English   español  
Por favor, use este identificador para citar o enlazar a este item: http://hdl.handle.net/10261/11328
Compartir / Impacto:
Estadísticas
Add this article to your Mendeley library MendeleyBASE
Citado 30 veces en Web of Knowledge®  |  Pub MebCentral Ver citas en PubMed Central  |  Ver citas en Google académico
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Exportar otros formatos: Exportar EndNote (RIS)Exportar bibText (RIS)Exportar csv (RIS)
Título

Cytochrome P4501A induction caused by the imidazole derivative Prochloraz in a rainbow trout cell line

AutorBabín, M.; Casado, Susana; Chana López, Antonio ; Herradón García, Bernardo ; Segner, Helmut; Tarazona, José V.; Navas, José M.
Palabras claveCytochrome P4501A
Prochloraz
Aryl hydrocarbon receptor
RTL-W1
Hepatocyte
Fecha de publicación10-ago-2005
EditorElsevier
CitaciónToxicology in Vitro 19(7): 899-902 (2005)
ResumenA variety of aquatic pollutants are able to induce cytochrome P4501A (CYP1A) in fish by ligand binding to the aryl hydrocarbon receptor (AhR). High-affinity AhR ligands are planar aromatic polycyclic molecules such as the prototypical ligand, 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD). The present work investigates the ability of the imidazole derivative, Prochloraz (PRO), to induce CYP1A. Computational studies on the molecular structure of PRO indicated that it is highly unlikely for PRO to have both aromatic rings of the molecule, i.e. the imidazole and the benzene ring, in the same plane. Thus, the possible conformers do not take planar structures, in contrast to the typically planar AhR ligands. Experimentally, the capability of PRO to induce CYP1A was assessed using the rainbow trout liver cell line, RTL-W1, as in vitro model. PRO increased in a concentration-dependent way the catalytic activity of CYP1A (determined as 7-ethoxyresorufin-O-deethylase, EROD, activity) in RTL-W1 cells. The potency of PRO was lower than that of a reference AhR-ligand, β-naphthoflavone (βNF). In addition to the catalytic level, PRO activated CYP1A also at the transcriptional level as determined by RT-PCR analysis of CYP1A mRNA. These results indicate that PRO, although its structure is not corresponding to the typical features of CYP1A-inducing AhR ligands, still is able to activate CYP1A expression.
Descripción4 pages, 2 figures.-- PMID: 16095870 [PubMed].-- Printed version published Oct 2005.-- Issue title: Thirteenth International Workshop on In Vitro Toxicology (Zegrze, Poland, Sep 4-11, 2004).
Versión del editorhttp://dx.doi.org/10.1016/j.tiv.2005.06.037
URIhttp://hdl.handle.net/10261/11328
DOI10.1016/j.tiv.2005.06.037
ISSN0887-2333
Aparece en las colecciones: (IQOG) Artículos
Ficheros en este ítem:
No hay ficheros asociados a este ítem.
Mostrar el registro completo
 



NOTA: Los ítems de Digital.CSIC están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.