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Do Nardil/Marplan affect Lamictal levels?

Posted by PeterMartin on March 19, 2022, at 0:01:16

Can someone w/ a bit of knowledge about drug metabolism take a look at this study which mentions the method Phenelzine (Nardil) is broken down, and then make an educated guess as to whether or not it would potentially raise (or lower) blood levels of Lamictal?

I've never seen Marplan/Nardil listed as having an interaction w/ Lamictal due to the way it was broken down. If changing the dose of those changes the levels of Lamictal than that could mean a lot for mood issues I've had at times. (thinking I'm adjusting one, but in fact two changes are being made).

Thanks for any insight:

An evaluation of potential mechanism-based inactivation of human drug metabolizing cytochromes P450 by monoamine oxidase inhibitors, including isoniazid
Thomas M Polasek 1, David J Elliot, Andrew A Somogyi, Elizabeth M J Gillam, Benjamin C Lewis, John O Miners
Affiliations expand
PMID: 16669850 PMCID: PMC1885050 DOI: 10.1111/j.1365-2125.2006.02627.x
Free PMC article
Aims: To characterize potential mechanism-based inactivation (MBI) of major human drug-metabolizing cytochromes P450 (CYP) by monoamine oxidase (MAO) inhibitors, including the antitubercular drug isoniazid.

Methods: Human liver microsomal CYP1A2, CYP2C9, CYP2C19, CYP2D6 and CYP3A activities were investigated following co- and preincubation with MAO inhibitors. Inactivation kinetic constants (KI and kinact) were determined where a significant preincubation effect was observed. Spectral studies were conducted to elucidate the mechanisms of inactivation.

Results: Hydrazine MAO inhibitors generally exhibited greater inhibition of CYP following preincubation, whereas this was less frequent for the propargylamines, and tranylcypromine and moclobemide. Phenelzine and isoniazid inactivated all CYP but were most potent toward CYP3A and CYP2C19. Respective inactivation kinetic constants (KI and kinact) for isoniazid were 48.6 microm and 0.042 min-1 and 79.3 microm and 0.039 min-1. Clorgyline was a selective inactivator of CYP1A2 (6.8 microm and 0.15 min-1). Inactivation of CYP was irreversible, consistent with metabolite-intermediate complexation for isoniazid and clorgyline, and haeme destruction for phenelzine. With the exception of phenelzine-mediated CYP3A inactivation, glutathione and superoxide dismutase failed to protect CYP from inactivation by isoniazid and phenelzine. Glutathione partially slowed (17%) the inactivation of CYP1A2 by clorgyline. Alternate substrates or inhibitors generally protected against CYP inactivation.

Conclusions: These data are consistent with mechanism-based inactivation of human drug-metabolizing CYP enzymes and suggest that impaired metabolic clearance may contribute to clinical drug-drug interactions with some MAO inhibitors.




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