Inhibition of anandamide amidase activity in mouse brain microsomes by cannabinoids

K Watanabe; Y Kayano; T Matsunaga; I Yamamoto; H Yoshimura

doi:10.1248/bpb.19.1109

Inhibition of anandamide amidase activity in mouse brain microsomes by cannabinoids

Biol Pharm Bull. 1996 Aug;19(8):1109-11. doi: 10.1248/bpb.19.1109.

Authors

K Watanabe¹, Y Kayano, T Matsunaga, I Yamamoto, H Yoshimura

Affiliation

¹ Department of Hygienic Chemistry, Faculty of Pharmaceutical Sciences, Hokuriku University, Kanazawa, Japan.

PMID: 8874830
DOI: 10.1248/bpb.19.1109

Abstract

Mouse brain microsomes contain an amidase that catalyzes the hydrolysis of N-arachidonylethanolamide to arachidonic acid and ethanolamine. The enzymatic activity is dependent on the protein concentration of the microsomes and observed over a wide range of pH, 7.4 to 9.5. Kinetic analysis indicated that K(m) (microM) and Vmax (nmol/min/mg protein) were 17.7 +/- 4.1 and 1.81 +/- 0.32, respectively. Cannabidiol (CBD), cannabinol (CBN) and delta 9-tetrahydrocannabinol (delta 9-THC) significantly inhibited the hydrolysis of the amide by mouse brain microsomes. At a concentration of 160 microM, the inhibitory potency decreased in the following order, CBD (66%) > CBN (46%) > delta 9-THC (31%).

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amidohydrolases / antagonists & inhibitors*
Animals
Brain / enzymology*
Cannabinoids / pharmacology*
Hydrogen-Ion Concentration
Male
Mice
Microsomes / enzymology*

Substances

Cannabinoids
Amidohydrolases
arachidonoylethanolamide synthase