The neurotoxin, β-N-methylamino-l-alanine (BMAA) interacts with the strychnine-insensitive glycine modulatory site of the N-methyl-d-aspartate receptor

C. N. Allen, I. Omelchenko, S. M. Ross, P. Spencer

Research output: Contribution to journalArticle

16 Scopus citations


Electrophysiological and receptor binding techniques were used to determine whether the neurotoxin β-N-4-methylamino-l-alanine (BMAA), a monocarboxylic amino acid, can act at the strychnine-insensitive glycine modulatory site to modify the activity of N-methyl-d-aspartate receptors. dl-BMAA but not l-BMAA reversibly potentiated the amplitude of NMDA-activated currents. Neither dl-BMAA nor l-BMAA were able independently to activate currents. The reversal potential and the potential-dependence of the amplitude were not affected by dl-BMAA. The dl-BMAA effect was reversibly antagonized by 7-chlorokynurenic acid. Concentration jump experiments showed that the time course of the "off" response of NMDA-activated currents in the presence of dl-BMAA is faster than in the presence of glycine, suggesting that dl-BMAA dissociates from the receptor more rapidly than glycine. dl-BMAA produced a concentration-dependent displacement of [3H]glycine binding which was additive with that of 7-chlorokynurenic acid. These data indicate that d-BMAA could act as a stereospecific modulator of NMDA receptor function by acting as an agonist at the strychnine-insensitive glycine modulatory site of the NMDA receptor.

Original languageEnglish (US)
Pages (from-to)651-658
Number of pages8
Issue number6
StatePublished - Jun 1995



  • N-methyl-d-aspartate receptor
  • excitotoxicity
  • strychnine-insensitive glycine modulatory site
  • β-N-methylamino-l-alanine

ASJC Scopus subject areas

  • Pharmacology
  • Cellular and Molecular Neuroscience

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