Quercetin interaction with the (Ca2+ + Mg2+)-ATPase of sarcoplasmic reticulum.
In sarcoplasmic reticulum vesicles or in the (Ca2+ + Mg2+)-ATPase purified from sarcoplasmic reticulum, quercetin inhibited ATP hydrolysis, Ca2+ uptake, ATP-Pi exchange, ATP synthesis coupled to Ca2+ efflux, ATP-ADP exchange, and steady state phosphorylation of the ATPase by inorganic phosphate. Steady state phosphorylation of the ATPase by ATP was not inhibited. Quercetin also inhibited ATP and ADP binding but not the binding of Ca2+. The inhibition of ATP-dependent Ca2+ transport by quercetin was reversible, and ATP, Ca2+, and dithiothreitol did not affect the inhibitory action of quercetin.
D000244:Adenosine Diphosphate / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D001693:Biological Transport, Active / Q000187:drug effects; D017301:Ca(2+) Mg(2+)-ATPase; D002118:Calcium / Q000378:metabolism; D000252:Calcium-Transporting ATPases / Q000378:metabolism*; D005419:Flavonoids / Q000494:pharmacology*; D007700:Kinetics; D010710:Phosphates / Q000378:metabolism; D011485:Protein Binding; D011794:Quercetin / Q000494:pharmacology*; D012519:Sarcoplasmic Reticulum / Q000201:enzymology*
D005419:Flavonoids; D010710:Phosphates; D000244:Adenosine Diphosphate; D000255:Adenosine Triphosphate; D011794:Quercetin; D017301:Ca(2+) Mg(2+)-ATPase; D000252:Calcium-Transporting ATPases; D002118:Calcium