ArticleJournal of proteome research2012
Mass spectrometric characterization of human N-acylethanolamine-hydrolyzing acid amidase.
Article in Journal of proteome research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
15 citing papers in PubMed, 36 citations in OpenAlex.
- Pharmacological Inhibition of N-Acylethanolamine Acid Amidase (NAAA) Mitigates Intestinal Fibrosis Through Modulation of Macrophage Activity.Journal of Crohn's & colitis · 2025Article
- Benzoxazole-derivatives enhance progranulin expression and reverse the aberrant lysosomal proteome caused by GRN haploinsufficiency.Nature communications · 2024Article
- Fluorescence-Based Enzyme Activity Assay: Ascertaining the Activity and Inhibition of Endocannabinoid Hydrolytic Enzymes.International journal of molecular sciences · 2024Review
- Discovery and SAR Evolution of Pyrazole Azabicyclo[3.2.1]octane Sulfonamides as a Novel Class of Non-CovalentJournal of medicinal chemistry · 2021Article
- The rise and fall of anandamide: processes that control synthesis, degradation, and storage.Molecular and cellular biochemistry · 2021Review
- Natural Potent NAAA Inhibitor Atractylodin Counteracts LPS-Induced Microglial Activation.Frontiers in pharmacology · 2020Article
- Molecular mechanism of activation of the immunoregulatory amidase NAAA.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Secretion, isotopic labeling and deglycosylation of N-acylethanolamine acid amidase for biophysical studies.Protein expression and purification · 2018Article
- Preparation and In Vivo Use of an Activity-based Probe for N-acylethanolamine Acid Amidase.Journal of visualized experiments : JoVE · 2016Article
- Activity-Based Probe for N-Acylethanolamine Acid Amidase.ACS chemical biology · 2015Article
- 3-Aminoazetidin-2-one derivatives as N-acylethanolamine acid amidase (NAAA) inhibitors suitable for systemic administration.ChemMedChem · 2014Article
- 2012 Division of medicinal chemistry award address. Trekking the cannabinoid road: a personal perspective.Journal of medicinal chemistry · 2014Article
- Endogenous molecules stimulating N-acylethanolamine-hydrolyzing acid amidase (NAAA).ACS chemical neuroscience · 2012Article
- β-Lactones Inhibit N-acylethanolamine Acid Amidase by S-Acylation of the Catalytic N-Terminal Cysteine.ACS medicinal chemistry letters · 2012Article
- Biochemical and mass spectrometric characterization of human N-acylethanolamine-hydrolyzing acid amidase inhibition.PloS one · 2012Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
N-Acylethanolamine-hydrolyzing acid amidase (NAAA) is a lysosomal enzyme that primarily degrades palmitoylethanolamine (PEA), a lipid amide that inhibits inflammatory responses. We developed a HEK293 cell line stably expressing the NAAA pro-enzyme (zymogen) and a single step chromatographic purification of the protein from the media. Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry MALDI-TOF MS analysis of the zymogen (47.7 kDa) treated with peptide-N-glycosidase F (PNGase F) identified 4 glycosylation sites, and acid cleavage of the zymogen into α- and β-subunits (14.6 and 33.3 kDa) activated the enzyme. Size exclusion chromatography estimated the mass of the active enzyme as 45 ± 3 kDa, suggesting formation of an α/β heterodimer. MALDI-TOF MS fingerprinting covered more than 80% of the amino acid sequence, including the N-terminal peptides, and evidence for the lack of a disulfide bond between subunits. The significance of the cysteine residues was established by their selective alkylation resulting in almost complete loss of activity. The purified enzyme was kinetically characterized with PEA and a novel fluorogenic substrate, N-(4-methyl coumarin) palmitamide (PAMCA). The production of sufficient quantities of NAAA and a high throughput assay could be useful in discovering novel inhibitors and determining the structure and function of this enzyme.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.