Abstract
Deregulation of metabolic pathways has increasingly been appreciated as a major driver of cancer in recent years. The principal cancer-associated alterations in metabolism include abnormal uptake of glucose and amino acids and the preferential use of metabolic pathways for the production of biomass and nicotinamide adenine dinucleotide phosphate (NADPH). Aldo-keto reductases (AKRs) are NADPH dependent cytosolic enzymes that can catalyze the reduction of carbonyl groups to primary and secondary alcohols using electrons from NADPH. Aldose reductase, also known as AKR1B1, catalyzes the conversion of excess glucose to sorbitol and has been studied extensively for its role in a number of diabetic pathologies. In recent years, however, high expression of the AKR1B and AKR1C family of enzymes has been strongly associated with worse outcomes in different cancer types. This review provides an overview of the catalysis-dependent and independent data emerging on the molecular mechanisms of the functions of AKRBs in different tumor models with an emphasis of the role of these enzymes in chemoresistance, inflammation, oxidative stress and epithelial-to-mesenchymal transition.
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Abbreviations
- 4HNE:
-
4-hydroxy-trans-2-nonenal
- AKR:
-
Aldo-keto reductase
- BLBC:
-
Basal-like breast cancer
- CRC:
-
Colorectal carcinoma
- EMT:
-
epithelial-to-mesenchymal transition
- HCC:
-
Hepatocellular carcinoma
- NADPH:
-
nicotinamide adenine dinucleotide phosphate
- NSCLC:
-
Non-small cell lung carcinoma
- PAAD:
-
Pancreatic adenocarcinoma
- ROS:
-
Reactive oxygen species
- SORD:
-
sorbitol dehydrogenase
References
Bryant KL, Mancias JD, Kimmelman AC, Der CJ (2014) KRAS: feeding pancreatic cancer proliferation. Trends Biochem Sci 39:91–100. https://doi.org/10.1016/j.tibs.2013.12.004
Cheng BY et al (2018) Irak1 augments cancer stemness and drug resistance via the ap-1/akr1b10 signaling cascade in hepatocellular carcinoma. Cancer Res 78:2332–2342. https://doi.org/10.1158/0008-5472.CAN-17-2445
Chung YT et al (2012) Overexpression and oncogenic function of aldo-keto reductase family 1B10 (AKR1B10) in pancreatic carcinoma. Mod Pathol 25:758–766. https://doi.org/10.1038/modpathol.2011.191
Colaprico A et al (2016) TCGAbiolinks: an R/Bioconductor package for integrative analysis of TCGA data. Nucleic Acids Res 44(8):e71. https://doi.org/10.1093/nar/gkv1507
Connor JP, Esbona K, Matkowskyj KA (2017) AKR1B10 expression by immunohistochemistry in surgical resections and fine needle aspiration cytology material in patients with cystic pancreatic lesions; potential for improved nonoperative diagnosis. Hum Pathol 70:77–83. https://doi.org/10.1016/j.humpath.2017.10.006
Corcoran A, Cotter TG (2013) Redox regulation of protein kinases. FEBS J 280:1944–1965. https://doi.org/10.1111/febs.12224
Cubillos-Angulo JM et al (2020) Systems biology analysis of publicly available transcriptomic data reveals a critical link between AKR1B10 gene expression, smoking and occurrence of lung cancer. PLoS One 15(2):e0222552. https://doi.org/10.1371/journal.pone.0222552
Demirkol S (2018) Prediction of prognosis and chemosensitivity in gastrointestinal cancers. Bilkent University. Retrieved from http://repository.bilkent.edu.tr/handle/11693/35716
Demirkol Canli S et al (2020) Evaluation of an aldo-keto reductase gene signature with prognostic significance in colon cancer via activation of epithelial to mesenchymal transition and the p70S6K pathway. Carcinogenesis 41:1219–1228. https://doi.org/10.1093/carcin/bgaa072
Distefano JK, Davis B (2019) Diagnostic and prognostic potential of akr1b10 in human hepatocellular carcinoma. Cancers 11:1–13. https://doi.org/10.3390/cancers11040486
Endo S et al (2011) Roles of rat and human aldo-keto reductases in metabolism of farnesol and geranylgeraniol. Chem Biol Interact 191:261–268. https://doi.org/10.1016/j.cbi.2010.12.017
Faubert B et al (2017) Lactate metabolism in human lung tumors. Cell 171:358–371.e9. https://doi.org/10.1016/j.cell.2017.09.019
Finkel T (2011) Signal transduction by reactive oxygen species. J Cell Biol 194:7–15. https://doi.org/10.1083/jcb.201102095
Fukumoto SI et al (2005) Overexpression of the aldo-keto reductase family protein AKR1B10 is highly correlated with smokers’ non-small cell lung carcinomas. Clin Cancer Res 11:1776–1785. https://doi.org/10.1158/1078-0432.CCR-04-1238
Gallego O et al (2007) Structural basis for the high all-trans-retinaldehyde reductase activity of the tumor marker AKR1B10. Proc Natl Acad Sci U S A 104:20764–20769. https://doi.org/10.1073/pnas.0705659105
Geng N, Jin Y, Li Y, Zhu S, Bai H (2020) AKR1B10 inhibitor epalrestat facilitates sorafenib-induced apoptosis and autophagy via targeting the mtor pathway in hepatocellular carcinoma. Int J Med Sci 17:1246–1256. https://doi.org/10.7150/ijms.42956
Ha SY, Song DH, Lee JJ, Lee HW, Cho SY, Park CK (2014) High expression of aldo-keto reductase 1B10 is an independent predictor of favorable prognosis in patients with hepatocellular carcinoma. Gut Liver 8:648–654. https://doi.org/10.5009/gnl13406
Habib E, Linher-Melville K, Lin HX, Singh G (2015) Expression of xCT and activity of system xc- are regulated by NRF2 in human breast cancer cells in response to oxidative stress. Redox Biol 5:33–42. https://doi.org/10.1016/j.redox.2015.03.003
Han C et al (2018) Immunohistochemistry detects increased expression of Aldo-Keto reductase family 1 member B10 (AKR1B10) in early-stage hepatocellular carcinoma. Med Sci Monit 24:7414–7423. https://doi.org/10.12659/MSM.910738
Heiden MGV, Cantley LC, Thompson CB (2009) Understanding the Warburg effect: the metabolic requirements of cell proliferation. Science 324:1029–1033. https://doi.org/10.1126/science.1160809
Hlaváč V et al (2014) The role of cytochromes P450 and aldo-keto reductases in prognosis of breast carcinoma patients. Medicine (Baltimore) 93:e255. https://doi.org/10.1097/MD.0000000000000255
Hung JJ, Yeh YC, Hsu WH (2018) Prognostic significance of AKR1B10 in patients with resected lung adenocarcinoma. Thorac Cancer 9:1492–1499. https://doi.org/10.1111/1759-7714.12863
Ji J et al (2020) The AKR1B1 inhibitor epalrestat suppresses the progression of cervical cancer. Mol Biol Rep 47:6091–6103. https://doi.org/10.1007/s11033-020-05685-z
Jin J, Liao W, Yao W, Zhu R, Li Y, He S (2016) Aldo-keto reductase family 1 member B 10 mediates liver cancer cell proliferation through sphingosine-1-phosphate. Sci Rep 6:22746. https://doi.org/10.1038/srep22746
Kakehashi A, Wei M, Fukushima S, Wanibuchi H (2013) Oxidative stress in the carcinogenicity of chemical carcinogens. Cancers (Basel) 5:1332–1354. https://doi.org/10.3390/cancers5041332
Kishore TKK, Ganugula R, Gade DR, Reddy GB, Nagini S (2016) Gedunin abrogates aldose reductase, PI3K/Akt/mToR, and NF-κB signaling pathways to inhibit angiogenesis in a hamster model of oral carcinogenesis. Tumour Biol 37:2083–2093. https://doi.org/10.1007/s13277-015-4003-0
Krause N, Wegner A (2020) Fructose metabolism in cancer. Cell 9:2635. https://doi.org/10.3390/cells9122635
Li H, Yang AL, Chung YT, Zhang W, Liao J, Yang GY (2013) Sulindac inhibits pancreatic carcinogenesis in LSL-krasg12d-LSL-Trp53R172H-Pdx-1-Cre mice via suppressing aldo-keto reductase family 1B10 (AKR1B10). Carcinogenesis 34:2090–2098. https://doi.org/10.1093/carcin/bgt170
Liou GY, Storz P (2010) Reactive oxygen species in cancer. Free Radic Res 44:479–496. https://doi.org/10.3109/10715761003667554
Liu H, Heaney AP (2011) Refined fructose and cancer. Expert Opin Ther Targets 15:1049–1059. https://doi.org/10.1517/14728222.2011.588208
Liu TA et al (2015) Regulation of Aldo-keto-reductase family 1 B10 by 14-3-3 epsilon and their prognostic impact of hepatocellular carcinoma. Oncotarget 6:38967–38982. https://doi.org/10.18632/oncotarget.5734
Liu W et al (2019a) AKR1B10 (Aldo-keto reductase family 1 B10) promotes brain metastasis of lung cancer cells in a multi-organ microfluidic chip model. Acta Biomater 91:195–208. https://doi.org/10.1016/j.actbio.2019.04.053
Liu Y et al (2019b) Compensatory upregulation of aldo-keto reductase 1B10 to protect hepatocytes against oxidative stress during hepatocarcinogenesis. Am J Cancer Res 9:2730–2748
Love MI, Huber W, Anders S (2014) Moderated estimation of fold change and dispersion for RNA-seq data with DESeq2. Genome Biol 15:550. https://doi.org/10.1186/s13059-014-0550-8
Ma J, Yan R, Zu X, Cheng JM, Rao K, Liao DF, Cao D (2008) Aldo-keto reductase family 1 B10 affects fatty acid synthesis by regulating the stability of acetyl-CoA carboxylase-α in breast cancer cells. J Biol Chem 283:3418–3423. https://doi.org/10.1074/jbc.M707650200
Ma J et al (2012) AKR1B10 overexpression in breast cancer: association with tumor size, lymph node metastasis and patient survival and its potential as a novel serum marker. Int J Cancer 131:E862–E871. https://doi.org/10.1002/ijc.27618
Macleod AK et al (2016) Aldo-keto reductases are biomarkers of NRF2 activity and are co-ordinately overexpressed in non-small cell lung cancer. Br J Cancer 115:1530–1539. https://doi.org/10.1038/bjc.2016.363
Marisa L et al (2013) Gene expression classification of colon cancer into molecular subtypes: characterization, validation, and prognostic value. PLoS Med 10:e1001453. https://doi.org/10.1371/journal.pmed.1001453
Martin HJ, Maser E (2009) Role of human aldo-keto-reductase AKR1B10 in the protection against toxic aldehydes. Chem Biol Interact 178:145–150. https://doi.org/10.1016/j.cbi.2008.10.021
Matsunaga T et al (2014a) Exposure to 9,10-phenanthrenequinone accelerates malignant progression of lung cancer cells through up-regulation of aldo-keto reductase 1B10. Toxicol Appl Pharmacol 278:180–189. https://doi.org/10.1016/j.taap.2014.04.024
Matsunaga T et al (2014b) Nitric oxide confers cisplatin resistance in human lung cancer cells through upregulation of aldo-keto reductase 1B10 and proteasome. Free Radic Res 48:1371–1385. https://doi.org/10.3109/10715762.2014.957694
Mindnich RD, Penning TM (2009) Aldo-keto reductase (AKR) superfamily: genomics and annotation. Hum Genomics 3:362–370. https://doi.org/10.1186/1479-7364-3-4-362
Mori M et al (2017) Aldo-keto reductase family 1 member B10 is associated with hepatitis B virus-related hepatocellular carcinoma risk. Hepatol Res 47:E85–E93. https://doi.org/10.1111/hepr.12725
Morikawa Y et al (2015) Acquisition of doxorubicin resistance facilitates migrating and invasive potentials of gastric cancer MKN45 cells through up-regulating Aldo-keto reductase 1B10. Chem Biol Interact 230:30–39. https://doi.org/10.1016/j.cbi.2015.02.005
Mounir M et al (2019) New functionalities in the TCGAbiolinks package for the study and integration of cancer data from GDC and GTEx. PLoS Comput Biol 15(3):e1006701. https://doi.org/10.1371/journal.pcbi.1006701
Müller T, Hengstermann A (2012) Nrf2: friend and foe in preventing cigarette smoking-dependent lung disease. Chem Res Toxicol 25:1805–1824. https://doi.org/10.1021/tx300145n
Nakarai C et al (2014) Expression of AKR1C3 and CNN3 as markers for detection of lymph node metastases in colorectal cancer. Clin Exp Med 15:333–341. https://doi.org/10.1007/s10238-014-0298-1
Nishinaka T, Miura T, Okumura M, Nakao F, Nakamura H, Terada T (2011) Regulation of aldo-keto reductase AKR1B10 gene expression: involvement of transcription factor Nrf2. Chem Biol Interact 191:185–191. https://doi.org/10.1016/j.cbi.2011.01.026
Ohashi T, Idogawa M, Sasaki Y, Suzuki H, Tokino T (2013) AKR1B10, a transcriptional target of p53, is downregulated in colorectal cancers associated with poor prognosis. Mol Cancer Res 11:1554–1563. https://doi.org/10.1158/1541-7786.MCR-13-0330-T
Ooi A et al (2011) An antioxidant response phenotype shared between hereditary and sporadic type 2 papillary renal cell carcinoma. Cancer Cell 20:511–523. https://doi.org/10.1016/j.ccr.2011.08.024
Palackal NT, Lee SH, Harvey RG, Blair IA, Penning TM (2002) Activation of polycyclic aromatic hydrocarbon trans-dihydrodiol proximate carcinogens by human aldo-keto reductase (AKR1C) enzymes and their functional overexpression in human lung carcinoma (A549) cells. J Biol Chem 277:24799–24808. https://doi.org/10.1074/jbc.M112424200
Penning TM (2005) AKR1B10: a new diagnostic marker of non-small cell lung carcinoma in smokers. Clin Cancer Res 11:1687–1690. https://doi.org/10.1158/1078-0432.CCR-05-0071
Penning TM (2015) The aldo-keto reductases (AKRs): overview. Chem Biol Interact 234:236–246. https://doi.org/10.1016/j.cbi.2014.09.024
Penning TM (2017) Aldo-Keto reductase regulation by the Nrf2 system: implications for stress response, chemotherapy drug resistance, and carcinogenesis. Chem Res Toxicol 30:162–176. https://doi.org/10.1021/acs.chemrestox.6b00319
Pollak N, Dölle C, Ziegler M (2007) The power to reduce: pyridine nucleotides – small molecules with a multitude of functions. Biochem J 402:205–218. https://doi.org/10.1042/BJ20061638
Quinn AM, Harvey RG, Penning TM (2008) Oxidation of PAH trans-dihydrodiols by human aldo-keto reductase AKR1B10. Chem Res Toxicol 21:2207–2215. https://doi.org/10.1021/tx8002005
Ramana KV, Srivastava SK (2006) Mediation of aldose reductase in lipopolysaccharide-induced inflammatory signals in mouse peritoneal macrophages. Cytokine 36:115–122. https://doi.org/10.1016/j.cyto.2006.11.003
Ramana KV, Tammali R, Srivastava SK (2010) Inhibition of aldose reductase prevents growth factor-induced g 1-s phase transition through the AKT/phosphoinositide 3-kinase/E2F-1 pathway in human colon cancer cells. Mol Cancer Ther 9:813–824. https://doi.org/10.1158/1535-7163.MCT-09-0795
Reczek CR, Chandel NS (2015) ROS-dependent signal transduction. Curr Opin Cell Biol 33:8–13. https://doi.org/10.1016/j.ceb.2014.09.010
Reddy AK, Uday Kumar P, Srinivasulu M, Triveni B, Sharada K, Ismail A, Bhanuprakash Reddy G (2017) Overexpression and enhanced specific activity of aldoketo reductases (AKR1B1 and AKR1B10) in human breast cancers. Breast 31:137–143. https://doi.org/10.1016/j.breast.2016.11.003
Röhrig F, Schulze A (2016) The multifaceted roles of fatty acid synthesis in cancer. Nat Rev Cancer 16:732–749. https://doi.org/10.1038/nrc.2016.89
Rojo de la Vega M, Chapman E, Zhang DD (2018) NRF2 and the hallmarks of cancer. Cancer Cell 34:21–43. https://doi.org/10.1016/j.ccell.2018.03.022
Ruiz FX et al (2009) Aldo-keto reductases from the AKR1B subfamily: retinoid specificity and control of cellular retinoic acid levels. Chem Biol Interact 178:171–177. https://doi.org/10.1016/j.cbi.2008.10.027
Saraswat M, Mrudula T, Kumar PU, Suneetha A, Rao TS, Srinivasulu M, Reddy GB (2006) Overexpression of aldose reductase in human cancer tissues. Med Sci Monit 12:CR525–CR529
Saraswathy R, Anand S, Kunnumpurath SK, Kurian RJ, Kaye AD, Vadivelu N (2014) Chromosomal aberrations and exon 1 mutation in the AKR1B1 gene in patients with diabetic neuropathy. Ochsner J 14:339–342
Sato S et al (2012) Up-regulated aldo-keto reductase family 1 member B10 in chronic hepatitis C: association with serum alpha-fetoprotein and hepatocellular carcinoma. Liver Int 32:1382–1390. https://doi.org/10.1111/j.1478-3231.2012.02827.x
Saxena A, Tammali R, Ramana KV, Srivastava SK (2012) Aldose reductase inhibition prevents colon cancer growth by restoring phosphatase and tensin homolog through modulation of miR-21 and FOXO3a. Antiox Redox Signal 18:1249–1262. https://doi.org/10.1089/ars.2012.4643
Saxena A, Shoeb M, Ramana KV, Srivastava SK (2013) Aldose reductase inhibition suppresses colon cancer cell viability by modulating microRNA-21 mediated programmed cell death 4 (PDCD4) expression. Eur J Cancer 49:3311–3319. https://doi.org/10.1016/j.ejca.2013.05.031
Schwab A et al (2018) Polyol pathway links glucose metabolism to the aggressiveness of cancer cells. Cancer Res 78:1604–1618. https://doi.org/10.1158/0008-5472.CAN-17-2834
Semmo N, Weber T, Idle JR, Beyoglu D (2015) Metabolomics reveals that aldose reductase activity due to AKR1B10 is upregulated in hepatitis C virus infection. J Viral Hepat 22:617–624. https://doi.org/10.1111/jvh.12376
Shen Y, Zhong L, Johnson S, Cao D (2011) Human aldo-keto reductases 1B1 and 1B10: a comparative study on their enzyme activity toward electrophilic carbonyl compounds. Chem Biol Interact 191:192–198. https://doi.org/10.1016/j.cbi.2011.02.004
Shen Y et al (2015) Impaired self-renewal and increased colitis and dysplastic lesions in colonic mucosa of AKR1B8-deficient mice. Clin Cancer Res 21:1466–1476. https://doi.org/10.1158/1078-0432.CCR-14-2072
Sheng X et al (2017) Adipocytes sequester and metabolize the chemotherapeutic daunorubicin. Mol Cancer Res 15:1704–1713. https://doi.org/10.1158/1541-7786.MCR-17-0338
Shoeb M, Ramana KV, Srivastavan SK (2013) Aldose reductase inhibition enhances TRAIL-induced human colon cancer cell apoptosis through AKT/FOXO3a-dependent upregulation of death receptors. Free Radic Biol Med 63:280–290. https://doi.org/10.1016/j.freeradbiomed.2013.05.039
Singh A et al (2006) Dysfunctional KEAP1-NRF2 interaction in non-small-cell lung cancer. PLoS Med 3:e420. https://doi.org/10.1371/journal.pmed.0030420
Skrzydlewska E, Sulkowski S, Koda M, Zalewski B, Kanczuga-Koda L, Sulkowska M (2005) Lipid peroxidation and antioxidant status in colorectal cancer. World J Gastroenterol 11:403–406. https://doi.org/10.3748/wjg.v11.i3.403
Srivastava S, Chandra A, Bhatnagar A, Srivastava SK, Ansari NH (1995) Lipid peroxidation product, 4-Hydroxynonenal and its conjugate with GSH are excellent substrates of bovine lens aldose reductase. Biochem Biophys Res Commun 217:741–746. https://doi.org/10.1006/bbrc.1995.2835
Srivastava SK, Ramana KV, Bhatnagar A (2005) Role of aldose reductase and oxidative damage in diabetes and the consequent potential for therapeutic options. Endocr Rev 26(3):380–392. https://doi.org/10.1210/er.2004-0028
Srivastava SK et al (2011) Aldose reductase inhibition suppresses oxidative stress-induced inflammatory disorders. Chem Biol Interact 191:330–338. https://doi.org/10.1016/j.cbi.2011.02.023
Stapelfeld C, Neumann KT, Maser E (2017) Different inhibitory potential of sex hormones on NNK detoxification in vitro: a possible explanation for gender-specific lung cancer risk. Cancer Lett 405:120–126. https://doi.org/10.1016/j.canlet.2017.07.016
Suzen S, Buyukbingol E (2005) Recent studies of aldose reductase enzyme inhibition for diabetic complications. Curr Med Chem 10:1329–1352. https://doi.org/10.2174/0929867033457377
Taguchi K, Yamamoto M (2021) The Keap1–Nrf2 system as a molecular target of cancer treatment. Cancers 13:1–21. https://doi.org/10.3390/cancers13010046
Tammali R, Ramana KV, Singhal SS, Awasthi S, Srivastava SK (2006) Aldose reductase regulates growth factor-induced cyclooxygenase-2 expression and prostaglandin E2 production in human colon cancer cells. Cancer Res 66:9705–9713. https://doi.org/10.1158/0008-5472.CAN-06-2105
Tammali R, Srivastava SK, Ramana KV (2011) Targeting aldose reductase for the treatment of cancer. Curr Cancer Drug Targets 11:560–571. https://doi.org/10.2174/156800911795655958
Tanawattanasuntorn T, Thongpanchang T, Rungrotmongkol T, Hanpaibool C, Graidist P, Tipmanee V (2021) (-)-Kusunokinin as a potential aldose reductase inhibitor: equivalency observed via AKR1B1 dynamics simulation. ACS Omega 6(1):606–614. https://doi.org/10.1021/acsomega.0c05102
Taskoparan B, Seza EG, Demirkol S, Tuncer S, Stefek M, Gure AO, Banerjee S (2017) Opposing roles of the aldo-keto reductases AKR1B1 and AKR1B10 in colorectal cancer. Cell Oncol (Dordr) 40:563–578. https://doi.org/10.1007/s13402-017-0351-7
Uchida K (2003) 4-Hydroxy-2-nonenal: a product and mediator of oxidative stress. Prog Lipid Res 42:318–343. https://doi.org/10.1016/S0163-7827(03)00014-6
van Weverwijk A et al (2019) Metabolic adaptability in metastatic breast cancer by AKR1B10-dependent balancing of glycolysis and fatty acid oxidation. Nat Commun 10(1):2698. https://doi.org/10.1038/s41467-019-10592-4
Wang J, Zhou Y, Fei X, Chen X, Chen Y (2018) Biostatistics mining associated method identifies AKR1B10 enhancing hepatocellular carcinoma cell growth and degenerated by miR-383-5p. Sci Rep 8:11094. https://doi.org/10.1038/s41598-018-29271-3
Wierenga RK (2001) The TIM-barrel fold: a versatile framework for efficient enzymes. FEBS Lett 492:193–198. https://doi.org/10.1016/S0014-5793(01)02236-0
Wu X et al (2017) AKR1B1 promotes basal-like breast cancer progression by a positive feedback loop that activates the EMT program. J Exp Med 214:1065–1079. https://doi.org/10.1084/jem.20160903
Yang L, Zhang J, Zhang S, Dong W, Lou X, Liu S (2013) Quantitative evaluation of aldo-keto reductase expression in hepatocellular carcinoma (HCC) cell lines. Genomics Proteomics Bioinformatics 11:230–240. https://doi.org/10.1016/j.gpb.2013.04.001
Zhang L et al (2013) Inhibitor selectivity between aldo-keto reductase superfamily members AKR1B10 and AKR1B1: role of Trp112 (Trp111). FEBS Lett 587:3681–3686. https://doi.org/10.1016/j.febslet.2013.09.031
Zhang W, Li H, Yang Y, Liao J, Yang GY (2014) Knockdown or inhibition of aldo-keto reductase 1B10 inhibits pancreatic carcinoma growth via modulating Kras-E-cadherin pathway. Cancer Lett 355:273–280. https://doi.org/10.1016/j.canlet.2014.09.031
Zhang J, Wang N, Li Q, Zhou Y, Luan Y (2021) A two-pronged photodynamic nanodrug to prevent metastasis of basal-like breast cancer. Chem Commun (Camb) Feb 3. https://doi.org/10.1039/d0cc08162k
Zhao JX et al (2017) Aldose reductase interacts with AKT1 to augment hepatic AKT/mTOR signaling and promote hepatocarcinogenesis. Oncotarget 8:66987–67000. https://doi.org/10.18632/oncotarget.17791
Zhong L, Liu Z, Yan R, Johnson S, Zhao Y, Fang X, Cao D (2009) Aldo-keto reductase family 1 B10 protein detoxifies dietary and lipid-derived alpha, beta-unsaturated carbonyls at physiological levels. Biochem Biophys Res Commun 387(2):245–250. https://doi.org/10.1016/j.bbrc.2009.06.123
Zhou Z, Zhao Y, Gu L, Niu X, Lu S (2018) Inhibiting proliferation and migration of lung cancer using small interfering RNA targeting on Aldo-keto reductase family 1 member B10. Mol Med Rep 17:2153–2160. https://doi.org/10.3892/mmr.2017.8173
Zu X et al (2016) Aldo-keto reductase 1B10 protects human colon cells from DNA damage induced by electrophilic carbonyl compounds. Mol Carcinog 56:118–129. https://doi.org/10.1002/mc.22477
Acknowledgements
Ilir Sheraj is gratefully acknowledged for analyzing TCGA data and generating Fig. 2. Cagdas Ermis is gratefully acknowledged for generating the images used in Fig. 1. Dr. Seçil Demirkol Canli, Esin Gulce Seza, Ilir Sheraj, Ismail Guderer and Cagdas Ermis are gratefully acknowledged for critically reading the manuscript. This work was supported by TUBITAK project 118Z688 and the COST action CA17118.
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Banerjee, S. (2021). Aldo Keto Reductases AKR1B1 and AKR1B10 in Cancer: Molecular Mechanisms and Signaling Networks. In: Turksen, K. (eds) Cell Biology and Translational Medicine, Volume 14. Advances in Experimental Medicine and Biology(), vol 1347. Springer, Cham. https://doi.org/10.1007/5584_2021_634
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