Assay of NAT Activity.

Acyltransferases / metabolism Animals Phosphatidylcholines Phosphatidylethanolamines / metabolism Phospholipases A / metabolism Phospholipids Rats
COS-7 cell Ca-NAT N-Acylphosphatidylethanolamine N-Acyltransferase NAPE PLAAT family Radioisotope Rat brain Thin-layer chromatography cPLA2ε

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
Historique:
entrez: 24 9 2022
pubmed: 25 9 2022
medline: 28 9 2022
Statut: ppublish

Résumé

In animal tissues, N-acyltransferase (NAT) catalyzes the first reaction in the biosynthetic pathway of bioactive N-acylethanolamines, in which an acyl chain is transferred from the sn-1 position of the donor phospholipid, such as phosphatidylcholine, to the amino group of phosphatidylethanolamine, resulting in the formation of N-acylphosphatidylethanolamine. NAT has long been known to be stimulated by Ca

Identifiants

DOI: 10.1007/978-1-0716-2728-0_17 PMID: 36152189
pubmed: 36152189
doi: 10.1007/978-1-0716-2728-0_17
doi:

Substances chimiques

Phosphatidylcholines 0
Phosphatidylethanolamines 0
Phospholipids 0
Acyltransferases EC 2.3.-
Phospholipases A EC 3.1.1.32

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

213-224

Informations de copyright

© 2023. The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature.

Références

Ueda N, Tsuboi K, Uyama T (2013) Metabolism of endocannabinoids and related N-acylethanolamines: canonical and alternative pathways. FEBS J 280:1874–1894
doi: 10.1111/febs.12152
Hussain Z, Uyama T, Tsuboi K, Ueda N (2017) Mammalian enzymes responsible for the biosynthesis of N-acylethanolamines. Biochim Biophys Acta 1862:1546–1561
doi: 10.1016/j.bbalip.2017.08.006
Di Marzo V, Fontana A, Cadas H, Schinelli S, Cimino G, Schwartz J-C, Piomelli D (1994) Formation and inactivation of endogenous cannabinoid anandamide in central neurons. Nature 372:686–691
doi: 10.1038/372686a0
Cadas H, di Tomaso E, Piomelli D (1997) Occurrence and biosynthesis of endogenous cannabinoid precursor, N-arachidonoyl phosphatidylethanolamine, in rat brain. J Neurosci 17:1226–1242
doi: 10.1523/JNEUROSCI.17-04-01226.1997
Hansen HS, Moesgaard B, Hansen HH, Petersen G (2000) N-Acylethanolamines and precursor phospholipids – relation to cell injury. Chem Phys Lipids 108:135–150
doi: 10.1016/S0009-3084(00)00192-4
Ogura Y, Parsons WH, Kamat SS, Cravatt BF (2016) A calcium-dependent acyltransferase that produces N-acyl phosphatidylethanolamines. Nat Chem Biol 12:669–671
doi: 10.1038/nchembio.2127
Jin X–H, Okamoto Y, Morishita J, Tsuboi K, Tonai T, Ueda N (2007) Discovery and characterization of a Ca
Uyama T, Tsuboi K, Ueda N (2017) An involvement of phospholipase A/acyltransferase family proteins in peroxisome regulation and plasmalogen metabolism. FEBS Lett 591:2745–2760
doi: 10.1002/1873-3468.12787
Shinohara N, Uyama T, Jin X-H, Tsuboi K, Tonai T, Houchi H, Ueda N (2011) Enzymological analysis of the tumor suppressor A-C1 reveals a novel group of phospholipid-metabolizing enzymes. J Lipid Res 52:1927–1935
doi: 10.1194/jlr.M015081
Jin X-H, Uyama T, Wang J, Okamoto Y, Tonai T, Ueda N (2009) cDNA cloning and characterization of human and mouse Ca
doi: 10.1016/j.bbalip.2008.09.006
Uyama T, Morishita J, Okamoto Y, Tsuboi K, Tonai T, Ueda N (2009) The tumor suppressor gene H-Rev107 functions as a novel Ca
doi: 10.1194/jlr.M800453-JLR200
Uyama T, Jin X–H, Tsuboi K, Tonai T, Ueda N (2009) Characterization of the human tumor suppressors TIG3 and HRASLS2 as phospholipid-metabolizing enzymes. Biochim Biophys Acta 1791:1114–1124
Hussain Z, Uyama T, Kawai K, Binte Mustafiz SS, Tsuboi K, Araki N, Ueda N (2018) Phosphatidylserine-stimulated production of N-acyl-phosphatidylethanolamines by Ca
doi: 10.1016/j.bbalip.2018.02.002
Uyama T, Ikematsu N, Inoue M, Shinohara N, Jin X–H, Tsuboi K, Tonai T, Tokumura A, Ueda N (2012) Generation of N-acylphosphatidylethanolamine by members of the phospholipase A/acyltransferase (PLA/AT) family. J Biol Chem 287:31905–31919
Binte Mustafiz SS, Uyama T, Morito K, Takahashi N, Kawai K, Hussain Z, Tsuboi K, Araki N, Yamamoto K, Tanaka T, Ueda N (2019) Intracellular Ca
doi: 10.1016/j.bbalip.2019.158515
Golczak M, Kiser PD, Sears AE, Lodowski DT, Blaner WS, Palczewski K (2012) Structural basis for the acyltransferase activity of lecithin:retinol acyltransferase-like proteins. J Biol Chem 287:23790–23807
doi: 10.1074/jbc.M112.361550
Natarajan V, Schmid PC, Schmid HHO (1986) N-Acylethanolamine phospholipid metabolism in normal and ischemic rat brain. Biochim Biophys Acta 878:32–41
doi: 10.1016/0005-2760(86)90341-3
Schmid PC, Reddy PV, Natarajan V, Schmid HHO (1983) Metabolism of N-acylethanolamine phospholipids by a mammalian phosphodiesterase of the phospholipase D type. J Biol Chem 258:9302–9306
doi: 10.1016/S0021-9258(17)44667-9

Auteurs

Toru Uyama (T)

Department of Biochemistry, Kagawa University School of Medicine, Miki, Kagawa, Japan.

Natsuo Ueda (N)

Department of Biochemistry, Kagawa University School of Medicine, Miki, Kagawa, Japan. ueda.natsuo@kagawa-u.ac.jp.

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Classifications MeSH

questionsmedicales.fr › Enzymes et coenzymes › Enzymes › Transferases › Acyltransferases › Assay of NAT Activity.
questionsmedicales.fr › Eucaryotes › Animaux › Assay of NAT Activity.
questionsmedicales.fr › Lipides › Lipides membranaires › Phospholipides › Glycérophosphate › Acides phosphatidiques › Glycérophospholipides › Phosphatidylcholines › Assay of NAT Activity.
questionsmedicales.fr › Lipides › Lipides membranaires › Phospholipides › Glycérophosphate › Acides phosphatidiques › Glycérophospholipides › Phosphatidyléthanolamine › Assay of NAT Activity.
questionsmedicales.fr › Enzymes et coenzymes › Enzymes › Hydrolases › Esterases › Carboxylic ester hydrolases › Phospholipases A › Assay of NAT Activity.
questionsmedicales.fr › Lipides › Lipides membranaires › Phospholipides › Assay of NAT Activity.
questionsmedicales.fr › Eucaryotes › Animaux › Chordés › Vertébrés › Mammifères › Eutheria › Rodentia › Muridae › Murinae › Rats › Assay of NAT Activity.