No abstract

The present study documents that adrenomedullin (AM), a vasoactive peptide originally identified in pheochromocytoma tissue and present in the testis, in vitro affects the function of testicular peritubular myoid cells (TPMC), a contractile cell type located in the seminiferous tubule wall. AM stimulated cAMP production by cultured TPMC taken from 16-day-old rats, and this effect was completely inhibited by the AM antagonist AM-(22-52) and partially by the CGRP (calcitonin gene-related peptide) antagonist CGRP-(8-37). Studies on TPMC contractile activity documented that AM inhibits TPMC contraction induced by endothelin-1 (ET-1) and that its effect is antagonized by AM-(22-52). Neutralizing AM produced by TPMC with the addition of anti-AM antibody induced a significant increase of ET-1-induced contraction. When exposed to the protein kinase A inhibitor H-89, AM inhibitory activity on ET-1-induced TPMC contraction was suppressed, whereas the nitric oxide synthase inhibitor N:(G)-nitro-L-arginine methyl esther did not modify AM activity. In conclusion, our study indicates that AM stimulates cAMP production and inhibits the contraction induced by ET-1 in TPMC in vitro, and that AM produced by TPMC has an autocrine effect. We propose that AM may have a role in the control of seminiferous tubule contraction.

Adrenomedullin (AM) is a recently cloned vasorelaxing peptide that belongs to the calcitonin gene-related peptide family. AM inhibits the contraction of several types of smooth muscle cells and is present in the testis as well as in many other organs. The authors investigated whether testicular peritubular myoid cells (PMC) possess specific receptors for AM. Binding of AM to PMC was saturable in a time-dependent manner and 125I-AM binding was effectively displaced by cold AM. The study documents that testicular peritubular myoid cells are a target for adrenomedullin and suggests a role for this peptide in the paracrine regulation of the testis.