Dantrolene and azumolene inhibit [3H] PN200-110 binding to porcine skeletal muscle dihydropyridine receptors
| Autor: | Jerome Parness, Kirk J. Hogan, Roberto Coronado, Roque El-Hayek, Héctor H. Valdivia |
|---|---|
| Rok vydání: | 1992 |
| Předmět: |
Dihydropyridines
medicine.medical_specialty Swine medicine.drug_class Biophysics Hydantoin Receptors Nicotinic Pharmacology Tritium Biochemistry Dantrolene chemistry.chemical_compound Caffeine Internal medicine medicine Animals Receptors Cholinergic Receptor Oxazoles Molecular Biology Muscle Relaxants Central Ryanodine Chemistry Ryanodine receptor Muscles Endoplasmic reticulum Imidazoles Dihydropyridine Skeletal muscle Ryanodine Receptor Calcium Release Channel Muscle relaxant Cell Biology Sarcoplasmic Reticulum medicine.anatomical_structure Endocrinology Calcium Channels Isradipine Malignant Hyperthermia medicine.drug |
| Zdroj: | Biochemical and Biophysical Research Communications. 187:894-900 |
| ISSN: | 0006-291X |
| DOI: | 10.1016/0006-291x(92)91281-t |
| Popis: | We tested whether the hydantoin muscle relaxants dantrolene, azumolene, or aminodantrolene could alter the binding of [3H]PN200-110 to transverse tubule dihydropyridine receptors or the binding of [3H]ryanodine to junctional sarcoplasmic reticulum Ca2+ release channels. All three drugs inhibited [3H]PN200-110 binding with azumolene (IC50 approximately 20 microM) 3-5 times more potent than dantrolene or aminodantrolene. In contrast, 100 microM azumolene and dantrolene produced a small inhibition of [3H]ryanodine binding (less than 25%) while aminodantrolene was essentially inert. Hence there was a preferential interaction of hydantoins with dihydropyridine receptors instead of ryanodine receptors. Skeletal muscle dihydropyridine receptors may participate in the mechanism of action of dantrolene and azumolene. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|