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Updated: Aug 27, 2025
Preparation and In Vivo Use of an Activity-based Probe for N-acylethanolamine Acid Amidase
Published on: November 23, 2016
Radiometric Assay of FAAH Activity.
Monica Bari1, Monica Feole2, Marina Fava3
1Department of Experimental Medicine, Tor Vergata University of Rome, Rome, Italy. bari@med.uniroma2.it.
Fatty acid amide hydrolase (FAAH) enzyme activity is measured by tracking the breakdown of anandamide (AEA). This method quantifies the radioactive ethanolamine product to assess FAAH function.
Area of Science:
- Biochemistry
- Enzymology
- Neuroscience
Background:
- Fatty acid amide hydrolase (FAAH) is a key intracellular enzyme.
- FAAH hydrolyzes endogenous anandamide (AEA), a lipid mediator.
- AEA hydrolysis terminates its biological effects, producing arachidonic acid and ethanolamine.
Purpose of the Study:
- To describe a method for measuring FAAH activity.
- To quantify the enzymatic activity of FAAH.
Main Methods:
- Utilizes a radioactive substrate: [14C-ethanolamine]-AEA.
- Measures FAAH activity by quantifying the radioactive product, [14C]-ethanolamine.
Main Results:
- The described method allows for the measurement of FAAH activity.
- Quantification of [14C]-ethanolamine indicates the extent of AEA hydrolysis.
Conclusions:
- This method provides a means to assess FAAH enzymatic function.
- The study details a specific assay for FAAH activity using radiolabeled AEA.
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