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Identification and hypotensive activity of proadrenomedullin N‐terminal 20 peptide (PAMP)
Author(s) -
Kitamura Kazuo,
Kangawa Kenji,
Ishiyama Yuichiro,
Washimine Hisanori,
Ichiki Yoshinari,
Kawamoto Mari,
Minamino Naoto,
Matsuo Hisayuki,
Eto Tanenao
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)00810-8
Subject(s) - chemistry , identification (biology) , peptide , terminal (telecommunication) , pharmacology , biochemistry , medicine , biology , computer science , telecommunications , botany
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.