Inhibition of phosphoinositide hydrolysis by the novel neurotoxin β-N-oxalyl-l-α, β-diaminopropionic acid (l-BOAA)

George C. Ormandy, Richard S. Jope

Research output: Contribution to journalArticlepeer-review

7 Scopus citations

Abstract

Inhibition by a recently isolated neurotoxic amino acid, β-N-oxalyl-l-α, β-diaminopropionic acid, (l-BOAA), of stimulated phosphoinositide hydrolysis was studied in rat brain cerebral cortical slices. l-BOAA inhibited the norepinephrine-stimulated response but did not affect hydrolysis induced by 55 mM K+, carbachol in the presence of 20 mM K+. The inhibition was concentration-dependent with an IC50 of 300 μM. This inhibition was insensitive to the excitatory amino acid antagonists, γ-glutamylglycine, glutamic acid diethyl ether, CNQX, AP-4, AP-7, or kynurenate. Thus, we propose that the l-BOAA-mediated inhibition of the norepinephrine-stimulated response was due to an interaction at a novel site, which may also be sensitive to quisqualate (see discussion). The mechanism of the inhibition is still unknown but was not prevented by inhibition of phospholipase A2 or polyamine synthesis and it was not affected by blockade of chloride channels. However, the presence of 20 mM K+ completely blocked the inhibitory effect of l-BOAA on norepinephrine-stimulated phosphoinositide hydrolysis.

Original languageEnglish (US)
Pages (from-to)53-57
Number of pages5
JournalBrain research
Volume510
Issue number1
DOIs
StatePublished - Feb 26 1990
Externally publishedYes

Keywords

  • Norepinephrine
  • Phosphoinositide hydrolysis
  • Potassium ion
  • β-N-Oxalyl-l-α, β-diaminopropionic acid

ASJC Scopus subject areas

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

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