INHIBITION OF CATECHOLAMINE SYNTHESIS BY PROADRENOMEDULLIN N-TERMINAL-20-PEPTIDE IN CULTURED BOVINE ADRENAL-MEDULLARY CELLS

被引：23

作者：

NIINA, H

KOBAYASHI, H

KITAMURA, K

KATOH, F

ETO, T

WADA, A

机构：

[1] MIYAZAKI MED COLL,DEPT PHARMACOL,MIYAZAKI 88916,JAPAN

[2] MIYAZAKI MED COLL,DEPT INTERNAL MED 1,MIYAZAKI 88916,JAPAN

来源：

EUROPEAN JOURNAL OF PHARMACOLOGY | 1995年 / 286卷 / 01期

关键词：

PAMP (PROADRENOMEDULLIN N-TERMINAL 20 PEPTIDE); CATECHOLAMINE SYNTHESIS; TYROSINE HYDROXYLASE; NICOTINIC RECEPTOR; ADRENAL MEDULLA;

D O I：

10.1016/0014-2999(95)00528-S

中图分类号：

R9 [药学];

学科分类号：

1007 ;

摘要：

In cultured bovine adrenal medullary cells, proadrenomedullin N-terminal 20 peptide (PAMP), at concentrations greater than or equal to 3 mu M, inhibited carbachol-induced [C-14]catecholamine synthesis from [C-14]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.

引用

页码：95 / 97

页数：3

共 9 条

[1]

HAYCOCK JW, 1982, J BIOL CHEM, V257, P2641

[2] GENOMIC STRUCTURE OF HUMAN ADRENOMEDULLIN GENE [J].