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Kinetics of the Mechanism of Action of Monoamine Oxidase in the Regulation of Na + , K + ‐ATPase Activity in Rat Brain
Author(s) -
Mayanil C. S. K.,
Baquer N. Z.
Publication year - 1985
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1985.tb07107.x
Subject(s) - monoamine oxidase , mechanism of action , kinetics , chemistry , atpase , phosphorus 32 , enzyme , biochemistry , physics , nucleotide , in vitro , quantum mechanics , gene
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‐hydroxyphenylacetylaldehyde (product of MAO‐catalysed reaction with dopamine as substrate). It was observed that at 2.6 μ M MHB, the activation of Na + ,K + ‐ATPase may be the result of the removal of the inhibitory Ca 2+ , thereby increasing the V max . Double‐reciprocal plots of P i versus MHB showed that Ca 2+ counteracted the effect of the aldehyde not by changing the K m , but be decreasing the V max 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.