6533b851fe1ef96bd12aa245

RESEARCH PRODUCT

Activity and immunohistochemistry of DT-diaphorase in hamster and human kidney tumours.

Francisco J. RomeroLars ErnsterElena MonsalveAntonio CremadesAntonio Llombart-boschJuan Segura-aguilar

subject

MaleCancer ResearchPathologymedicine.medical_specialtyDiethylstilbestrolHamsterBiologyKidneychemistry.chemical_compoundCricetinaemedicineNAD(P)H Dehydrogenase (Quinone)AnimalsHumansDiethylstilbestrolchemistry.chemical_classificationKidneyGlutathione PeroxidaseMesocricetusSuperoxide DismutaseGlutathione peroxidaseWilms' tumorGeneral Medicinemedicine.diseaseMolecular biologyImmunohistochemistryKidney NeoplasmsClear cell renal cell carcinomamedicine.anatomical_structurechemistryGlutathione disulfideImmunohistochemistryRabbitsmedicine.drug

description

We have studied the biochemical and immunohistochemical changes of DT-diaphorase in diethylstilbestrol (DES)-induced hamster kidney tumours and human biopsies from normal kidneys and renal clear cell carcinoma. The activities of primary and secondary antioxidants in these hamster and human tissues are also reported. DT-diaphorase is decreased in the different subcellular fractions of hamster and human tissues. In hamster kidney the activities of the one-electron quinone reductases show a nearly two-fold increase. Immunohistochemical findings confirm the decrease in DT-diaphorase in hamster and human tissues. This image is of special interest in the case of nephroblastoma (Wilms' tumour), since it has been proposed that the DES-induced tumour is a 'nephroblastoma-like' one. Primary anti oxidant enzymatic activities, i.e. superoxide dismutase and glutathione peroxidase, are increased in hamster kidney bearing DES-induced tumours and decreased in human renal clear cell carcinoma. Glutathione disulphide reductase is decreased in hamster and human tumours. The role of these enzymatic activities in the carcinogenic process is also discussed.

10.1093/carcin/15.8.1631https://pubmed.ncbi.nlm.nih.gov/8055643