Open AccessPituitary Adenylate Cyclase-Activating Polypeptide (PACAP) Receptor mRNA in the Rat Adrenal Gland: Localization by In Situ Hybridization and Identification of Splice Variants.
Author(s) -
Hiroyuki Nogi,
Hitoshi Hashimoto,
Takashi Fujita,
Nami Hagihara,
Takehisa Matsuda,
Akemichi Baba
Publication year - 1997
Publication title -
japanese journal of pharmacology/japanese journal of pharmacology
Language(s) - English
Resource type - Journals
eISSN - 1347-3506
pISSN - 0021-5198
DOI - 10.1254/jjp.75.203
Subject(s) - adrenal medulla , in situ hybridization , adrenal gland , autocrine signalling , pituitary adenylate cyclase activating peptide , adenylate kinase , paracrine signalling , messenger rna , chromaffin cell , biology , medicine , endocrinology , receptor , microbiology and biotechnology , cyclase , pituitary gland , catecholamine , neuropeptide , gene , biochemistry , stimulation , vasoactive intestinal peptide , hormone
The distribution of mRNA for pituitary adenylate cyclase-activating polypeptide receptor (PACAP-R) was examined by in situ hybridization in rat adrenal gland. In the adrenal medulla, PACAP-R mRNA was expressed in almost all chromaffin cells without any significant expression in the cortical region. Using the reverse transcription-polymerase chain reaction, we analyzed the mRNA expression of PACAP-R splice variant forms in the adrenal gland. The predominant forms observed were the variant having a 28-amino acid insert in the third intracellular loop (termed PACAP-R-hop1). As PACAP is localized in the noradrenaline secreting cells of the adrenal chromaffin cells, and stimulates catecholamine release, the present results suggest that PACAP may serve as a paracrine or autocrine regulatory factor for the chromaffin cells through PACAP-R.