Structure elucidation and biological activity of an unusual adipokinetic hormone from corpora cardiaca of the butterfly, Vanessa cardui

Eur J Biochem. 2000 Sep;267(17):5502-8. doi: 10.1046/j.1432-1327.2000.01611.x.

Abstract

A structurally unusual member of the adipokinetic hormone/red pigment-concentrating hormone peptide family was isolated from corpora cardiaca of the painted lady butterfly, Vanessa cardui. Its primary structure was assigned by Edman degradation and nano-electrospray-time-of-flight mass spectrometry as pQLTFTSSWGGK (Vac-AKH). Vac-AKH represents the first 11mer and the first nonamidated peptide in this family. The peptide shows significant adipokinetic activity in adult specimens of V. cardui. Injection of 10 pmol of synthetic Vac-AKH into 4-day-old decapitated males resulted in an approximately 150% increase of hemolymph lipids after 90 min. Half maximal adipokinetic activity was achieved with about 0. 1 pmol of Vac-AKH. During a 2-h incubation of corpora cardiaca/corpora allata complexes in medium containing 50 mM KCl, significant amounts of Vac-AKH were released from the glands.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Butterflies
  • Chromatography, High Pressure Liquid
  • Insect Hormones / chemistry*
  • Insect Hormones / isolation & purification
  • Insect Hormones / metabolism*
  • Lipid Metabolism
  • Male
  • Mass Spectrometry / methods
  • Oligopeptides / chemistry*
  • Oligopeptides / isolation & purification
  • Oligopeptides / metabolism*
  • Pyrrolidonecarboxylic Acid / analogs & derivatives
  • Spectrophotometry, Ultraviolet

Substances

  • Insect Hormones
  • Oligopeptides
  • adipokinetic hormone
  • Pyrrolidonecarboxylic Acid