Inhibition of phosphorylase kinase, and tyrosine protein kinase activities by quercetin.
Quercetin, a naturally occurring bioflavonoid inhibited the activities of phosphorylase kinase and a partially purified tyrosine protein kinase from rat lung. The inhibition was rapid and concentration dependent. Quercetin at 100 microM inhibited the activities of phosphorylase kinase and tyrosine protein kinase by about 95 and 80-90 percent respectively. ATP reversed the quercetin mediated inhibition of tyrosine protein kinase but not of phosphorylase kinase. These data suggest that quercetin has differential effect on different protein kinase activities and it may be used as a tool to probe the role of various protein kinases in cell function.
D000255:Adenosine Triphosphate / Q000494:pharmacology; D000818:Animals; D001667:Binding, Competitive; D005419:Flavonoids / Q000494:pharmacology*; D007700:Kinetics; D010764:Phosphorylase Kinase / Q000037:antagonists & inhibitors*; D047428:Protein Kinase Inhibitors; D011505:Protein-Tyrosine Kinases; D011794:Quercetin / Q000494:pharmacology*; D051381:Rats
D005419:Flavonoids; D047428:Protein Kinase Inhibitors; D000255:Adenosine Triphosphate; D011794:Quercetin; D010764:Phosphorylase Kinase; D011505:Protein-Tyrosine Kinases