Binding characteristics of a new 1,5-benzothiazepine, clentiazem, to rat cerebral cortex and skeletal muscle membranes
| Autor: | Osasi Takaiti, Minezo Otsuka, Tatsuo Suzuki, Motoaki Ohashi, Hideo Kurosawa, Kazuaki Naito |
|---|---|
| Rok vydání: | 1991 |
| Předmět: |
Male
medicine.medical_specialty Biology Pharmacology Tritium Clentiazem chemistry.chemical_compound Diltiazem Radioligand Assay Nitrendipine Internal medicine medicine Animals heterocyclic compounds Binding site Cerebral Cortex Binding Sites Membranes Muscles Skeletal muscle Biological membrane Rats Inbred Strains Stereoisomerism Calcium Channel Blockers Rats Membrane Endocrinology medicine.anatomical_structure chemistry Cerebral cortex cardiovascular system medicine.drug |
| Zdroj: | European journal of pharmacology. 194(2-3) |
| ISSN: | 0014-2999 |
| Popis: | The binding properties of a new 1,5-benzothiazepine, clentiazem (TA-3090), were investigated in rat cerebral cortex and skeletal muscle membranes with [3H]diltiazem and [3H]nitrendipine as radioligands. Clentiazem inhibited [3H]diltiazem binding to cerebral cortex membranes at the same concentrations as diltiazem at 2 degrees C. However, at 37 degrees C clentiazem was 3 times more potent to inhibit binding than diltiazem. [3H]Nitrendipine binding was modulated by clentiazem in a temperature-dependent manner. At 37 degrees C clentiazem significantly enhanced [3H]nitrendipine binding to rat cerebral cortex membranes, whereas it has an inhibitory effect on [3H]nitrendipine binding at 0 degree C and no effect at 25 degrees C. Of two optical isomers of clentiazem and four of diltiazem, only d-cis isomers (clentiazem and diltiazem) increased [3H]nitrendipine binding, indicating that both compounds have the same stereoselectivity for increasing [3H]nitrendipine binding. These results suggest that clentiazem binds to the same 1,5-benzothiazepine binding sites as diltiazem but with greater affinity. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|