Open AccessEffects of triethyl lead on various cholinergic parameters in the rat brain in vitro.
Author(s) -
Fumio Hoshi,
Haruo Kobayashi,
Akira Yuyama,
Naonori Matsusaka
Publication year - 1991
Publication title -
japanese journal of pharmacology/japanese journal of pharmacology
Language(s) - English
Resource type - Journals
eISSN - 1347-3506
pISSN - 0021-5198
DOI - 10.1254/jjp.55.27
Subject(s) - lead acetate , acetylcholine , chemistry , acetylcholinesterase , quinuclidinyl benzilate , muscarinic acetylcholine receptor , cholinergic , in vitro , choline , choline acetyltransferase , acetylcholine receptor , neurotoxicity , aché , pharmacology , biochemistry , receptor , toxicity , endocrinology , biology , enzyme , organic chemistry
The effects of triethyl lead acetate (triethyl Pb) on the cholinergic system in the brain of the rats were investigated in vitro. Triethyl Pb, at concentrations below 10(-4) M, inhibited the depolarized release of acetylcholine (ACh) from slices of cortex and they synthesis of ACh in such slices, while it potentiated in a dose-dependent manner the non-depolarized release of ACh. In contrast, lead inhibited noncompetitively the high-affinity uptake of choline into synaptosomes with a Ki of 4.03 X 10(-6) M and the activity of choline acetyltransferase with a Ki of 4.07 X 10(-5) M. Triethyl Pb has an inhibitory effect (IC50 not equal to 5 X 10(-5) M) on the binding of [3H]quinuclidinyl benzilate to muscarinic ACh receptors. Triethyl Pb inhibited acetylcholinesterase activity slightly at 5 X 10(-5) and 10(-4) M. It is suggested that ACh transmission, in particular the synthesis of ACh and the release of ACh, is susceptible to organolead neurotoxicity.