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Anandamide activates human platelets through a pathway independent of the arachidonate cascade
Author(s) -
Maccarrone Mauro,
Bari Monica,
Menichelli Adriana,
Del Principe Domenico,
Finazzi Agrò Alessandro
Publication year - 1999
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/s0014-5793(99)00308-7
Subject(s) - anandamide , fatty acid amide hydrolase , chemistry , palmitoylethanolamide , platelet , endocannabinoid system , biochemistry , platelet activation , eicosanoid , arachidonic acid , cannabinoid receptor , enzyme , receptor , agonist , biology , immunology
Anandamide (arachidonoylethanolamide, AnNH) is shown to activate human platelets, a process which was not inhibited by acetylsalicylic acid (aspirin). Unlike AnNH, hydroperoxides generated thereof by lipoxygenase activity, and the congener (13‐hydroxy)linoleoylethanolamide, were unable to activate platelets, though they counteracted AnNH‐mediated stimulation. On the other hand, palmitoylethanolamide neither activated human platelets nor blocked the AnNH effects. AnNH inactivation by human platelets was afforded by a high‐affinity transporter, which was activated by nitric oxide‐donors up to 225% of the control. The internalized AnNH could thus be hydrolyzed by a fatty acid amide hydrolase (FAAH), characterized here for the first time.