The aldo-keto reductase superfamily and its role in drug metabolism and detoxification

Drug Metabolism Reviews

Volumn 40, Issue 4, 2008, Pages 553-624

  Barski, Oleg A ^a   Tipparaju, Srinivas M ^a   Bhatnagar, Aruni ^a  

^a University of Louisville School of Medicine   (United States)

Author keywords

, barrel; AKR; Aldo keto reductase; Carbonyl reduction; Detoxification; Gene homology; Pharmaceutical; Structural motif; Xenobiotic

Indexed keywords

1 [5 (4 FLUOROBENZYL) 2 FURYL] 3 (1,2,4 TRIAZOL 3 YL) 1,3 PROPANEDIONE; 4 (METHYLNITROSAMINO) 1 (3 PYRIDYL) 1 BUTANOL; ACETOHEXAMIDE; AFLATOXIN; AFLATOXIN B1; ALDEHYDE REDUCTASE; ASCORBIC ACID; BEFUNOLOL; DOLASETRON MESILATE; ETACRYNIC ACID; GLUCOSE; GLUCURONIC ACID; HALOPERIDOL; HYDROXYSTEROID DEHYDROGENASE; IMIRESTAT; NAFIMIDONE; NALOXONE; NALTREXONE; NONSTEROID ANTIINFLAMMATORY AGENT; OXIDOREDUCTASE; PROSTAGLANDIN; SORBINIL; STEROID; STEROID 5BETA REDUCTASE; SUCCINIC SEMIALDEHYDE; TIMIPERONE; TRICYCLIC AROMATIC COMPOUND; UNINDEXED DRUG; VOLTAGE GATED POTASSIUM CHANNEL; XYLULOSE;

BIOSYNTHESIS; DRUG DETOXIFICATION; DRUG METABOLISM; ENZYME ANALYSIS; ENZYME MECHANISM; ENZYME STRUCTURE; GENE STRUCTURE; LIPID PEROXIDATION; PROTEIN CONFORMATION; PROTEIN LOCALIZATION; PROTEIN MOTIF; REVIEW; STRUCTURE ANALYSIS; XENOBIOTIC METABOLISM;

ALCOHOL OXIDOREDUCTASES; ANIMALS; HUMANS; METABOLIC DETOXICATION, DRUG; PHARMACEUTICAL PREPARATIONS; PROTEIN STRUCTURE, SECONDARY;

EID: 54549110136     PISSN: 03602532     EISSN: 10979883     Source Type: Journal    
DOI: 10.1080/03602530802431439     Document Type: Review

References (324)

1. + channels in mouse ventricular myocytes. Circ. Res. 96:451-458.
2. Amaro, R., Tajkhorshid, E., Luthey-Schulten, Z. (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.
3. Atalla, A., Breyer-Pfaff, U., Maser, E. (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.
4. Atalla, A. Maser, E. (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.
5. + channels. Proc Natl Acad Sci U S A 95:11703-11708.
6. Azuma, Y., Nishinaka, T., Ushijima, S., Soh, J., Katsuyama, M., Lu, H. P., 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.
7. Bachur, N. R. (1976). Cytoplasmic aldo-keto reductases: a class of drug metabolizing enzymes. Science 193:595-597.
8. Barski, O. A., Gabbay, K. H., Bohren, K. M. (1996). The C-terminal loop of aldehyde reductase determines the substrate and inhibitor specificity. Biochemistry 35:14276-14280.
9. Barski, O. A., Gabbay, K. H., Bohren, K. M. (1999). Characterization of the human aldehyde reductase gene and promoter. Genomics 60:188-198.
10. Barski, O. A., Gabbay, K. H., Grimshaw, C. E., Bohren, K. M. (1995). Mechanism of human aldehyde reductase: characterization of the active site pocket. Biochemistry 34:11264-11275.
11. Barski, O. A., Papusha, V. Z., Ivanova, M. M., Rudman, D. M., Finegold, M. J. (2005). Developmental expression and function of aldehyde reductase in proximal tubules of the kidney. Am J Physiol Renal Physiol 289:F200-F207.
12. Barski, O. A., Papusha, V. Z., Kunkel, G. R., Gabbay, K. H. (2004). Regulation of aldehyde reductase expression by STAF and CHOP. Genomics 83:119-129.
13. Bauman, D. R., Rudnick, S. I., Szewczuk, L. M., Jin, Y., Gopishetty, S., Penning, T. M. (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.
14. Baynes, J. W., Thorpe, S. R. (1999). Role of oxidative stress in diabetic complications: a new perspective on an old paradigm. Diabetes 48:1-9.
15. + bound to 3 alpha-hydroxysteroid/ dihydrodiol dehydrogenase. Structure 5:799-812.
16. +. Biochemistry 35:10702-10711.
17. Berliner, J. A., Territo, M. C., Sevanian, A., Ramin, S., Kim, J. A., Bamshad, B., et al. (1990). Minimally modified low-density lipoprotein stimulates monocyte endothelial interactions. J Clin Invest 85:1260-1266.
18. Bhatnagar, A., Liu, S., Das, B., Ansari, N. H., Srivastava, S. K. (1990). Inhibition-kinetics of human kidney aldose and aldehyde reductases by aldose reductase inhibitors. Biochem Pharmacol 39:1115-1124.
19. Bhatnagar, A., Liu, S. Q., Srivastava, S., Ramana, K. V., Srivastava, S. K. (2004). Aldose reductase and the stress response. Aldo-Keto Reductases Toxicant Metab 865:199-211.
20. Bhatnagar, A., Liu, S. Q., Ueno, N., Chakrabarti, B., Srivastava, S. K. (1994). Human placental aldose reductase: role of Cys-298 in substrate and inhibitor binding. Biochim Biophys Acta 1205:207-214.
21. Bhatnagar, A., Srivastava, S. K. (1992). Aldose reductase: congenial and injurious profiles of an enigmatic enzyme. Biochem Med Metab Biol 48:91-121.
22. Bohren, K. M., Barski, O. A., Gabbay, K. G. (1996). Characterization of a novel murine aldo-keto reductase. In: Weiner et al. (Eds.), Enzymology and Molecular Biology of Carbonyl Metabolism 6 (pp. 455-464). New York: Plenum Press.
23. Bohren, K. M., Grimshaw, C. E., Lai, C. J., Harrison, D. H., Ringe, D., Petsko, G. A., 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.
24. Bohren, K. M., Page, J. L., Shankar, R., Henry, S. P., Gabbay, K. H. (1991). Expression of human aldose and aldehyde reductases. Site-directed mutagenesis of a critical lysine 262. J Biol Chem 266:p24031-24037.
25. Bosron, W. F., Prairie, R. L. (1972). Triphosphopyridine nucleotide-linked aldehyde reductase. I. Purification and properties of the enzyme from pig kidney cortex. J Biol Chem 247:4480-4485.
26. Branlant, G. (1982). Properties of an aldose reductase from pig lens. Comparative studies of an aldehyde reductase from pig lens. Eur J Biochem 129:99-104.
27. Branlant, G., Biellmann, J. F. (1980). Purification and some properties of aldehyde reductases from pig liver. Eur J Biochem 105:611-621.
28. Breyer-Pfaff, U., Martin, H. J., Ernst, M., Maser, E. (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.
29. Breyer-Pfaff, U., Nill, K. (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.
30. Breyer-Pfaff, U., Nill, K. (2004). Carbonyl reduction of naltrexone and dolasetron by oxidoreductases isolated from human liver cytosol. J Pharm Pharmacol 56:1601-1606.
31. Bril, V., Buchanan, R. A. (2006). Long-term effects of ranirestat (AS-3201) on peripheral nerve function in patients with diabetic sensorimotor polyneuropathy. Diabetes Care 29:68-72.
32. Brownlee, M. (1992). Glycation products and the pathogenesis of diabetic complications. Diabetes Care 15:1835-1843.
33. Brownlee, M. (2001). Biochemistry and molecular cell biology of diabetic complications. Nature 414:813-820.
34. Burczynski, M. E., Lin, H. K., Penning, T. M. (1999). Isoform-specific induction of a human aldoketo 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.
35. Buzzi, A., Wu, Y., Frantseva, M. V., Velazquez, J. L. P., Cortez, M. A., Liu, C. C., et al. (2006). Succinic semialdehyde dehydrogenase deficiency: GABA(B) receptor-mediated function. Brain Res 1090:15-22.
36. Byrns, M. C., Steckelbroeck, S., Penning, T. M. (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.
37. Campbell, M., Trimble, E. R. (2005). Modification of PI3K and MAPK-dependent chemotaxis in aortic vascular smooth muscle cells by protein kinase C betaII. Circ Res 96:197-206.
38. Campomanes, C. R., Carroll, K. I., Manganas, L. N., Hershberger, M. E., Gong, B., Antonucci, D. E., et al. (2002). Kv beta subunit oxidoreductase activity and Kv1 potassium channel trafficking. J Biol.Chem 277:8298-8305.
39. Camu, F., Van Lersberghe, C., Lauwers, M. H. (1992). Cardiovascular risks and benefits of perioperative nonsteroidal anti-inflammatory drug treatment. Drugs 44(Suppl 5):42-51.
40. Cao, D., Fan, S. T., Chung, S. M. (1998). Identification and characterization of a novel human aldose reductase-like gene. J Biol Chem 273:11429-11435.
41. Chang, W. H. (1992). Reduced haloperidol - a factor in determining the therapeutic benefit of haloperidol treatment. Psychopharmacology 106:289-296.
42. Chen, D. B., Westfall, S. D., Fong, H. W., Roberson, M. S., Davis, J. S. (1998). Prostaglandin F2alpha stimulates the Raf/MEK1/mitogen-activated protein kinase signaling cascade in bovine luteal cells. Endocrinology 139:3876-3885.
43. Chung, S. S. M., Chung, S. K. (2003). Genetic analysis of aldose reductase in diabetic complications. Curr Med Chem 10:1375-1387.
44. Connor, J. X., McCormack, K., Pletsch, A., Gaeta, S., Ganetzky, B., Chiu, S. Y., et al. (2005). Genetic modifiers of the Kv beta 2-null phenotype in mice. Genes Brain Behav 4:77-88.
45. Crosas, B., Hyndman, D. J., Gallego, O., Martras, S., Pares, X., Flynn, T. G., 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.
46. Davidge, S. T. (2001). Prostaglandin H synthase and vascular function. Circ Res 89:650-660.
47. Davidson, W. S., Walton, D. J., Flynn, T. G. (1978). A comparative study of the tissue and species distribution of NADPH-dependent aldehyde reductase. Comp Biochem Physiol B 60:309-315.
48. Demaine, A. G. (2003). Polymorphisms of the aldose reductase gene and susceptibility to diabetic microvascular complications. Curr Med Chem 10:1389-1398.
49. Desmond, J. C., Mountford, J. C., Drayson, M. T., Walker, E. A., Hewison, M., Ride, J. P., 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.
50. Deyashiki, Y., Ohshima, K., Nakanishi, M., Sato, K., Matsuura, K., Hara, A. (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.
51. Dhagat, U., Carbone, V., Chung, R. P. T., Schulze-Briese, C., Endo, S., Hara, A., 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.
52. Dhagat, U., Endo, S., Hara, A., El Kabbani, O. (2008a). Inhibition of 3(17)alpha-hydroxysteroid dehydrogenase (AKR1C21) by aldose reductase inhibitors. Bioorg Med Chem 16:3245-3254.
53. Dhagat, U., Endo, S., Sumii, R., Hara, A., El Kabbani, O. (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.
54. Dozier, B., Watanabe, K., Duffy, D. (2008). Two pathways for prostaglandin F2{alpha} (PGF2{alpha}) synthesis by the primate periovulatory follicle. Reproduction 136:53-63.
55. Du, Y., Tsai, S., Keller, J. R., Williams, S. C. (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.
56. Dvornik, E., Simard-Duquesne, N., Krami, M., Sestanj, K., Gabbay, K. H., Kinoshita, J. H., et al. (1973). Polyol accumulation in galactosemic and diabetic rats: control by an aldose reductase inhibitor. Science 182:1146-1148.
57. Dyck, P. J., Zimmerman, B. R., Vilen, T. H., Minnerath, S. R., Karnes, J. L., Yao, J. K., et al. (1988). Nerve glucose, fructose, sorbitol, myo-inositol, and fiber degeneration and regeneration in diabetic neuropathy. N Engl J Med 319:542-548.
58. Eaton, R. P., Sibbitt, W. L., Jr., Harsh, A. (1985). The effect of an aldose reductase inhibiting agent on limited joint mobility in diabetic patients. JAMA 253:1437-1440.
59. +/NADPH and alrestatin-like inhibitors. Biochemistry 33:7157-7165.
60. el-Kabbani, O., Judge, K., Ginell, S. L., Myles, D. A., DeLucas, L. J., Flynn, T. G. (1995). Structure of porcine aldehyde reductase holoenzyme. Nat Struct Biol 2:687-692.
61. Ellis, E. M. (2002). Microbial aldo-keto reductases. FEMS Microbiol Lett 216:123-131.
62. Ellis, E. M., Judah, D. J., Neal, G. E., Hayes, J. D. (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.
63. Endo, S., Matsumoto, K., Matsunaga, T., Ishikura, S., Tajima, K., El Kabbani, O., et al. (2006). Substrate specificity of a mouse aldo-keto reductase (AKR1C12). Biol Pharmaceut Bull 29:2488-2492.
64. Endo, S., Matsunaga, T., Horie, K., Tajima, K., Bunai, Y., Carbone, V., 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.
65. + channel beta-subunit (Hkv-beta-1.3) is produced via alternative messenger - RNA splicings. J Biol Chem 270:28531-28534.
66. Esterbauer, H., Schaur, R. J., Zollner, H. (1991). Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde, and related aldehydes. Free Radic Biol Med 11:81-128.
67. Faucher, F., Cantin, L., Jesus-Tran, K. P., Lemieux, M., Luu-The, V., Labrie, F., 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.
68. Feather, M. S., Flynn, T. G., Munro, K. A., Kubiseski, T. J., Walton, D. J. (1995). Catalysis of reduction of carbohydrate 2-oxoaldehydes (osones) by mammalian aldose reductase and aldehyde reductase. Biochim Biophys Acta 1244:10-16.
69. + channel beta subunit to specifically enhance Kv2.2 (CDRK) expression. J Biol Chem 271:26341-26348.
70. Fujii, Y., Watanabe, K., Hayashi, H., Urade, Y., Kuramitsu, S., Kagamiyama, H., et al. (1990). Purification and characterization of Rho-crystallin from Japanese common bullfrog lens. J Biol Chem 265:9914-9923.
71. Fukumoto, S., Yamauchi, N., Moriguchi, H., Hippo, Y., Watanabe, A., Shibahara, J., 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.
72. Gabbay, K. H. (1975). Hyperglycemia, polyol metabolism, and complications of diabetes mellitus. Annu Rev Med 26:521-536.
73. Gabbay, K. H. (2004). Aldose reductase inhibition in the treatment of diabetic neuropathy: where are we in 2004? Curr Diab Rep 4:405-408.
74. Gabbay, K. H., Merola, L. O., Field, R. A. (1966). Sorbitol pathway: presence in nerve and cord with substrate accumulation in diabetes. Science 151:209-210.
75. Gallego, O., Belyaeva, O. V., Porte, S., Ruiz, F. X., Stetsenko, A. V., Shabrova, E. V., et al. (2006). Comparative functional analysis of human medium-chain dehydrogenases, short-chain dehydrogenases/reductases, and aldo-keto reductases with retinoids. Biochem J 399:101-109.
76. Gallego, O., Ruiz, F. X., Ardevol, A., Dominguez, M., Alvarez, R., de Lera, A. R., 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.
77. Gardner, R., Kazi, S., Ellis, E. M. (2004). Detoxication of the environmental pollutant acrolein by a rat liver aldo-keto reductase. Toxicol Lett 148:65-72.
78. Gersl, V., Mazurova, Y., Bajgar, J., Melka, M., Hrdina, R., Palicka, V. (1996). Lack of cardiotoxicity of a new antineoplastic agent, a synthetic derivative of indenoisochinoline: comparison with daunorubicin in rabbits. Arch Toxicol 70:645-651.
79. Gibson, K. M., Hoffmann, G. F., Hodson, A. K., Bottiglieri, T., Jakobs, C. (1998). 4-hydroxybutyric acid and the clinical phenotype of succinic semialdehyde dehydrogenase deficiency, an inborn error of GABA metabolism. Neuropediatrics 29:14-22.
80. + channel inactivation, spike broadening, and after-hyperpolarization in Kv beta 1.1-deficient mice with impaired learning. Learn Mem 5:257-273.
81. Glass, C. K., Witztum, J. L. (2001). Atherosclerosis: the road ahead. Cell 104:503-516.
82. Gonzalez, J. P., Brogden, R. N. (1988). Naltrexone - a review of Its pharmacodynamic and pharmacokinetic properties and therapeutic efficacy in the management of opioid dependence. Drugs 35:192-213.
83. Grimshaw, C. E. (1992). Aldose reductase: model for a new paradigm of enzymic perfection in detoxification catalysts. Biochemistry 31:10139-10145.
84. Grimshaw, C. E., Bohren, K. M., Lai, C. J., Gabbay, K. H. (1995). Human aldose reductase - rate constants for a mechanism including interconversion of ternary complexes by recombinant wild-type enzyme. Biochemistry 34:14356-14365.
85. Gu, C., Jan, Y. N., Jan, L. Y. (2003). A conserved domain in axonal targeting of Kv1 (Shaker) voltage-gated potassium channels. Science 301:646-649.
86. Guengerich, F. P., Cai, H., McMahon, M., Hayes, J. D., Sutter, T. R., Groopman, J. D., et al. (2001). Reduction of aflatoxin B1 dialdehyde by rat and human aldo-keto reductases. Chem Res Toxicol 14:727-737.
87. Gui, T., Tanimoto, T., Kokai, Y., Nishimura, C. (1995). Presence of a closely related subgroup in the aldo-ketoreductase family of the mouse. Eur J Biochem 227:448-453.
88. + channel beta subunit. Cell 97:943-952.
89. + channels. Science 289: 123-127.
90. Hara, A., Hasebe, K., Hayashibara, M., Matsuura, K., Nakayama, T., Sawada, H. (1986). Dihydrodiol dehydrogenases in guinea pig liver. Biochem Pharmacol 35:4005-4012.
91. Harrison, D. H., Bohren, K. M., Ringe, D., Petsko, G. A., Gabbay, K. H. (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.
92. Hayashi, H., Fujii, Y., Watanabe, K., Hayaishi, O. (1990). Enzymatic formation of prostaglandin-F2-alpha in human brain. Neurochem Res 15:385-392.
93. Hayes, J. D., Judah, D. J., McLellan, L. I., Neal, G. E. (1991). Contribution of the glutathione S-transferases to the mechanisms of resistance to aflatoxin B1. Pharmacol Ther 50:443-472.
94. Hayes, J. D., Judah, D. J., Neal, G. E. (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.
95. Hegyi, H., Gerstein, M. (1999). The relationship between protein structure and function: a comprehensive survey with application to the yeast genome. J Mol Biol 288:147-164.
96. Heredia, V. V., Penning, T. M. (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.
97. Hers, H. G. (1960). [Aldose reductase.]. Biochim Biophys Acta 37:120-126.
98. Higaki, Y., Usami, N., Shintani, S., Ishikura, S., El Kabbani, O., Hara, A. (2003). Selective and potent inhibitors of human 20 alpha-hydroxysteroid dehydrogenase (AKR1C1) that metabolizes neurosteroids derived from progesterone. Chemico Biol Interact 143:503-513.
99. Hinshelwood, A., McGarvie, G., Ellis, E. (2002a). Characterisation of a novel mouse liver aldo-keto reductase AKR7A5. FEBS Lett 523:213-218.
100. Hinshelwood, A., McGarvie, G., Ellis, E. (2002b). Characterisation of a novel mouse liver aldo-keto reductase AKR7A5. FEBS Lett 523:213-218.
101. Hinshelwood, A., McGarvie, G., Ellis, E. M. (2003). Substrate specificity of mouse aldo-keto reductase AKR7A5. Chemico Biol Interact 143:263-269.
102. Ho, H. T., Chung, S. K., Law, J. W., Ko, B. C., Tam, S. C., Brooks, H. L., et al. (2000). Aldose reductase-deficient mice develop nephrogenic diabetes insipidus. Mol Cell Biol 20, 5840-5846.
103. Hocker, B., Claren, J., Sterner, R. (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.
104. Hoffman, P. L., Wermuth, B., von Wartburg, J. P. (1980). Human brain aldehyde reductases: relationship to succinic semialdehyde reductase and aldose reductase. J Neurochem 35:354-366.
105. Horiuchi, S. (2002). The liver is the main site for metabolism of circulating advanced glycation end products. J Hepatol 36:123-125.
106. Horkko, S., Bird, D. A., Miller, E., Itabe, H., Leitinger, N., Subbanagounder, G., 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.
107. Huang, Z. L., Urade, Y., Hayaishi, O. (2007). Prostaglandins and adenosine in the regulation of sleep and wakefulness. Curr Opin Pharmacol 7:33-38.
108. Hutchison, J. B., Steimer, T. (1981). Brain 5beta-reductase: a correlate of behavioral sensitivity to androgen. Science 213:244-246.
109. Hyndman, D. J., Flynn, T. G. (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.
110. Ikeda, S., Okuda-Ashitaka, E., Masu, Y., Suzuki, T., Watanabe, K., Nakao, M., et al. (1999). Cloning and characterization of two novel aldo-keto reductases (AKR1C12 and AKR1C13) from mouse stomach. FEBS Lett 459:433-437.
111. Imamura, Y., Sanai, K., Seri, K., Akita, H. (2001). Hypoglycemic effect of S(-)-hydroxyhexamide, a major metabolite of acetohexamide, and its enantiomer R(+)-hydroxyhexamide. Life Sci 69:1947-1955.
112. Imamura, Y., Shimada, H. (2005). Differential pharmacokinetics of acetohexamide in male Wistar-Imamichi and Sprague-Dawley rats: role of microsomal carbonyl reductase. Biol Pharm Bull 28:185-187.
113. Ireland, L. S., Harrison, D. J., Neal, G. E., Hayes, J. D. (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.
114. Ishida, M., Choi, J. H., Hirabayashi, K., Matsuwaki, T., Suzuki, M., Yamanouchi, K., et al. (2007). Reproductive phenotypes in mice with targeted disruption of the 20 alpha-hydroxysteroid dehydrogenase gene. J Reprod Dev 53:499-508.
115. Ishida, M., Hirabayashi, K., Suzuki, M., Yamanouchi, K., Nishihara, M. (2003). Cloning and chromosomal localization of mouse 20 alpha-hydroxysteroid dehydrogenase gene. J Reprod Dev 49:79-85.
116. Ishikura, S., Usami, N., Nakajima, S., Kameyama, A., Shiraishi, H., Carbone, V., 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.
117. Jaspan, J., Maselli, R., Herold, K., Bartkus, C. (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.
118. Jez, J. M., Bennett, M. J., Schlegel, B. P., Lewis, M., Penning, T. M. (1997a). Comparative anatomy of the aldo-keto reductase superfamily. Biochem J 326:625-636.
119. Jez, J. M., Flynn, T. G., Penning, T. M. (1997b). A new nomenclature for the aldo-keto reductase superfamily. Biochem Pharmacol 54:639-647.
120. Jez, J. M., Schlegel, B. P., Penning, T. M. (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.
121. Ji, Q., Aoyama, C., Chen, P. K., Stolz, A., Liu, P. (2005). Localization and altered expression of AKR1C family members in human ovarian tissues. Mol Cell Probes 19:261-266.
122. Ji, Q., Chang, L., VanDenBerg, D., Stanczyk, F. Z., Stolz, A. (2003). Selective reduction of AKR1C2 in prostate cancer and its role in DHT metabolism. Prostate 54:275-289.
123. Jin, Y., Penning, T. M. (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.
124. Jin, Y., Penning, T. M. (2007). Aldo-keto reductases and bioactivation/detoxication. Annu Rev Pharmacol Toxicol 47:263-292.
125. Johnson, D. N., Egner, P. A., Obrian, G., Glassbrook, N., Roebuck, B. D., Sutter, T. R., 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.
126. Jornvall, H., Persson, B., Krook, M., Atrian, S., Gonzalezduarte, R., Jeffery, J., et al. (1995). Short-chain dehydrogenases reductases (Sdr). Biochemistry 34:6003-6013.
127. Jurgens, C., Strom, A., Wegener, D., Hettwer, S., Wilmanns, M., Sterner, R. (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.
128. Jurgens, G., Chen, Q., Esterbauer, H., Mair, S., Ledinski, G., Dinges, H. P. (1993). Immunostaining of human autopsy aortas with antibodies to modified apolipoprotein B and apoprotein(a). Arterioscler Thromb 13:1689-1699.
129. Kador, P. F., Sharpless, N. E. (1983). Pharmacophor requirements of the aldose reductase inhibitor site. Mol Pharmacol 24:521-531.
130. Kaiserova, H., Kvasnickova, E. (2005). Inhibition study of rabbit liver cytosolic reductases involved in daunorubicin toxication. J Enz Inhib Med Chem 20:477-483.
131. Kaiserova, K., Srivastava, S., Hoetker, J. D., Awe, S. O., Tang, X. L., Cai, J., et al. (2006). Redox activation of aldose reductase in the ischemic heart. J Biol Chem 281:15110-15120.
132. Kaiserova, K., Tang, X. L., Srivastava, S., Bhatnagar, A. (2008). Role of nitric oxide in regulating aldose reductase activation in the ischemic heart. J Biol Chem 283:9101-9112.
133. Kallberg, Y., Oppermann, U., Jornvall, H., Persson, B. (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.
134. Kallberg, Y., Oppermann, U., Jornvall, H., Persson, B. (2002b). Short-chain dehydrogenases/reductases (SDRs) - coenzyme-based functional assignments in completed genomes. Eur J Biochem 269:4409-4417.
135. Keenan, C., Ghaffar, S., Grant, A. W., Hinshelwood, A., Li, D., McGarvie, G., et al. (2006). Succinic semialdehyde reductases: contribution to gamma-hydroxybutyrate catabolism and subcellular localization. In: H.Weiner, H., B. Plapp, B., R. Lindahl, R., Maser, E. (Eds.), Enzymology and Molecular Biology of Carbonyl Metabolism 12 (pp. 388-395). West Lafayette, Indiana, USA: Purdue University Press.
136. Kelly, V. P., Ireland, L. S., Ellis, E. M., Hayes, J. D. (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.
137. Kelly, V. P., Sherratt, P. J., Crouch, D. H., Hayes, J. D. (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.
138. Kensler, T. W., Curphey, T. J., Maxiutenko, Y., Roebuck, B. D. (2000). Chemoprotection by organosulfur inducers of phase 2 enzymes: dithiolethiones and dithiins. Drug Metabol Drug Interact 17:3-22.
139. Kilunga, K. B., Inoue, T., Okano, Y., Kabututu, Z., Martin, S. K., Lazarus, M., 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.
140. Kinoshita, J. H. (1990). A thirty-year journey in the polyol pathway. Exp Eye Res 50:567-573.
141. Kishimoto, M., Kawamori, R., Kamada, T., Inaba, T. (1994). Carbonyl reductase activity for acetohexamide in human erythrocytes. Drug Metab Dispos 22:367-370.
142. Kita, T., Kume, N., Yokode, M., Ishii, K., Arai, H., Horiuchi, H., et al. (2000). Oxidized-LDL and atherosclerosis. Role of LOX-1. Ann N Y Acad Sci 902:95-100.
143. Knight, L. P., Primiano, T., Groopman, J. D., Kensler, T. W., Sutter, T. R. (1999). cDNA cloning, expression, and activity of a second human aflatoxin B1-metabolizing member of the aldoketo reductase superfamily, AKR7A3. Carcinogenesis 20:1215-1223.
144. Kotokorpi, P., Gardmo, C., Nystrom, C. S., Mode, A. (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.
145. Kozma, E., Brown, E., Ellis, E. M., Lapthorn, A. J. (2002). The crystal structure of rat liver AKR7A1 - a dimeric member of the aldo-keto reductase superfamily. J Biol Chem 277:16285-16293.
146. Kratzer, R., Egger, S., Nidetzky, B. (2008). Integration of enzyme, strain, and reaction engineering to overcome limitations of baker's yeast in the asymmetric reduction of alpha-keto esters. Biotechnol Bioeng (in press) Pubmed ID: 18623228.
147. Kudo, S., Ishizaki, T. (1999). Pharmacokinetics of haloperidol - an update. Clin Pharmacokinet 37:435-456.
148. Lau, E. T., Cao, D., Lin, C., Chung, S. K., Chung, S. S. (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.
149. Lavrentyev, E. N., Estes, A. M., Malik, K. U. (2007). Mechanism of high glucose-induced angiotensin II production in rat vascular smooth muscle cells. Circ Res 101:455-464.
150. Lee, A. Y., Chung, S. K., Chung, S. S. (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.
151. Lee, Y. S., Hodoscek, M., Brooks, B. R., Kador, P. F. (1998). Catalytic mechanism of aldose reductase studied by the combined potentials of quantum mechanics and molecular mechanics. Biophys Chem 70:203-216.
152. Lefrancois-Martinez, A. M., Tournaire, C., Martinez, A., Berger, M., Daoudal, S., Tritsch, P., 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.
153. Leicher, T., Bahring, R., Isbrandt, D., Pongs, O. (1998). Coexpression of the KCNA3B gene product with Kv1.5 leads to a novel A-type potassium. J Biol Chem 273:35095-35101.
154. Leitinger, N., Tyner, T. R., Oslund, L., Rizza, C., Subbanagounder, G., Lee, H., 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.
155. Lemonde, H. A., Custard, E. J., Bouquet, J., Duran, M., Overmars, H., Scambler, P. J., 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.
156. Li, S., Hanna, E., Breau, R., Ratanatharathorn, V., Xia, X., Suen, J. (2004). Preferential expression of hPGFS in primary SCCHN and tumour cell lines derived from respiratory and digestive organs. Br J Cancer 90:1093-1099.
157. Linster, C. L., Van Schaftingen, E. (2003). Rapid stimulation of free glucuronate formation by nonglucuronidable xenobiotics in isolated rat hepatocytes. J Biol Chem 278:36328-36333.
158. Linster, C. L., Schaftingen, E. (2007). Vitamin C. Biosynthesis, recycling, and degradation in mammals. FEBS J 274:1-22.
159. Liston, T. E., Roberts, L. J. (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.
160. Liu, S. Q., Bhatnagar, A., Srivastava, S. K. (1992). Does sorbinil bind to the substrate binding site of aldose reductase? Biochem Pharmacol 44:2427-2429.
161. Liu, S. Q., Bhatnagar, A., Srivastava, S. K. (1993). Bovine lens aldose reductase. pH-dependence of steady-state kinetic parameters, and nucleotide binding. J Biol Chem 268:25494-25499.
162. + channel. J Biol Chem 276:11812-11820.
163. Lou, H., Hammond, L., Sharma, V., Sparkes, R. S., Lusis, A. J., Stolz, A. (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.
164. Lyon, R. C., Johnston, S. M., Watson, D. G., McGarvie, G., Ellis, E. M. (2007). Synthesis and catabolism of gamma-hydroxybutyrate in SH-SY5Y human neuroblastoma cells - role of the aldoketo reductase AKR7A2. J Biol Chem 282:25986-25992.
165. Ma, H. C., Ratnam, K., & Penning, T. M. (2000). Mutation of nicotinamide pocket residues in rat liver 3 alpha-hydroxysteroid dehydrogenase reveals different modes of cofactor binding. Biochemistry 39:102-109.
166. Ma, J., Yan, R., Zu, X., Cheng, J. M., Rao, K., Liao, D. F., 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.
167. Makino, S., Zaragoza, D. B., Mitchell, B. F., Robertson, S., Olson, D. M. (2007). Prostaglandin F2alpha and its receptor as activators of human decidua. Semin Reprod Med 25:60-68.
168. Manganas, L. N., Trimmer, J. S. (2000). Subunit composition determines Kv1 potassium channel surface expression. J Biol Chem 275:29685-29693.
169. Mano, Y., Suzuki, K., Yamada, K., Shimazono, N. (1961). Enzymatic studies on TPN-L-hexonate dehydrogenase from rat liver. J Biochem 49:618-634.
170. Martin, H. J. O., Breyer-Pfaff, U., Wsol, V., Venz, S., Block, S., Maser, E. (2006). Purification and characterization of AKR1B10 from human liver: role in carbonyl reduction of xenobiotics. Drug Metab Dispos 34:464-470.
171. Maser, E. (2004). Significance of reductases in the detoxification of the tobacco-specific carcinogen NNK. Trends Pharmacol Sci 25:235-237.
172. Maser, E., Friebertshauser, J., Volker, B. (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.
173. Maser, E., Stinner, B., Atalla, A. (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.
174. Mason, R. M., Wahab, N. A. (2003). Extracellular matrix metabolism in diabetic nephropathy. J Am Soc Nephrol 14:1358-1373.
175. Matsumoto, K., Endo, S., Ishikura, S., Matsunaga, T., Tajima, K., El Kabbani, O., et al. (2006). Enzymatic properties of a member (AKR1C20) of the aldo-keto reductase family. Biol Pharmaceut Bull 29:539-542.
176. Matsumoto, T., Ono, Y., Kurono, M., Kuromiya, A., Nakamura, K., Bril, V. (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.
177. Matsuura, K., Shiraishi, H., Hara, A., Sato, K., Deyashiki, Y., Ninomiya, M., 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 Biochem124:940-946.
178. + channel beta subunit Kv beta 2 (Kcnab2). J Biol Chem 277:13219-13228.
179. McLellan, L. I., Judah, D. J., Neal, G. E., Hayes, J. D. (1994). Regulation of aflatoxin B1-metabolizing aldehyde reductase and glutathione S-transferase by chemoprotectors. Biochem J 00:117-124.
180. Minotti, G., Licata, S., Saponiero, A., Menna, P., Calafiore, A. M., Di Giammarco, G., 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.
181. Miyata, T., Ueda, Y., Yamada, Y., Izuhara, Y., Wada, T., Jadoul, M., 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.
182. Miyata, T., van Ypersele, D. S., Kurokawa, K., Baynes, J. W. (1999). Alterations in nonenzymatic biochemistry in uremia: origin and significance of "carbonyl stress" in long-term uremic complications. Kidney Int 55:389-399.
183. Mode, A., Rafter, I. (1985). The sexually differentiated delta 4-3-ketosteroid 5 beta-reductase of rat liver. Purification, characterization, and quantitation. J Biol Chem 260:7137-7141.
184. Mordente, A., Meucci, E., Martorana, G. E., Giardina, B., Minotti, G. (2001). Human heart cytosolic reductases and anthracycline cardiotoxicity. IUBMB Life 52:83-88.
185. Mordente, A., Minotti, G., Martorana, G. E., Silvestrini, A., Giardina, B., Meucci, E. (2003). Anthracycline secondary alcohol metabolite formation in human or rabbit heart: biochemical aspects and pharmacologic implications. Biochem Pharmacol 66:989-998.
186. Mylari, B. L., Larson, E. R., Beyer, T. A., Zembrowski, W. J., Aldinger, C. E., Dee, M. F., 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.
187. Nagaraj, N. S., Beckers, S., Mensah, J. K., Waigel, S., Vigneswaran, N., Zacharias, W. (2006). Cigarette smoke condensate induces cytochromes P450 and aldo-keto reductases in oral cancer cells. Toxicol Lett 165:182-194.
188. Nagaraj, R. H., Shipanova, I. N., Faust, F. M. (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.
189. Nagaya, N., Papazian, D. M. (1997). Potassium channel alpha and beta subunits assemble in the endoplasmic reticulum. J Biol Chem 272:3022-3027.
190. Need, A. C., Irvine, E. E., Giese, K. P. (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.
191. Negre-Salvayre, A., Coatrieux, C., Ingueneau, C., Salvayre, R. (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.
192. Nicolucci, A., Carinci, F., Cavaliere, D., Scorpiglione, N., Belfiglio, M., Labbrozzi, D., 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.
193. Nidetzky, B., Neuhauser, W., Haltrich, D., Kulbe, K. D. (1996). Continuous enzymatic production of xylitol with simultaneous coenzyme regeneration in a charged membrane reactor. Biotechnol Bioeng 52:387-396.
194. Nishizawa, M., Nakajima, T., Yasuda, K., Kanzaki, H., Sasaguri, Y., Watanabe, K., et al. (2000). Close kinship of human 20 alpha-hydroxysteroid dehydrogenase gene with three aldo-keto reductase genes. Genes Cells 5:111-125.
195. Niwa, T., Miyazaki, T., Katsuzaki, T., Tatemichi, N., Takei, Y. (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.
196. Niwa, T., Tsukushi, S. (2001). 3-deoxyglucosone and AGEs in uremic complications: inactivation of glutathione peroxidase by 3-deoxyglucosone. Kidney Int Suppl 78:S37-S41.
197. O'Connor, T., Ireland, L. S., Harrison, D. J., Hayes, J. D. (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.
198. Oates, P. J. (2002). Polyol pathway and diabetic peripheral neuropathy. Int Rev Neurobiol 50:325-392.
199. Ohara, H., Miyabe, Y., Deyashiki, Y., Matsuura, K., Hara, A. (1995). Reduction of drug ketones by dihydrodiol dehydrogenases, carbonyl reductase, and aldehyde reductase of human liver. Biochem Pharmacol 50:221-227.
200. Oka, T. (2004). Prostaglandin E2 as a mediator of fever: the role of prostaglandin E (EP) receptors. Front Biosci 9:3046-3057.
201. Okuda, A., Okuda, K. (1984). Purification and characterization of delta 4-3-ketosteroid 5 betareductase. J Biol Chem 259:7519-7524.
202. Old, S. E., Sato, S., Kador, P. F., Carper, D. A. (1990). In vitro expression of rat lens aldose reductase in Escherichia coli. Proc Natl Acad Sci U S A 87:4942-4945.
203. Oppermann, U., Filling, C., Hult, M., Shafqat, N., Wu, X. Q., Lindh, M., et al. (2003). Short-chain dehydrogenases/reductases (SDR): the 2002 update. Chemico Biol Interact 143:247-253.
204. Palackal, N. T., Burczynski, M. E., Harvey, R. G., Penning, T. M. (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.
205. Palermo, M., Marazzi, M. G., Hughes, B. A., Stewart, P. M., Clayton, P. T., Shackleton, C. H. (2008). Human delta(4)-3-oxosteroid 5beta-reductase (AKR1D1) deficiency and steroid metabolism. Steroids 73:417-423.
206. Papari-Zareei, M., Brandmaier, A., Auchus, R. J. (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.
207. Pawlowski, J. E., Penning, T. M. (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.
208. Penning, T. M. (1997). Molecular endocrinology of hydroxysteroid dehydrogenases. Endocr Rev 18:281-305.
209. Penning, T. M., Burczynski, M. E., Jez, J. M., Hung, C. F., Lin, H. K., Ma, H. C., 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.
210. Penning, T. M., Drury, J. E. (2007). Human aldo-keto reductases: function, gene regulation, and single nucleotide polymorphisms. Arch Biochem Biophys 464:241-250.
211. Penning, T. M., Jin, Y., Heredia, V. V., Lewis, M. (2003). Structure-function relationships in 3alpha-hydroxysteroid dehydrogenases: a comparison of the rat and human isoforms. J Steroid Biochem Mol Biol 85:247-255.
212. Penning, T. M., Jin, Y., Steckelbroeck, S., Rizner, T. L., Lewis, M. (2004). Structure-function of human 3 alpha-hydroxysteroid dehydrogenases: genes and proteins. Mol Cell Endocrinol 215:63-72.
213. Penning, T. M., Talalay, P. (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.
214. Petrash, J. M., Harter, T. M., Devine, C. S., Olins, P. O., Bhatnagar, A., Liu, S., 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.
215. Pfeifer, M. A., Schumer, M. P., Gelber, D. A. (1997). Aldose reductase inhibitors: the end of an era or the need for different trial designs? Diabetes 46(Suppl 2):S82-S89.
216. Piekorz, R. P., Gingras, B., Hoffmeyer, A., Ihle, J. N., Weinstein, Y. (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.
217. Podjarny, A., Cachau, R. E., Schneider, T., Van Zandt, M., Joachimiak, A. (2004). Subatomic and atomic crystallographic studies of aldose reductase: implications for inhibitor binding. Cell Mol Life Sci 61:763-773.
218. Pollak, N., Dolle, C., Ziegler, M. (2007). The power to reduce: pyridine nucleotides - small molecules with a multitude of functions. Biochem J 402;205-218.
219. + channel beta subunits. Mol Funct Divers Ion Chan Recept 868:344-355.
220. Propper, D., Maser, E. (1997). Carbonyl reduction of daunorubicin in rabbit liver and heart. Pharmacol Toxicol 80:240-245.
221. Ramana, K. V., Bhatnagar, A., Srivastava, S., Yadav, U. C., Awasthi, S., Awasthi, Y. C., 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.
222. Ramana, K. V., Chandra, D., Srivastava, S., Bhatnagar, A., Aggarwal, B. B., Srivastava, S. K. (2002). Aldose reductase mediates mitogenic signaling in vascular smooth muscle cells. Jf Biol Chem 277:32063-32070.
223. Ramana, K. V., Chandra, D., Srivastava, S., Bhatnagar, A., Srivastava, S. K. (2003a). Aldose reductase mediates the mitogenic signals of cytokines. Chem Biol Interact 143-144, 587-596.
224. Ramana, K. V., Chandra, D., Srivastava, S., Bhatnagar, A., Srivastava, S. K. (2003b). Nitric oxide regulates the polyol pathway of glucose metabolism in vascular smooth muscle cells. FASEB J 17:417-425.
225. Ramana, K. V., Fadl, A. A., Tammali, R., Reddy, A. B., Chopra, A. K., Srivastava, S. K. (2006b). Aldose reductase mediates the lipopolysaccharide- induced release of inflammatory mediators in RAW264.7 murine macrophages. J Biol Chem 281:33019-33029.
226. Ramana, K. V., Friedrich, B., Srivastava, S., Bhatnagar, A., Srivastava, S. K. (2004). Activation of nuclear factor-kappaB by hyperglycemia in vascular smooth muscle cells is regulated by aldose reductase. Diabetes 53:2910-2920.
227. Ramana, K. V., Friedrich, B., Tammali, R., West, M. B., Bhatnagar, A., Srivastava, S. K. (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.
228. Ramana, K. V., Tammali, R., Reddy, A. B., Bhatnagar, A., Srivastava, S. K. (2007). Aldose reductase-regulated tumor necrosis factor-alpha production is essential for high glucose-induced vascular smooth muscle cell growth. Endocrinology 148:4371-4384.
229. Ramana, K. V., Willis, M. S., White, M. D., Horton, J. W., DiMaio, J. M., Srivastava, D., et al. (2006c). Endotoxin-induced cardiomyopathy and systemic inflammation in mice is prevented by aldose reductase inhibition. Circulation 114:1838-1846.
230. Ratnam, K., Ma, H., Penning, T. M. (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.
231. Reddy, C. C., Swan, J. S., Hamilton, G. A. (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.
232. + channels altered by presence of beta-subunit. Nature 369:289-294.
233. Rosemond, M. J. C., John-Williams, L., Yamaguchi, T., Fujishita, T., Walsh, J. S. (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.
234. Rosemond, M. J. C., Walsh, J. S. (2004). Human carbonyl reduction pathways and a strategy for their study in vitro. Drug Metab Rev 36:335-361.
235. Ruef, J., Liu, S. Q., Bode, C., Tocchi, M., Srivastava, S., Runge, M. S., 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.
236. Ruiz, F., Hazemann, I., Mitschler, A., Joachimiak, A., Schneider, T., Karplus, M., 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.
237. Rush, W. R., Alexander, O. F., Hall, D. J., Dow, R. J., Tokes, L., Kurz, L., et al. (1990). The metabolism of nafimidone hydrochloride in the dog, primates, and man. Xenobiotica 20:123-132.
238. Sales, K. J., Milne, S. A., Williams, A. R., Anderson, R. A., Jabbour, H. N. (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.
239. Sanai, M., Endo, S., Matsunaga, T., Ishikura, S., Tajima, K., El Kabbani, O., 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.
240. Sato, K., Inazu, A., Yamaguchi, S., Nakayama, T., Deyashiki, Y., Sawada, H., 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.
241. Sato, S., Kador, P. F. (1990). Inhibition of aldehyde reductase by aldose-reductase inhibitors. Biochem Pharmacol 40:1033-1042.
242. Schlegel, B. P., Jez, J. M., Penning, T. M. (1998a). Mutagenesis of 3 alpha-hydroxysteroid dehydrogenase reveals a "push-pull" mechanism for proton transfer in aldo-keto reductases. Biochemistry 37:3538-3548.
243. Schlegel, B. P., Ratnam, K., Penning, T. M. (1998b). Retention of NADPH-linked quinone reductase activity in an aldo-keto reductase following mutation of the catalytic tyrosine. Biochemistry 37:11003-11011.
244. Sestanj, K., Bellini, F., Fung, S., Abraham, N., Treasurywala, A., Humber, L., 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.
245. Setchell, K. D., Suchy, F. J., Welsh, M. B., Zimmer-Nechemias, L., Heubi, J., Balistreri, W. F. (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.
246. Sewing, S., Roeper, J., Pongs, O. (1996). Kv beta 1 subunit binding specific for shaker-related potassium channel alpha subunits. Neuron 16:455-463.
247. Shaw, S., Wang, X., Redd, H., Alexander, G. D., Isales, C. M., Marrero, M. B. (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.
248. Sherbet, D. P., Papari-Zareei, M., Khan, N., Sharma, K. K., Brandmaier, A., Rambally, S., et al. (2007). Cofactors, redox state, and directional preferences of hydroxysteroid dehydrogenases. Mol Cell Endocrinol 265:83-88.
249. + channel surface expression through effects early in biosynthesis. Neuron 16:843-852.
250. Shimoda, K., Shibasaki, M., Inaba, T., Cheung, S. W., Someya, T., Takahashi, S. (1998a). Carbonyl reduction of timiperone in human liver cytosol. Pharmacol Toxicol 83:164-168.
251. Shimoda, K., Someya, T., Morita, S., Hirokane, G., Yokono, A., Shibasaki, M., et al. (1998b). Plasma concentrations of timiperone and its reduced metabolite in the patients on timiperone. Psychiatry Clin Neurosci 52:535-540.
252. Shinmura, K., Bolli, R., Liu, S. Q., Tang, X. L., Kodani, E., Xuan, Y. T., et al. (2002). Aldose reductase is an obligatory mediator of the late phase of ischemic preconditioning. Circ Res 91:240-246.
253. Shinohara, M., Thornalley, P. J., Giardino, I., Beisswenger, P., Thorpe, S. R., Onorato, J., 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.
254. Sima, A. A., Bril, V., Nathaniel, V., McEwen, T. A., Brown, M. B., Lattimer, S. A., 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.
255. Singh, R., White, M. A., Ramana, K. V., Petrash, J. M., Watowich, S. J., Bhatnagar, A., et al. (2006). Structure of a glutathione conjugate bound to the active site of aldose reductase. Proteins 64:101-110.
256. Smithgall, T. E., Penning, T. M. (1986). Inhibition of trans-dihydrodiol oxidation by the nonsteroidal anti-inflammatory drugs. Carcinogenesis 7:583-588.
257. Song, Z. T., Fu, D. T. W., Chan, Y. S., Leung, S., Chung, S. S. M., Chung, S. K. (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.
258. Spite, M., Baba, S. P., Ahmed, Y., Barski, O. A., Nijhawan, K., Petrash, J. M., et al. (2007). Substrate specificity and catalytic efficiency of aldo-keto reductases with phospholipid aldehydes. Biochem J 405:95-105.
259. Srivastava, S., Chandra, A., Ansari, N. H., Srivastava, S. K., Bhatnagar, A. (1998a). Identification of cardiac oxidoreductase(s) involved in the metabolism of the lipid peroxidation-derived aldehyde-4-hydroxynonenal. Biochem J 329:469-475.
260. Srivastava, S., Chandra, A., Bhatnagar, A., Srivastava, S. K., Ansari, N. H. (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.
261. Srivastava, S., Chandrasekar, B., Bhatnagar, A., Prabhu, S. D. (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.
262. Srivastava, S., Conklin, D. J., Liu, S. Q., Prakash, N., Boor, P. J., Srivastava, S. K., 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.
263. Srivastava, S., Dixit, B. L., Ramana, K. V., Chandra, A., Chandra, D., Zacarias, A., et al. (2001b). Structural and kinetic modifications of aldose reductase by S-nitrosothiols. Biochem J 358:111-118.
264. Srivastava, S., Harter, T. M., Chandra, A., Bhatnagar, P., Srivastava, S. K., Petrash, J. M. (1998b). Kinetic studies of FR-1, a growth factor-inducible aldo-keto reductase. Biochemistry 37:12909-12917.
265. Srivastava, S., Spite, M., Trent, J. O., West, M. B., Ahmed, Y., Bhatnagar, A. (2004b). Aldose reductase-catalyzed reduction of aldehyde phospholipids. J Biol Chem 279:53395-53406.
266. Srivastava, S., Spite, M., Trent, J. O., West, M. B., Ahmed, Y., Bhatnagar, A. (2004a). Aldose reductase-catalyzed reduction of aldehyde phospholipids. J Biol Chem 279:53395-53406.
267. Srivastava, S., Tammali, R., Chandra, D., Greer, D. A., Ramana, K. V., Bhatnagar, A., et al. (2005a). Regulation of lens aldose reductase activity by nitric oxide. Exp Eye Res 81:664-672.
268. Srivastava, S., Watowich, S. J., Petrash, J. M., Srivastava, S. K., Bhatnagar, A. (1999). Structural and kinetic determinants of aldehyde reduction by aldose reductase. Biochemistry 38:42-54.
269. Srivastava, S. K., Ramana, K. V., Bhatnagar, A. (2005b). Role of aldose reductase and oxidative damage in diabetes and the consequent potential for therapeutic options. Endocr Rev 26:380-392.
270. Srivastava, S. K., Ramana, K. V., Srivastava, S., Bhatnagar, A. (2004c). Aldose reductase detoxifies lipid aldehydes and their glutathione conjugates. Aldo-Keto Reductases Toxicant Metab 865:37-48.
271. Stanbrough, M., Bubley, G. J., Ross, K., Golub, T. R., Rubin, M. A., Penning, T. M., et al. (2006). Increased expression of genes converting adrenal androgens to testosterone in androgen-independent prostate cancer. Cancer Res 66:2815-2825.
272. Steckelbroeck, S., Oyesanmi, B., Jin, Y., Lee, S. H., Kloosterboer, H. J., Penning, T. M. (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.
273. Steuber, H., Heine, A., Podjarny, A., Klebe, G. (2008). Merging the binding sites of aldose and aldehyde reductase for detection of inhibitor selectivity-determining features. J Mol Biol 379:991-1016.
274. Stolz, A., Hammond, L., Lou, H., Takikawa, H., Ronk, M., Shively, J. E. (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.
275. Subbanagounder, G., Leitinger, N., Schwenke, D. C., Wong, J. W., Lee, H., Rizza, C., 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.
276. Suzuki, D., Miyata, T. (1999). Carbonyl stress in the pathogenesis of diabetic nephropathy. Intern Med 38:309-314.
277. Suzuki, K., Koh, Y. H., Mizuno, H., Hamaoka, R., Taniguchi, N. (1998). Overexpression of aldehyde reductase protects PC12 cells from the cytotoxicity of methylglyoxal or 3-deoxyglucosone. J Biochem (Tokyo) 123:353-357.
278. Suzuki-Yamamoto, T., Nishizawa, M., Fukui, M., Okuda-Ashitaka, E., Nakajima, T., Ito, S., et al. (1999). cDNA cloning, expression, and characterization of human prostaglandin F synthase. FEBS Lett 462:335-340.
279. Thomas, T., Thomas, G., McLendon, C., Sutton, T., Mullan, M. (1996). beta-amyloid-mediated vasoactivity and vascular endothelial damage. Nature 380:168-171.
280. Thornalley, P. J. (2003). Use of aminoguanidine (Pimagedine) to prevent the formation of advanced glycation endproducts. Arch Biochem Biophys 419:31-40.
281. Thornalley, P. J., Langborg, A., Minhas, H. S. (1999). Formation of glyoxal, methylglyoxal, and 3-deoxyglucosone in the glycation of proteins by glucose. Biochem J 344: t-16.
282. Tipparaju, S. M., Barski, O. A., Srivastava, S., Bhatnagar, A. (2008). Catalytic mechanism and substrate specificity of the beta-subunit of the voltage-gated potassium channel. Biochemistry 47:8840-8854.
283. + channels. Biochem Biophys Res Commun 359:269-276.
284. + channels by oxidized and reduced pyridine nucleotide coenzymes. Am J Physiol Cell Physiol 288:C366-C376.
285. Tselepis, A. D., John, C. M. (2002). Inflammation, bioactive lipids, and atherosclerosis: potential roles of a lipoprotein-associated phospholipase A2, platelet-activating factor-acetylhydrolase. Atheroscler Suppl 3:57-68.
286. Upadhyaya, P., Kenney, P. M. J., Hochalter, J. B., Wang, M. Y., Hecht, S. S. (1999). Tumorigenicity and metabolism of 4-(methylnitrosamino)-1-(3-pyridyl) -1-butanol enantiomers and metabolites in the A/J mouse. Carcinogenesis 20:1577-1582.
287. Urade, Y., Watanabe, K., Eguchi, N., Fujii, Y., Hayaishi, O. (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.
288. Urzhumtsev, A., Tete-Favier, F., Mitschler, A., Barbanton, J., Barth, P., Urzhumtseva, L., 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.
289. Val, P., Martinez, A., Sahut-Barnola, I., Jean, C., Veyssiere, G., Lefrancois-Martinez, A. M. (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.
290. van Boekel, M. A., van Aalten, D. M., Caspers, G. J., Roll, B., de Jong, W. W. (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.
291. Vander, J. D., Kolb, N. S., Vander, J. T., Chino, J., Martinez, F. J., Hunsaker, L. A., et al. (1995). Substrate specificity of human aldose reductase: identification of 4- hydroxynonenal as an endogenous substrate. Biochim Biophys Acta 1249:117-126.
292. Vander, J. D., Robinson, B., Taylor, K. K., Hunsaker, L. A. (1992). Reduction of trioses by NADPH-dependent aldo-keto reductases. Aldose reductase, methylglyoxal, and diabetic complications. J Biol Chem 267:4364-4369.
293. Varma, T., Liu, S. Q., West, M., Thongboonkerd, V., Ruvolo, P. P., May, W. S., et al. (2003). Protein kinase C-dependent phosphorylation and mitochondrial translocation of aldose reductase. FEBS Lett 534:175-179.
294. Vega, M. C., Lorentzen, E., Linden, A., Wilmanns, M. (2003). Evolutionary markers in the (beta/alpha)8-barrel fold. Curr Opin Chem Biol 7:694-701.
295. Vergnes, L., Phan, J., Stolz, A., Reue, K. (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.
296. Verma, M., Martin, H. J., Haq, W., O'Connor, T. R., Maser, E., Balendiran, G. K. (2008). Inhibiting wild-type and C299S mutant AKR1B10; a homologue of aldose reductase upregulated in cancers. Eur J Pharmacol 584:213-221.
297. Verzijl, N., DeGroot, J., Bank, R. A., Bayliss, M. T., Bijlsma, J. W. J., Lafeber, F. P. J. G., 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.
298. Verzijl, N., DeGroot, J., Ben Zaken, C., Braun-Benjamin, O., Maroudas, A., Bank, R. A., 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.
299. Vlassara, H., Palace, M. R. (2002). Diabetes and advanced glycation endproducts. J Intern Med 251:87-101.
300. Watanabe, K., Iguchi, Y., Iguchi, S., Arai, Y., Hayaishi, O., Roberts, L. J. (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.
301. Watanabe, K., Yoshida, R., Shimizu, T., Hayaishi, O. (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.
302. Watson, A. D., Leitinger, N., Navab, M., Faull, K. F., Horkko, S., Witztum, J. L., 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.
303. Weiss, R. B. (1992). The anthracyclines - will we ever find a better doxorubicin. Sem Oncol 19:670-686.
304. Wendt, T., Tanji, N., Guo, J., Hudson, B. I., Bierhaus, A., Ramasamy, R., et al. (2003). Glucose, glycation, and RAGE: implications for amplification of cellular dysfunction in diabetic nephropathy. J Am Soc Nephrol 14:1383-1395.
305. Weng, J., Cao, Y., Moss, N., Zhou, M. (2006). Modulation of voltage-dependent Shaker family potassium channels by an aldo-keto reductase. J Biol Chem 281:15194-15200.
306. Wermuth, B. (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.
307. Wermuth, B. (1985). Aldo-keto reductases. Prog Clin Biol Res 174:209-230.
308. Wermuth, B. (1991). Inhibition of aldehyde reductase by carboxylic acids. Adv Exp Med Biol 284:197-204.
309. Wermuth, B., Monder, C. (1983). Aldose and aldehyde reductase exhibit isocorticosteroid reductase activity. Eur J Biochem 131:423-426.
310. Wermuth, B., Munch, J. D., von Wartburg, J. P. (1977). Purification and properties of NADPH-dependent aldehyde reductase from human liver. J Biol Chem 252:3821-3828.
311. Whittle, S. R., Turner, A. J. (1981). Biogenic aldehyde metabolism in rat brain. Differential sensitivity of aldehyde-reductase isoenzymes to sodium valproate. Biochim Biophys Acta 657:94-105.
312. Wilson, D. K., Bohren, K. M., Gabbay, K. H., Quiocho, F. A. (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.
313. Wilson, D. K., Nakano, T., Petrash, J. M., Quiocho, F. A. (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.
314. Wilson, D. K., Tarle, I., Petrash, J. M., Quiocho, F. A. (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.
315. Wise, E., Yew, W. S., Babbitt, P. C., Gerlt, J. A., Rayment, I. (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.
316. Wsol, V., Szotakova, B., Martin, H. J., Maser, E. (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.
317. Wsol, V., Szotakova, B., Skalova, L., Maser, E. (2004). The novel anticancer drug oracin: different stereo specificity and cooperativity for carbonyl reduction by purified human liver 11 betahydroxysteroid dehydrogenase type 1. Toxicology 197:253-261.
318. Yabe-Nishimura, C. (1998). Aldose reductase in glucose toxicity: a potential target for the prevention of diabetic complications [in process citation]. Pharmacol Rev 50:21-33.
319. Yamano, S., Ichinose, F., Todaka, T., Toki, S. (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.
320. Yan, R. L., Zu, X. Y., Ma, J., Liu, Z. W., Adeyanju, M., Cao, D. L. (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.
321. Ye, Q., Hyndman, D., Green, N., Li, X., Korithoski, B., Jia, Z., et al. (2001). Crystal structure of an aldehyde reductase Y50F mutant-NADP complex and its implications for substrate binding. Proteins 44:12-19.
322. Yee, D. J., Balsanek, V., Bauman, D. R., Penning, T. M., Sames, D. (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.
323. Yoshitake, H., Takahashi, M., Ishikawa, H., Nojima, M., Iwanari, H., Watanabe, A., 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.
324. Zeindl-Eberhart, E., Klugbauer, S., Dimitrijevic, N., Jungblut, P. R., Lamer, S., Rabes, H. M. (2001). Proteome analysis of rat hepatomas: carcinogen-dependent tumor-associated protein variants. Electrophoresis 22:3009-3018.