Murine Aldo-Keto Reductases: Identification of AKR1B8 as an ortholog of human AKR1B10
Aldo-keto reductase family 1 member B10 (AKR1B10), over expressed in multiple human cancers, may be implicated in cancer development and progression via detoxifying cellular reactive carbonyls and regulating fatty acid synthesis. Aldo Keto Reductases are implicated in a wide range of biological proc...
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| Format: | Others |
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OpenSIUC
2009
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| Online Access: | https://opensiuc.lib.siu.edu/theses/98 https://opensiuc.lib.siu.edu/cgi/viewcontent.cgi?article=1105&context=theses |
| Summary: | Aldo-keto reductase family 1 member B10 (AKR1B10), over expressed in multiple human cancers, may be implicated in cancer development and progression via detoxifying cellular reactive carbonyls and regulating fatty acid synthesis. Aldo Keto Reductases are implicated in a wide range of biological processes, including carbonyl detoxification, osmolytic regulation, tumor development and therapeutics. The mouse is an ideal modeling organism greatly contributing to human disease investigations. For modeling study of AKR1B10, we are seeking to identify the ortholog of AKR1B10 in mice. Here we show that out of three aldo-keto reductases in mice i.e., aldo-keto reductase family 1 member B3 (AKR1B3), aldo-keto reductase family 1 member B7 (AKR1B7) and aldo-keto reductase family 1 member B8 (AKR1B8), AKR1B8 is the mouse ortholog of human AKR1B10. In this study, we compared the three mouse AKR homolog's i.e. AKR1B3, AKR1B7, and AKR1B8 with human AKR1B10. AKR1B8 shows highest similarities in amino acid sequence, computerized structures, substrate spectra and specificity, and tissue distributions to AKR1B10. More importantly, like the human AKR1B10, the mouse AKR1B8 associates with murine acetyl-CoA carboxylase-α (ACCA) and mediates fatty acid synthesis in colon cancer cells. Taken together, our data suggest that murine AKR1B8 is the ortholog of the human AKR1B10. |
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