Avermectin B1a inhibits the binding of strychnine to the glycine receptor of rat spinal cord
Neuroscience LettersPublished 1 April 1982
David Y. Graham, Friedhelm Pfeiffer, Heinrich Betz
Citations43
SJR quartileQ2
SJR score0.77
SNIP0.67
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TL;DR
The binding of the glycine receptor antagonist, strychnine, to both membranes and solubilized receptor from rat spinal cord, was inhibited by avermectin B1a with Ki values of 1.3 microM and 3.6 microM.
Abstract
The anthelmintic drug, avermectin B1a, has been reported to interfere with gamma-aminobutyric acid-mediated chloride conductance. Also, enhancement of diazepam binding to mammalian brain membranes by avermectin B1a has led to the suggestion that avermectin B1a interacts with the 'benzodiazepine receptor-gamma-aminobutyric acid receptor-chloride ionophore' complex. Here we report an interaction of avermectin B1a with the glycine receptor. The binding of the glycine receptor antagonist, strychnine, to both membranes and solubilized receptor from rat spinal cord, was inhibited by avermectin B1a with Ki values of 1.3 microM and 3.6 microM, and Hill coefficients of 0.46 and 0.62, respectively.
Keywords
MedicineAgricultural and Biological Sciences
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