potassium-bromate has been researched along with Urinary-Bladder-Neoplasms* in 2 studies
2 other study(ies) available for potassium-bromate and Urinary-Bladder-Neoplasms
| Article | Year |
|---|---|
Complementation of the oxidatively damaged DNA repair defect in Cockayne syndrome A and B cells by Escherichia coli formamidopyrimidine DNA glycosylase.
Repair of the oxidized purine 8-oxo-7,8-dihydroguanine (8-oxoGua) is inefficient in cells belonging to the B complementation group of Cockayne syndrome (CS-B), a developmental and neurological disorder characterized by defective transcription-coupled repair. We show here that cells belonging to the A complementation group (CS-A) are also defective in repair of 8-oxoGua and we demonstrate that expression of the Escherichia coli formamidopyrimidine DNA glycosylase (FPG) completely corrects the repair deficiency in both CS-A and CS-B cells. Phenotypically, CS-A cells are normally sensitive to toxicity and micronuclei induced by the oxidizing agent potassium bromate. CS-B cells display sensitivity to elevated concentrations of potassium bromate but this is not compensated by FPG expression, suggesting toxicity of lesions that are not FPG substrates. The data indicate that 8-oxoGua is not a major toxic and clastogenic lesion in CS cells. Topics: Adolescent; Adult; Aged; Aged, 80 and over; Bromates; Carcinogens; Cell Survival; Cells, Cultured; Cockayne Syndrome; Colony-Forming Units Assay; DNA Damage; DNA Repair; DNA-Formamidopyrimidine Glycosylase; Escherichia coli; Female; Fibroblasts; Genetic Complementation Test; Genetic Vectors; Humans; Kidney; Male; Micronucleus Tests; Transcription, Genetic; Urinary Bladder Neoplasms | 2007 |
Accelerated repair and reduced mutagenicity of oxidative DNA damage in human bladder cells expressing the E. coli FPG protein.
Repair of some oxidized purines such as 8-oxo-7,8-dihydroguanine (8-oxoG) is inefficient in human cells in comparison to repair of other major endogenous lesions (e.g. uracil, abasic sites or oxidized pyrimidines). This is due to the poor catalytic properties of hOGG1, the major DNA glycosylase involved in 8-oxoG removal. The formamidopyrimidine DNA glycosylase (FPG) protein from E. coli is endowed with a potent 8-oxoG glycolytic activity coupled with a beta,delta-AP lyase. In this study, we have expressed FPG fused to the enhanced green fluorescent protein (EGFP) in human bladder cells to accelerate the repair of oxidative DNA damage. Cells expressing the fusion protein EGFP-FPG repaired 8-oxoG and AP sites at accelerated rates, in particular via the single-nucleotide insertion base excision repair (BER) pathway and were resistant to mutagenicity of the oxidizing carcinogen potassium bromate. FPG may stably protect human cells from some harmful effects of oxidative DNA damage. Topics: Bromates; Carcinogens; Cell Culture Techniques; DNA Damage; DNA Repair; DNA-Formamidopyrimidine Glycosylase; Escherichia coli Proteins; Fibroblasts; Green Fluorescent Proteins; Guanine; Humans; Oxidative Stress; Reactive Oxygen Species; Urinary Bladder; Urinary Bladder Neoplasms | 2006 |