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Avermectin B 1a Modulation of γ‐Aminobutyric Acid Receptors in Rat Brain Membranes
Author(s) -
Pong ShengShung,
Wang Ching Chung
Publication year - 1982
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1982.tb08639.x
Subject(s) - receptor , membrane , aminobutyric acid , chemistry , neuroscience , modulation (music) , biophysics , gamma aminobutyric acid , biochemistry , microbiology and biotechnology , biology , physics , acoustics
Avermectin B 1a stimulates high‐affinity binding of [ 3 H]‐γ‐aminobutyric acid (GABA) to receptors in washed rat brain membranes. Scatchard analysis of the data indicates that the drug does not significantly alter the apparent dissociation constant of GABA binding, but increases the detectable number of binding sites from 3.2 to 5.1 pmol/mg protein. (+)‐Bicuculline completely blocks control and avermectin B 1a ‐stimulated GABA binding, whereas picrotoxin antagonizes specifically the avermectin B 1a ‐stimulated GABA binding. The avermectin B 1a ‐stimulated GABA binding is also chloride ion‐dependent, whereas GABA binding in the control is not. These observations suggest that the mechanism of avermectin B 1a stimulation of GABA binding may involve the chloride ion channel.