Kinetics of the mechanism of action of monoamine oxidase in the regulation of Na+,K+-ATPase activity in rat brain.

Abstract:

: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.

journal_name

J Neurochem

authors

Mayanil CS,Baquer NZ

doi

10.1111/j.1471-4159.1985.tb07107.x

subject

Has Abstract

pub_date

1985-01-01 00:00:00

pages

25-30

issue

1

eissn

0022-3042

issn

1471-4159

journal_volume

44

pub_type

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