The hop-derived compounds xanthohumol, isoxanthohumol and 8-prenylnaringenin are tight-binding inhibitors of human aldo-keto reductases 1B1 and 1B10

References

• Zanoli P, Zavatti M. Pharmacognostic and pharmacological profile of Humulus lupulus L. J Ethnopharmacol 2008;116:383–96.
   PubMed Web of Science ®Google Scholar
• Van Cleemput M, Heyerick A, Libert C, et al. Hop bitter acids efficiently block inflammation independent of GRalpha, PPARalpha, or PPARgamma. Mol Nutr Food Res 2009;53:1143–55.
   PubMed Web of Science ®Google Scholar
• Stevens JF, Page JE. Xanthohumol and related prenylflavonoids from hops and beer: to your good health! Phytochemistry 2004;65:1317–30.
   PubMed Web of Science ®Google Scholar
• Anioł M, Świderska A, Stompor M, et al. Antiproliferative activity and synthesis of 8-prenylnaringenin derivatives by demethylation of 7-O- and 4′-O-substituted isoxanthohumols. Med Chem Res 2012;21:4230–8.
   PubMed Web of Science ®Google Scholar
• Adegbola P, Aderibigbe I, Hammed W, et al. Antioxidant and anti-inflammatory medicinal plants have potential role in the treatment of cardiovascular disease: a review. Am J Cardiovasc Dis 2017;7:19–32.
   PubMed Web of Science ®Google Scholar
• Samarghandian S, Farkhondeh T, Samini F. Honey and health: a review of recent clinical research. Pharmacognosy Res 2017;9:121–7.
   PubMed Web of Science ®Google Scholar
• Zakaryan H, Arabyan E, Oo A, et al. Flavonoids: promising natural compounds against viral infections. Arch Virol 2017;162:2539–51.
   PubMed Web of Science ®Google Scholar
• Liu M, Hansen P, Wang G, et al. Pharmacological profile of xanthohumol, a prenylated flavonoid from hops (Humulus lupulus). Molecules 2015;20:754–79.
   PubMed Web of Science ®Google Scholar
• Stevens JF, Taylor AW, Nickerson GB, et al. Prenylflavonoid variation in Humulus lupulus: distribution and taxonomic significance of xanthogalenol and 4’-O-methylxanthohumol. Phytochemistry 2000;53:759–75.
   PubMed Web of Science ®Google Scholar
• Nikolic D, Li Y, Chadwick LR, et al. Metabolism of 8-prenylnaringenin, a potent phytoestrogen from hops (Humulus lupulus l.), by human liver microsomes. Drug Metab Dispos 2004;32:272–9.
   PubMed Web of Science ®Google Scholar
• Yilmazer M, Stevens JF, Buhler DR. In vitro glucuronidation of xanthohumol, a flavonoid in hop and beer, by rat and human liver microsomes. FEBS Lett 2001;491:252–6.
   PubMed Web of Science ®Google Scholar
• Yilmazer M, Stevens JF, Deinzer ML, et al. In vitro biotransformation of xanthohumol, a flavonoid from hops (Humulus lupulus), by rat liver microsomes. Drug Metab Dispos Biol Fate Chem 2001;29:223–31.
   PubMed Web of Science ®Google Scholar
• Nookandeh A, Frank N, Steiner F, et al. Xanthohumol metabolites in faeces of rats. Phytochemistry 2004;65:561–70.
   PubMed Web of Science ®Google Scholar
• Martinez SE, Davies NM. Enantiospecific pharmacokinetics of isoxanthohumol and its metabolite 8-prenylnaringenin in the rat. Mol Nutr Food Res 2015;59:1674–89.
   PubMed Web of Science ®Google Scholar
• Legette L, Karnpracha C, Reed RL, et al. Human pharmacokinetics of xanthohumol, an antihyperglycemic flavonoid from hops. Mol Nutr Food Res 2014;58:248–55.
   PubMed Web of Science ®Google Scholar
• Guo J, Nikolic D, Chadwick LR, et al. Identification of human hepatic cytochrome P450 enzymes involved in the metabolism of 8-Prenylnaringenin and isoxanthohumol from hopf (Humulus lupulus l.). Drug Metab Dispos 2006;34:1152–9.
   PubMed Web of Science ®Google Scholar
• Costa R, Rodrigues I, Guardão L, et al. Modulation of VEGF signaling in a mouse model of diabetes by xanthohumol and 8-prenylnaringenin: unveiling the angiogenic paradox and metabolism interplay. Mol Nutr Food Res 2017;61:1600488.
   Web of Science ®Google Scholar
• Costa R, Rodrigues I, Guardão L, et al. Xanthohumol and 8-prenylnaringenin ameliorate diabetic-related metabolic dysfunctions in mice. J Nutr Biochem 2017;45:39–47.
   PubMed Web of Science ®Google Scholar
• Colgate EC, Miranda CL, Stevens JF, et al. Xanthohumol, a prenylflavonoid derived from hops induces apoptosis and inhibits NF-kappaB activation in prostate epithelial cells. Cancer Lett 2007;246:201–9.
   PubMed Web of Science ®Google Scholar
• Negrão R, Duarte D, Costa R, et al. Isoxanthohumol modulates angiogenesis and inflammation via vascular endothelial growth factor receptor, tumor necrosis factor alpha and nuclear factor kappa B pathways: isoxanthohumol modulates angiogenesis and inflammation. BioFactors 2013;39:608–22.
   PubMed Web of Science ®Google Scholar
• Wang Q, Ding Z, Liu J, et al. Xanthohumol, a novel anti-HIV-1 agent purified from Hops. Antiviral Res 2004;64:189–94.
   PubMed Web of Science ®Google Scholar
• Cos P, Maes L, Vlietinck A, et al. Plant-derived leading compounds for chemotherapy of human immunodefiency virus (HIV) infection – an update (1998–2007). Planta Med 2008;74:1323–37.
   PubMed Web of Science ®Google Scholar
• Ramana KV, Srivastava SK. Aldose reductase: a novel therapeutic target for inflammatory pathologies. Int J Biochem Cell Biol 2010;42:17–20.
   PubMed Web of Science ®Google Scholar
• Jin J, Liao W, Yao W, et al. Aldo-keto Reductase Family 1 member B 10 mediates liver cancer cell proliferation through sphingosine-1-phosphate. Sci Rep 2016;6:22746.
   PubMed Web of Science ®Google Scholar
• Alexiou P, Pegklidou K, Chatzopoulou M, et al. Aldose reductase enzyme and its implication to major health problems of the 21(st) century. Curr Med Chem 2009;16:734–52.
   PubMed Web of Science ®Google Scholar
• Zhang W, Li H, Yang Y, et al. Knockdown or inhibition of aldo-keto reductase 1B10 inhibits pancreatic carcinoma growth via modulating Kras-E-cadherin pathway. Cancer Lett 2014;355:273–80.
   PubMed Web of Science ®Google Scholar
• Balestri F, Cappiello M, Moschini R, et al. Modulation of aldose reductase activity by aldose hemiacetals. Biochim Biophys Acta BBA - Gen Subj 2015;1850:2329–39.
   PubMed Web of Science ®Google Scholar
• Chung YT, Matkowskyj KA, Li H, et al. Overexpression and oncogenic function of aldo-keto reductase family 1B10 (AKR1B10) in pancreatic carcinoma. Mod Pathol 2012;25:758–66.
   PubMed Web of Science ®Google Scholar
• Kurahashi T, Kwon M, Homma T, et al. Reductive detoxification of acrolein as a potential role for aldehyde reductase (AKR1A) in mammals. Biochem Biophys Res Commun 2014;452:136–41.
   PubMed Web of Science ®Google Scholar
• Ellis EM. Reactive carbonyls and oxidative stress: potential for therapeutic intervention. Pharmacol Ther 2007;115:13–24.
   PubMed Web of Science ®Google Scholar
• Rotondo R, Moschini R, Renzone G, et al. Human carbonyl reductase 1 as efficient catalyst for the reduction of glutathionylated aldehydes derived from lipid peroxidation. Free Radic Biol Med 2016;99:323–32.
   PubMed Web of Science ®Google Scholar
• Bains OS, Takahashi RH, Pfeifer TA, et al. Two allelic variants of aldo-keto reductase 1A1 exhibit reduced in vitro metabolism of daunorubicin. Drug Metab Dispos 2008;36:904–10.
   PubMed Web of Science ®Google Scholar
• O’connor T, Ireland LS, Harrison DJ, et al. Major differences exist in the function and tissue-specific expression of human aflatoxin B1 aldehyde reductase and the principal human aldo-keto reductase AKR1 family members. Biochem J 1999;343(Pt 2):487–504.
   PubMed Web of Science ®Google Scholar
• Srivastava SK, Ramana KV, Bhatnagar A. Role of aldose reductase and oxidative damage in diabetes and the consequent potential for therapeutic options. Endocr Rev 2005;26:380–92.
   PubMed Web of Science ®Google Scholar
• Yabe-Nishimura C. Aldose reductase in glucose toxicity: a potential target for the prevention of diabetic complications. Pharmacol Rev 1998;50:21–33.
   PubMed Web of Science ®Google Scholar
• El-Kabbani O, Ruiz F, Darmanin C, et al. Aldose reductase structures: implications for mechanism and inhibition. Cell Mol Life Sci CMLS 2004;61:750–62.
   PubMed Web of Science ®Google Scholar
• González RG, Barnett P, Aguayo J, et al. Direct measurement of polyol pathway activity in the ocular lens. Diabetes 1984;33:196–9.
   PubMed Web of Science ®Google Scholar
• Tang WH, Martin KA, Hwa J. Aldose reductase, oxidative stress, and diabetic mellitus. Front Pharmacol 2012;3:87.
   Web of Science ®Google Scholar
• Hwang JJ, Jiang L, Hamza M, et al. The human brain produces fructose from glucose. JCI Insight 2017;2:e90508.
   PubMed Web of Science ®Google Scholar
• Brings S, Fleming T, Freichel M, et al. Dicarbonyls and advanced glycation end-products in the development of diabetic complications and targets for intervention. Int J Mol Sci 2017;18:984.
   Web of Science ®Google Scholar
• Del Corso A, Cappiello M, Mura U. From a dull enzyme to something else: facts and perspectives regarding aldose reductase. Curr Med Chem 2008;15:1452–61.
   PubMed Web of Science ®Google Scholar
• Kanchan D, Kale S, Somani G, et al. Thymol, a monoterpene, inhibits aldose reductase and high-glucose-induced cataract on isolated goat lens. J Pharm Bioallied Sci 2016;8:277.
   PubMed Web of Science ®Google Scholar
• El Gamal H, Eid AH, Munusamy S. Renoprotective effects of aldose reductase inhibitor epalrestat against high glucose-induced cellular injury. Bio Med Res Int 2017;2017:1–11.
   Web of Science ®Google Scholar
• Ramana KV. Aldose reductase: new insights for an old enzyme. Biomol Concepts 2011;2:103–114.
   PubMedGoogle Scholar
• Barski OA, Tipparaju SM, Bhatnagar A. The aldo-keto reductase superfamily and its role in drug metabolism and detoxification. Drug Metab Rev 2008;40:553–624.
   PubMed Web of Science ®Google Scholar
• Suryanarayana P, Kumar PA, Saraswat M, et al. Inhibition of aldose reductase by tannoid principles of Emblica officinalis: implications for the prevention of sugar cataract. Mol Vis 2004;10:148–54.
   PubMed Web of Science ®Google Scholar
• Kato A, Kobayashi K, Narukawa K, et al. 6,7-Dihydroxy-4-phenylcoumarin as inhibitor of aldose reductase 2. Bioorg Med Chem Lett 2010;20:5630–3.
   PubMed Web of Science ®Google Scholar
• Ibrar A, Tehseen Y, Khan I, et al. Coumarin-thiazole and -oxadiazole derivatives: synthesis, bioactivity and docking studies for aldose/aldehyde reductase inhibitors. Bioorganic Chem 2016;68:177–86.
   PubMed Web of Science ®Google Scholar
• Carbone V, Zhao H-T, Chung R, et al. Correlation of binding constants and molecular modelling of inhibitors in the active sites of aldose reductase and aldehyde reductase. Bioorg Med Chem 2009;17:1244–50.
   PubMed Web of Science ®Google Scholar
• Gallego O, Ruiz FX, Ardevol A, et al. Structural basis for the high all-trans-retinaldehyde reductase activity of the tumor marker AKR1B10. Proc Natl Acad Sci 2007;104:20764–9.
   PubMed Web of Science ®Google Scholar
• Matsunaga T, Shintani S, Hara A. Multiplicity of mammalian reductases for xenobiotic carbonyl compounds. Drug Metab Pharmacokinet 2006;21:1–18.
   PubMed Web of Science ®Google Scholar
• Jin Y, Penning TM. Aldo-keto reductases and bioactivation/detoxication. Annu Rev Pharmacol Toxicol 2007;47:263–92.
   PubMed Web of Science ®Google Scholar
• Endo S, Matsunaga T, Mamiya H, et al. Kinetic studies of AKR1B10, human aldose reductase-like protein: endogenous substrates and inhibition by steroids. Arch Biochem Biophys 2009;487:1–9.
   PubMed Web of Science ®Google Scholar
• Yang ZN, Davis GJ, Hurley TD, et al. Catalytic efficiency of human alcohol dehydrogenases for retinol oxidation and retinal reduction. Alcohol Clin Exp Res 1994;18:587–91.
   PubMed Web of Science ®Google Scholar
• Hyndman DJ, Flynn TG. Sequence and expression levels in human tissues of a new member of the aldo-keto reductase family. Biochim Biophys Acta 1998;1399:198–202.
   PubMed Web of Science ®Google Scholar
• Cao D, Fan ST, Chung SS. Identification and characterization of a novel human aldose reductase-like gene. J Biol Chem 1998;273:11429–35.
   PubMed Web of Science ®Google Scholar
• Fukumoto S, Yamauchi N, Moriguchi H, et al. Overexpression of the aldo-keto reductase family protein AKR1B10 is highly correlated with smokers’ non-small cell lung carcinomas. Clin Cancer Res 2005;11:1776–85.
   PubMed Web of Science ®Google Scholar
• Jung Y-J, Lee EH, Lee CG, et al. AKR1B10-inhibitory Selaginella tamariscina extract and amentoflavone decrease the growth of A549 human lung cancer cells in vitro and in vivo. J Ethnopharmacol 2017;202:78–84.
   PubMed Web of Science ®Google Scholar
• Li H, Yang AL, Chung YT, et al. Sulindac inhibits pancreatic carcinogenesis in LSL-KrasG12D-LSL-Trp53R172H-Pdx-1-Cre mice via suppressing aldo-keto reductase family 1B10 (AKR1B10). Carcinogenesis 2013;34:2090–8.
   PubMed Web of Science ®Google Scholar
• Matkowskyj KA, Bai H, Liao J, et al. Aldoketoreductase family 1B10 (AKR1B10) as a biomarker to distinguish hepatocellular carcinoma from benign liver lesions. Hum Pathol 2014;45:834–43.
   PubMed Web of Science ®Google Scholar
• Riou P, Kjaer S, Garg R, et al. 14-3-3 proteins interact with a hybrid prenyl-phosphorylation motif to inhibit G proteins. Cell 2013;153:640–53.
   PubMed Web of Science ®Google Scholar
• Gao J, Liao J, Yang G-Y. CAAX-box protein, prenylation process and carcinogenesis. Am J Transl Res 2009;1:312–25.
   PubMed Web of Science ®Google Scholar
• Skarydova L, Tomanova R, Havlikova L, et al. Deeper insight into the reducing biotransformation of bupropion in the human liver. Drug Metab Pharmacokinet 2014;29:177–84.
   PubMed Web of Science ®Google Scholar
• Martin H-J, Breyer-Pfaff U, Wsol V, et al. Purification and characterization of AKR1B10 from human liver: role in carbonyl reduction of xenobiotics. Drug Metab Dispos 2005;34:464–70.
   PubMed Web of Science ®Google Scholar
• Copeland RA. Enzymes: a practical introduction to structure, mechanism, and data analysis. 2nd ed. New York, NY: Wiley; 2000.
   Google Scholar
• Bisswanger H. Enzyme kinetics. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA; 2008.
   Google Scholar
• Rastelli G, Antolini L, Benvenuti S, et al. Structural bases for the inhibition of aldose reductase by phenolic compounds. Bioorg Med Chem 2000;8:1151–8.
   PubMed Web of Science ®Google Scholar
• Jung HA, Moon HE, Oh SH, et al. Kinetics and molecular docking studies of kaempferol and its prenylated derivatives as aldose reductase inhibitors. Chem Biol Interact 2012;197:110–8.
   PubMed Web of Science ®Google Scholar
• Jung HA, Yoon NY, Kang SS, et al. Inhibitory activities of prenylated flavonoids from Sophora flavescens against aldose reductase and generation of advanced glycation endproducts. J Pharm Pharmacol 2008;60:1227–36.
   PubMed Web of Science ®Google Scholar
• Shim SH, Kim Y, Lee JY, et al. Aldose reductase inhibitory activity of the compounds from the seed of Psoralea corylifolia. J Korean Soc Appl Biol Chem 2009;52:568–72.
   Google Scholar
• Huang L, He R, Luo W, et al. Aldo-keto reductase family 1 member B10 inhibitors: potential drugs for cancer treatment. Recent Pat Anticancer Drug Discov 2016;11:184–96.
   PubMed Web of Science ®Google Scholar
• Cousido-Siah A, Ruiz FX, Fanfrlík J, et al. IDD388 polyhalogenated derivatives as probes for an improved structure-based selectivity of AKR1B10 inhibitors. ACS Chem Biol 2016;11:2693–705.
   PubMed Web of Science ®Google Scholar
• Kabir A, Endo S, Toyooka N, et al. Evaluation of compound selectivity of aldo-keto reductases using differential scanning fluorimetry. J Biochem (Tokyo) 2016;161:215–222.
   Web of Science ®Google Scholar
• Chen W, Chen X, Zhou S, et al. Design and synthesis of polyhydroxy steroids as selective inhibitors against AKR1B10 and molecular docking. Steroids 2016;110:1–8.
   PubMed Web of Science ®Google Scholar
• Takemura M, Endo S, Matsunaga T, et al. Selective inhibition of the tumor marker aldo-keto reductase family member 1B10 by oleanolic acid. J Nat Prod 2011;74:1201–6.
   PubMed Web of Science ®Google Scholar
• Zemanova L, Hofman J, Novotna E, et al. Flavones inhibit the activity of AKR1B10, a promising therapeutic target for cancer treatment. J Nat Prod 2015;78:2666–74.
   PubMed Web of Science ®Google Scholar
• Mohamadi-Nejad A, Moosavi-Movahedi AA, Hakimelahi GH, et al. Thermodynamic analysis of human serum albumin interactions with glucose: insights into the diabetic range of glucose concentration. Int J Biochem Cell Biol 2002;34:1115–24.
   PubMed Web of Science ®Google Scholar
• Harris GS, Kozarich JW. Steroid 5alpha-reductase inhibitors in androgen-dependent disorders. Curr Opin Chem Biol 1997;1:254–9.
   PubMed Web of Science ®Google Scholar
• Copeland RA. Evaluation of enzyme inhibitors in drug discovery. A guide for medicinal chemists and pharmacologists. Methods Biochem Anal 2005;46:1–265.
   PubMedGoogle Scholar