Frozen sections of normal adrenal glands, obtained from patients undergoing unilateral nephrectomy for kidney cancer, were labeled in vitro with human [125I]ADM(1-52). Autoradiography showed the presence of abundant ADM binding sites in the zona glomerulosa (ZG) and the outermost portion of the zona fasciculata, which were completely displaced by the addition of an excess of cold ADM(1-52). Calcitonin gene-related peptide (CGRP) and the non-selective ligand of the CGRP-receptor subtypes 1 and 2 CGRP(8-37) eliminated [125I]ADM(1-52) binding in the ZG, while the selective ligand of CGRP receptor subtype 2 [Cys(acm)2,7]-CGRP and CGRP(1-8) were ineffective. These findings confirm the presence of ADM binding sites in the human ZG, and provide the first morphological evidence that ADM and CGRP interact with a common receptor of the CGRP1 subtype.

Adrenomedullin and calcitonin gene-related peptide (CGRP) interact with a common recveptor of the CGRP1 subtype in the human adrenal zona glomerulosa.

BELLONI, ANNA SANDRA;ANDREIS, GIACOMINA PAOLA;NUSDORFER, GASTONE
1999

Abstract

Frozen sections of normal adrenal glands, obtained from patients undergoing unilateral nephrectomy for kidney cancer, were labeled in vitro with human [125I]ADM(1-52). Autoradiography showed the presence of abundant ADM binding sites in the zona glomerulosa (ZG) and the outermost portion of the zona fasciculata, which were completely displaced by the addition of an excess of cold ADM(1-52). Calcitonin gene-related peptide (CGRP) and the non-selective ligand of the CGRP-receptor subtypes 1 and 2 CGRP(8-37) eliminated [125I]ADM(1-52) binding in the ZG, while the selective ligand of CGRP receptor subtype 2 [Cys(acm)2,7]-CGRP and CGRP(1-8) were ineffective. These findings confirm the presence of ADM binding sites in the human ZG, and provide the first morphological evidence that ADM and CGRP interact with a common receptor of the CGRP1 subtype.
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Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/11577/2470693
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