Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adenosine Diphosphate / pharmacology
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Amides
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Amidohydrolases / blood
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Amidohydrolases / genetics
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Amino Acid Sequence
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Arachidonic Acid / blood
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Arachidonic Acid / pharmacology
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Arachidonic Acids / blood
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Arachidonic Acids / pharmacology*
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Blood Platelets / drug effects
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Blood Platelets / metabolism
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Calcium / blood
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Cannabinoids / blood
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Cannabinoids / pharmacology*
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Endocannabinoids
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Ethanolamines
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Humans
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In Vitro Techniques
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Molecular Sequence Data
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Palmitic Acids / pharmacology
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Platelet Activation / drug effects*
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Platelet Activation / physiology
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Polyunsaturated Alkamides
Substances
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Amides
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Arachidonic Acids
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Cannabinoids
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Endocannabinoids
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Ethanolamines
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Palmitic Acids
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Polyunsaturated Alkamides
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Arachidonic Acid
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Adenosine Diphosphate
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palmidrol
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Amidohydrolases
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fatty-acid amide hydrolase
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Calcium
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anandamide