Binding of [3H]desglycinyl remacemide to rat brain membranes: Association with the benzomorphan attachment site of the N-methyl-D-aspartic acid receptor channel

M. S. Ahmed, A. Mather, S. J. Enna

Research output: Contribution to journalArticle

5 Scopus citations

Abstract

Desglycinyl remacemide (DGR), a biologically active metabolite of remacemide, was radiolabeled in an attempt to develop a ligand binding assay to identify its site of action. Incubation of the radioligand with membranes obtained from P2 fractions of whole rat brain revealed a single population of specific [3H]-DGR binding sites having a K(d) of 290 nM and a B(max) of 1.3 pmole/mg protein. The specific binding of [3H]-DGR is most enriched in the P2 subcellular fraction and is heterogeneously distributed throughout the brain. The binding of [3H]-DGR to rat brain membranes was inhibited most potently by MK-801 and SKF-10,047. In contrast, haloperidol, and other sigma receptor-active agents, were relatively inactive at this site. These data suggest that DGR interacts with a channel blocking site on the NMDA receptor.

Original languageEnglish (US)
Pages (from-to)46-50
Number of pages5
JournalBrain Research
Volume827
Issue number1-2
DOIs
StatePublished - May 8 1999
Externally publishedYes

Keywords

  • Anticonvulsant
  • Desglycinyl remacemide
  • MK- 801
  • Phencyclidine
  • Remacemide
  • SKF-10,047

ASJC Scopus subject areas

  • Neuroscience(all)
  • Clinical Neurology
  • Developmental Biology
  • Molecular Biology

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