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  • Title: Inhibition of catecholamine synthesis by proadrenomedullin N-terminal 20 peptide in cultured bovine adrenal medullary cells.
    Author: Niina H, Kobayashi H, Kitamura K, Katoh F, Eto T, Wada A.
    Journal: Eur J Pharmacol; 1995 Nov 03; 286(1):95-7. PubMed ID: 8566156.
    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.
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