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The MAP kinase signal transduction pathway is activated by the endogenous cannabinoid anandamide
Author(s) -
Wartmann Markus,
Campbell Debra,
Subramanian Asha,
Burstein Sumner H.,
Davis Roger J.
Publication year - 1995
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(95)00027-7
Subject(s) - anandamide , endocannabinoid system , signal transduction , endogeny , microbiology and biotechnology , chemistry , mitogen activated protein kinase , cannabinoid , cannabinoid receptor , biology , biochemistry , receptor , agonist
Anandamide is an endogenous ligand for δ 9 ‐tetrahy‐drocannabinol (THC) receptors. Incubation of cultured cells with anandamide or THC causes increased arachidonic acid release and eicosanoid biosynthesis. Here we demonstrate that the MAP kinase signal transduction pathway contributes to this response. Treatment of WI‐38 fibroblasts with anandamide causes increased MAP kinase activity and increased phosphorylation of the arachidonate‐specific cytoplasmic phospholipase A 2 (cPLA 2 ). Significantly, MAP kinase phosphorylates and activates cPLA 2 [Lin, et al., Cell , 72 (1993) 269–278]. The MAP kinase signal transduction pathway may therefore mediate the effects of anadamide on cPLA 2 activation and arachidonic acid release.