2-Iodoimipramine, a novel ligand for the serotonin transporter

Mol Pharmacol. 1989 Oct;36(4):620-6.

Abstract

Iodoimipramine was synthesized by iodinating imipramine with ICI. Iodoimipramine competitively inhibits [3H]imipramine binding with a KI of 0.52 nM and also inhibits [3H]serotonin transport competitively, suggesting that serotonin, imipramine, and iodoimipramine all bind to the same site on the serotonin transporter. Association of [125I]iodoimipramine to platelet membranes in Na+ requires 20 min to reach equilibrium at 25 degrees and 1.5 hr at 0 degrees. [125I] Iodoimipramine binding at equilibrium is saturable and Na+ dependent, with a KD of 0.58 nM and a Bmax of 1.3 pmol/mg at 25 degrees. Serotonin competitively inhibits [125I]iodoimipramine binding, with a KI of 1.3 microM. [125I]Iodoimipramine bound at 0 degrees in the presence of Na+ does not dissociate unless the temperature is raised or Na+ is removed from the medium. At 25 degrees, dissociation of [125I] iodoimipramine from platelet membranes in the presence of Na+ is only partial, with 40% of the ligand remaining persistently bound over 5 hr after a 50-fold dilution.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Binding, Competitive
  • Biological Transport / drug effects
  • Blood Platelets / metabolism*
  • Carrier Proteins / metabolism*
  • Cell Membrane / metabolism
  • Humans
  • Imipramine / analogs & derivatives*
  • Imipramine / chemical synthesis
  • Imipramine / metabolism
  • In Vitro Techniques
  • Kinetics
  • Ligands
  • Serotonin / metabolism*
  • Serotonin Plasma Membrane Transport Proteins
  • Temperature

Substances

  • Carrier Proteins
  • Ligands
  • Serotonin Plasma Membrane Transport Proteins
  • 2-iodoimipramine
  • Serotonin
  • Imipramine