Latency is the major determinant of UDP-glucuronosyltransferase activity in isolated hepatocytes.
FEBS Lett
; 328(1-2): 149-52, 1993 Aug 09.
Article
en En
| MEDLINE
| ID: mdl-8393805
The glucuronidation of p-nitrophenol was measured in intact, saponin- and alamethicin-treated isolated mouse hepatocytes. In saponin-permeabilized cells the elevation of extrareticular UDP-glucuronic acid concentration enhanced the rate of glucuronidation threefold. When intracellular membranes were also permeabilized by alamethicin, a further tenfold increase in the glucuronidation of p-nitrophenol was present. Parallel measurements of the ER mannose 6-phosphatase activity revealed that saponin selectively permeabilized the plasma membrane, whereas alamethicin permeabilized both plasma membrane and ER membranes. The inhibition of p-nitrophenol glucuronidation by dbcAMP in intact hepatocytes was still present in saponin-treated cells and disappeared in alamethicin-permeabilized hepatocytes. It is suggested that the permeability of the endoplasmic reticulum membrane is a major determinant of glucuronidation not only in microsomes but in isolated hepatocytes as well.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Glucuronosiltransferasa
/
Hígado
Límite:
Animals
Idioma:
En
Revista:
FEBS Lett
Año:
1993
Tipo del documento:
Article
País de afiliación:
Hungria
Pais de publicación:
Reino Unido