Interference of sodium with [3H]-nitrendipine binding to cardiac membranes
نویسندگان
چکیده
منابع مشابه
Binding of a calcium antagonist, [3H]nitrendipine, to high affinity sites in bovine aortic smooth muscle and canine cardiac membranes.
[(3)H]Nitrendipine, a potent calcium channel antagonist [3-ethyl-5-methyl-1-1,4-dihydro-2,6 - dimethyl - 4 - (3 - nitrophenyl) - 3,5 - pyridine carboxylate], was used to label high affinity binding sites on membranes prepared from bovine aortic smooth muscle. The binding of [(3)H]nitrendipine is rapid (t(1/2) < 5 min) and reversible at 37 degrees C. The binding sites have a high affinity for [(...
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Binding of the dihydropyridine calcium antagonist [3H]nitrendipine was studied in cardiac myocytes incubated in normal and high potassium buffer so that we might examine the voltage dependence of dihydropyridine binding. Hearts were obtained from adult male Wistar rats, and isolated calcium tolerant myocytes were dissociated by enzymatic dispersion. Cells in 5.6 mM extracellular potassium showe...
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[3H]Nitrendipine binds to canine cardiac sarcolemma in a specific, saturable and rapid manner. Bepridil, a Ca++ channel inhibitor, stimulates this binding at submicromolar concentrations, but inhibits it noncompetitively at higher concentrations (IC50 = 15.8 microM). The increase in binding was due primarily to a 30% increase in the association rate constant (k+1) of [3H]nitrendipine, causing a...
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The effect of morphine on the binding of 3H-nitrendipine was studied in rat hippocampal preparations. Treatment of slices with morphine followed by the preparation of membrane fractions revealed the presence of low affinity binding sites. The effect of morphine was antagonized by naloxone. The effect was not observed when the membrane fraction was incubated with morphine. These results suggest ...
متن کاملBinding of [3H]forskolin to rat brain membranes.
[12-3H]Forskolin (27 Ci/mmol) has been used to study binding sites in rat brain tissue by using both centrifugation and filtration assays. The binding isotherm measured in the presence of 5 mM MgCl2 by using the centrifugation assay is described best by a two-site model: Kd1 = 15 nM, Bmax1 (maximal binding) = 270 fmol/mg of protein; Kd2 = 1.1 microM; Bmax2 = 4.2 pmol/mg of protein. Only the hig...
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ژورنال
عنوان ژورنال: British Journal of Pharmacology
سال: 1985
ISSN: 0007-1188
DOI: 10.1111/j.1476-5381.1985.tb12935.x