A new peptide, 5-HT-moduline, isolated and purified from mammalian brain specifically interacts with 5-HT1B/1D receptors

Behav Brain Res. 1996;73(1-2):313-17. doi: 10.1016/0166-4328(96)00120-9.


5-HT-Moduline (Leu-Ser-Ala-Leu) is a new endogenous peptide purified from rat brain which interacts specifically with 5-HT1B/1D receptors. The binding interaction of 5-HT-Moduline with 5-HT1B/1D receptors appeared to be a non-competitive process, since the Bmax value of [125I] cyanopindolol binding on rat brain cortical membranes was decreased without modification of the Kd. This interaction was conserved on NIH 3T3 cells expressing the 5-HT1B receptor (IC50 = 10(-11)M) suggesting that the binding site for 5-HT-Moduline is localized on the 5-HT1B receptor protein. The observed interaction may lead to functional alterations of 5-HT1B/1D receptors known to play an important role in regulating the release of 5-HT from serotonergic nerve terminals (autoreceptors) as well as the release of other neurotransmitters (heteroreceptors).

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Binding Sites / drug effects
  • Brain Chemistry / physiology*
  • Cell Line
  • Cerebral Cortex / drug effects
  • Cerebral Cortex / metabolism
  • Chromatography, High Pressure Liquid
  • In Vitro Techniques
  • Membranes / drug effects
  • Membranes / metabolism
  • Mice
  • Molecular Sequence Data
  • Neuropeptides / isolation & purification
  • Neuropeptides / pharmacology*
  • Oligopeptides / isolation & purification
  • Oligopeptides / pharmacology*
  • Pindolol / analogs & derivatives
  • Rats
  • Receptors, Serotonin / drug effects*


  • 5-HT-moduline
  • Neuropeptides
  • Oligopeptides
  • Receptors, Serotonin
  • cyanopindolol
  • Pindolol