Characteristics of [3H]ryanodine binding to the rabbit cerebral microsomes.
Specific binding of [3H]ryanodine to the rabbit cerebral microsomes was dependent on free Ca2+ at micromolar concentrations and significantly increased by AMP-PNP and caffeine. Scatchard analysis showed a high and a low affinity binding site. The results suggest the presence of ryanodine binding sites which are activated by Ca2+ but with low efficacy, and greatly modified by adenine nucleotide, Mg2+ and also by caffeine.
Kawai
T
T
Department of Chemical Pharmacology, Faculty of Pharmaceutical Sciences, Nagoya City University, Japan.
Ishii
Y
Y
Imaizumi
Y
Y
Watanabe
M
M
D000266:Adenylyl Imidodiphosphate / Q000494:pharmacology; D000818:Animals; D001921:Brain / Q000378:metabolism*; D002110:Caffeine / Q000494:pharmacology; D002118:Calcium / Q000494:pharmacology; D007700:Kinetics; D008274:Magnesium / Q000494:pharmacology; D008861:Microsomes / Q000378:metabolism*; D051381:Rats; D011950:Receptors, Cholinergic / Q000187:drug effects / Q000378:metabolism*; D012433:Ryanodine / Q000378:metabolism*; D019837:Ryanodine Receptor Calcium Release Channel
D011950:Receptors, Cholinergic; D019837:Ryanodine Receptor Calcium Release Channel; D012433:Ryanodine; D000266:Adenylyl Imidodiphosphate; D002110:Caffeine; D008274:Magnesium; D002118:Calcium