Monoamine oxidase A inhibition by
fluoxetine: an in vitro and in vivo study

Mukherjee J, Yang ZY
Franklin McLean Institute,
Department of Radiology,
The University of Chicago,
Illinois 60637, USA.
Synapse 1999 Mar 15; 31(4):285-9


Monoamine oxidase A (MAO-A) inhibition was investigated both in vitro and in vivo in rat brains by using the radioligand, 18F-fluoroclorgyline (N-[3-(2',4'-dichlorophenoxy)-2-18F-fluoropropyl]-N-methylpropa rgylamine). In vitro binding affinities of six compounds, clorgyline, Ro 41-1049, deprenyl, fluoxetine, norfluoxetine and citalopram, were studied. Fluoxetine and norfluoxetine showed in vitro affinities of 36.5 and 68 microM for MAO-A, respectively. Fluoxetine and norfluoxetine also significantly inhibited (more than 20%) the binding of the radioligand in vivo while citalopram and deprenyl showed very poor affinities in vitro for MAO-A and had no effect in vivo. The in vivo effects of the various drugs were directly comparable to their in vitro affinities for binding to MAO-A as seen in the correlation plot of percent control in vivo binding of 18F-fluoroclorgyline and binding affinity, -log IC50 (R2 = 0.979). An acute dose of 20 mg/kg of fluoxetine inhibited binding of 18F-fluoroclorgyline by more than 20%, while lower doses had some significant effects. These results provide evidence on the in vitro and in vivo inhibition of monoamine oxidase A by fluoxetine.
MAO-B inhibition
Fluoxetine weekly
Fluoxetine and MAO-B
Fluoxetine and GABA(A)
Fluoxetine v moclobemide
Antidepressant mechanisms
Comparisons and metabolites
Antidepressants and cell growth
Fluoxetine and corticosteroid receptors

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