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The endogenous cannabinoid anandamide was identified as an agonist for the recombinant human VR1 (hVR1) by screening a large array of bioactive substances using a FLIPR-based calcium assay. Further electrophysiological studies showed that anandamide (10 or 100 microM) and capsaicin (1 microM) produced similar inward currents in hVR1 transfected, but not in parental, HEK293 cells. These currents were abolished by capsazepine (1 microM). In the FLIPR anandamide and capsaicin were full agonists at hVR1, with pEC(50) values of 5. 94+/-0.06 (n=5) and 7.13+/-0.11 (n=8) respectively. The response to anandamide was inhibited by capsazepine (pK(B) of 7.40+/-0.02, n=6), but not by the cannabinoid receptor antagonists AM630 or AM281. Furthermore, pretreatment with capsaicin desensitized the anandamide-induced calcium response and vice versa. In conclusion, this study has demonstrated for the first time that anandamide acts as a full agonist at the human VR1.

Original publication

DOI

10.1038/sj.bjp.0703050

Type

Journal article

Journal

Br J Pharmacol

Publication Date

01/2000

Volume

129

Pages

227 - 230

Keywords

Arachidonic Acids, Binding, Competitive, Calcium, Calcium Channels, Cannabinoids, Capsaicin, Cell Line, Cloning, Molecular, Electrophysiology, Endocannabinoids, Ethanolamines, Humans, Hydrogen-Ion Concentration, Palmitic Acids, Patch-Clamp Techniques, Polyunsaturated Alkamides, Receptors, Drug, Recombinant Proteins, TRPV Cation Channels