Inhibitory effect of strychnine on acetylcholine receptor activation in bovine adrenal medullary chromaffin cells
Autor: | Gemma A. J. Kuijpers, Soledad Calvo, Leoncio A. Vergara, Gal Yadid |
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Rok vydání: | 1994 |
Předmět: |
medicine.medical_specialty
Glycine Nicotinic Antagonists Membrane Potentials chemistry.chemical_compound Catecholamines Receptors Glycine Internal medicine Enterochromaffin Cells medicine Animals Nicotinic Antagonist Glycine receptor Cells Cultured Acetylcholine receptor Pharmacology Chemistry Strychnine Nicotinic acetylcholine receptor medicine.anatomical_structure Endocrinology Nicotinic agonist Adrenal Medulla Chromaffin cell Calcium Cattle Acetylcholine Research Article medicine.drug |
Zdroj: | British Journal of Pharmacology. 113:471-478 |
ISSN: | 0007-1188 |
DOI: | 10.1111/j.1476-5381.1994.tb17013.x |
Popis: | 1. Strychnine, which is known as a potent and selective antagonist of the inhibitory glycine receptor in the central nervous system, inhibits the nicotinic stimulation of catecholamine release from bovine cultured adrenal chromaffin cells in a concentration-dependent (1-100 microM) manner. At 10 microM nicotine, the IC50 value for strychnine is approximately 30 microM. Strychnine also inhibits the nicotine-induced membrane depolarization and increase in intracellular Ca2+ concentration. 2. The inhibitory action of strychnine is reversible and is selective for nicotinic stimulation, with no effect observed on secretion elicited by a high external K+ concentration, histamine or angiotensin II. 3. Strychnine competes with nicotine in its effect, but not modify the apparent positive cooperatively of the nicotine binding sites. In the absence of nicotine, strychnine has no effect on catecholamine release. Glycine does not affect catecholamine release nor the inhibitory action of strychnine on this release. 4. These results suggest that strychnine interacts with the agonist binding site of the nicotinic acetylcholine receptor in chromaffin cells, thus exerting a pharmacological effect independently of the glycine receptor. |
Databáze: | OpenAIRE |
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