A conformationally constrained competitive inhibitor of the sodium-dependent glutamate transporter in forebrain synaptosomes: L-anti-endo-3,4-methanopyrrolidine dicarboxylate

Neurosci Lett. 1994 Jun 20;174(2):193-7. doi: 10.1016/0304-3940(94)90019-1.

Abstract

A series of L-3,4-methanopyrrolidine dicarboxylate isomers were investigated as potential inhibitors of the high affinity, sodium-dependent glutamate transporter in rat forebrain synaptosomes. Of the isomers tested, only L-anti-endo-3,4-methanopyrrolidine dicarboxylate (L-anti-endo-MPDC) blocked the uptake of [3H]D-aspartate, a non-metabolized substrate. Kinetic analysis demonstrated that L-anti-endo-MPDC is a potent competitive inhibitor (Ki = 5 microM) comparable to that of L-glutamate and L-trans-2,4-pyrrolidine dicarboxylate (L-trans-2,4-PDC). Conformational analysis of L-glutamate, L-trans-2,4-PDC and L-anti-endo-MPDC are used to refine the pharmacophore model of the transporter binding site.

Publication types

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

MeSH terms

  • Amino Acid Transport System X-AG
  • Animals
  • Aspartic Acid / metabolism
  • Binding Sites
  • Biological Transport / physiology
  • Dicarboxylic Acids / chemistry
  • Dicarboxylic Acids / pharmacokinetics
  • Dicarboxylic Acids / pharmacology*
  • Glycoproteins / antagonists & inhibitors*
  • In Vitro Techniques
  • Kinetics
  • Male
  • Molecular Conformation
  • Prosencephalon / metabolism*
  • Prosencephalon / ultrastructure
  • Protein Binding
  • Pyrrolidines / chemistry
  • Pyrrolidines / pharmacokinetics
  • Pyrrolidines / pharmacology*
  • Rats
  • Rats, Sprague-Dawley
  • Sodium / physiology*
  • Synaptosomes / metabolism*

Substances

  • 3,4-methanopyrrolidine dicarboxylate
  • Amino Acid Transport System X-AG
  • Dicarboxylic Acids
  • Glycoproteins
  • Pyrrolidines
  • Aspartic Acid
  • Sodium