【 摘 要 】
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.
【 授权许可】
Unknown
【 预 览 】
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RO201912020309056ZK.pdf | 282KB | ![]() |