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Properties and tissue distribution of a novel aldo-keto reductase encoding in a rat gene (Akr1b10).

Authors: Endo, S  Matsunaga, T  Kuragano, T  Ohno, S  Kitade, Y  Tajima, K  El-Kabbani, O  Hara, A 
Citation: Endo S, etal., Arch Biochem Biophys. 2010 Nov 15;503(2):230-7. Epub 2010 Aug 13.
Pubmed: (View Article at PubMed) PMID:20709016
DOI: Full-text: DOI:10.1016/j.abb.2010.08.010

A recent rat genomic sequencing predicts a gene Akr1b10 that encodes a protein with 83% sequence similarity to human aldo-keto reductase (AKR) 1B10. In this study, we isolated the cDNA for the rat AKR1B10 (R1B10) from rat brain, and examined the enzymatic properties of the recombinant protein. R1B10 utilized NADPH as the preferable coenzyme, and reduced various aldehydes (including cytotoxic 4-hydroxy-2-hexenal and 4-hydroxy- and 4-oxo-2-nonenals) and alpha-dicarbonyl compounds (such as methylglyoxal and 3-deoxyglucosone), showing low K(m) values of 0.8-6.1muM and 3.7-67muM, respectively. The enzyme also reduced glyceraldehyde and tetroses (K(m)=96-390muM), although hexoses and pentoses were inactive and poor substrates, respectively. Among the substrates, 4-oxo-2-nonenal was most efficiently reduced into 4-oxo-2-nonenol, and its cytotoxicity against bovine endothelial cells was decreased by the overexpression of R1B10. R1B10 showed low sensitivity to aldose reductase inhibitors, and was activated to approximately two folds by valproic acid, and alicyclic and aromatic carboxylic acids. The mRNA for R1B10 was expressed highly in rat brain and heart, and at low levels in other rat tissues and skin fibroblasts. The results suggest that R1B10 functions as a defense system against oxidative stress and glycation in rat tissues.

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RGD Object Information
RGD ID: 6903952
Created: 2012-10-09
Species: All species
Last Modified: 2012-10-09
Status: ACTIVE



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RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.