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Activation of phospholipase A 2 by cannabinoids
Author(s) -
Evans A.T.,
Formukong E.,
Evans F.J.
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)81420-5
Subject(s) - cannabinol , cannabidiol , chemistry , phospholipase , cannabinoid , tetrahydrocannabinol , phospholipase d , pharmacology , cannabinoid receptor , stimulation , prostaglandin , phospholipase a2 , enzyme , biochemistry , receptor , cannabis , biology , endocrinology , medicine , agonist , psychiatry
Cannabinoids Δ 1 ‐tetrahydrocannabinol, cannabinol, cannabidiol and cannabigerol have been shown to affect directly the activity of phospholipase A 2 in a cell‐free assay. The compounds produced a biphasic activation of the enzyme, with EC 50 values in the range 6.0–20.0 × 10 −6 M and IC 50 values in the range 50.0–150.0 × 10 −6 M. These results correlated well with the relative potencies reported for the stimulation of prostaglandin release from human synovial cells in vitro, confirming that activation of phospholipase A 2 is the predominant action of cannabinoids on arachidonate metabolism in tissue culture. However, since Δ 1 ‐tetrahydrocannabinol is unique among these compounds in possessing cataleptic activity, it is unlikely that phospholipase A 2 is the major receptor mediating the psychotropic effects of cannabis.