Assay of NAAA Activity.
Anti-inflammatory agent
HEK293 cell
N-acylethanolamine acid amidase
NAAA
Palmitoylethanolamide
Radioisotope
Rat lung
Thin-layer chromatography
Journal
Methods in molecular biology (Clifton, N.J.)
ISSN: 1940-6029
Titre abrégé: Methods Mol Biol
Pays: United States
ID NLM: 9214969
Informations de publication
Date de publication:
2023
2023
Historique:
entrez:
24
9
2022
pubmed:
25
9
2022
medline:
28
9
2022
Statut:
ppublish
Résumé
N-acylethanolamine-hydrolyzing acid amidase (NAAA) is a lysosomal hydrolase degrading various N-acylethanolamines at acidic pH. NAAA prefers anti-inflammatory and analgesic palmitoylethanolamide to other N-acylethanolamines as a substrate, and its specific inhibitors are shown to exert anti-inflammatory and analgesic actions in animal models. Therefore, these inhibitors are expected as a new class of therapeutic agents. Here, we introduce an NAAA assay system, using [
Identifiants
pubmed: 36152194
doi: 10.1007/978-1-0716-2728-0_22
doi:
Substances chimiques
Amides
0
Analgesics
0
Anti-Inflammatory Agents
0
Enzyme Inhibitors
0
Ethanolamines
0
N-acylethanolamines
0
Palmitic Acids
0
palmidrol
6R8T1UDM3V
Amidohydrolases
EC 3.5.-
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
261-274Informations de copyright
© 2023. The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature.
Références
Tsuboi K, Uyama T, Okamoto Y, Ueda N (2018) Endocannabinoids and related N-acylethanolamines: biological activities and metabolism. Inflamm Regen 38:28
doi: 10.1186/s41232-018-0086-5
Tsuboi K, Sun Y-X, Okamoto Y, Araki N, Tonai T, Ueda N (2005) Molecular characterization of N-acylethanolamine-hydrolyzing acid amidase, a novel member of the choloylglycine hydrolase family with structural and functional similarity to acid ceramidase. J Biol Chem 280:11082–11092
doi: 10.1074/jbc.M413473200
Gorelik A, Gebai A, Illes K, Piomelli D, Nagar B (2018) Molecular mechanism of activation of the immunoregulatory amidase NAAA. Proc Natl Acad Sci U S A 115:E10032–E10040
doi: 10.1073/pnas.1811759115
Sun Y-X, Tsuboi K, Zhao L-Y, Okamoto Y, Lambert DM, Ueda N (2005) Involvement of N-acylethanolamine-hydrolyzing acid amidase in the degradation of anandamide and other N-acylethanolamines in macrophages. Biochim Biophys Acta 1736:211–220
doi: 10.1016/j.bbalip.2005.08.010
Tsuboi K, Zhao L-Y, Okamoto Y, Araki N, Ueno M, Sakamoto H, Ueda N (2007) Predominant expression of lysosomal N-acylethanolamine-hydrolyzing acid amidase in macrophages revealed by immunochemical studies. Biochim Biophys Acta 1771:623–632
doi: 10.1016/j.bbalip.2007.03.005
Piomelli D, Scalvini L, Fotio Y, Lodola A, Spadoni G, Tarzia G, Mor M (2020) N-Acylethanolamine acid amidase (NAAA): structure, function, and inhibition. J Med Chem 63:7475–7490
doi: 10.1021/acs.jmedchem.0c00191
Sasso O, Summa M, Armirotti A, Pontis S, De Mei C, Piomelli D (2018) The N-acylethanolamine acid amidase inhibitor ARN077 suppresses inflammation and pruritus in a mouse model of allergic dermatitis. J Invest Dermatol 138:562–569
doi: 10.1016/j.jid.2017.07.853
Pontis S, Palese F, Summa M, Realini N, Lanfranco M, De Mei C, Piomelli D (2020) N-Acylethanolamine acid amidase contributes to disease progression in a mouse model of multiple sclerosis. Pharmacol Res 160:105064
doi: 10.1016/j.phrs.2020.105064
Ueda N, Yamanaka K, Yamamoto S (2001) Purification and characterization of an acid amidase selective for N-palmitoylethanolamine, a putative endogenous anti-inflammatory substance. J Biol Chem 276:35552–35557
doi: 10.1074/jbc.M106261200
Petrosino S, Ahmad A, Marcolongo G, Esposito E, Allarà M, Verde R, Cuzzocrea S, Di Marzo V (2015) Diacerein is a potent and selective inhibitor of palmitoylethanolamide inactivation with analgesic activity in a rat model of acute inflammatory pain. Pharmacol Res 91:9–14
doi: 10.1016/j.phrs.2014.10.008
Solorzano C, Zhu C, Battista N, Astarita G, Lodola A, Rivara S, Mor M, Russo R, Maccarrone M, Antonietti F, Duranti A, Tontini A, Cuzzocrea S, Tarzia G, Piomelli D (2009) Selective N-acylethanolamine-hydrolyzing acid amidase inhibition reveals a key role for endogenous palmitoylethanolamide in inflammation. Proc Natl Acad Sci U S A 106:20966–20971
doi: 10.1073/pnas.0907417106
West JM, Zvonok N, Whitten KM, Wood JT, Makriyannis A (2012) Mass spectrometric characterization of human N-acylethanolamine-hydrolyzing acid amidase. J Proteome Res 11:972–981
doi: 10.1021/pr200735a