alexa Dual inhibition of alpha beta-hydrolase domain 6 and fatty acid amide hydrolase increases endocannabinoid levels in neurons.
Biochemistry

Biochemistry

Biochemistry & Physiology: Open Access

Author(s): Marrs WR, Horne EA, OrtegaGutierrez S, Cisneros JA, Xu C,

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Abstract Agonists at cannabinoid receptors, such as the phytocannabinoid Δ(9)-tetrahydrocannabinol, exert a remarkable array of therapeutic effects but are also associated with undesirable psychoactive side effects. Conversely, targeting enzymes that hydrolyze endocannabinoids (eCBs) allows for more precise fine-tuning of cannabinoid receptor signaling, thus providing therapeutic relief with reduced side effects. Here, we report the development and characterization of an inhibitor of eCB hydrolysis, UCM710, which augments both N-arachidonoylethanolamine and 2-arachidonoylglycerol levels in neurons. This compound displays a unique pharmacological profile in that it inhibits fatty acid amide hydrolase and α/β-hydrolase domain 6 but not monoacylglycerol lipase. Thus, UCM710 represents a novel tool to delineate the therapeutic potential of compounds that manipulate a subset of enzymes that control eCB signaling.
This article was published in J Biol Chem and referenced in Biochemistry & Physiology: Open Access

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