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

Mauro MacCarrone, Laura Fiorucci, Fulvio Erba, Monica Bari, Alessandro Finazzi-Agrò, Franca Ascoli

Research output: Contribution to journalArticlepeer-review

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 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. (C) 2000 Federation of European Biochemical Societies.

Original languageEnglish
Pages (from-to)176-180
Number of pages5
JournalFEBS Letters
Volume468
Issue number2-3
DOIs
Publication statusPublished - Feb 25 2000

Keywords

  • Anandamide
  • Endocannabinoid
  • Inflammation
  • Lipoxygenase
  • Nitric oxide
  • Tryptase

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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