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Human mast cells take up and hydrolyze anandamide under the control of 5‐lipoxygenase and do not express cannabinoid receptors
Author(s) -
Maccarrone Mauro,
Fiorucci Laura,
Erba Fulvio,
Bari Monica,
Finazzi-Agrò Alessandro,
Ascoli Franca
Publication year - 2000
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(00)01223-0
Subject(s) - anandamide , palmitoylethanolamide , fatty acid amide hydrolase , cannabinoid receptor , endocannabinoid system , chemistry , cannabinoid , biochemistry , cyclooxygenase , receptor , enzyme , antagonist
Human mast cells (HMC‐1) take up anandamide (arachidonoyl‐ethanolamide, AEA) with a saturable process ( K m =200±20 nM, V max =25±3 pmol min −1 mg protein −1 ), enhanced two‐fold over control by nitric oxide‐donors. Internalized AEA was hydrolyzed by a fatty acid amide hydrolase (FAAH), whose activity became measurable only in the presence of 5‐lipoxygenase, but not cyclooxygenase, inhibitors. FAAH ( K m =5.0±0.5 μM, V max =160±15 pmol min −1 mg protein −1 ) was competitively inhibited by palmitoylethanolamide. HMC‐1 cells did not display a functional cannabinoid receptor on their surface and neither AEA nor palmitoylethanolamide affected tryptase release from these cells.