Kinetics of the mechanism of action of monoamine oxidase in the regulation of Na+,K+-ATPase activity in rat brain.
Kinetic studies on the action of monoamine oxidase (MAO) in the regulation of Na+,K+-ATPase were performed using 3-methoxy-4-hydroxybenzaldehyde (MHB), which is an analogue of 3-methoxy-4-hydroxy-phenylacetylaldehyde (product of MAO-catalysed reaction with dopamine as substrate). It was observed that at 2.6 microM MHB, the activation of Na+,K+-ATPase may be the result of the removal of the inhibitory Ca2+, thereby increasing the Vmax. Double-reciprocal plots of Pi versus MHB showed that Ca2+ counteracted the effect of the aldehyde not by changing the Km, but be decreasing the Vmax of the Na+,K+-ATPase stimulation. The removal of 3',5'-cyclic AMP-dependent protein kinase from the microsomes by sodium dodecyl sulphate treatment abolished the activation and/or inhibition of the Na+,K+-ATPase by aldehyde; it can therefore be inferred that 3',5'-cyclic AMP-dependent protein kinase is involved in the regulation of Na+,K+-ATPase.
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D000818:Animals; D001547:Benzaldehydes / Q000378:metabolism; D001921:Brain / Q000201:enzymology*; D004298:Dopamine / Q000378:metabolism; D004533:Egtazic Acid / Q000494:pharmacology; D007700:Kinetics; D008861:Microsomes / Q000201:enzymology; D008995:Monoamine Oxidase / Q000378:metabolism*; D011494:Protein Kinases / Q000378:metabolism; D051381:Rats; D011919:Rats, Inbred Strains; D012967:Sodium Dodecyl Sulfate / Q000378:metabolism; D000254:Sodium-Potassium-Exchanging ATPase / Q000378:metabolism*; D013570:Synaptic Membranes / Q000201:enzymology
D001547:Benzaldehydes; D012967:Sodium Dodecyl Sulfate; D004533:Egtazic Acid; C100058:vanillin; D008995:Monoamine Oxidase; D011494:Protein Kinases; D000254:Sodium-Potassium-Exchanging ATPase; D004298:Dopamine