Pathophysiological function of adrenomedullin and proadrenomedullin N-terminal peptides in adrenal chromaffin cells

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Adrenomedullin (AM) and peptides of the proadrenomedullin N-terminal 20 peptide(PAMP20) family are multifunctional peptides abundantly expressed in the adrenal medulla. Thesepeptides are released by regulated exocytosis along with catecholamines upon stimulation of adrenalchromaffin cells. They are also released gradually during culture, and this release is stimulated by acyclic AMP-dependent pathway. The expression and release of AM increase under hypoxia inchromaffin cells. The expression of AM in pheochromocytoma PC12 cells is reduced during neuronaldifferentiation with nerve growth factor. On the other hand, PAMP20 and PAMP12 suppresscatecholamine release and synthesis by interfering with nicotinic cholinergic receptors. AM increasesblood flow in the adrenal gland, and causes a gradual release of catecholamine, but does not modifyregulated exocytosis upon the stimulation of cells.Current data indicate that the expression of these peptides is regulated by intracellularsignaling pathways, and changes under various physiological and pathological conditions. AM andPAMP20 family peptides have distinct physiological functions. PAMP20 and PAMP12 areendogenous peptides that modulate chromaffin cell function in an autocrine manner, whereas AM maymainly regulate vascular cell function in a paracrine manner.

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