Inhibitory effects of Pap against aldo-keto reductases family 1

AKR1C enzymes of human aldo-keto reductase (AKR) superfamily include four isoforms(AKR1C1, AKR1C2, AKR1C3, AKR1C4). All of the isoforms depend on NAD(p)(H) andcatalyze the oxidation and reduction reactions of wide range of substrates [1]. HumanAKR1C enzymes implicated in steroid metabolism including androgen, estrogen andprogesterone, neurosteroid and bile acid. Any changes in activity and gene regulation of theseisoforms can result in pathogenesis. Altered AKR1C expression has been reported inhormone dependent disease including prostate cancer, breast cancer and endometrial disease[2,3]. So, introducing new of chemicals that inhibit these enzymes may provide new agentsfor the chemical prevention or the treatment of various disease. Here, the inhibitory potentialand isoform selectivity of pap, an isoquinoline alkaloid on AKR1C enzymes has been testedhere using molecular docking.