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 hydrolized by a fatty acid amide hydrolase (FAAK), whose activity became measurable only in the presence of 5-lipoxygenase, but not cyclooxygenase, inhibitors. FAAH (K-m = 5.0 +/- 0.5 mu M, 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. (C) 2000 Federation of European Biochemical Societies.

Human mast cells take up and hydrolyze anandamide under the control of 5-lipoxygenase and do not express cannabinoid receptors

Maccarrone M;
2000-01-01

Abstract

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 hydrolized by a fatty acid amide hydrolase (FAAK), whose activity became measurable only in the presence of 5-lipoxygenase, but not cyclooxygenase, inhibitors. FAAH (K-m = 5.0 +/- 0.5 mu M, 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. (C) 2000 Federation of European Biochemical Societies.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11697/156032
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