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Matches in SemOpenAlex for { <https://semopenalex.org/work/W2040403308> ?p ?o ?g. }

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• W2040403308 abstract "1. The molecular basis of the state-dependent block of L-type Ca2+ channels by dihydropyridines is still poorly understood. Therefore, we studied the enantioselectivity of Ca2+ channel block by isradipine enantiomers at three holding potentials (-80, -60 and -40 mV) in Chinese hamster ovary (CHO) cells stably expressing the rabbit lung alpha1C-b-subunit. 2. The extent of enantioselectivity did not markedly change with the holding potential (IC50 ratios of 104-138), whereas the potency of both isradipine enantiomers increased with depolarisation of the holding potential. 3. In addition to its block of the peak Ca2+ channel current, Ipeak, (-)-isradipine inhibited the relative current at the end of the test pulse, the so-called Ilate, normalised to Ipeak (Ilate/Ipeak). This effect was unaffected by the holding potential and revealed distinct kinetics compared to the development of conventional block of Ipeak. 4. When these effects were studied using an alpha1C-b-mutant lacking the high-affinity dihydropyridine binding site, expressed in human embryonic kidney (HEK 293) cells, both enantiomers blocked Ilate/Ipeak to a similar degree. 5. Our data are discussed within the framework of the 'guarded receptor' and the 'modulated receptor' hypotheses. The very different properties of the block of Ilate/Ipeak compared to those of the conventional high-affinity block of Ipeak suggest the existence of an additional mechanism possibly mediated via a second, distinct binding site." @default.
• W2040403308 created "2016-06-24" @default.
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• W2040403308 date "1999-11-01" @default.
• W2040403308 modified "2023-10-08" @default.
• W2040403308 title "Dihydropyridine enantiomers block recombinant L‐type Ca²⁺ channels by two different mechanisms" @default.
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• W2040403308 doi "https://doi.org/10.1111/j.1469-7793.1999.00031.x" @default.
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