http://www.cnr.it/ontology/cnr/individuo/prodotto/ID8679
Use of an inhibitor to identify members of the hormone-sensitive lipase family (Articolo in rivista)
- Type
- Label
- Use of an inhibitor to identify members of the hormone-sensitive lipase family (Articolo in rivista) (literal)
- Anno
- 2006-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1021/bi0613978 (literal)
- Alternative label
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Ben Ali Y.; Chahinian H.; Petry S.; Muller G.; Lebrun R.; Verger R.; Carrière F.; Mandrich L.; Rossi M.; Manco G.; Sarda L.; Abousalham A. (literal)
- Pagina inizio
- Pagina fine
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
- Rivista
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
- Note
- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- Enzymology at interfaces and physiology of lipolysis, UPR 9025-CNRS, 31, Chemin Joseph Aiguier, 13402 Marseille Cedex 20,
France, Sanofi-AVentis Germany, 65926 Frankfurt am Main, Germany, Istituto di Biochimica delle Proteine, CNR, Via P.
Castellino 111, 80131 Napoli, Italy, and Laboratoire de Biochimie, UniVersite´ de ProVence, Centre St-Charles, 3 Place V.
Hugo, 13331 Marseille Cedex 3, France (literal)
- Titolo
- Use of an inhibitor to identify members of the hormone-sensitive lipase family (literal)
- Abstract
- Hormone-sensitive lipase (HSL) contributes importantly to the mobilization of fatty acids from the triacylglycerols stored in adipocytes, which provide the main source of energy in mammals. On the basis of amino acid sequence alignments and three-dimensional structures, this enzyme was previously found to be a suitable template for defining a family of serine carboxylester hydrolases. In this study, the HSL family members are characterized rather on the basis of their inhibition by 5-methoxy-3-(4- phenoxyphenyl)-3H-[1,3,4]oxadiazol-2-one (compound 7600). This compound inhibits mammalian HSL as well as other HSL family members, such as EST2 from the thermophilic eubacterium Alicyclobacillus acidocaldarius and AFEST from the hyperthermophilic archaeon Archaeoglobus fulgidus. Various carboxylester hydrolases that are not members of the HSL family were found not to be inhibited by compound 7600 under the same experimental conditions. These include nonlipolytic hydrolases such as Torpedo californica acetylcholinesterase and pig liver esterase, as well as lipolytic hydrolases such as human pancreatic lipase, dog gastric lipase, Thermomyces lanuginosus lipase, and Bacillus subtilis LipA. When vinyl esters were used as substrates, the residual activity of HSL, AFEST, and EST2 decreased with an increase in compound 7600 concentration in the incubation mixture. The inhibitor concentration at which the enzyme activity decreased to 50% after incubation for 5 min was 70, 20, and 15 nM with HSL, AFEST, and EST2, respectively. Treating EST2 and AFEST with the inhibitor resulted in an increase in the molecular mass, as established by performing matrix-assisted laser desorption ionization time-offlight mass spectrometry analysis. This increase in the molecular mass, which corresponds approximately to the molecular mass of the inhibitor, indicates that a covalent enzyme-inhibitor complex has been formed. Surface-enhanced laser desorption ionization time-of-flight mass spectrometry analysis of a trypsin digest of AFEST treated with the inhibitor or not treated showed the occurrence of an increase in the molecular masses of the GESAGG-containing peptide, which is compatible with the formation of a covalent complex with the inhibitor. (literal)
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