title: Inhibition of catecholamine synthesis by proadrenomedullin N-terminal 20 peptide in cultured bovine adrenal medullary cells.
abstract: In cultured bovine adrenal medullary cells, proadrenomedullin N-terminal 20 peptide (PAMP), at concentrations > or = 3 microM, inhibited carbachol-induced [14C]catecholamine synthesis from [14C]tyrosine. Carbachol-induced activation of tyrosine hydroxylase was also attenuated by PAMP. These results suggest that PAMP is a novel endogenous peptide that regulates catecholamine synthesis via the suppression of its rate-limiting enzyme in adrenal medullary cells.
authors.affiliation: Department of Pharmacology, Miyazaki Medical College, Japan.
authors.forename: H
authors.initials: H
authors.lastname: Niina
authors.forename: H
authors.initials: H
authors.lastname: Kobayashi
authors.forename: K
authors.initials: K
authors.lastname: Kitamura
authors.forename: F
authors.initials: F
authors.lastname: Katoh
authors.forename: T
authors.initials: T
authors.lastname: Eto
authors.forename: A
authors.initials: A
authors.lastname: Wada
mesh_terms: D000313:Adrenal Medulla / Q000378:metabolism*; D053607:Adrenomedullin; D000818:Animals; D002217:Carbachol / Q000037:antagonists & inhibitors; D002395:Catecholamines / Q000096:biosynthesis*; D002417:Cattle; D002478:Cells, Cultured; D010446:Peptide Fragments / Q000494:pharmacology*; D010455:Peptides; D011506:Proteins / Q000494:pharmacology*; D014446:Tyrosine 3-Monooxygenase / Q000037:antagonists & inhibitors
chemical_list: D002395:Catecholamines; D010446:Peptide Fragments; D010455:Peptides; D011506:Proteins; D053607:Adrenomedullin; D002217:Carbachol; D014446:Tyrosine 3-Monooxygenase