Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 387, Issue 2, Pages 245-250Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2009.06.123
Keywords
Aldo-keto reductase family 1 member B10; Alpha, beta-unsaturated carbonyls; Glutathione-conjugated carbonyls; Steady-state kinetics; Cytotoxicity
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Funding
- American Cancer Society [RSG-04-031-01-CCE]
- National Cancer Institute [CA122327, 122622]
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Alpha, beta-unsaturated carbonyls are highly reactive mutagens and carcinogens to which humans are exposed on a daily basis. This study demonstrates that aldo-keto reductase family 1 member B10 (AKR1B10) is a critical protein in detoxifying dietary and lipid-derived unsaturated carbonyls. Purified AKR1B10 recombinant protein efficiently catalyzed the reduction to less toxic alcohol forms of crotonaldehyde at 0.90 mu M, 4-hydroxynonenal (HNE) at 0.10 mu M, trans-2-hexanal at 0.10 mu M, and trans-2,4-hexadienal at 0.05 mu M, the concentrations at or lower than physiological exposures. Ectopically expressed AKR1B10 in 293T cells eliminated immediately HNE at I (subtoxic) or 5 mu M (toxic) by converting to 1,4-dihydroxynonene, protecting the cells from HNE toxicity. AKR1B10 protein also showed strong enzymatic activity toward glutathione-conjugated carbonyls. Taken together, our study results suggest that AKR1B10 specifically expressed in the intestine is physiologically important in protecting the host cell against dietary and lipid-derived cytotoxic carbonyls. (C) 2009 Elsevier Inc. All rights reserved.
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