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In vitro activation of brain protein kinase C by the cannabinoids

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, ISSN: 0167-4889, Vol: 1220, Issue: 2, Page: 163-170
1994
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Article Description

The cannabinoids have been shown to affect both membrane lipid ordering and the activities of several membrane-associated proteins. We have investigated the effects of the cannabinoids on protein kinase C, a lipid-dependent enzyme that functions as an important regulator of signal-transduction processes in the brain. The naturally occurring cannabinoid Δ 9 -tetrahydrocannabiol ( Δ 9 -THC) increased the activity of protein kinase C isolated from rat forebrain at concentrations of 10 μM and above. 11-OH- Δ 9 -THC, cannabinol and cannabidiol also increased protein kinase C activity in the same concentration range. Δ 9 -THC (10 μM) decreased the K act of protein kinase C for calcium from 28 μM to 18 μM and had no effect on the phosphatidylserine concentration-stimulation relationship. At a concentration of 30 μM, Δ 9 -THC increased the binding of [ 3 H]phorbol-12,13-dibutyrate ([ 3 H]PDBu) to protein kinase C and decreased the K d for [ 3 H]PDBu from 8.2 nM to 5.4 nM. Δ 9 -THC also had effects on lipid ordering of PS micelles, producing a significant increase in the fluorescence anisotropy of 1,6-diphenyl-1,3,5-hexatriene at a concentration of 10 μM. These data suggest that Δ 9 -THC activates protein kinase C via a novel mechanism, possibly as a result of effects on vesicle lipid physical characteristics.

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