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N-Acylethanolamine Acid Amidase (NAAA): Structure, Function, and Inhibition

Daniele Piomelli, Laura Scalvini, Yannick Fotio, Alessio Lodola, Gilberto Spadoni, Giorgio Tarzia, Marco Mor. J Med Chem. 2020;63(14):7475-7490.

ReviewHumansOther animals

Design
Review
Subjects
Not stated in the abstract
Dose used in the study
Not stated in the abstract
Duration
Not stated in the abstract
What was measured
How NAAA controls palmitoylethanolamide signalling at PPAR-alpha, its structure, and inhibition by covalent and non-covalent agents, and the potential of NAAA-targeting drugs

What the authors reported

NAAA is described as a lysosomal cysteine hydrolase in immune cells that deactivates PEA, with NAAA-regulated PEA signalling at PPAR-alpha presented as a control point for starting and resolving inflammation. The structural basis of inhibition is reviewed. No new data or numbers are given.

Limits of this study

A perspective review, not a trial. Funding and conflicts not stated in the abstract, though Daniele Piomelli holds NAAA inhibitor patent applications noted in related records.

Source

PubMed 32191459 · doi:10.1021/acs.jmedchem.0c00191

Entry checked against the abstract on PubMed on 2026-09-22. The dose shown is the dose the researchers used. It is not a recommendation. How to read this page.