Reversible in activation of purified (Na+ + K+)-ATPase from human renal tissue by cyclic AMP-dependent protein kinase.
Human renal (Na+ + K+)-ATPase (ATP phosphohydrolase, EC 3.6.1.3) preparations which exhibited a non-linear reaction rate, contained high levels of membrane-bound cyclic AMP-dependent protein kinase, while this latter activity was much less or absent in purified preparations. A non-linear reaction rate was observed in a purified preparation of (Na+ + K+)-ATPase by reconstituting the enzyme into lipid vesicles with cyclic AMP-dependent protein kinase. The addition of cyclic AMP to the ATPase assay of these lipid vesicles inactivated the (Na+ + K+)-ATPase. The cytoplasmic fraction of the cell contained a nondialyzable factor, which prevented (or reversed) the cyclic AMP-mediated inactivation of the enzyme.
D000251:Adenosine Triphosphatases / Q000037:antagonists & inhibitors*; D000242:Cyclic AMP / Q000494:pharmacology*; D003840:Deoxycholic Acid; D004789:Enzyme Activation; D006801:Humans; D007668:Kidney / Q000201:enzymology*; D007700:Kinetics; D008861:Microsomes / Q000201:enzymology; D011188:Potassium / Q000378:metabolism; D011494:Protein Kinases / Q000378:metabolism* / Q000494:pharmacology; D012964:Sodium / Q000378:metabolism
D003840:Deoxycholic Acid; D012964:Sodium; D000242:Cyclic AMP; D011494:Protein Kinases; D000251:Adenosine Triphosphatases; D011188:Potassium