Disease relevance of Akr1a1

• Purification and properties of aldose reductase and aldehyde reductase from EHS tumor cells [1].
• Supernatants from sonicated cells of Bacillus subtilis and Escherichia coli also showed C-nitrosoreductase activity but were devoid of aldehyde reductase activity [2].

High impact information on Akr1a1

• Chemoprevention of aflatoxin B1 hepatocarcinogenesis by coumarin, a natural benzopyrone that is a potent inducer of aflatoxin B1-aldehyde reductase, the glutathione S-transferase A5 and P1 subunits, and NAD(P)H:quinone oxidoreductase in rat liver [3].
• Metabolism of daunorubicin by a barbiturate-sensitive aldehyde reductase from rat liver [4].
• The aldehyde reductase may have important roles in the metabolism of exogeneous drugs as well as the aldehyde derivatives of the biogenic amines [4].
• Moreover, cell extract from COS-1 cells transfected with the rat ALR cDNA exhibited NADPH-dependent 3-DG-reducing activity and cross-reacted with antiserum raised against the purified rat 3-DG-reducing enzyme [5].
• Aldose reductase (alditol:NAD(P)+ 1-oxidoreductase, EC 1.1.1.21) and aldehyde reductase (alcohol:NADP+ oxidoreductase, EC 1.1.1.2) were purified to a homogeneity from rat testis [6].

Analytical, diagnostic and therapeutic context of Akr1a1

• The aldehyde reductase activity became concentrated roughly in parallel with the C-nitrosoreductase activity during the course of the purification and these two activities could not be separated even after further purification by 5'-AMP-Sepharose affinity chromatography [2].

References