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Synthesis, Internalization, and Localization of Atrial Natriuretic Peptide in Rat Adrenal Medulla^*

GÉRARD MOREL, JEAN-GUY CHABOT, TOMAS GARCIA-CABALLERO, FRANCIS GOSSARD, FRANCOISE DIHL, MARTHE BELLES-ISLES and SEYMOUR HEISLER

CNRS UA 559 (G.M., J.-G.C, T.G.-C, F.D.), Faculte de Medecine Lyon-Sud, Laboratoire d'Histobgie-Embryologie 69600 Oullins, France
NRC (F.G.), Biotechnology Research Institute Montreal, Quebec, Canada H4P 2R2
Unite de Bioregulation Cellulaire (M.B.-L, S.H.), Le Centre Hospitalier de I'Uniuersite Laval, Sainte-Foy Quebec, Canada GlV 4G2

Address correspondence and requests for reprints to: Gerard Morel, CNRS UA 559, Faculte de Medecine Lyon-Sud, Laboratoire d'Histologie-Embryologie, B.P. 12, Chemin du Petit-Revoyet, 69600 Oullins, France.

Abstract

Some, though not all studies, have indicated that atrial natriuretic peptide (ANP) can bind to adrenal medullary cells. ANP-like immunoreactivity (ANP-LI) has also been identified in catecholamine-secreting cells. Together, these findings suggest that ANP may be taken up and/or synthesized in the adrenal medulla. The present study was designed to ascertain, by in situ hybridization, whether adrenal chromaffin cells could synthesize ANP, to define by an in vivo ultrastructural autoradiographic approach, whether ANP could, in fact, bind to rat adrenal medulla cells, to determine whether there was a cellular [noradrenaline (NA) vs. adrenaline (A)] selectivity in the binding process, and to establish whether extracellular [125I]ANP could be internalized by these cells. The cellular and subcellular distribution of endogenous ANP-LI was also investigated in both cell types by cryoultramicrotomy and immunocytochemical approaches. The in situ hybridization studies indicate the presence of mRNA to ANP in about 15% of adrenal medullary cells. Intravenous injection of [125I]ANP resulted in a 3-fold, preferential and specific radiolabeling of A-as compared to NA-containing cells. In A-containing cells, plasma membranes were significantly labeled 2 and 5 min post injection; cytoplasmic matrix, mitochondria, and secretory granules throughout the time course studied (1-30 min post injection). Lysosomes, rough endoplasmic reticulum, Golgi apparatus, and nuclei were not labeled. ANP-LI was identified in both NA- and A-containing cells; in the former, it was almost exclusively localized in secretory vesicles, in the latter it was detected in plasma membranes, cytoplasmic matrix, nuclear euchromatin, some mitochondria and relatively fewer granules than in NA-containing cells.

The findings suggest that ANP may be synthesized primarily in NA-containing cells and that A-containing cells primarily bind and internalize the extracellular (endogenous or exogenous) atrial peptide. The data suggest that ANP secreted by adrenal medullary chromaffin cells may have distal paracrine actions or interactions with coreleased catecholamines and neuropeptides. Binding and internalization may reflect an action of ANP on the secretory function of A-containing cells. (Endocrinology 123: 149–158,1988)

Footnotes

^* The study was supported by grants from the Medical Council of Canada (to S.H.), the Quebec Heart Foundation (to S.H.) and the Echange France/Canada (CNRS/MRC) Program (to G.M. and S.H.).

Fellow of INSERM.

Fellow of Xunta de Galicia.

Received November 30, 1987.

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