Inhibition of catecholamine synthesis by proadrenomedullin N-terminal 20 peptide in cultured bovine adrenal medullary cells.
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.
Niina
H
H
Department of Pharmacology, Miyazaki Medical College, Japan.
Kobayashi
H
H
Kitamura
K
K
Katoh
F
F
Eto
T
T
Wada
A
A
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
D002395:Catecholamines; D010446:Peptide Fragments; D010455:Peptides; D011506:Proteins; D053607:Adrenomedullin; D002217:Carbachol; D014446:Tyrosine 3-Monooxygenase