Assistant Professor, Department of Pharmacology, Gouri Devi institute of Medical Sciences and Hospital, Rajbandh, West Bengal, India
Both a- and b-amyrin did not bind to the hCB receptor ,During homogenization of pig brain homogenates ,Arachidonic acid 2-AG hydroxylation was inhibited potently by b-amyrin, but not anandamide hydrolysis. Nevertheless. ,

A therapeutic strategy for treating chronic and inflammatory pain is to activate cannabinoid CB1 and CB2 receptors pharmacologically. Natural polyterpenes a- and b-amyrin bind specifically to CB1 receptors at 133 pM with a subnanomolecular Ki value. Both CB1 and CB2 receptors were inhibited by oral administration of a/b-amyrin in mice. Endocannabinoid system components were examined for their effects on amyrins. CHO-K1 cells co-transfected with hCB1 and hCB2 bind A- and b-amyrin to CB receptors. A study was conducted in U937 cells with BV2 cells, pig brain homogenates, and purified enzymes, in order to investigate the effect of these components on endocannabinoid transport. BV2 cells and pig brain homogenates did not contain b-amyrin or a-amyrin, which inhibited 1,2, and 3-AG breakdown as well as MAGL, a,b-hydrolases, and 2-AG breakdown. A cannabimimetic mechanism inhibiting 2-AG degradation mediates bamyrin's pharmacological effects rather than directly binding to CB receptors. Despite their potential, triterpenoids are largely unexplored because they inhibit enzymes involved in degrading 2-AG

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