Identification and hypotensive activity of proadrenomedullin N‐terminal 20 peptide (PAMP)

FEBS Letters

Ishiyama, Yuichiro¹  Ichiki, Yoshinari¹  Minamino, Naoto²  Eto, Tanenao¹  Kangawa, Kenji²  Kawamoto, Mari¹  Washimine, Hisanori¹  Kitamura, Kazuo¹  Matsuo, Hisayuki² 

[1] First Department of Internal Medicine, Miyazaki Medical College, 5200 Kihara, Kiyotake, Miyazaki 889-16, Japan;National Cardiovascular Center Research Institute, Fujishirodai, Suita, Osaka 565, Japan

关键词: Adrenomedullin;    Proadrenomedullin N-terminal 20 peptide (PAMP);    Peptide purification;    Amino acid sequence;    Hypotensive peptide;    PAMP;    proadrenomedullin N-terminal 20 peptide;    RIA;    radioimmunoassay;    ir-;    immunoreactive;    HPLC;    high performance liquid chromatography;    TFA;    trifluoroacetic acid;   

DOI  :  10.1016/0014-5793(94)00810-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Proadrenomedullin N-terminal 20 peptide (PAMP) is a candidate for a novel biologically active peptide processed from an adrenomedullin precursor. Using a radioimmunoassay for human PAMP, major and minor immunoreactive PAMPs were purified from porcine adrenal medulla and complete amino acid sequences were determined. The major immunoreactive peptide was PAMP itself with an amidated carboxy terminus. The minor one was determined to be PAMP[5–20]. An intravenous bolus injection of human PAMP in anesthetized rats caused a rapid and strong hypotensive effect in a dose dependent manner. The present data indicate that PAMP is an endogenous biologically active peptide which is processed from adrenomedullin precursor.

【 授权许可】

Unknown