Isolation and identification of a second diuretic hormone from Tenebrio molitor

Peptides. 1998;19(4):619-26. doi: 10.1016/s0196-9781(97)00475-0.


A diuretic hormone (DH) of unusual structure was isolated from extracts of heads of Tenebrio molitor. The hormone is a 47 amino acid peptide, Mr = 5,029.9, with the sequence AGALGESGASLSIVNSLDVLRNRLLLEIARKKAKEGANRNRQILLSL. This peptide increases cyclic AMP production in Malpighian tubules of T. molitor. We recently identified a smaller DH from T. molitor with 37 amino acids; these peptides have only 15 identical amino acids when aligned to maximize similarity to other members of the insect DH family. This family has sequence similarity to the corticotropin-releasing factor superfamily of vertebrate peptides.

Publication types

  • Comparative Study
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Corticotropin-Releasing Hormone / chemistry
  • Cyclic AMP / metabolism
  • Diuretics / chemistry*
  • Diuretics / pharmacology
  • Head
  • Hormones / chemistry*
  • Hormones / pharmacology
  • Insect Proteins / chemistry*
  • Insect Proteins / pharmacology
  • Malpighian Tubules / drug effects
  • Molecular Sequence Data
  • Multigene Family
  • Sequence Homology, Amino Acid
  • Tenebrio / chemistry*


  • Diuretics
  • Hormones
  • Insect Proteins
  • Corticotropin-Releasing Hormone
  • Cyclic AMP