The Aldo-Keto Reductase Superfamily and its Role in Drug Metabolism and Detoxification

REFERENCES

• F. Aimond, S. P. Kwak, K. J. Rhodes, and J. M. Nerbonne. (2005). Accessory kv beta 1 subunits differentially modulate the functional expression of voltage-gated K+ channels in mouse ventricular myocytes. Circ. Res. 96:451–458.
   PubMed Web of Science ®Google Scholar
• R. Amaro, E. Tajkhorshid, and Z. Luthey-Schulten. (2003). Developing an energy landscape for the novel function of a (beta/alpha)8 barrel: ammonia conduction through HisF. Proc Natl Acad Sci U S A 100:7599–7604.
   PubMed Web of Science ®Google Scholar
• A. Atalla, U. Breyer-Pfaff, and E. Maser. (2000). Purification and characterization of oxidoreductases-catalyzing carbonyl reduction of the tobacco-specific nitrosamine 4-methylnitrosamino-1-(3-pyridyl)-1-butanone (NNK) in human liver cytosol. Xenobiotica 30:755–769.
   PubMed Web of Science ®Google Scholar
• A. Atalla, and E. Maser. (2001). Characterization of enzymes participating in carbonyl reduction of 4-methylnitrosamino-1-(3-pyridyl)-1-butanone (NNK) in human placenta. Chemico Biol Interact 130:737–748.
   PubMed Web of Science ®Google Scholar
• V. Avdonin, J. Kasuya, M. A. Ciorba, B. Kaplan, T. Hoshi, and L. Iverson. (1998). Apoptotic proteins Reaper and Grim induce stable inactivation in voltage-gated K+ channels. Proc Natl Acad Sci U S A 95:11703–11708.
   PubMed Web of Science ®Google Scholar
• Y. Azuma, T. Nishinaka, S. Ushijima, J. Soh, M. Katsuyama, H. P. Lu, and et al (2004). Characterization of htAKR, a novel gene product in the aldo-keto reductase family specifically expressed in human testis. Mol Hum Reprod 10:527–533.
   PubMed Web of Science ®Google Scholar
• N. R. Bachur. (1976). Cytoplasmic aldo-keto reductases: a class of drug metabolizing enzymes. Science 193:595–597.
   PubMed Web of Science ®Google Scholar
• O. A. Barski, K. H. Gabbay, and K. M. Bohren. (1996). The C-terminal loop of aldehyde reductase determines the substrate and inhibitor specificity. Biochemistry 35:14276–14280.
   PubMed Web of Science ®Google Scholar
• O. A. Barski, K. H. Gabbay, and K. M. Bohren. (1999). Characterization of the human aldehyde reductase gene and promoter. Genomics 60:188–198.
   PubMed Web of Science ®Google Scholar
• O. A. Barski, K. H. Gabbay, C. E. Grimshaw, and K. M. Bohren. (1995). Mechanism of human aldehyde reductase: characterization of the active site pocket. Biochemistry 34:11264–11275.
   PubMed Web of Science ®Google Scholar
• O. A. Barski, V. Z. Papusha, M. M. Ivanova, D. M. Rudman, and M. J. Finegold. (2005). Developmental expression and function of aldehyde reductase in proximal tubules of the kidney. Am J Physiol Renal Physiol 289:F200–F207.
   PubMed Web of Science ®Google Scholar
• O. A. Barski, V. Z. Papusha, G. R. Kunkel, and K. H. Gabbay. (2004). Regulation of aldehyde reductase expression by STAF and CHOP. Genomics 83:119–129.
   PubMed Web of Science ®Google Scholar
• D. R. Bauman, S. I. Rudnick, L. M. Szewczuk, Y. Jin, S. Gopishetty, and T. M. Penning. (2005). Development of nonsteroidal anti-inflammatory drug analogs and steroid carboxylates selective for human aldo-keto reductase isoforms: potential antineoplastic agents that work independently of cyclo-oxygenase isozymes. Mol Pharmacol 67:60–68.
   PubMed Web of Science ®Google Scholar
• J. W. Baynes, and S. R. Thorpe. (1999). Role of oxidative stress in diabetic complications: a new perspective on an old paradigm. Diabetes 48:1–9.
   PubMed Web of Science ®Google Scholar
• M. J. Bennett, R. H. Albert, J. M. Jez, H. Ma, T. M. Penning, and M. Lewis. (1997). Steroid recognition and regulation of hormone action: crystal structure of testosterone and NADP+ bound to 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase. Structure 5:799–812.
   PubMed Web of Science ®Google Scholar
• M. J. Bennett, B. P. Schlegel, J. M. Jez, T. M. Penning, and M. Lewis. (1996). Structure of 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase complexed with NADP+. Biochemistry 35:10702–10711.
   PubMed Web of Science ®Google Scholar
• J. A. Berliner, M. C. Territo, A. Sevanian, S. Ramin, J. A. Kim, B. Bamshad, and et al (1990). Minimally modified low-density lipoprotein stimulates monocyte endothelial interactions. J Clin Invest 85:1260–1266.
   PubMed Web of Science ®Google Scholar
• A. Bhatnagar, S. Liu, B. Das, N. H. Ansari, and S. K. Srivastava. (1990). Inhibition-kinetics of human kidney aldose and aldehyde reductases by aldose reductase inhibitors. Biochem Pharmacol 39:1115–1124.
   PubMed Web of Science ®Google Scholar
• A. Bhatnagar, S. Q. Liu, S. Srivastava, K. V. Ramana, and S. K. Srivastava. (2004). Aldose reductase and the stress response. Aldo-Keto Reductases Toxicant Metab 865:199–211.
   Google Scholar
• A. Bhatnagar, S. Q. Liu, N. Ueno, B. Chakrabarti, and S. K. Srivastava. (1994). Human placental aldose reductase: role of Cys-298 in substrate and inhibitor binding. Biochim Biophys Acta 1205:207–214.
   PubMed Web of Science ®Google Scholar
• A. Bhatnagar, and S. K. Srivastava. (1992). Aldose reductase: congenial and injurious profiles of an enigmatic enzyme. Biochem Med Metab Biol 48:91–121.
   PubMedGoogle Scholar
• K. M. Bohren, O. A. Barski, and K. G. Gabbay. Characterization of a novel murine aldo-keto reductaseEnzymology and Molecular Biology of Carbonyl Metabolism 6 Weiner, and et al, and Plenum Press, New York, (1996) 455–464.
   Google Scholar
• K. M. Bohren, C. E. Grimshaw, C. J. Lai, D. H. Harrison, D. Ringe, G. A. Petsko, and et al (1994). Tyrosine-48 is the proton donor and histidine-110 directs substrate stereochemical selectivity in the reduction reaction of human aldose reductase: enzyme kinetics and crystal structure of the Y48H mutant enzyme. Biochemistry 33:2021–2032.
   PubMed Web of Science ®Google Scholar
• K. M. Bohren, J. L. Page, R. Shankar, S. P. Henry, and K. H. Gabbay. (1991). Expression of human aldose and aldehyde reductases. Site-directed mutagenesis of a critical lysine 262. J Biol Chem 266:24031–24037.
   PubMed Web of Science ®Google Scholar
• W. F. Bosron, and R. L. Prairie. (1972). Triphosphopyridine nucleotide-linked aldehyde reductase. I. Purification and properties of the enzyme from pig kidney cortex. J Biol Chem 247:4480–4485.
   PubMed Web of Science ®Google Scholar
• G. Branlant. (1982). Properties of an aldose reductase from pig lens. Comparative studies of an aldehyde reductase from pig lens. Eur J Biochem 129:99–104.
   PubMedGoogle Scholar
• G. Branlant, and J. F. Biellmann. (1980). Purification and some properties of aldehyde reductases from pig liver. Eur J Biochem 105:611–621.
   PubMedGoogle Scholar
• U. Breyer-Pfaff, H. J. Martin, M. Ernst, and E. Maser. (2004). Enantioselectivity of carbonyl reduction of 4-methylnitrosamino-1(3-pyridyl)-1-butanone by tissue fractions from human and rat and by enzymes isolated from human liver. Drug Metab Dispos 32:915–922.
   PubMed Web of Science ®Google Scholar
• U. Breyer-Pfaff, and K. Nill. (2000). High-affinity stereoselective reduction of the enantiomers of ketotifen and of ketonic nortriptyline metabolites by aldo-keto reductases from human liver. Biochem Pharmacol 59:249–260.
   PubMed Web of Science ®Google Scholar
• U. Breyer-Pfaff, and K. Nill. (2004). Carbonyl reduction of naltrexone and dolasetron by oxidoreductases isolated from human liver cytosol. J Pharm Pharmacol 56:1601–1606.
   PubMed Web of Science ®Google Scholar
• V. Bril, and R. A. Buchanan. (2006). Long-term effects of ranirestat (AS-3201) on peripheral nerve function in patients with diabetic sensorimotor polyneuropathy. Diabetes Care 29:68–72.
   PubMed Web of Science ®Google Scholar
• M. Brownlee. (1992). Glycation products and the pathogenesis of diabetic complications. Diabetes Care 15:1835–1843.
   PubMed Web of Science ®Google Scholar
• M. Brownlee. (2001). Biochemistry and molecular cell biology of diabetic complications. Nature 414:813–820.
   PubMed Web of Science ®Google Scholar
• M. E. Burczynski, H. K. Lin, and T. M. Penning. (1999). Isoform-specific induction of a human aldo-keto reductase by polycyclic aromatic hydrocarbons (PAHs), electrophiles, and oxidative stress: implications for the alternative pathway of PAH activation catalyzed by human dihydrodiol dehydrogenase. Cancer Res 59:607–614.
   PubMed Web of Science ®Google Scholar
• A. Buzzi, Y. Wu, M. V. Frantseva, J. L. P. Velazquez, M. A. Cortez, C. C. Liu, and et al (2006). Succinic semialdehyde dehydrogenase deficiency: GABA(B) receptor-mediated function. Brain Res 1090:15–22.
   PubMed Web of Science ®Google Scholar
• M. C. Byrns, S. Steckelbroeck, and T. M. Penning. (2008). An indomethacin analogue, N-(4-chlorobenzoyl)-melatonin, is a selective inhibitor of aldo-keto reductase 1C3 (type 2 3alpha-HSD, type 5 17beta-HSD, and prostaglandin F synthase), a potential target for the treatment of hormone dependent and hormone independent malignancies. Biochem Pharmacol 75:484–493.
   PubMed Web of Science ®Google Scholar
• M. Campbell, and E. R. Trimble. (2005). Modification of PI3K and MAPK-dependent chemotaxis in aortic vascular smooth muscle cells by protein kinase C betaII. Circ Res 96:197–206.
   PubMed Web of Science ®Google Scholar
• C. R. Campomanes, K. I. Carroll, L. N. Manganas, M. E. Hershberger, B. Gong, D. E. Antonucci, and et al (2002). Kv beta subunit oxidoreductase activity and Kv1 potassium channel trafficking. J Biol.Chem 277:8298–8305.
   PubMed Web of Science ®Google Scholar
• F. Camu, C. Van Lersberghe, and M. H. Lauwers. (1992). Cardiovascular risks and benefits of perioperative nonsteroidal anti-inflammatory drug treatment. Drugs 44 (Suppl 5):42–51.
   PubMedGoogle Scholar
• D. Cao, S. T. Fan, and S. M. Chung. (1998). Identification and characterization of a novel human aldose reductase-like gene. J Biol Chem 273:11429–11435.
   PubMed Web of Science ®Google Scholar
• W. H. Chang. (1992). Reduced haloperidol—a factor in determining the therapeutic benefit of haloperidol treatment. Psychopharmacology 106:289–296.
   PubMed Web of Science ®Google Scholar
• D. B. Chen, S. D. Westfall, H. W. Fong, M. S. Roberson, and J. S. Davis. (1998). Prostaglandin F2alpha stimulates the Raf/MEK1/mitogen-activated protein kinase signaling cascade in bovine luteal cells. Endocrinology 139:3876–3885.
   PubMed Web of Science ®Google Scholar
• S. S. M. Chung, and S. K. Chung. (2003). Genetic analysis of aldose reductase in diabetic complications. Curr Med Chem 10:1375–1387.
   PubMed Web of Science ®Google Scholar
• J. X. Connor, K. McCormack, A. Pletsch, S. Gaeta, B. Ganetzky, S. Y. Chiu, and et al (2005). Genetic modifiers of the Kv beta 2-null phenotype in mice. Genes Brain Behav 4:77–88.
   PubMed Web of Science ®Google Scholar
• B. Crosas, D. J. Hyndman, O. Gallego, S. Martras, X. Pares, T. G. Flynn, and et al (2003). Human aldose reductase and human small intestine aldose reductase are efficient retinal reductases: consequences for retinoid metabolism. Biochem J 373:973–979.
   PubMed Web of Science ®Google Scholar
• S. T. Davidge. (2001). Prostaglandin H synthase and vascular function. Circ Res 89:650–660.
   PubMed Web of Science ®Google Scholar
• W. S. Davidson, D. J. Walton, and T. G. Flynn. (1978). A comparative study of the tissue and species distribution of NADPH-dependent aldehyde reductase. Comp Biochem Physiol B 60:309–315.
   PubMed Web of Science ®Google Scholar
• A. G. Demaine. (2003). Polymorphisms of the aldose reductase gene and susceptibility to diabetic microvascular complications. Curr Med Chem 10:1389–1398.
   PubMed Web of Science ®Google Scholar
• J. C. Desmond, J. C. Mountford, M. T. Drayson, E. A. Walker, M. Hewison, J. P. Ride, and et al (2003). The aldo-keto reductase AKR1C3 is a novel suppressor of cell differentiation that provides a plausible target for the non-cyclo-oxygenase-dependent antineoplastic actions of nonsteroidal anti-inflammatory drugs. Cancer Res 63:505–512.
   PubMed Web of Science ®Google Scholar
• Y. Deyashiki, K. Ohshima, M. Nakanishi, K. Sato, K. Matsuura, and A. Hara. (1995). Molecular cloning and characterization of mouse estradiol 17 beta- dehydrogenase (A-specific), a member of the aldoketoreductase family. J Biol Chem 270:10461–10467.
   PubMed Web of Science ®Google Scholar
• U. Dhagat, V. Carbone, R. P. T. Chung, C. Schulze-Briese, S. Endo, A. Hara, and et al (2007). Structure of 3(17)alpha-hydroxysteroid dehydrogenase (AKR1C21) holoenzyme from an orthorhombic crystal form: an insight into the bifunctionality of the enzyme. Acta Crystallograph Sect F Struct Biol Cryst Comm 63:825–830.
   PubMed Web of Science ®Google Scholar
• U. Dhagat, S. Endo, A. Hara, and O. El Kabbani. (2008a). Inhibition of 3(17)alpha-hydroxysteroid dehydrogenase (AKR1C21) by aldose reductase inhibitors. Bioorg Med Chem 16:3245–3254.
   PubMed Web of Science ®Google Scholar
• U. Dhagat, S. Endo, R. Sumii, A. Hara, and O. El Kabbani. (2008b). Selectivity determinants of inhibitor binding to human 20alpha-hydroxysteroid dehydrogenase: crystal structure of the enzyme in ternary complex with coenzyme and the potent inhibitor 3,5-dichlorosalicylic acid. J Med Chem 51:4844–4848.
   PubMed Web of Science ®Google Scholar
• B. Dozier, K. Watanabe, and D. Duffy. Two pathways for prostaglandin F2{alpha} (PGF2{alpha}) synthesis by the primate periovulatory follicleReproduction., (2008) 13653–63.
   Google Scholar
• Y. Du, S. Tsai, J. R. Keller, and S. C. Williams. (2000). Identification of an interleukin-3-regulated aldoketo reductase gene in myeloid cells which may function in autocrine regulation of myelopoiesis. J Biol Chem 275:6724–6732.
   PubMed Web of Science ®Google Scholar
• E. Dvornik, N. Simard-Duquesne, M. Krami, K. Sestanj, K. H. Gabbay, J. H. Kinoshita, and et al (1973). Polyol accumulation in galactosemic and diabetic rats: control by an aldose reductase inhibitor. Science 182:1146–1148.
   PubMed Web of Science ®Google Scholar
• P. J. Dyck, B. R. Zimmerman, T. H. Vilen, S. R. Minnerath, J. L. Karnes, J. K. Yao, and et al (1988). Nerve glucose, fructose, sorbitol, myo-inositol, and fiber degeneration and regeneration in diabetic neuropathy. N Engl J Med 319:542–548.
   PubMed Web of Science ®Google Scholar
• R. P. Eaton, W. L. SibbittJr., and A Harsh. (1985). The effect of an aldose reductase inhibiting agent on limited joint mobility in diabetic patients. JAMA 253:1437–1440.
   PubMed Web of Science ®Google Scholar
• T. Ehrig, K. M. Bohren, F. G. Prendergast, and K. H. Gabbay. (1994). Mechanism of aldose reductase inhibition: binding of NADP+/NADPH and alrestatin-like inhibitors. Biochemistry 33:7157–7165.
   PubMed Web of Science ®Google Scholar
• O el-Kabbani, K. Judge, S. L. Ginell, D. A. Myles, L. J. DeLucas, and T. G. Flynn. (1995). Structure of porcine aldehyde reductase holoenzyme. Nat Struct Biol 2:687–692.
   PubMedGoogle Scholar
• E. M. Ellis. (2002). Microbial aldo-keto reductases. FEMS Microbiol Lett 216:123–131.
   PubMed Web of Science ®Google Scholar
• E. M. Ellis, D. J. Judah, G. E. Neal, and J. D. Hayes. (1993). An ethoxyquin-inducible aldehyde reductase from rat liver that metabolizes aflatoxin B1 defines a subfamily of aldo-keto reductases. Proc Natl Acad Sci U S A 90:10350–10354.
   PubMed Web of Science ®Google Scholar
• S. Endo, K. Matsumoto, T. Matsunaga, S. Ishikura, K. Tajima, O. El Kabbani, and et al (2006). Substrate specificity of a mouse aldo-keto reductase (AKR1C12). Biol Pharmaceut Bull 29:2488–2492.
   PubMed Web of Science ®Google Scholar
• S. Endo, T. Matsunaga, K. Horie, K. Tajima, Y. Bunai, V. Carbone, and et al (2007). Enzymatic characteristics of an aldo-keto reductase family protein (AKR1C15) and its localization in rat tissues. Arch Biochem Biophys 465:136–147.
   PubMed Web of Science ®Google Scholar
• S. K. England, V. N. Uebele, J. Kodali, P. B. Bennett, and M. M. Tamkun. (1995). A Novel K+ channel beta-subunit (Hkv-beta-1.3) is produced via alternative messenger—RNA splicings. J Biol Chem 270:28531–28534.
   PubMed Web of Science ®Google Scholar
• H. Esterbauer, R. J. Schaur, and H. Zollner. (1991). Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde, and related aldehydes. Free Radic Biol Med 11:81–128.
   PubMed Web of Science ®Google Scholar
• F. Faucher, L. Cantin, K. P. Jesus-Tran, M. Lemieux, V. Luu-The, F. Labrie, and et al (2007). Mouse 17-alpha-hydroxysteroid dehydrogenase (AKR1C21) binds steroids differently from other aldo-keto reductases: identification and characterization of amino acid residues critical for substrate binding. J Mol Biol 369:525–540.
   PubMed Web of Science ®Google Scholar
• M. S. Feather, T. G. Flynn, K. A. Munro, T. J. Kubiseski, and D. J. Walton. (1995). Catalysis of reduction of carbohydrate 2-oxoaldehydes (osones) by mammalian aldose reductase and aldehyde reductase. Biochim Biophys Acta 1244:10–16.
   PubMed Web of Science ®Google Scholar
• M. Fink, F. Duprat, F. Lesage, C. Heurteaux, G. Romey, J. Barhanin, and et al (1996). A new K+ channel beta subunit to specifically enhance Kv2.2 (CDRK) expression. J Biol Chem 271:26341–26348.
   PubMed Web of Science ®Google Scholar
• Y. Fujii, K. Watanabe, H. Hayashi, Y. Urade, S. Kuramitsu, H. Kagamiyama, and et al (1990). Purification and characterization of Rho-crystallin from Japanese common bullfrog lens. J Biol Chem 265:9914–9923.
   PubMed Web of Science ®Google Scholar
• S. Fukumoto, N. Yamauchi, H. Moriguchi, Y. Hippo, A. Watanabe, J. Shibahara, and 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.
   PubMed Web of Science ®Google Scholar
• K. H. Gabbay. (1975). Hyperglycemia, polyol metabolism, and complications of diabetes mellitus. Annu Rev Med 26:521–536.
   PubMed Web of Science ®Google Scholar
• K. H. Gabbay. (2004). Aldose reductase inhibition in the treatment of diabetic neuropathy: where are we in 2004?. Curr Diab Rep 4:405–408.
   PubMedGoogle Scholar
• K. H. Gabbay, L. O. Merola, and R. A. Field. (1966). Sorbitol pathway: presence in nerve and cord with substrate accumulation in diabetes. Science 151:209–210.
   PubMed Web of Science ®Google Scholar
• O. Gallego, O. V. Belyaeva, S. Porte, F. X. Ruiz, A. V. Stetsenko, E. V. Shabrova, and et al, and Comparative functional analysis of human medium-chain dehydrogenases, short-chain dehydrogenases/reductases, and aldo-keto reductases with retinoidsBiochem J. (2006) 399101–109.
   Google Scholar
• O. Gallego, F. X. Ruiz, A. Ardevol, M. Dominguez, R. Alvarez, A. R. de Lera, and 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.
   PubMed Web of Science ®Google Scholar
• R. Gardner, S. Kazi, and E. M. Ellis. (2004). Detoxication of the environmental pollutant acrolein by a rat liver aldo-keto reductase. Toxicol Lett 148:65–72.
   PubMed Web of Science ®Google Scholar
• V. Gersl, Y. Mazurova, J. Bajgar, M. Melka, R. Hrdina, and V. Palicka. (1996). Lack of cardiotoxicity of a new antineoplastic agent, a synthetic derivative of indenoisochinoline: comparison with daunorubicin in rabbits. Arch Toxicol 70:645–651.
   PubMed Web of Science ®Google Scholar
• K. M. Gibson, G. F. Hoffmann, A. K. Hodson, T. Bottiglieri, and C. Jakobs. (1998). 4-hydroxybutyric acid and the clinical phenotype of succinic semialdehyde dehydrogenase deficiency, an inborn error of GABA metabolism. Neuropediatrics 29:14–22.
   PubMed Web of Science ®Google Scholar
• K. P. Giese, J. F. Storm, D. Reuter, N. B. Fedorov, L. R. Shao, T. Leicher, and et al (1998). Reduced K+ channel inactivation, spike broadening, and after-hyperpolarization in Kv beta 1.1-deficient mice with impaired learning. Learn Mem 5:257–273.
   PubMed Web of Science ®Google Scholar
• C. K. Glass, and J. L. Witztum. (2001). Atherosclerosis: the road ahead. Cell 104:503–516.
   PubMed Web of Science ®Google Scholar
• J. P. Gonzalez, and R. N. Brogden. (1988). Naltrexone—a review of Its pharmacodynamic and pharmacokinetic properties and therapeutic efficacy in the management of opioid dependence. Drugs 35:192–213.
   PubMed Web of Science ®Google Scholar
• C. E. Grimshaw. (1992). Aldose reductase: model for a new paradigm of enzymic perfection in detoxification catalysts. Biochemistry 31:10139–10145.
   PubMed Web of Science ®Google Scholar
• C. E. Grimshaw, K. M. Bohren, C. J. Lai, and K. H. Gabbay. (1995). Human aldose reductase—rate constants for a mechanism including interconversion of ternary complexes by recombinant wild-type enzyme. Biochemistry 34:14356–14365.
   PubMed Web of Science ®Google Scholar
• C. Gu, Y. N. Jan, and L. Y. Jan. (2003). A conserved domain in axonal targeting of Kv1 (Shaker) voltage-gated potassium channels. Science 301:646–649.
   PubMed Web of Science ®Google Scholar
• F. P. Guengerich, H. Cai, M. McMahon, J. D. Hayes, T. R. Sutter, J. D. Groopman, and et al (2001). Reduction of aflatoxin B1 dialdehyde by rat and human aldo-keto reductases. Chem Res Toxicol 14:727–737.
   PubMed Web of Science ®Google Scholar
• T. Gui, T. Tanimoto, Y. Kokai, and C. Nishimura. (1995). Presence of a closely related subgroup in the aldo-ketoreductase family of the mouse. Eur J Biochem 227:448–453.
   PubMedGoogle Scholar
• J. M. Gulbis, S. Mann, and R. MacKinnon. (1999). Structure of a voltage-dependent K+ channel beta subunit. Cell 97:943–952.
   PubMed Web of Science ®Google Scholar
• J. M. Gulbis, M. Zhou, S. Mann, and R. MacKinnon. (2000). Structure of the cytoplasmic beta subunit-T1 assembly of voltage-dependent K+ channels. Science 289:123–127.
   PubMed Web of Science ®Google Scholar
• A. Hara, K. Hasebe, M. Hayashibara, K. Matsuura, T. Nakayama, and H. Sawada. (1986). Dihydrodiol dehydrogenases in guinea pig liver. Biochem Pharmacol 35:4005–4012.
   PubMed Web of Science ®Google Scholar
• D. H. Harrison, K. M. Bohren, D. Ringe, G. A. Petsko, and K. H. Gabbay. (1994). An anion binding site in human aldose reductase: mechanistic implications for the binding of citrate, cacodylate, and glucose 6-phosphate. Biochemistry 33:2011–2020.
   PubMed Web of Science ®Google Scholar
• H. Hayashi, Y. Fujii, K. Watanabe, and O. Hayaishi. (1990). Enzymatic formation of prostaglandin-F2-alpha in human brain. Neurochem Res 15:385–392.
   PubMed Web of Science ®Google Scholar
• J. D. Hayes, D. J. Judah, L. I. McLellan, and G. E. Neal. (1991). Contribution of the glutathione S-transferases to the mechanisms of resistance to aflatoxin B1. Pharmacol Ther 50:443–472.
   PubMed Web of Science ®Google Scholar
• J. D. Hayes, D. J. Judah, and G. E. Neal. (1993). Resistance to aflatoxin B1 is associated with the expression of a novel aldo-keto reductase which has catalytic activity towards a cytotoxic aldehyde-containing metabolite of the toxin. Cancer Res 53:3887–3894.
   PubMed Web of Science ®Google Scholar
• H. Hegyi, and M. Gerstein. (1999). The relationship between protein structure and function: a comprehensive survey with application to the yeast genome. J Mol Biol 288:147–164.
   PubMed Web of Science ®Google Scholar
• V. V. Heredia, and T. M. Penning. (2004). Dissection of the physiological interconversion of 5 alpha-DHT and 3 alpha-diol by rat 3 alpha-HSD via transient kinetics shows that the chemical step is rate-determining: effect of mutating cofactor and substrate-binding pocket residues on catalysis. Biochemistry 43:12028–12037.
   PubMed Web of Science ®Google Scholar
• H. G. Hers. (1960). [Aldose reductase.]. Biochim Biophys Acta 37:120–126.
   PubMed Web of Science ®Google Scholar
• Y. Higaki, N. Usami, S. Shintani, S. Ishikura, O. El Kabbani, and A. Hara. (2003). Selective and potent inhibitors of human 20 alpha-hydroxysteroid dehydrogenase (AKR1C1) that metabolizes neurosteroids derived from progesterone. Chemico Biol Interact 143:503–513.
   PubMed Web of Science ®Google Scholar
• A. Hinshelwood, G. McGarvie, and E. Ellis. (2002a). Characterisation of a novel mouse liver aldo-keto reductase AKR7A5. FEBS Lett 523:213–218.
   PubMed Web of Science ®Google Scholar
• A. Hinshelwood, G. McGarvie, and E. Ellis. (2002b). Characterisation of a novel mouse liver aldo-keto reductase AKR7A5. FEBS Lett 523:213–218.
   PubMed Web of Science ®Google Scholar
• A. Hinshelwood, G. McGarvie, and E. M. Ellis. (2003). Substrate specificity of mouse aldo-keto reductase AKR7A5. Chemico Biol Interact 143:263–269.
   PubMed Web of Science ®Google Scholar
• H. T. Ho, S. K. Chung, J. W. Law, B. C. Ko, S. C. Tam, H. L. Brooks, and et al (2000). Aldose reductase-deficient mice develop nephrogenic diabetes insipidus. Mol Cell Biol 20:5840–5846.
   PubMed Web of Science ®Google Scholar
• B. Hocker, J. Claren, and R. Sterner. (2004). Mimicking enzyme evolution by generating new (beta-alpha)8-barrels from (beta-alpha)4-half-barrels. Proc Natl Acad Sci U S A 101:16448–16453.
   PubMed Web of Science ®Google Scholar
• P. L. Hoffman, B. Wermuth, and J. P. von Wartburg. (1980). Human brain aldehyde reductases: relationship to succinic semialdehyde reductase and aldose reductase. J Neurochem 35:354–366.
   PubMed Web of Science ®Google Scholar
• S. Horiuchi. (2002). The liver is the main site for metabolism of circulating advanced glycation end products. J Hepatol 36:123–125.
   PubMed Web of Science ®Google Scholar
• S. Horkko, D. A. Bird, E. Miller, H. Itabe, N. Leitinger, G. Subbanagounder, and et al (1999). Monoclonal autoantibodies specific for oxidized phospholipids or oxidized phospholipid-protein adducts inhibit macrophage uptake of oxidized low-density lipoproteins. J Clin Invest 103:117–128.
   PubMed Web of Science ®Google Scholar
• Z. L. Huang, Y. Urade, and O. Hayaishi. (2007). Prostaglandins and adenosine in the regulation of sleep and wakefulness. Curr Opin Pharmacol 7:33–38.
   PubMed Web of Science ®Google Scholar
• J. B. Hutchison, and T. Steimer. (1981). Brain 5beta-reductase: a correlate of behavioral sensitivity to androgen. Science 213:244–246.
   PubMed Web of Science ®Google Scholar
• D. J. Hyndman, and T. G. Flynn. (1998). Sequence and expression levels in human tissues of a new member of the aldo-keto reductase family. Biochim Biophys Acta Gene Struct Expr 1399:198–202.
   PubMed Web of Science ®Google Scholar
• S. Ikeda, E. Okuda-Ashitaka, Y. Masu, T. Suzuki, K. Watanabe, M. Nakao, and et al (1999). Cloning and characterization of two novel aldo-keto reductases (AKR1C12 and AKR1C13) from mouse stomach. FEBS Lett 459:433–437.
   PubMed Web of Science ®Google Scholar
• Y. Imamura, K. Sanai, K. Seri, and H. Akita. (2001). Hypoglycemic effect of S(-)-hydroxyhexamide, a major metabolite of acetohexamide, and its enantiomer R(+)-hydroxyhexamide. Life Sci 69:1947–1955.
   PubMed Web of Science ®Google Scholar
• Y. Imamura, and H. Shimada. (2005). Differential pharmacokinetics of acetohexamide in male Wistar-Imamichi and Sprague-Dawley rats: role of microsomal carbonyl reductase. Biol Pharm Bull 28:185–187.
   PubMed Web of Science ®Google Scholar
• L. S. Ireland, D. J. Harrison, G. E. Neal, and J. D. Hayes. (1998). Molecular cloning, expression, and catalytic activity of a human AKR7 member of the aldo-keto reductase superfamily: evidence that the major 2-carboxybenzaldehyde reductase from human liver is a homologue of rat aflatoxin B1-aldehyde reductase. Biochem J 332:21–34.
   PubMed Web of Science ®Google Scholar
• M. Ishida, J. H. Choi, K. Hirabayashi, T. Matsuwaki, M. Suzuki, K. Yamanouchi, and et al (2007). Reproductive phenotypes in mice with targeted disruption of the 20 alpha-hydroxysteroid dehydrogenase gene. J Reprod Dev 53:499–508.
   PubMed Web of Science ®Google Scholar
• M. Ishida, K. Hirabayashi, M. Suzuki, K. Yamanouchi, and M. Nishihara. (2003). Cloning and chromosomal localization of mouse 20 alpha-hydroxysteroid dehydrogenase gene. J Reprod Dev 49:79–85.
   PubMed Web of Science ®Google Scholar
• S. Ishikura, N. Usami, S. Nakajima, A. Kameyama, H. Shiraishi, V. Carbone, and et al (2004). Characterization of two isoforms of mouse 3(17)alpha-hydroxysteroid dehydrogenases of the aldo-keto reductase family. Biol Pharm Bull 27:1939–1945.
   PubMed Web of Science ®Google Scholar
• J. Jaspan, R. Maselli, K. Herold, and C. Bartkus. (1983). Treatment of severely painful diabetic neuropathy with an aldose reductase inhibitor: relief of pain and improved somatic and autonomic nerve function. Lancet 2:758–762.
   PubMed Web of Science ®Google Scholar
• J. M. Jez, M. J. Bennett, B. P. Schlegel, M. Lewis, and T. M. Penning. (1997a). Comparative anatomy of the aldo-keto reductase superfamily. Biochem J 326:625–636.
   PubMed Web of Science ®Google Scholar
• J. M. Jez, T. G. Flynn, and T. M. Penning. (1997b). A new nomenclature for the aldo-keto reductase superfamily. Biochem Pharmacol 54:639–647.
   PubMed Web of Science ®Google Scholar
• J. M. Jez, B. P. Schlegel, and T. M. Penning. (1996). Characterization of the substrate binding site in rat liver 3alpha- hydroxysteroid/dihydrodiol dehydrogenase. The roles of tryptophans in ligand binding and protein fluorescence. J Biol Chem 271:30190–30198.
   PubMed Web of Science ®Google Scholar
• Q. Ji, C. Aoyama, P. K. Chen, A. Stolz, and P. Liu. (2005). Localization and altered expression of AKR1C family members in human ovarian tissues. Mol Cell Probes 19:261–266.
   PubMed Web of Science ®Google Scholar
• Q. Ji, L. Chang, D. VanDenBerg, F. Z. Stanczyk, and A. Stolz. (2003). Selective reduction of AKR1C2 in prostate cancer and its role in DHT metabolism. Prostate 54:275–289.
   PubMed Web of Science ®Google Scholar
• Y. Jin, and T. M. Penning. (2006). Multiple steps determine the overall rate of the reduction of 5 alpha-dihydrotestosterone catalyzed by human type 3 3 alpha-hydroxysteroid dehydrogenase: implications for the elimination of androgens. Biochemistry 45:13054–13063.
   PubMed Web of Science ®Google Scholar
• Y. Jin, and T. M. Penning. (2007). Aldo-keto reductases and bioactivation/detoxication. Annu Rev Pharmacol Toxicol 47:263–292.
   PubMed Web of Science ®Google Scholar
• D. N. Johnson, P. A. Egner, G. Obrian, N. Glassbrook, B. D. Roebuck, T. R. Sutter, and et al (2008). Quantification of urinary aflatoxin b1 dialdehyde metabolites formed by aflatoxin aldehyde reductase using isotope dilution tandem mass spectrometry. Chem Res Toxicol 21:752–760.
   PubMed Web of Science ®Google Scholar
• H. Jornvall, B. Persson, M. Krook, S. Atrian, R. Gonzalezduarte, J. Jeffery, and et al (1995). Short-chain dehydrogenases reductases (Sdr). Biochemistry 34:6003–6013.
   PubMed Web of Science ®Google Scholar
• C. Jurgens, A. Strom, D. Wegener, S. Hettwer, M. Wilmanns, and R. Sterner. (2000). Directed evolution of a (beta alpha)8-barrel enzyme to catalyze related reactions in two different metabolic pathways. Proc Natl Acad Sci U S A 97:9925–9930.
   PubMed Web of Science ®Google Scholar
• G. Jurgens, Q. Chen, H. Esterbauer, S. Mair, G. Ledinski, and H. P. Dinges. (1993). Immunostaining of human autopsy aortas with antibodies to modified apolipoprotein B and apoprotein(a). Arterioscler Thromb 13:1689–1699.
   PubMed Web of Science ®Google Scholar
• P. F. Kador, and N. E. Sharpless. (1983). Pharmacophor requirements of the aldose reductase inhibitor site. Mol Pharmacol 24:521–531.
   PubMed Web of Science ®Google Scholar
• H. Kaiserova, and E. Kvasnickova. (2005). Inhibition study of rabbit liver cytosolic reductases involved in daunorubicin toxication. J Enz Inhib Med Chem 20:477–483.
   PubMed Web of Science ®Google Scholar
• K. Kaiserova, S. Srivastava, J. D. Hoetker, S. O. Awe, X. L. Tang, J. Cai, and et al (2006). Redox activation of aldose reductase in the ischemic heart. J Biol Chem 281:15110–15120.
   PubMed Web of Science ®Google Scholar
• K. Kaiserova, X. L. Tang, S. Srivastava, and A. Bhatnagar. (2008). Role of nitric oxide in regulating aldose reductase activation in the ischemic heart. J Biol Chem 283:9101–9112.
   PubMed Web of Science ®Google Scholar
• Y. Kallberg, U. Oppermann, H. Jornvall, and B. Persson. (2002a). Short-chain dehydrogenase/reductase (SDR) relationships: a large family with eight clusters common to human, animal, and plant genomes. Prot Sci 11:636–641.
   PubMed Web of Science ®Google Scholar
• Y. Kallberg, U. Oppermann, H. Jornvall, and B. Persson. (2002b). Short-chain dehydrogenases/reductases (SDRs)—coenzyme-based functional assignments in completed genomes. Eur J Biochem 269:4409–4417.
   PubMedGoogle Scholar
• C. Keenan, S. Ghaffar, A. W. Grant, A. Hinshelwood, D. Li, G. McGarvie, and et al, and Succinic semialdehyde reductases: contribution to gamma-hydroxybutyrate catabolism and subcellular localizationEnzymology and Molecular Biology of Carbonyl MetabolismH. Weiner, B. Plapp, R. Lindahl, and E. Maser. Purdue University Press, West Lafayette, IndianaUSA, (2006) 12388–395.
   Google Scholar
• V. P. Kelly, L. S. Ireland, E. M. Ellis, and J. D. Hayes. (2000). Purification from rat liver of a novel constitutively expressed member of the aldo-keto reductase 7 family that is widely distributed in extrahepatic tissues. Biochem J 348:t–400.
   Google Scholar
• V. P. Kelly, P. J. Sherratt, D. H. Crouch, and J. D. Hayes. (2002). Novel homodimeric and heterodimeric rat gamma-hydroxybutyrate synthases that associate with the Golgi apparatus define a distinct subclass of aldo-keto reductase 7 family proteins. Biochem J 366:847–861.
   PubMed Web of Science ®Google Scholar
• T. W. Kensler, T. J. Curphey, Y. Maxiutenko, and B. D. Roebuck. (2000). Chemoprotection by organosulfur inducers of phase 2 enzymes: dithiolethiones and dithiins. Drug Metabol Drug Interact 17:3–22.
   PubMedGoogle Scholar
• K. B. Kilunga, T. Inoue, Y. Okano, Z. Kabututu, S. K. Martin, M. Lazarus, and et al (2005). Structural and mutational analysis of Trypanosoma brucei prostaglandin H-2 reductase provides insight into the catalytic mechanism of aldo-ketoreductases. J Biol Chem 280:26371–26382.
   PubMed Web of Science ®Google Scholar
• J. H. Kinoshita. (1990). A thirty-year journey in the polyol pathway. Exp Eye Res 50:567–573.
   PubMed Web of Science ®Google Scholar
• M. Kishimoto, R. Kawamori, T. Kamada, and T. Inaba. (1994). Carbonyl reductase activity for acetohexamide in human erythrocytes. Drug Metab Dispos 22:367–370.
   PubMed Web of Science ®Google Scholar
• T. Kita, N. Kume, M. Yokode, K. Ishii, H. Arai, H. Horiuchi, and et al (2000). Oxidized-LDL and atherosclerosis. Role of LOX-1. Ann N Y Acad Sci 902:95–100.
   PubMed Web of Science ®Google Scholar
• L. P. Knight, T. Primiano, J. D. Groopman, T. W. Kensler, and T. R. Sutter. (1999). cDNA cloning, expression, and activity of a second human aflatoxin B1-metabolizing member of the aldo-keto reductase superfamily, AKR7A3. Carcinogenesis 20:1215–1223.
   PubMed Web of Science ®Google Scholar
• P. Kotokorpi, C. Gardmo, C. S. Nystrom, and A. Mode. (2004). Activation of the glucocorticoid receptor or liver X receptors interferes with growth hormone-induced akr1b7 gene expression in rat hepatocytes. Endocrinology 145:5704–5713.
   PubMed Web of Science ®Google Scholar
• E. Kozma, E. Brown, E. M. Ellis, and A. J. Lapthorn. (2002). The crystal structure of rat liver AKR7A1—a dimeric member of the aldo-keto reductase superfamily. J Biol Chem 277:16285–16293.
   PubMed Web of Science ®Google Scholar
• R. Kratzer, S. Egger, and B. Nidetzky. Integration of enzyme, strain, and reaction engineering to overcome limitations of baker's yeast in the asymmetric reduction of alpha-keto estersBiotechnol Bioeng. (2008) (in press) Pubmed ID: 18623228.
   Google Scholar
• S. Kudo, and T. Ishizaki. (1999). Pharmacokinetics of haloperidol—an update. Clin Pharmacokinet 37:435–456.
   PubMed Web of Science ®Google Scholar
• E. T. Lau, D. Cao, C. Lin, S. K. Chung, and S. S. Chung. (1995). Tissue-specific expression of two aldose reductase-like genes in mice: abundant expression of mouse vas deferens protein and fibroblast growth factor-regulated protein in the adrenal gland. Biochem J 312:609–615.
   PubMed Web of Science ®Google Scholar
• E. N. Lavrentyev, A. M. Estes, and K. U. Malik. (2007). Mechanism of high glucose–induced angiotensin II production in rat vascular smooth muscle cells. Circ Res 101:455–464.
   PubMed Web of Science ®Google Scholar
• A. Y. Lee, S. K. Chung, and S. S. Chung. (1995). Demonstration that polyol accumulation is responsible for diabetic cataract by the use of transgenic mice expressing the aldose reductase gene in the lens. Proc Natl Acad Sci U S A 92:2780–2784.
   PubMed Web of Science ®Google Scholar
• Y. S. Lee, M. Hodoscek, B. R. Brooks, and P. F. Kador. (1998). Catalytic mechanism of aldose reductase studied by the combined potentials of quantum mechanics and molecular mechanics. Biophys Chem 70:203–216.
   PubMed Web of Science ®Google Scholar
• A. M. Lefrancois-Martinez, C. Tournaire, A. Martinez, M. Berger, S. Daoudal, P. Tritsch, and et al (1999). Product of side-chain cleavage of cholesterol, isocaproaldehyde, is an endogenous specific substrate of mouse vas deferens protein, an aldose reductase-like protein in adrenocortical cells. J Biol Chem 274:32875–32880.
   PubMed Web of Science ®Google Scholar
• T. Leicher, R. Bahring, D. Isbrandt, and O. Pongs. (1998). Coexpression of the KCNA3B gene product with Kv1.5 leads to a novel A-type potassium. J Biol Chem 273:35095–35101.
   PubMed Web of Science ®Google Scholar
• N. Leitinger, T. R. Tyner, L. Oslund, C. Rizza, G. Subbanagounder, H. Lee, and et al (1999). Structurally similar oxidized phospholipids differentially regulate endothelial binding of monocytes and neutrophils. Proc Natl Acad Sci U S A 96:12010–12015.
   PubMed Web of Science ®Google Scholar
• H. A. Lemonde, E. J. Custard, J. Bouquet, M. Duran, H. Overmars, P. J. Scambler, and et al (2003). Mutations in SRD5B1 (AKR1D1), the gene encoding delta(4)-3-oxosteroid 5beta-reductase, in hepatitis and liver failure in infancy. Gut 52:1494–1499.
   PubMed Web of Science ®Google Scholar
• S. Li, E. Hanna, R. Breau, V. Ratanatharathorn, X. Xia, and J. Suen. (2004). Preferential expression of hPGFS in primary SCCHN and tumour cell lines derived from respiratory and digestive organs. Br J Cancer 90:1093–1099.
   PubMed Web of Science ®Google Scholar
• C. L. Linster, and E. Van Schaftingen. (2003). Rapid stimulation of free glucuronate formation by nonglucuronidable xenobiotics in isolated rat hepatocytes. J Biol Chem 278:36328–36333.
   PubMed Web of Science ®Google Scholar
• C. L. Linster, and E. Schaftingen. (2007). Vitamin C. Biosynthesis, recycling, and degradation in mammals. FEBS J 274:1–22.
   PubMed Web of Science ®Google Scholar
• T. E. Liston, and L. J. Roberts. (1985). Transformation of prostaglandin-D2 to 9-alpha,11B-(15S)-trihydroxyprosta-(5Z,13E)-dien-1-oic acid (9-alpha,11-beta-prostaglandin-F2)—a unique biologically active prostaglandin produced enzymatically in vivo in humans. Proc Natl Acad Sci U S A 82:6030–6034.
   PubMed Web of Science ®Google Scholar
• S. Q. Liu, A. Bhatnagar, and S. K. Srivastava. (1992). Does sorbinil bind to the substrate binding site of aldose reductase?. Biochem Pharmacol 44:2427–2429.
   PubMed Web of Science ®Google Scholar
• S. Q. Liu, A. Bhatnagar, and S. K. Srivastava. (1993). Bovine lens aldose reductase. pH-dependence of steady-state kinetic parameters, and nucleotide binding. J Biol Chem 268:25494–25499.
   PubMed Web of Science ®Google Scholar
• S. Q. Liu, H. Jin, A. Zacarias, S. Srivastava, and A. Bhatnagar. (2001). Binding of pyridine nucleotide coenzymes to the beta-subunit of the voltage-sensitive K+ channel. J Biol Chem 276:11812–11820.
   PubMed Web of Science ®Google Scholar
• H. Lou, L. Hammond, V. Sharma, R. S. Sparkes, A. J. Lusis, and A. Stolz. (1994). Genomic organization and chromosomal localization of a novel human hepatic dihydrodiol dehydrogenase with high-affinity bile-acid binding. J Biol Chem 269:8416–8422.
   PubMed Web of Science ®Google Scholar
• R. C. Lyon, S. M. Johnston, D. G. Watson, G. McGarvie, and E. M. Ellis. (2007). Synthesis and catabolism of gamma-hydroxybutyrate in SH-SY5Y human neuroblastoma cells—role of the aldo-keto reductase AKR7A2. J Biol Chem 282:25986–25992.
   PubMed Web of Science ®Google Scholar
• H. C. Ma, K. Ratnam, and T. M. Penning. (2000). Mutation of nicotinamide pocket residues in rat liver 3 alpha-hydroxysteroid dehydrogenase reveals different modes of cofactor binding. Biochemistry 39:102–109.
   PubMed Web of Science ®Google Scholar
• J. Ma, R. Yan, X. Zu, J. M. Cheng, K. Rao, D. F. Liao, and et al (2008). Aldo-keto reductase family 1 B10 affects fatty-acid synthesis by regulating the stability of acetyl-CoA carboxylase-{alpha} in breast cancer cells. J Biol Chem. 283:3418–3423.
   PubMed Web of Science ®Google Scholar
• S. Makino, D. B. Zaragoza, B. F. Mitchell, S. Robertson, and D. M. Olson. (2007). Prostaglandin F2alpha and its receptor as activators of human decidua. Semin Reprod Med 25:60–68.
   PubMed Web of Science ®Google Scholar
• L. N. Manganas, and J. S. Trimmer. (2000). Subunit composition determines Kv1 potassium channel surface expression. J Biol Chem 275:29685–29693.
   PubMed Web of Science ®Google Scholar
• Y. Mano, K. Suzuki, K. Yamada, and N. Shimazono. (1961). Enzymatic studies on TPN-L-hexonate dehydrogenase from rat liver. J Biochem 49:618–634.
   PubMed Web of Science ®Google Scholar
• H. J. O. Martin, U. Breyer-Pfaff, V. Wsol, S. Venz, S. Block, and E. Maser. (2006). Purification and characterization of AKR1B10 from human liver: role in carbonyl reduction of xenobiotics. Drug Metab Dispos 34:464–470.
   PubMed Web of Science ®Google Scholar
• E. Maser. (2004). Significance of reductases in the detoxification of the tobacco-specific carcinogen NNK. Trends Pharmacol Sci 25:235–237.
   PubMed Web of Science ®Google Scholar
• E. Maser, J. Friebertshauser, and B. Volker. (2003). Purification, characterization, and NNK carbonyl reductase activities of 11beta-hydroxysteroid dehydrogenase type 1 from human liver: enzyme cooperativity and significance in the detoxification of a tobacco-derived carcinogen. Chem Biol Interact, 143–144 435–448.
   Google Scholar
• E. Maser, B. Stinner, and A. Atalla. (2000). Carbonyl reduction of 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone (NNK) by cytosolic enzymes in human liver and lung. Cancer Lett 148:135–144.
   PubMed Web of Science ®Google Scholar
• R. M. Mason, and N. A. Wahab. (2003). Extracellular matrix metabolism in diabetic nephropathy. J Am Soc Nephrol 14:1358–1373.
   PubMed Web of Science ®Google Scholar
• K. Matsumoto, S. Endo, S. Ishikura, T. Matsunaga, K. Tajima, O. El Kabbani, and et al (2006). Enzymatic properties of a member (AKR1C20) of the aldo-keto reductase family. Biol Pharmaceut Bull 29:539–542.
   PubMed Web of Science ®Google Scholar
• T. Matsumoto, Y. Ono, M. Kurono, A. Kuromiya, K. Nakamura, and V. Bril. (2008). Ranirestat (AS-3201), a potent aldose reductase inhibitor, reduces sorbitol levels and improves motor nerve conduction velocity in streptozotocin-diabetic rats. J Pharmacol Sci 107:231–237.
   PubMed Web of Science ®Google Scholar
• K. Matsuura, H. Shiraishi, A. Hara, K. Sato, Y. Deyashiki, M. Ninomiya, and et al (1998). Identification of a principal mRNA species for human 3 alpha-hydroxysteroid dehydrogenase isoform (AKR1C3) that exhibits high prostaglandin D-2 11-ketoreductase activity. J Biochem 124:940–946.
   PubMed Web of Science ®Google Scholar
• K. McCormack, J. X. Connor, L. Zhou, L. L. Ho, B. Ganetzky, S. Y. Chiu, and et al (2002). Genetic analysis of the mammalian K+ channel beta subunit Kv beta 2 (Kcnab2). J Biol Chem 277:13219–13228.
   PubMed Web of Science ®Google Scholar
• L. I. McLellan, D. J. Judah, G. E. Neal, and J. D. Hayes. (1994). Regulation of aflatoxin B1-metabolizing aldehyde reductase and glutathione S-transferase by chemoprotectors. Biochem J 00:117–124.
   Google Scholar
• G. Minotti, S. Licata, A. Saponiero, P. Menna, A. M. Calafiore, G. Di Giammarco, and et al (2000). Anthracycline metabolism and toxicity in human myocardium: Comparisons between doxorubicin, epirubicin, and a novel disaccharide analogue with a reduced level of formation and [4Fe-4S] reactivity of its secondary alcohol metabolite. Chem Res Toxicol 13:1336–1341.
   PubMed Web of Science ®Google Scholar
• T. Miyata, Y. Ueda, Y. Yamada, Y. Izuhara, T. Wada, M. Jadoul, and et al (1998). Accumulation of carbonyls accelerates the formation of pentosidine, an advanced glycation end product: carbonyl stress in uremia. J Am Soc Nephrol 9:2349–2356.
   PubMed Web of Science ®Google Scholar
• T. Miyata, D. S. van Ypersele, K. Kurokawa, and J. W. Baynes. (1999). Alterations in nonenzymatic biochemistry in uremia: origin and significance of “carbonyl stress” in long-term uremic complications. Kidney Int 55:389–399.
   PubMed Web of Science ®Google Scholar
• A. Mode, and I. Rafter. (1985). The sexually differentiated delta 4-3-ketosteroid 5 beta-reductase of rat liver. Purification, characterization, and quantitation. J Biol Chem 260:7137–7141.
   PubMed Web of Science ®Google Scholar
• A. Mordente, E. Meucci, G. E. Martorana, B. Giardina, and G. Minotti. (2001). Human heart cytosolic reductases and anthracycline cardiotoxicity. IUBMB Life 52:83–88.
   PubMed Web of Science ®Google Scholar
• A. Mordente, G. Minotti, G. E. Martorana, A. Silvestrini, B. Giardina, and E. Meucci. (2003). Anthracycline secondary alcohol metabolite formation in human or rabbit heart: biochemical aspects and pharmacologic implications. Biochem Pharmacol 66:989–998.
   PubMed Web of Science ®Google Scholar
• B. L. Mylari, E. R. Larson, T. A. Beyer, W. J. Zembrowski, C. E. Aldinger, M. F. Dee, and et al (1991). Novel, potent aldose reductase inhibitors: 3,4-dihydro-4-oxo-3-[[5-(trifluoromethyl)-2-benzothiazolyl] methyl]-1-phthalazineacetic acid (zopolrestat) and congeners. J Med Chem 34:108–122.
   PubMed Web of Science ®Google Scholar
• N. S. Nagaraj, S. Beckers, J. K. Mensah, S. Waigel, N. Vigneswaran, and W. Zacharias. (2006). Cigarette smoke condensate induces cytochromes P450 and aldo-keto reductases in oral cancer cells. Toxicol Lett 165:182–194.
   PubMed Web of Science ®Google Scholar
• R. H. Nagaraj, I. N. Shipanova, and F. M. Faust. (1996). Protein cross-linking by the Maillard reaction. isolation, characterization, and in vivo detection of a lysine-lysine cross-link derived from methylglyoxal. J Biol Chem 271:19338–19345.
   PubMed Web of Science ®Google Scholar
• N. Nagaya, and D. M. Papazian. (1997). Potassium channel alpha and beta subunits assemble in the endoplasmic reticulum. J Biol Chem 272:3022–3027.
   PubMed Web of Science ®Google Scholar
• A. C. Need, E. E. Irvine, and K. P. Giese. (2003). Learning and memory impairments in K-v beta 1.1-null mutants are rescued by environmental enrichment or ageing. Eur J Neurosci 18:1640–1644.
   PubMed Web of Science ®Google Scholar
• A. Negre-Salvayre, C. Coatrieux, C. Ingueneau, and R. Salvayre. (2008). Advanced lipid peroxidation end products in oxidative damage to proteins. Potential role in diseases and therapeutic prospects for the inhibitors. Br J Pharmacol 153:6–20.
   PubMed Web of Science ®Google Scholar
• A. Nicolucci, F. Carinci, D. Cavaliere, N. Scorpiglione, M. Belfiglio, D. Labbrozzi, and et al (1996). A meta-analysis of trials on aldose reductase inhibitors in diabetic peripheral neuropathy. The Italian Study Group. The St. Vincent Declaration [see comments]. Diabet Med 13:1017–1026.
   PubMed Web of Science ®Google Scholar
• B. Nidetzky, W. Neuhauser, D. Haltrich, and K. D. Kulbe. (1996). Continuous enzymatic production of xylitol with simultaneous coenzyme regeneration in a charged membrane reactor. Biotechnol Bioeng 52:387–396.
   PubMed Web of Science ®Google Scholar
• M. Nishizawa, T. Nakajima, K. Yasuda, H. Kanzaki, Y. Sasaguri, K. Watanabe, and et al (2000). Close kinship of human 20 alpha-hydroxysteroid dehydrogenase gene with three aldo-keto reductase genes. Genes Cells 5:111–125.
   PubMed Web of Science ®Google Scholar
• T. Niwa, T. Miyazaki, T. Katsuzaki, N. Tatemichi, and Y. Takei. (1996). Serum levels of 3-deoxyglucosone and tissue contents of advanced glycation end products are increased in streptozotocin-induced diabetic rats with nephropathy. Nephron 74:580–585.
   PubMedGoogle Scholar
• T. Niwa, and S. Tsukushi. (2001). 3-deoxyglucosone and AGEs in uremic complications: inactivation of glutathione peroxidase by 3-deoxyglucosone. Kidney Int Suppl 78:S37–S41.
   PubMedGoogle Scholar
• T O'Connor, L. S. Ireland, D. J. Harrison, and J. D. Hayes. (1999). 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 343:t–504.
   Google Scholar
• P. J. Oates. (2002). Polyol pathway and diabetic peripheral neuropathy. Int Rev Neurobiol 50:325–392.
   PubMed Web of Science ®Google Scholar
• H. Ohara, Y. Miyabe, Y. Deyashiki, K. Matsuura, and A. Hara. (1995). Reduction of drug ketones by dihydrodiol dehydrogenases, carbonyl reductase, and aldehyde reductase of human liver. Biochem Pharmacol 50:221–227.
   PubMed Web of Science ®Google Scholar
• T. Oka. (2004). Prostaglandin E2 as a mediator of fever: the role of prostaglandin E (EP) receptors. Front Biosci 9:3046–3057.
   PubMed Web of Science ®Google Scholar
• A. Okuda, and K. Okuda. (1984). Purification and characterization of delta 4-3-ketosteroid 5 beta-reductase. J Biol Chem 259:7519–7524.
   PubMed Web of Science ®Google Scholar
• S. E. Old, S. Sato, P. F. Kador, and D. A. Carper. (1990). In vitro expression of rat lens aldose reductase in Escherichia coli. Proc Natl Acad Sci U S A 87:4942–4945.
   PubMed Web of Science ®Google Scholar
• U. Oppermann, C. Filling, M. Hult, N. Shafqat, X. Q. Wu, M. Lindh, and et al (2003). Short-chain dehydrogenases/reductases (SDR): the 2002 update. Chemico Biol Interact 143:247–253.
   PubMed Web of Science ®Google Scholar
• N. T. Palackal, M. E. Burczynski, R. G. Harvey, and T. M. Penning. (2001). The ubiquitous aldehyde reductase (AKR1A1) oxidizes proximate carcinogen trans-dihydrodiols to o-quinones: potential role in polycyclic aromatic hydrocarbon activation. Biochemistry 40:10901–10910.
   PubMed Web of Science ®Google Scholar
• M. Palermo, M. G. Marazzi, B. A. Hughes, P. M. Stewart, P. T. Clayton, and C. H. Shackleton. (2008). Human delta(4)-3-oxosteroid 5beta-reductase (AKR1D1) deficiency and steroid metabolism. Steroids 73:417–423.
   PubMed Web of Science ®Google Scholar
• M. Papari-Zareei, A. Brandmaier, and R. J. Auchus. (2006). Arginine 276 controls the directional preference of AKR1C9 (rat liver 3 alpha-hydroxysteroid dehydrogenase) in human embryonic kidney 293 cells. Endocrinology 147:1591–1597.
   PubMed Web of Science ®Google Scholar
• J. E. Pawlowski, and T. M. Penning. (1994). Overexpression and mutagenesis of the cDNA for rat-liver 3-alpha-hydroxysteroid dihydrodiol dehydrogenase—role of cysteines and tyrosines in catalysis. J Biol Chem 269:13502–13510.
   PubMed Web of Science ®Google Scholar
• T. M. Penning. (1997). Molecular endocrinology of hydroxysteroid dehydrogenases. Endocr Rev 18:281–305.
   PubMed Web of Science ®Google Scholar
• T. M. Penning, M. E. Burczynski, J. M. Jez, C. F. Hung, H. K. Lin, H. C. Ma, and et al (2000). Human 3 alpha-hydroxysteroid dehydrogenase isoforms (AKR1C1–AKR1C4) of the aldo-keto reductase superfamily: functional plasticity and tissue distribution reveals roles in the inactivation and formation of male and female sex hormones. Biochem J 351:67–77.
   PubMed Web of Science ®Google Scholar
• T. M. Penning, and J. E. Drury. (2007). Human aldo-keto reductases: function, gene regulation, and single nucleotide polymorphisms. Arch Biochem Biophys 464:241–250.
   PubMed Web of Science ®Google Scholar
• T. M. Penning, Y. Jin, V. V. Heredia, and M. Lewis. (2003). Structure-function relationships in 3alpha-hydroxysteroid dehydrogenases: a comparison of the rat and human isoforms. J Steroid Biochem Mol Biol 85:247–255.
   PubMed Web of Science ®Google Scholar
• T. M. Penning, Y. Jin, S. Steckelbroeck, T. L. Rizner, and M. Lewis. (2004). Structure-function of human 3 alpha-hydroxysteroid dehydrogenases: genes and proteins. Mol Cell Endocrinol 215:63–72.
   PubMed Web of Science ®Google Scholar
• T. M. Penning, and P. Talalay. (1983). Inhibition of a major NAD(P)-linked oxidoreductase from rat liver cytosol by steroidal and nonsteroidal anti-inflammatory agents and by prostaglandins. Proc Natl Acad Sci U S A 80:4504–4508.
   PubMed Web of Science ®Google Scholar
• J. M. Petrash, T. M. Harter, C. S. Devine, P. O. Olins, A. Bhatnagar, S. Liu, and et al (1992). Involvement of cysteine residues in catalysis and inhibition of human aldose reductase. Site-directed mutagenesis of Cys-80, -298, and -303. J Biol Chem 267:24833–24840.
   PubMed Web of Science ®Google Scholar
• M. A. Pfeifer, M. P. Schumer, and D. A. Gelber. (1997). Aldose reductase inhibitors: the end of an era or the need for different trial designs?. Diabetes 46 (Suppl 2):S82–S89.
   PubMedGoogle Scholar
• R. P. Piekorz, B. Gingras, A. Hoffmeyer, J. N. Ihle, and Y. Weinstein. (2005). Regulation of progesterone levels during pregnancy and parturition by signal transducer and activator of transcription 5- and 20-alpha-hydroxysteroid dehydrogenase. Mol Endocrinol 19:431–440.
   PubMed Web of Science ®Google Scholar
• A. Podjarny, R. E. Cachau, T. Schneider, M. Van Zandt, and A. Joachimiak. (2004). Subatomic and atomic crystallographic studies of aldose reductase: implications for inhibitor binding. Cell Mol Life Sci 61:763–773.
   PubMed Web of Science ®Google Scholar
• N. Pollak, C. Dolle, and M. Ziegler. (2007). The power to reduce: pyridine nucleotides—small molecules with a multitude of functions. Biochem J 402:205–218.
   PubMed Web of Science ®Google Scholar
• O. Pongs, T. Leicher, M. Berger, J. Roeper, R. Bahring, D. Wray, and et al (1999). Functional and molecular aspects of voltage-gated K+ channel beta subunits. Mol Funct Divers Ion Chan Recept 868:344–355.
   Google Scholar
• D. Propper, and E. Maser. (1997). Carbonyl reduction of daunorubicin in rabbit liver and heart. Pharmacol Toxicol 80:240–245.
   PubMedGoogle Scholar
• K. V. Ramana, A. Bhatnagar, S. Srivastava, U. C. Yadav, S. Awasthi, Y. C. Awasthi, and et al (2006a). Mitogenic responses of vascular smooth muscle cells to lipid peroxidation-derived aldehyde 4-hydroxy-trans-2-nonenal (HNE): role of aldose reductase-catalyzed reduction of the HNE-glutathione conjugates in regulating cell growth. J Biol Chem 281:17652–17660.
   PubMed Web of Science ®Google Scholar
• K. V. Ramana, D. Chandra, S. Srivastava, A. Bhatnagar, B. B. Aggarwal, and S. K. Srivastava. (2002). Aldose reductase mediates mitogenic signaling in vascular smooth muscle cells. Jf Biol Chem 277:32063–32070.
   Google Scholar
• K. V. Ramana, D. Chandra, S. Srivastava, A. Bhatnagar, and S. K. Srivastava. (2003a). Aldose reductase mediates the mitogenic signals of cytokines. Chem Biol Interact 143–144 587–596.
   Google Scholar
• K. V. Ramana, D. Chandra, S. Srivastava, A. Bhatnagar, and S. K. Srivastava. (2003b). Nitric oxide regulates the polyol pathway of glucose metabolism in vascular smooth muscle cells. FASEB J 17:417–425.
   PubMed Web of Science ®Google Scholar
• K. V. Ramana, A. A. Fadl, R. Tammali, A. B. Reddy, A. K. Chopra, and S. K. Srivastava. (2006b). Aldose reductase mediates the lipopolysaccharide-induced release of inflammatory mediators in RAW264.7 murine macrophages. J Biol Chem 281:33019–33029.
   PubMed Web of Science ®Google Scholar
• K. V. Ramana, B. Friedrich, S. Srivastava, A. Bhatnagar, and S. K. Srivastava. (2004). Activation of nuclear factor-kappaB by hyperglycemia in vascular smooth muscle cells is regulated by aldose reductase. Diabetes 53:2910–2920.
   PubMed Web of Science ®Google Scholar
• K. V. Ramana, B. Friedrich, R. Tammali, M. B. West, A. Bhatnagar, and S. K. Srivastava. (2005). Requirement of aldose reductase for the hyperglycemic activation of protein kinase C and formation of diacylglycerol in vascular smooth muscle cells. Diabetes 54:818–829.
   PubMed Web of Science ®Google Scholar
• K. V. Ramana, R. Tammali, A. B. Reddy, A. Bhatnagar, and S. K. Srivastava. (2007). Aldose reductase–regulated tumor necrosis factor-alpha production is essential for high glucose–induced vascular smooth muscle cell growth. Endocrinology 148:4371–4384.
   PubMed Web of Science ®Google Scholar
• K. V. Ramana, M. S. Willis, M. D. White, J. W. Horton, J. M. DiMaio, D. Srivastava, and et al (2006c). Endotoxin-induced cardiomyopathy and systemic inflammation in mice is prevented by aldose reductase inhibition. Circulation 114:1838–1846.
   PubMed Web of Science ®Google Scholar
• K. Ratnam, H. Ma, and T. M. Penning. (1999). The arginine 276 anchor for NADP(H) dictates fluorescence kinetic transients in 3 alpha-hydroxysteroid dehydrogenase, a representative aldo-keto reductase. Biochemistry 38:7856–7864.
   PubMed Web of Science ®Google Scholar
• C. C. Reddy, J. S. Swan, and G. A. Hamilton. (1981). myo-Inositol oxygenase from hog kidney. I. Purification and characterization of the oxygenase and of an enzyme complex containing the oxygenase and D-glucuronate reductase. J Biol Chem 256:8510–8518.
   PubMed Web of Science ®Google Scholar
• J. Rettig, S. H. Heinemann, F. Wunder, C. Lorra, D. N. Parcej, J. O. Dolly, and et al (1994). Inactivation properties of voltage-gated K+ channels altered by presence of beta-subunit. Nature 369:289–294.
   PubMed Web of Science ®Google Scholar
• M. J. C. Rosemond, L. John-Williams, T. Yamaguchi, T. Fujishita, and J. S. Walsh. (2004). Enzymology of a carbonyl reduction clearance pathway for the HIV integrase inhibitor, S-1360: role of human liver cytosolic aldo-keto reductases. Chemico Biol Interact 147:129–139.
   PubMed Web of Science ®Google Scholar
• M. J. C. Rosemond, and J. S. Walsh. (2004). Human carbonyl reduction pathways and a strategy for their study in vitro. Drug Metab Rev 36:335–361.
   PubMed Web of Science ®Google Scholar
• J. Ruef, S. Q. Liu, C. Bode, M. Tocchi, S. Srivastava, M. S. Runge, and et al (2000). Involvement of aldose reductase in vascular smooth muscle cell growth and lesion formation after arterial injury. Arterioscler Thromb Vasc Biol 20:1745–1752.
   PubMed Web of Science ®Google Scholar
• F. Ruiz, I. Hazemann, A. Mitschler, A. Joachimiak, T. Schneider, M. Karplus, and et al (2004). The crystallographic structure of the aldose reductase-IDD552 complex shows direct proton donation from tyrosine 48. Acta Crystallogr D Biol Crystallogr 60:1347–1354.
   PubMed Web of Science ®Google Scholar
• W. R. Rush, O. F. Alexander, D. J. Hall, R. J. Dow, L. Tokes, L. Kurz, and et al (1990). The metabolism of nafimidone hydrochloride in the dog, primates, and man. Xenobiotica 20:123–132.
   PubMed Web of Science ®Google Scholar
• K. J. Sales, S. A. Milne, A. R. Williams, R. A. Anderson, and H. N. Jabbour. (2004). Expression, localization, and signaling of prostaglandin F2 alpha receptor in human endometrial adenocarcinoma: regulation of proliferation by activation of the epidermal growth factor receptor and mitogen-activated protein kinase signaling pathways. J Clin Endocrinol Metab 89:986–993.
   PubMed Web of Science ®Google Scholar
• M. Sanai, S. Endo, T. Matsunaga, S. Ishikura, K. Tajima, O. El Kabbani, and et al (2007). Rat NAD(+)-dependent 3 alpha-hydroxysteroid dehydrogenase (AKR1C17): a member of the aldo-keto reductase family highly expressed in kidney cytosol. Arch Biochem Biophys 464:122–129.
   PubMed Web of Science ®Google Scholar
• K. Sato, A. Inazu, S. Yamaguchi, T. Nakayama, Y. Deyashiki, H. Sawada, and et al (1993). Monkey 3-deoxyglucosone reductase: tissue distribution and purification of three multiple forms of the kidney enzyme that are identical with dihydrodiol dehydrogenase, aldehyde reductase, and aldose reductase. Arch Biochem Biophys 307:286–294.
   PubMed Web of Science ®Google Scholar
• S. Sato, and P. F. Kador. (1990). Inhibition of aldehyde reductase by aldose-reductase inhibitors. Biochem Pharmacol 40:1033–1042.
   PubMed Web of Science ®Google Scholar
• B. P. Schlegel, J. M. Jez, and T. M. Penning. (1998a). Mutagenesis of 3 alpha-hydroxysteroid dehydrogenase reveals a “push-pull” mechanism for proton transfer in aldo-keto reductases. Biochemistry 37:3538–3548.
   PubMed Web of Science ®Google Scholar
• B. P. Schlegel, K. Ratnam, and T. M. Penning. (1998b). Retention of NADPH-linked quinone reductase activity in an aldo-keto reductase following mutation of the catalytic tyrosine. Biochemistry 37:11003–11011.
   PubMed Web of Science ®Google Scholar
• K. Sestanj, F. Bellini, S. Fung, N. Abraham, A. Treasurywala, L. Humber, and et al (1984). N-[5-(trifluoromethyl)-6-methoxy-1-naphthalenyl]thioxomethyl]-N-methylglycine (Tolrestat), a potent, orally active aldose reductase inhibitor. J Med Chem 27:255–256.
   PubMed Web of Science ®Google Scholar
• K. D. Setchell, F. J. Suchy, M. B. Welsh, L. Zimmer-Nechemias, J. Heubi, and W. F. Balistreri. (1988). Delta 4-3-oxosteroid 5 beta-reductase deficiency described in identical twins with neonatal hepatitis. A new inborn error in bile-acid synthesis. J Clin Invest 82:2148–2157.
   PubMed Web of Science ®Google Scholar
• S. Sewing, J. Roeper, and O. Pongs. (1996). Kv beta 1 subunit binding specific for shaker-related potassium channel alpha subunits. Neuron 16:455–463.
   PubMed Web of Science ®Google Scholar
• S. Shaw, X. Wang, H. Redd, G. D. Alexander, C. M. Isales, and M. B. Marrero. (2003). High glucose augments the angiotensin II-induced activation of JAK2 in vascular smooth muscle cells via the polyol pathway. J Biol Chem 278:30634–30641.
   PubMed Web of Science ®Google Scholar
• D. P. Sherbet, M. Papari-Zareei, N. Khan, K. K. Sharma, A. Brandmaier, S. Rambally, and et al (2007). Cofactors, redox state, and directional preferences of hydroxysteroid dehydrogenases. Mol Cell Endocrinol 265:83–88.
   PubMed Web of Science ®Google Scholar
• G. Shi, K. Nakahira, S. Hammond, K. J. Rhodes, L. E. Schechter, and J. S. Trimmer. (1996). Beta subunits promote K+ channel surface expression through effects early in biosynthesis. Neuron 16:843–852.
   PubMed Web of Science ®Google Scholar
• K. Shimoda, M. Shibasaki, T. Inaba, S. W. Cheung, T. Someya, and S. Takahashi. (1998a). Carbonyl reduction of timiperone in human liver cytosol. Pharmacol Toxicol 83:164–168.
   PubMedGoogle Scholar
• K. Shimoda, T. Someya, S. Morita, G. Hirokane, A. Yokono, M. Shibasaki, and et al (1998b). Plasma concentrations of timiperone and its reduced metabolite in the patients on timiperone. Psychiatry Clin Neurosci 52:535–540.
   PubMed Web of Science ®Google Scholar
• K. Shinmura, R. Bolli, S. Q. Liu, X. L. Tang, E. Kodani, Y. T. Xuan, and et al (2002). Aldose reductase is an obligatory mediator of the late phase of ischemic preconditioning. Circ Res 91:240–246.
   PubMed Web of Science ®Google Scholar
• M. Shinohara, P. J. Thornalley, I. Giardino, P. Beisswenger, S. R. Thorpe, J. Onorato, and et al (1998). Overexpression of glyoxalase-I in bovine endothelial cells inhibits intracellular advanced glycation end-product formation and prevents hyperglycemia-induced increases in macromolecular endocytosis. J Clin Invest 101:1142–1147.
   PubMed Web of Science ®Google Scholar
• A. A. Sima, V. Bril, V. Nathaniel, T. A. McEwen, M. B. Brown, S. A. Lattimer, and et al (1988). Regeneration and repair of myelinated fibers in sural-nerve biopsy specimens from patients with diabetic neuropathy treated with sorbinil. N Engl J Med 319:548–555.
   PubMed Web of Science ®Google Scholar
• R. Singh, M. A. White, K. V. Ramana, J. M. Petrash, S. J. Watowich, A. Bhatnagar, and et al (2006). Structure of a glutathione conjugate bound to the active site of aldose reductase. Proteins 64:101–110.
   PubMed Web of Science ®Google Scholar
• T. E. Smithgall, and T. M. Penning. (1986). Inhibition of trans-dihydrodiol oxidation by the nonsteroidal anti-inflammatory drugs. Carcinogenesis 7:583–588.
   PubMed Web of Science ®Google Scholar
• Z. T. Song, D. T. W. Fu, Y. S. Chan, S. Leung, S. S. M. Chung, and S. K. Chung. (2003). Transgenic mice overexpressing aldose reductase in Schwann cells show more severe nerve conduction velocity deficit and oxidative stress under hyperglycemic stress. Mol Cell Neurosci 23:638–647.
   PubMed Web of Science ®Google Scholar
• M. Spite, S. P. Baba, Y. Ahmed, O. A. Barski, K. Nijhawan, J. M. Petrash, and et al (2007). Substrate specificity and catalytic efficiency of aldo-keto reductases with phospholipid aldehydes. Biochem J 405:95–105.
   PubMed Web of Science ®Google Scholar
• S. Srivastava, A. Chandra, N. H. Ansari, S. K. Srivastava, and A. Bhatnagar. (1998a). Identification of cardiac oxidoreductase(s) involved in the metabolism of the lipid peroxidation-derived aldehyde-4-hydroxynonenal. Biochem J 329:469–475.
   PubMed Web of Science ®Google Scholar
• S. Srivastava, A. Chandra, A. Bhatnagar, S. K. Srivastava, and N. H. Ansari. (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.
   PubMed Web of Science ®Google Scholar
• S. Srivastava, B. Chandrasekar, A. Bhatnagar, and S. D. Prabhu. (2002). Lipid peroxidation–derived aldehydes and oxidative stress in the failing heart: role of aldose reductase. Am.J Physiol Heart Circ.Physiol 283:H2612–H2619.
   PubMed Web of Science ®Google Scholar
• S. Srivastava, D. J. Conklin, S. Q. Liu, N. Prakash, P. J. Boor, S. K. Srivastava, and et al (2001a). Identification of biochemical pathways for the metabolism of oxidized low-density lipoprotein derived aldehyde-4-hydroxy trans-2-nonenal in vascular smooth muscle cells. Atherosclerosis 158:339–350.
   PubMed Web of Science ®Google Scholar
• S. Srivastava, B. L. Dixit, K. V. Ramana, A. Chandra, D. Chandra, A. Zacarias, and et al (2001b). Structural and kinetic modifications of aldose reductase by S-nitrosothiols. Biochem J 358:111–118.
   PubMed Web of Science ®Google Scholar
• S. Srivastava, T. M. Harter, A. Chandra, P. Bhatnagar, S. K. Srivastava, and J. M. Petrash. (1998b). Kinetic studies of FR-1, a growth factor–inducible aldo-keto reductase. Biochemistry 37:12909–12917.
   PubMed Web of Science ®Google Scholar
• S. Srivastava, M. Spite, J. O. Trent, M. B. West, Y. Ahmed, and A. Bhatnagar. (2004b). Aldose reductase–catalyzed reduction of aldehyde phospholipids. J Biol Chem 279:53395–53406.
   PubMed Web of Science ®Google Scholar
• S. Srivastava, M. Spite, J. O. Trent, M. B. West, Y. Ahmed, and A. Bhatnagar. (2004a). Aldose reductase–catalyzed reduction of aldehyde phospholipids. J Biol Chem 279:53395–53406.
   PubMed Web of Science ®Google Scholar
• S. Srivastava, R. Tammali, D. Chandra, D. A. Greer, K. V. Ramana, A. Bhatnagar, and et al (2005a). Regulation of lens aldose reductase activity by nitric oxide. Exp Eye Res 81:664–672.
   PubMed Web of Science ®Google Scholar
• S. Srivastava, S. J. Watowich, J. M. Petrash, S. K. Srivastava, and A. Bhatnagar. (1999). Structural and kinetic determinants of aldehyde reduction by aldose reductase. Biochemistry 38:42–54.
   PubMed Web of Science ®Google Scholar
• S. K. Srivastava, K. V. Ramana, and A. Bhatnagar. (2005b). Role of aldose reductase and oxidative damage in diabetes and the consequent potential for therapeutic options. Endocr Rev 26:380–392.
   PubMed Web of Science ®Google Scholar
• S. K. Srivastava, K. V. Ramana, S. Srivastava, and A. Bhatnagar. (2004c). Aldose reductase detoxifies lipid aldehydes and their glutathione conjugates. Aldo-Keto Reductases Toxicant Metab 865:37–48.
   Google Scholar
• M. Stanbrough, G. J. Bubley, K. Ross, T. R. Golub, M. A. Rubin, T. M. Penning, and et al (2006). Increased expression of genes converting adrenal androgens to testosterone in androgen-independent prostate cancer. Cancer Res 66:2815–2825.
   PubMed Web of Science ®Google Scholar
• S. Steckelbroeck, B. Oyesanmi, Y. Jin, S. H. Lee, H. J. Kloosterboer, and T. M. Penning. (2006). Tibolone metabolism in human liver is catalyzed by 3 alpha/3 beta-hydroxysteroid dehydrogenase activities of the four isoforms of the aldo-keto reductase (AKR)1C subfamily. J Pharmacol Exp Ther 316:1300–1309.
   PubMed Web of Science ®Google Scholar
• H. Steuber, A. Heine, A. Podjarny, and G. Klebe. (2008). Merging the binding sites of aldose and aldehyde reductase for detection of inhibitor selectivity-determining features. J Mol Biol 379:991–1016.
   PubMed Web of Science ®Google Scholar
• A. Stolz, L. Hammond, H. Lou, H. Takikawa, M. Ronk, and J. E. Shively. (1993). cDNA cloning and expression of the human hepatic bile acid-binding protein. A member of the monomeric reductase gene family. J Biol Chem 268:10448–10457.
   PubMed Web of Science ®Google Scholar
• G. Subbanagounder, N. Leitinger, D. C. Schwenke, J. W. Wong, H. Lee, C. Rizza, and et al (2000). Determinants of bioactivity of oxidized phospholipids. Specific oxidized fatty acyl groups at the sn-2 position. Arterioscler Thromb Vasc Biol 20:2248–2254.
   PubMed Web of Science ®Google Scholar
• D. Suzuki, and T. Miyata. (1999). Carbonyl stress in the pathogenesis of diabetic nephropathy. Intern Med 38:309–314.
   PubMed Web of Science ®Google Scholar
• K. Suzuki, Y. H. Koh, H. Mizuno, R. Hamaoka, and N. Taniguchi. (1998). Overexpression of aldehyde reductase protects PC12 cells from the cytotoxicity of methylglyoxal or 3-deoxyglucosone. J Biochem (Tokyo) 123:353–357.
   PubMed Web of Science ®Google Scholar
• T. Suzuki-Yamamoto, M. Nishizawa, M. Fukui, E. Okuda-Ashitaka, T. Nakajima, S. Ito, and et al (1999). cDNA cloning, expression, and characterization of human prostaglandin F synthase. FEBS Lett 462:335–340.
   PubMed Web of Science ®Google Scholar
• T. Thomas, G. Thomas, C. McLendon, T. Sutton, and M. Mullan. (1996). beta-amyloid-mediated vasoactivity and vascular endothelial damage. Nature 380:168–171.
   PubMed Web of Science ®Google Scholar
• P. J. Thornalley. (2003). Use of aminoguanidine (Pimagedine) to prevent the formation of advanced glycation endproducts. Arch Biochem Biophys 419:31–40.
   PubMed Web of Science ®Google Scholar
• P. J. Thornalley, A. Langborg, and H. S. Minhas. (1999). Formation of glyoxal, methylglyoxal, and 3-deoxyglucosone in the glycation of proteins by glucose. Biochem J 344:t–16.
   Google Scholar
• S. M. Tipparaju, O. A. Barski, S. Srivastava, and A. Bhatnagar. (2008). Catalytic mechanism and substrate specificity of the beta-subunit of the voltage-gated potassium channel. Biochemistry 47:8840–8854.
   PubMed Web of Science ®Google Scholar
• S. M. Tipparaju, S. Q. Liu, O. A. Barski, and A. Bhatnagar. (2007). NADPH binding to beta-subunit regulates inactivation of voltage-gated K+ channels. Biochem Biophys Res Commun 359:269–276.
   PubMed Web of Science ®Google Scholar
• S. M. Tipparaju, N. Saxena, S. Q. Liu, R. Kumar, and A. Bhatnagar. (2005). Differential regulation of voltage-gated K+ channels by oxidized and reduced pyridine nucleotide coenzymes. Am J Physiol Cell Physiol 288:C366–C376.
   PubMed Web of Science ®Google Scholar
• A. D. Tselepis, and C. M. John. (2002). Inflammation, bioactive lipids, and atherosclerosis: potential roles of a lipoprotein-associated phospholipase A2, platelet-activating factor-acetylhydrolase. Atheroscler Suppl 3:57–68.
   PubMed Web of Science ®Google Scholar
• P. Upadhyaya, P. M. J. Kenney, J. B. Hochalter, M. Y. Wang, and S. S. Hecht. (1999). Tumorigenicity and metabolism of 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanol enantiomers and metabolites in the A/J mouse. Carcinogenesis 20:1577–1582.
   PubMed Web of Science ®Google Scholar
• Y. Urade, K. Watanabe, N. Eguchi, Y. Fujii, and O. Hayaishi. (1990). 9-alpha,11-beta-prostaglandin-F2 formation in various bovine-tissues—different Isozymes of prostaglandin-D2 11-ketoreductase, contribution of prostaglandin-F synthetase and its cellular-localization. J Biol Chem 265:12029–12035.
   PubMed Web of Science ®Google Scholar
• A. Urzhumtsev, F. Tete-Favier, A. Mitschler, J. Barbanton, P. Barth, L. Urzhumtseva, and et al (1997). A “specificity” pocket inferred from the crystal structures of the complexes of aldose reductase with the pharmaceutically important inhibitors tolrestat and sorbinil. Structure 5:601–612.
   PubMed Web of Science ®Google Scholar
• P. Val, A. Martinez, I. Sahut-Barnola, C. Jean, G. Veyssiere, and A. M. Lefrancois-Martinez. (2002). A 77-base-pair LINE-like sequence elicits androgen-dependent mvdp/akr1-b7 expression in mouse vas deferens, but is dispensable for adrenal expression in rats. Endocrinology 143:3435–3448.
   PubMed Web of Science ®Google Scholar
• M. A. van Boekel, D. M. van Aalten, G. J. Caspers, B. Roll, and W. W. de Jong. (2001). Evolution of the aldose reductase-related gecko eye lens protein rhoB-crystallin: a sheep in wolf's clothing. J Mol Evol 52:239–248.
   PubMed Web of Science ®Google Scholar
• J. D. Vander, N. S. Kolb, J. T. Vander, J. Chino, F. J. Martinez, L. A. Hunsaker, and et al (1995). Substrate specificity of human aldose reductase: identification of 4- hydroxynonenal as an endogenous substrate. Biochim Biophys Acta 1249:117–126.
   PubMed Web of Science ®Google Scholar
• J. D. Vander, B. Robinson, K. K. Taylor, and L. A. Hunsaker. (1992). Reduction of trioses by NADPH-dependent aldo-keto reductases. Aldose reductase, methylglyoxal, and diabetic complications. J Biol Chem 267:4364–4369.
   PubMed Web of Science ®Google Scholar
• T. Varma, S. Q. Liu, M. West, V. Thongboonkerd, P. P. Ruvolo, W. S. May, and et al (2003). Protein kinase C–dependent phosphorylation and mitochondrial translocation of aldose reductase. FEBS Lett 534:175–179.
   PubMed Web of Science ®Google Scholar
• M. C. Vega, E. Lorentzen, A. Linden, and M. Wilmanns. (2003). Evolutionary markers in the (beta/alpha)8-barrel fold. Curr Opin Chem Biol 7:694–701.
   PubMed Web of Science ®Google Scholar
• L. Vergnes, J. Phan, A. Stolz, and K. Reue. (2003). A cluster of eight hydroxysteroid dehydrogenase genes belonging to the aldo-keto reductase supergene family on mouse chromosome 13. J Lipid Res 44:503–511.
   PubMed Web of Science ®Google Scholar
• M. Verma, H. J. Martin, W. Haq, T. R O'Connor, E. Maser, and G. K. Balendiran. (2008). Inhibiting wild-type and C299S mutant AKR1B10; a homologue of aldose reductase upregulated in cancers. Eur J Pharmacol 584:213–221.
   PubMed Web of Science ®Google Scholar
• N. Verzijl, J. DeGroot, R. A. Bank, M. T. Bayliss, J. W. J. Bijlsma, F. P. J. G. Lafeber, and et al (2001). Age-related accumulation of the advanced glycation end-product pentosidine in human articular cartilage aggrecan: the use of pentosidine levels as a quantitative measure of protein turnover. Matrix Biol 20:409–417.
   PubMed Web of Science ®Google Scholar
• N. Verzijl, J. DeGroot, C. Ben Zaken, O. Braun-Benjamin, A. Maroudas, R. A. Bank, and et al (2002). Cross-linking by advanced glycation end products increases the stiffness of the collagen network in human articular cartilage—a possible mechanism through which age is a risk factor for osteoarthritis. Arthr Rheum 46:114–123.
   PubMed Web of Science ®Google Scholar
• H. Vlassara, and M. R. Palace. (2002). Diabetes and advanced glycation endproducts. J Intern Med 251:87–101.
   PubMed Web of Science ®Google Scholar
• K. Watanabe, Y. Iguchi, S. Iguchi, Y. Arai, O. Hayaishi, and L. J. Roberts. (1986). Stereospecific conversion of prostaglandin-D2 to (5Z,13E)-(15S)-9-alpha,-11-beta,15-trihydroxyprosta-5,13-dien-1-oic acid (9-alpha,11-beta-prostaglandin-F2) and of prostaglandin-H2 to prostaglandin-F2-alpha by bovine lung prostaglandin-F synthase. Proc Natl Acad Sci U S Am 83:1583–1587.
   PubMed Web of Science ®Google Scholar
• K. Watanabe, R. Yoshida, T. Shimizu, and O. Hayaishi. (1985). Enzymatic Formation of prostaglandin-F2-alpha from prostaglandin-H2 and prostaglandin-D2 - purification and properties of prostaglandin-F synthetase from bovine lung. J Biol Chem 260:7035–7041.
   PubMed Web of Science ®Google Scholar
• A. D. Watson, N. Leitinger, M. Navab, K. F. Faull, S. Horkko, J. L. Witztum, and et al (1997). Structural identification by mass spectrometry of oxidized phospholipids in minimally oxidized low-density lipoprotein that induce monocyte/endothelial interactions and evidence for their presence in vivo. J Biol Chem 272:13597–13607.
   PubMed Web of Science ®Google Scholar
• R. B. Weiss. (1992). The anthracyclines—will we ever find a better doxorubicin. Sem Oncol 19:670–686.
   PubMed Web of Science ®Google Scholar
• T. Wendt, N. Tanji, J. Guo, B. I. Hudson, A. Bierhaus, R. Ramasamy, and et al (2003). Glucose, glycation, and RAGE: implications for amplification of cellular dysfunction in diabetic nephropathy. J Am Soc Nephrol 14:1383–1395.
   PubMed Web of Science ®Google Scholar
• J. Weng, Y. Cao, N. Moss, and M. Zhou. (2006). Modulation of voltage-dependent Shaker family potassium channels by an aldo-keto reductase. J Biol Chem 281:15194–15200.
   PubMed Web of Science ®Google Scholar
• B. Wermuth. (1981). Purification and properties of an NADPH-dependent carbonyl reductase from human brain—relationship to prostaglandin 9-ketoreductase and xenobiotic ketone reductase. J Biol Chem 256:1206–1213.
   PubMed Web of Science ®Google Scholar
• B. Wermuth. (1985). Aldo-keto reductases. Prog Clin Biol Res 174:209–230.
   PubMedGoogle Scholar
• B. Wermuth. (1991). Inhibition of aldehyde reductase by carboxylic acids. Adv Exp Med Biol 284:197–204.
   PubMedGoogle Scholar
• B. Wermuth, and C. Monder. (1983). Aldose and aldehyde reductase exhibit isocorticosteroid reductase activity. Eur J Biochem 131:423–426.
   PubMedGoogle Scholar
• B. Wermuth, J. D. Munch, and J. P. von Wartburg. (1977). Purification and properties of NADPH-dependent aldehyde reductase from human liver. J Biol Chem 252:3821–3828.
   PubMed Web of Science ®Google Scholar
• S. R. Whittle, and A. J. Turner. (1981). Biogenic aldehyde metabolism in rat brain. Differential sensitivity of aldehyde-reductase isoenzymes to sodium valproate. Biochim Biophys Acta 657:94–105.
   PubMed Web of Science ®Google Scholar
• D. K. Wilson, K. M. Bohren, K. H. Gabbay, and F. A. Quiocho. (1992). An unlikely sugar substrate site in the 1.65 A structure of the human aldose reductase holoenzyme implicated in diabetic complications. Science 257:81–84.
   PubMed Web of Science ®Google Scholar
• D. K. Wilson, T. Nakano, J. M. Petrash, and F. A. Quiocho. (1995). 1.7 A structure of FR-1, a fibroblast growth factor–induced member of the aldo-keto reductase family, complexed with coenzyme and inhibitor. Biochemistry 34:14323–14330.
   PubMed Web of Science ®Google Scholar
• D. K. Wilson, I. Tarle, J. M. Petrash, and F. A. Quiocho. (1993). Refined 1.8 A structure of human aldose reductase complexed with the potent inhibitor zopolrestat. Proc Natl Acad Sci U S A 90:9847–9851.
   PubMed Web of Science ®Google Scholar
• E. Wise, W. S. Yew, P. C. Babbitt, J. A. Gerlt, and I. Rayment. (2002). Homologous (beta/alpha)8-barrel enzymes that catalyze unrelated reactions: orotidine 5′-monophosphate decarboxylase and 3-keto-L-gulonate 6-phosphate decarboxylase. Biochemistry 41:3861–3869.
   PubMed Web of Science ®Google Scholar
• V. Wsol, B. Szotakova, H. J. Martin, and E. Maser. (2007). Aldo-keto reductases (AKR) from the AKR1C subfamily catalyze the carbonyl reduction of the novel anticancer drug oracin in man. Toxicology 238:111–118.
   PubMed Web of Science ®Google Scholar
• V. Wsol, B. Szotakova, L. Skalova, and E. Maser. (2004). The novel anticancer drug oracin: different stereo specificity and cooperativity for carbonyl reduction by purified human liver 11 beta-hydroxysteroid dehydrogenase type 1. Toxicology 197:253–261.
   PubMed Web of Science ®Google Scholar
• C. Yabe-Nishimura. (1998). Aldose reductase in glucose toxicity: a potential target for the prevention of diabetic complications [in process citation]. Pharmacol Rev 50:21–33.
   PubMed Web of Science ®Google Scholar
• S. Yamano, F. Ichinose, T. Todaka, and S. Toki. (1999). Purification and characterization of two major forms of naloxone reductase from rabbit liver cytosol, new members of aldo-keto reductase superfamily. Biol Pharm Bull 22:1038–1046.
   PubMed Web of Science ®Google Scholar
• R. L. Yan, X. Y. Zu, J. Ma, Z. W. Liu, M. Adeyanju, and D. L. Cao. (2007). Aldo-keto reductase family 1 B10 gene silencing results in growth inhibition of colorectal cancer cells: implication for cancer intervention. Int J Cancer 121:2301–2306.
   PubMed Web of Science ®Google Scholar
• Q. Ye, D. Hyndman, N. Green, X. Li, B. Korithoski, Z. Jia, and et al (2001). Crystal structure of an aldehyde reductase Y50F mutant-NADP complex and its implications for substrate binding. Proteins 44:12–19.
   PubMed Web of Science ®Google Scholar
• D. J. Yee, V. Balsanek, D. R. Bauman, T. M. Penning, and D. Sames. (2006). Fluorogenic metabolic probes for direct activity readout of redox enzymes: selective measurement of human AKR1C2 in living cells. Proc Natl Acad Sci U S A 103:13304–13309.
   Google Scholar
• H. Yoshitake, M. Takahashi, H. Ishikawa, M. Nojima, H. Iwanari, A. Watanabe, and et al (2007). Aldo-keto reductase family 1, member B10 in uterine carcinomas: a potential risk factor of recurrence after surgical therapy in cervical cancer. Int J Gynecol Cancer 17:1300–1306.
   PubMed Web of Science ®Google Scholar
• E. Zeindl-Eberhart, S. Klugbauer, N. Dimitrijevic, P. R. Jungblut, S. Lamer, and H. M. Rabes. (2001). Proteome analysis of rat hepatomas: carcinogen-dependent tumor-associated protein variants. Electrophoresis 22:3009–3018.
   PubMed Web of Science ®Google Scholar