively. PACAP acts by binding to three different receptors, that are classified by their binding affinity for PACAP and VIP (vasoactive intestinal polypeptide): PAC(1) R (PACAP-specific receptor) exclusively binds PACAP, while VPAC(1) R (VIP/PACAP receptor, subtype 1) and VPAC(2) R (VIP/PACAP receptor, subtype 2) bind both PACAP and VIP. PACAP, first discovered in the brain, was then localized in several peripheral tissues of mammals, including the ovary. Besides mammals, PACAP and its receptors have been reported in fish too; however, less is known about the presence of PACAP in the fish ovary and the studies are limited to teleosts. The aim of our work was to study the distribution of the PACAP/PACAP-Rs system in the ovary of the cartilaginous fish Torpedo marmorata. Using in situ hybridization (ISH) and immunohistochemistry techniques, we demonstrated that PACAP and its receptors are widely represented in the Torpedo ovary in a stage-dependent manner. Moreover, our findings suggest an involvement of this peptide in the whole follicologenesis, probably influencing steroidogenesis, follicle development, and oocyte growth. J. Exp. Zool. 9999A:1-9, 2012. © 2012 Wiley Periodicals, Inc.
  Journal of Experimental Zoology Part A Ecological Genetics and Physiology 10/2012; · 1.64 Impact Factor
• Article: Expression of VIP and its Receptors in the Testis of the Spotted Ray Torpedo marmorata (Risso 1880).

  Marisa Agnese, Luigi Rosati, Francesco Muriano, Salvatore Valiante, Vincenza Laforgia, Piero Andreuccetti, Marina Prisco
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  ABSTRACT: The aim of this work was to study, by immunoprecipitation, in situ hybridization and immunohistochemistry, and the expression of the vasoactive intestinal peptide (VIP) and of its receptors (VPAC(1)R and VPAC(2)R) in the testis of a nonmammalian vertebrate, the cartilaginous fish Torpedo marmorata. We demonstrated that, differently from mammals, VIP and VPAC(2)R were widely distributed in the testicular cells while the VPAC(1)R had a limited distribution. In details, we showed that VIP and VPAC(2)R were present in mitotic and differentiating germ cells as well as in the cells involved in the steroidogenesis, i.e., Leydig, Sertoli cells, and prespermatogonia and spermatogonia. The possibility that VIP is involved in the spermatogenesis and particularly in the steroidogenesis of T. marmorata is discussed.
  Journal of Molecular Neuroscience 07/2012; 48(3):638-46. · 2.50 Impact Factor
• Article: novel localization of orexin A in the tubular cytotypes of the rat testis

  Simona Tafuri, Roberta Lo Muto, Luigi Michele Pavone, Salvatore Valiante, Anna Costagliola, Norma Staiano, Alfredo Vittoria
  Regulatory Peptides 01/2010; 164:53. · 2.11 Impact Factor
• Article: Neuropeptide Y modulates thyroid activity in the lizard, Podarcis sicula (Reptlia, Lacertide).

  R. Sciarrillo, A. Capaldo, S. Valiante, V. Laforgia, De Falco, M
  Current Trends in Endocrinology. 01/2010; 4:91-97.