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Further arguments in favour of direct covalent binding of Ochratoxin A (OTA) after metabolic biotransformation.
Pfohl-Leszkowicz, A; Castegnaro, M.
Afiliación
  • Pfohl-Leszkowicz A; INP/ENSAT, UMR CNRS/INPT/UPS 5503, Department Bioprocess & Microbial Engineering, 1 Avenue Agrobiopole, Auzeville-Tolosane, France. leszkowicz@ensat.fr
Food Addit Contam ; 22 Suppl 1: 75-87, 2005.
Article en En | MEDLINE | ID: mdl-16332625
Ochratoxin A (OTA) is nephrotoxic to all animal species, carcinogenic for rats and mice and probably implicated in human Balkan endemic nephropathy and the associated urothelial tract tumour. Controversial results concerning genotoxicity and biotransformation of OTA have been generated. By (32)P post-labelling technique, a dose- and time-dependent DNA adduct formation is observed in vivo and in vitro. Use of several inducers or inhibitors of biotransforming enzymes (including cytochrome P 450, cyclooxygenase, lipoxygenase, glutathione-S-transferase), demonstrated that OTA is biotransformed into genotoxic derivatives damaging for DNA. Authentic C8dG-OTA standards have been synthesized by photo-oxidation. Both of them (C-C8 & O-C8) co-migrate on TLC with two adducts formed by in vitro incubation of OTA in the presence of kidney microsomes, and in vivo in kidney of pig or rodent fed OTA as well as in kidney and bladder tumour of humans exposed to OTA. Several OTA metabolites have been isolated from tissues or cells treated by OTA. The open ring lactone (OP-OTA) and quinone OTA (OTQ) are genotoxic.
Asunto(s)
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Ocratoxinas Límite: Animals / Humans Idioma: En Revista: Food Addit Contam Asunto de la revista: CIENCIAS DA NUTRICAO Año: 2005 Tipo del documento: Article País de afiliación: Francia Pais de publicación: Reino Unido
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Ocratoxinas Límite: Animals / Humans Idioma: En Revista: Food Addit Contam Asunto de la revista: CIENCIAS DA NUTRICAO Año: 2005 Tipo del documento: Article País de afiliación: Francia Pais de publicación: Reino Unido