Alkyl-substituted gamma-butyrolactones act at a distinct site allosterically linked to the TBPS/picrotoxinin site on the GABAA receptor complex
| Autor: | James A. Ferrendelli, Douglas F. Covey, Michael G. Bouley, Katherine D. Holland |
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| Rok vydání: | 1993 |
| Předmět: |
Stereochemistry
Allosteric regulation Biology In Vitro Techniques Sulfur Radioisotopes Binding Competitive Dissociation (chemistry) Rats Sprague-Dawley chemistry.chemical_compound Non-competitive inhibition 4-Butyrolactone Animals Binding site Receptor Molecular Biology chemistry.chemical_classification GABAA receptor General Neuroscience Receptors GABA-A Rats Kinetics chemistry Biochemistry Female Neurology (clinical) Lactone Developmental Biology Picrotoxin |
| Zdroj: | Brain research. 615(1) |
| ISSN: | 0006-8993 |
| Popis: | Effects of alkyl-substituted gamma-butyrolactones and gamma-thiobutyrolactones on [35S]t-butylbicyclophosphorothionate (35S-TBPS) dissociation from the picrotoxinin receptor were studied. Unlike picrotoxinin, these lactones accelerated the dissociation rate of 35S-TBPS. Thus, previous reports that these lactones change the Kd but not the Bmax of 35S-TBPS in equilibrium binding experiments is explained not by competitive inhibition, but by an allosteric interaction with the 35S-TBPS binding site. These results indicate that modulatory effects of alkyl-substituted gamma-butyrolactones may result from their action at a distinct site on the gamma-aminobutyric acid (GABA)A receptor. |
| Databáze: | OpenAIRE |
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