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Vol. 58, Issue 4, 814-820, October 2000
Department of Biochemistry and Molecular Biology I, School of
Biology, Complutense University, Madrid, Spain
Cannabinoids exert most of their effects through the
CB1 receptor. This G-protein-coupled receptor has been
shown to be functionally coupled to inhibition of adenylyl cyclase,
modulation of ion channels, and activation of extracellular
signal-regulated kinase. Using Chinese hamster ovary cells
stably transfected with the CB1 receptor cDNA, we show here
that 
9-tetrahydrocannabinol (THC), the major active
component of marijuana, induces the activation of c-Jun N-terminal
kinase (JNK). Western blot analysis showed that both JNK-1 and JNK-2
were stimulated by THC. The effect of THC was also exerted by
endogenous cannabinoids (anandamide and 2-arachidonoylglycerol) and
synthetic cannabinoids (CP-55,940, HU-210, and methanandamide), and was
prevented by the selective CB1 antagonist SR141716.
Pertussis toxin, wortmannin, and a Ras farnesyltransferase inhibitor
peptide blocked, whereas mastoparan mimicked, the CB1
receptor-evoked activation of JNK, supporting the involvement of a
Gi/Go-protein, phosphoinositide 3'-kinase and
Ras. THC-induced JNK stimulation was prevented by tyrphostin AG1296,
pointing to the implication of platelet-derived growth factor receptor
transactivation, and was independent of ceramide generation.
Experiments performed with several types of neural cells that
endogenously express the CB1 receptor suggested that
long-term JNK activation may be involved in THC-induced cell death. The
CB1 cannabinoid receptor was also shown to be coupled to
the activation of p38 mitogen-activated protein kinase. Data indicate
that activation of JNK and p38 mitogen-activated protein kinase may be
responsible for some of the cellular responses elicited by the
CB1 cannabinoid receptor.
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