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Publication Date:
March 2011
ISSN:
1868-503X
DOI:
10.1515/bmc.2011.010

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Biomolecular Concepts

Editor-in-Chief: Jollès, Pierre / Mansuy, Isabelle

Editorial Board Member: Avila, Jesus / Bollen, Mathieu / Bonetto, Valentina / Cera, Enrico / Jorgensen, Erik / Jörnvall, Hans / Lagasse, Eric / Norman, Robert / Pinna, Lorenzo / Raghavan, K. Vijay / Venetianer, Pal / Wahli, Walter

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Human aldo-keto reductases: structure, substrate specificity and roles in tumorigenesis

Jun Ma1 / 1

1Department of Medical Microbiology, Immunology and Cell Biology, Simmons Cancer Institute, Southern Illinois University School of Medicine, 913 N. Rutledge Street, Springfield, IL 62794, USA

Citation Information: BioMolecular Concepts. Volume 2, Issue 1-2, Pages 115–126, ISSN (Online) 1868-503X, ISSN (Print) 1868-5021, DOI: 10.1515/bmc.2011.010, March 2011

Publication History:
Published Online:
2011-03-17

Abstract

The aldo-keto reductase (AKR) superfamily consists of over 150 protein members sharing similar structure and enzymatic activities. To date, 13 human AKRs have been identified, and they participate in xenobiotic detoxification, biosynthesis and metabolism. Increasing evidence suggests the involvement of human AKR proteins in cancer development, progression and treatment. Some proteins demonstrate multiple functional features in addition to being a reductase for carbonyl groups. This review article discusses the most recent progress made in the study of humans AKRs.

Keywords: aldo-keto reductases; AKR1B1; AKR1B10; AKR1C; anticancer agents; carbonyls; polycyclic aromatic hydrocarbons; prostaglandins; retinaldehyde; tumorigenesis

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