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Titolo:
Pharmacological properties of rat brain fatty acid amidohydrolase in different subcellular fractions using palmitoylethanolamide as substrate
Autore:
Tiger, G; Stenstrom, A; Fowler, CJ;
Indirizzi:
Umea Univ, Dept Pharmacol & Clin Neurosci, SE-90187 Umea, Sweden Umea Univ Umea Sweden SE-90187 ol & Clin Neurosci, SE-90187 Umea, Sweden
Titolo Testata:
BIOCHEMICAL PHARMACOLOGY
fascicolo: 6, volume: 59, anno: 2000,
pagine: 647 - 653
SICI:
0006-2952(20000315)59:6<647:PPORBF>2.0.ZU;2-5
Fonte:
ISI
Lingua:
ENG
Soggetto:
ANANDAMIDE AMIDOHYDROLASE; ENZYME; DEGRADATION; HYDROLYSIS; AMIDASE; AMIDES;
Keywords:
palmitoylethanolamide; anandamide; fatty acid amide hydrolase; ibuprofen; rat brain; subcellular fractions;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
24
Recensione:
Indirizzi per estratti:
Indirizzo: Tiger, G Umea Univ, Dept Pharmacol & Clin Neurosci, SE-90187 Umea, Sweden Umea Univ Umea Sweden SE-90187 Neurosci, SE-90187 Umea, Sweden
Citazione:
G. Tiger et al., "Pharmacological properties of rat brain fatty acid amidohydrolase in different subcellular fractions using palmitoylethanolamide as substrate", BIOCH PHARM, 59(6), 2000, pp. 647-653

Abstract

In the present study, the pharmacological properties of fatty acid amide hydrolase (FAAH) in subcellular fractions of rat brain were investigated using palmitoylethanolamide (PEA) and arachidonyl ethanolamide (anandamide, AEA) as substrates. FAAH hydrolysed [H-3]PEA in crude homogenates with medianK-m and V-max values of 2.9 mu M and 2.14 nmol.(mg protein)(-1).min(-1), respectively. [H-3]PEA hydrolysis was inhibited both by non-radioactive AEA (with a K-i Value very similar to the K-m Value for [H-3]AEA as substrate using the same assay) and by R(-)ibuprofen (mixed-type inhibition K-i and K-i' values 88 and 720 mu M, respectively). FAAH activity towards both [H-3]PEA and [H-3]AEA was in the order microsomal > synaptosomal = mitochondrial > crude nuclear > myelin = cytosol, but there were no differences between the relative activities towards the two substrates in any of the fractions. [H-3]PEA hydrolysis in mitochondrial, myelin, microsomal, and synaptosomal fractions was inhibited by oleyl trifluoromethylketone, phenylmethylsulphonyl fluoride, and the R(-)- and S(+)-enantiomers of the nonsteroidal anti-inflammatory drug ibuprofen, with mean IC50 Values in the ranges 0.028-0.041,0.31-0.52, 67-110, and 130-260 mu M, respectively. It is concluded that the pharmacological properties of FAAH in the different subcellular fractionsare very similar. (C) 2000 Elsevier Science Inc.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/04/20 alle ore 19:31:55