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Numerous analogs of fatty acyl ethanolamides potentiate the intrinsic biological activity of endocannabinoids.1 This potentiation is ascribed either to inhibition of AEA reuptake into neurons, or inhibition of fatty acid amide hydrolase (FAAH) within the neurons. 2 However, Ueda, et al. has recently cloned another amidase, the acidic PEAase that promotes the hydrolysis of palmitoylethanolamide.3 N-Cyclohexanecarbonyltetradecylamine is an analog of N-cyclohexanecarbonyl-pentadecylamine, a selective inhibitor of acidic PEAase with an IC50 value of 4.5 μM, that contains 1 less carbon in the alkyl chain.4 The biological activity of N-cyclohexanecarbonyltetradecylamine has not been documented. | [References]
1. Khanolkar, A.D., and Makriyannis, A. Structure-activity relationships of anandamide, an endogenous cannabinoid ligand Life Sci. 65,607-616(1999).
2. Deutsch, D.G., Glaser, S.T., Howell, J.M., et al. The cellular uptake of anandamide is coupled to its breakdown by fatty-acid amide hydrolase J. Biol. Chem. 276(10),6967-6973(2001).
3. Ueda, N., Yamanaka, K., and Yamamoto, S. Purification and characterization of an acid amidase selective for N-palmitoylethanolamine, a putative endogenous anti-inflammatory substance J. Biol. Chem. 276(38),35552-35557(2001).
4. Tsuboi, K., Hilligsmann, C., Vandevoorde, S., et al. N-cyclohexanecarbonylpentadecylamine: A selective inhibitor of the acid amidase hydrolysing N-acylethanolamines, as a tool to distinguish acid amidase from fatty acid amide hydrolase Biochem. J. 379,99-106(2004). |
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