ArticleChemical research in toxicology2008
Oxidation of PAH trans-dihydrodiols by human aldo-keto reductase AKR1B10.
Article in Chemical research in toxicology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 81 citations in OpenAlex.
- ExploringMolecules (Basel, Switzerland) · 2026Article
- The pan-cancer landscape of aldo-keto reductase1B10 reveals that its expression is diminished in gastric cancer.Frontiers in immunology · 2024Article
- Aldo-keto reductases: Role in cancer development and theranostics.Oncology research · 2024Review
- Overexpression of AKR1B10 Predicts Poor Prognosis in Gastric Cancer Patients Undergoing Surgical Resection.Current oncology (Toronto, Ont.) · 2022Article
- Role of Human Aldo-Keto Reductases in the Nitroreduction of 1-Nitropyrene and 1,8-Dinitropyrene.Chemical research in toxicology · 2022Article
- The expression and significance of AKR1B10 in laryngeal squamous cell carcinoma.Scientific reports · 2021Article
- The Role of AKR1B10 in Physiology and Pathophysiology.Metabolites · 2021Review
- Aldo Keto Reductases AKR1B1 and AKR1B10 in Cancer: Molecular Mechanisms and Signaling Networks.Advances in experimental medicine and biology · 2021Review
- Modulation of retinoid signaling: therapeutic opportunities in organ fibrosis and repair.Pharmacology & therapeutics · 2020Review
- The Photodynamic Properties and the Genotoxicity of Heat-Treated Silicalite-1 Films.Materials (Basel, Switzerland) · 2019Article
- Selective Inhibition of Human AKR1B10 byMolecules (Basel, Switzerland) · 2018Article
- Aldo-Keto Reductase Regulation by the Nrf2 System: Implications for Stress Response, Chemotherapy Drug Resistance, and Carcinogenesis.Chemical research in toxicology · 2017Article
- Aldo-Keto Reductase Family 1 Member B10 Inhibitors: Potential Drugs for Cancer Treatment.Recent patents on anti-cancer drug discovery · 2016Review
- Article
- Mechanisms of activation of the transcription factor Nrf2 by redox stressors, nutrient cues, and energy status and the pathways through which it attenuates degenerative disease.Free radical biology & medicine · 2015Review
- Cytochrome P450 1b1 in polycyclic aromatic hydrocarbon (PAH)-induced skin carcinogenesis: Tumorigenicity of individual PAHs and coal-tar extract, DNA adduction and expression of select genes in the Cyp1b1 knockout mouse.Toxicology and applied pharmacology · 2015Article
- Human aldo-keto reductases and the metabolic activation of polycyclic aromatic hydrocarbons.Chemical research in toxicology · 2014Review
- Role of abnormal lipid metabolism in development, progression, diagnosis and therapy of pancreatic cancer.World journal of gastroenterology · 2014Review
- Heat shock protein 90-α mediates aldo-keto reductase 1B10 (AKR1B10) protein secretion through secretory lysosomes.The Journal of biological chemistry · 2013Article
- Sulindac inhibits pancreatic carcinogenesis in LSL-KrasG12D-LSL-Trp53R172H-Pdx-1-Cre mice via suppressing aldo-keto reductase family 1B10 (AKR1B10).Carcinogenesis · 2013Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
AKR1B10 has been identified as a potential biomarker for human nonsmall cell lung carcinoma and as a tobacco exposure and response gene. AKR1B10 functions as an efficient retinal reductase in vitro and may regulate retinoic acid homeostasis. However, the possibility that this enzyme is able to activate polycyclic aromatic hydrocarbon (PAH) trans-dihydrodiols to form reactive and redox-active o-quinones has not been investigated to date. AKR1B10 was found to oxidize a wide range of PAH trans-dihydrodiol substrates in vitro to yield PAH o-quinones. Reactions of AKR1B10 proceeded with improper stereochemistry, since it was specific for the minor (+)-benzo[a]pyrene-7S,8S-dihydrodiol diastereomer formed in vivo. However, AKR1B10 displayed reasonable activity in the oxidation of both the (-)-R,R and (+)-S,S stereoisomers of benzo[g]chrysene-11,12-dihydrodiol and oxidized the potentially relevant, albeit minor, (+)-benz[a]anthracene-3S,4S-dihydrodiol metabolite. We find that AKR1B10 is therefore likely to play a contributing role in the activation of PAH trans-dihydrodiols in human lung. AKR1B10 retinal reductase activity was confirmed in vitro and found to be 5- to 150-fold greater than the oxidation of PAH trans-dihydrodiols examined. AKR1B10 was highly expressed at the mRNA and protein levels in human lung adenocarcinoma A549 cells, and robust retinal reductase activity was measured in lysates of these cells. The much greater catalytic efficiency of retinal reduction compared to PAH trans-dihydrodiol metabolism suggests AKR1B10 may play a greater role in lung carcinogenesis through dysregulation of retinoic acid homeostasis than through oxidation of PAH trans-dihydrodiols.
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