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

FEBS Lett. 1994 Aug 29;351(1):35-7. doi: 10.1016/0014-5793(94)00810-8.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adrenomedullin
  • Amino Acid Sequence
  • Animals
  • Antihypertensive Agents / isolation & purification
  • Antihypertensive Agents / pharmacology*
  • Chromatography, Gel
  • Chromatography, High Pressure Liquid
  • Chromatography, Ion Exchange
  • Humans
  • Male
  • Molecular Sequence Data
  • Peptide Fragments / chemistry
  • Peptide Fragments / isolation & purification
  • Peptide Fragments / pharmacology*
  • Peptides*
  • Proteins / chemistry
  • Proteins / isolation & purification
  • Proteins / pharmacology*
  • Radioimmunoassay
  • Rats
  • Rats, Wistar
  • Swine

Substances

  • Antihypertensive Agents
  • Peptide Fragments
  • Peptides
  • Proteins
  • Adrenomedullin