Activation of a thioesterase specific for very-long-chain fatty acids by adrenergic agonists in perfused hearts.
Biochim Biophys Acta
; 1451(1): 101-8, 1999 Aug 12.
Article
em En
| MEDLINE
| ID: mdl-10446392
ABSTRACT
We have recently described an acyl-CoA thioesterase specific for very-long-chain fatty acids, named ARTISt, that regulates steroidogenesis through the release of arachidonic acid in adrenal zona fasciculata cells. In this paper we demonstrate the presence of the protein as a 43 kDa band and its mRNA in cardiac tissue. The activity of the protein was measured using an heterologous cell-free assay in which it is recombined with adrenal microsomes and mitochondria to activate mitochondrial steroidogenesis. Isoproterenol and phenylephrine activate the enzyme in a dose-dependent manner (10(-10)-10(-6) M). Both propranolol (10(-5) M) and prazosin (10(-5) M) block the action of isoproterenol and phenylephrine respectively. Antipeptide antibodies against the serine lipase motif of the protein and the Cys residue present in the catalytic domain also block the activity of the protein. Taken together, our results confirm the presence of ARTISt in heart and provide evidence for a catecholamine-activated regulatory pathway of the enzyme in that tissue.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Tioléster Hidrolases
/
Agonistas Adrenérgicos
/
Ácidos Graxos
/
Coração
Limite:
Animals
Idioma:
En
Revista:
Biochim Biophys Acta
Ano de publicação:
1999
Tipo de documento:
Article