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Titolo:
Purification and characterization of an acid amidase selective for N-palmitoylethanolamine, a putative endogenous anti-inflammatory substance
Autore:
Ueda, N; Yamanaka, K; Yamamoto, S;
Indirizzi:
Kagawa Med Univ, Dept Biochem, Miki, Kagawa 7610793, Japan Kagawa Med Univ Miki Kagawa Japan 7610793 em, Miki, Kagawa 7610793, Japan Univ Tokushima, Sch Med, Dept Biochem, Tokushima 7708503, Japan Univ Tokushima Tokushima Japan 7708503 Biochem, Tokushima 7708503, Japan Kyoto Womens Univ, Fac Home Econ, Dept Food & Nutr, Higashiyama Ku, Kyoto 6058501, Japan Kyoto Womens Univ Kyoto Japan 6058501 gashiyama Ku, Kyoto 6058501, Japan
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 38, volume: 276, anno: 2001,
pagine: 35552 - 35557
SICI:
0021-9258(20010921)276:38<35552:PACOAA>2.0.ZU;2-Z
Fonte:
ISI
Lingua:
ENG
Soggetto:
CANNABINOID-RECEPTOR-LIGAND; RAT-BRAIN MICROSOMES; ANANDAMIDE AMIDOHYDROLASE; ENZYMATIC-SYNTHESIS; ACYLETHANOLAMINES; ACYLPHOSPHATIDYLETHANOLAMINE; PHOSPHODIESTERASE; IDENTIFICATION; BIOSYNTHESIS; DEGRADATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
50
Recensione:
Indirizzi per estratti:
Indirizzo: Yamamoto, S Kagawa Med Univ, Dept Biochem, 1750-1 Ikenobe, Miki, Kagawa 7610793, Japan Kagawa Med Univ 1750-1 Ikenobe Miki Kagawa Japan 7610793 Japan
Citazione:
N. Ueda et al., "Purification and characterization of an acid amidase selective for N-palmitoylethanolamine, a putative endogenous anti-inflammatory substance", J BIOL CHEM, 276(38), 2001, pp. 35552-35557

Abstract

N-Arachidonoylethanolamine (anandamide) is canna-bimimetic, and N-palmitoylethanolamine is anti-inflammatory and immunosuppressive. We found an amidase that is more active with the latter than the former in contrast to the previously known anandamide amidohydrolase for which N-palmitoylethanolamineis a poor substrate. Proteins solubilized by freezing and thawing from the12,000 x g pellet of various rat organs hydrolyzed [C-14]N-palmitoylethanolamine to palmitic acid and ethanolamine. The specific enzyme activity was higher in the order of lung > spleen > small intestine > thymus > cecum, and high activity was found in peritoneal and alveolar macrophages. The enzyme with a molecular mass of 31 kDa was purified from rat lung to a specific activity of 1.8 mu mol/min/mg protein. Relative reactivities of the enzyme with various N-acylethanolamines (100 muM) were as follows: N-palmitoylethanolamine, 100%; N-myristoylethanolamine, 48%; N-stearoylethanolamine, 21%; N-oleoylethanolamine, 20%; N-linoleoylethanolamine, 13%; anandamide, 8%. The enzyme was the most active at pH 5 and was activated 7-fold by Triton X-100. The enzyme was almost insensitive to methyl arachidonyl fluorophosphonate, which inhibited anandamide amidohydrolase potently. Thus, the new enzyme referred to as N-palmitoylethanolamine hydrolase was clearly distinguishable from anandamide amidohydrolase.

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Documento generato il 22/01/20 alle ore 09:33:04