Activation of aldo-keto reductase family member 1B14 (AKR1B14) by bile acids: Activation mechanism and bile acid-binding site

Biochimie

Volumn 93, Issue 9, 2011, Pages 1476-1486

  Endo, Satoshi ^a   Matsunaga, Toshiyuki ^a   Fujita, Anna ^a   Kuragano, Tsukasa ^a   Soda, Midori ^a   Sundaram, Krithika ^b   Dhagat, Urmi ^b   Tajima, Kazuo ^c   El Kabbani, Ossama ^b   Hara, Akira ^a  

^a GIFU PHARMACEUTICAL UNIVERSITY   (Japan)

^b MONASH UNIVERSITY   (Australia)

^c HOKURIKU UNIVERSITY   (Japan)

Author keywords

Activation mechanism; AKR1B14; AKR1B7; Aldo keto reductase; Bile acid

Indexed keywords

ALDO KETO REDUCTASE 1B14; BILE ACID; GLYCOCHENODEOXYCHOLIC ACID; OXIDOREDUCTASE; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; BINDING SITE; CRYSTAL STRUCTURE; DISSOCIATION; ENDOTHELIUM CELL; ENZYME ACTIVATION; ESCHERICHIA COLI; FLUORESCENCE; KINETICS; MOLECULAR DOCKING; MUTAGENESIS; NONHUMAN; PH;

ALDEHYDE REDUCTASE; ANIMALS; BILE ACIDS AND SALTS; BINDING SITES; CATTLE; CELLS, CULTURED; ENZYME ACTIVATION; HISTIDINE; HYDROGEN-ION CONCENTRATION; LEUCINE; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; NADP; RATS;

RATTUS;

EID: 79960841556     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2011.04.022     Document Type: Article

References (46)

1. R.D. Mindnich, and T.M. Penning Aldo-keto reductase (AKR) superfamily: genomics and annotation Hum. Genomics 3 2009 362 370
2. O.A. Barski, S.M. Tipparaju, and A. Bhatnagar The aldo-keto reductase superfamily and its role in drug metabolism and detoxification Drug Metab. Rev. 40 2008 553 624
3. C. Yabe-Nishimura Aldose reductase in glucose toxicity: a potential target for the prevention of diabetic complications Pharmacol. Rev. 50 1998 21 33 (Pubitemid 28158840)
4. J.M. Petrash All in the family: aldose reductase and closely related aldo-keto reductases Cell. Mol. Life Sci. 61 2004 737 749 (Pubitemid 38659658)
5. B. Crosas, D.J. Hyndman, O. Gallego, S. Martras, X. Parés, T.G. Flynn, and J. Farrés Human aldose reductase and human small intestine aldose reductase are efficient retinal reductases: consequences for retinoid metabolism Biochem. J. 373 2003 973 979 (Pubitemid 36981109)
6. 2α synthase activities of aldo-keto reductase 1B1, 1B3 and 1B7 J. Biochem. 145 2009 161 168
7. D. Cao, S.T. Fan, and S.S. Chung Identification and characterization of a novel human aldose reductase-like gene J. Biol. Chem. 273 1998 11429 11435 (Pubitemid 28272034)
8. D.J. Hyndman, and T.G. Flynn Sequence and expression levels in human tissues of a new member of the aldo-keto reductase family Biochim. Biophys. Acta 1399 1998 198 202 (Pubitemid 28410465)
9. E.A. Pailhoux, A. Martinez, G.M. Veyssiere, and C.G. Jean Androgen-dependent protein from mouse vas deferens. cDNA cloning and protein homology with the aldo-keto reductase superfamily J. Biol. Chem. 265 1990 19932 19936 (Pubitemid 120013952)
10. P.J. Donohue, G.F. Alberts, B.S. Hampton, and J.A. Winkles A delayed-early gene activated by fibroblast growth factor-1 encodes a protein related to aldose reductase J. Biol. Chem. 269 1994 8604 8609 (Pubitemid 24200289)
11. S. Srivastava, T.M. Harter, A. Chandra, A. Bhatnagar, S.K. Srivastava, and J.M. Petrash Kinetic studies of FR-1, a growth factor-inducible aldo-keto reductase Biochemistry 37 1998 12909 12917 (Pubitemid 28433524)
12. S. Endo, T. Matsunaga, H. Mamiya, A. Hara, Y. Kitade, K. Tajima, and O. El-Kabbani Characterization of a rat NADPH-dependent aldo-keto reductase (AKR1B13) induced by oxidative stress Chem. Biol. Interact. 178 2009 151 157
13. P. Val, A. Martinez, I. Sahut-Barnola, C. Jean, G. Veyssire, and A.M. Lefranois-Martinez 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 2002 3435 3448
14. S. Endo, T. Matsunaga, A. Fujita, K. Tajima, O. El-Kabbani, and A. Hara Rat aldose reductase-like protein (AKR1B14) efficiently reduces the lipid peroxidation product 4-oxo-2-nonenal Biol. Pharm. Bull. 33 2010 1886 1890
15. S. Endo, T. Matsunaga, T. Kuragano, S. Ohno, Y. Kitade, K. Tajima, O. El-Kabbani, and A. Hara Properties and tissue distribution of a novel aldo-keto reductase encoding in a rat gene (Akr1b10) Arch. Biochem. Biophys. 503 2010 230 237
16. A.M. Lefranois-Martinez, C. Tournaire, A. Martinez, M. Berger, S. Daoudal, D. Tritsch, G. Veyssire, and C. Jean 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 1999 32875 32880 (Pubitemid 129535323)
17. A. Martinez, C. Aigueperse, P. Val, M. Dussault, C. Tournaire, M. Berger, G. Veyssire, C. Jean, and A. Lefranois Martinez Physiological functions and hormonal regulation of mouse vas deferens protein (AKR1B7) in steroidogenic tissues Chem. Biol. Interact. 130-132 2001 903 917 (Pubitemid 32295874)
18. D.H. Volle, J.J. Repa, A. Mazur, C.L. Cummins, P. Val, J. Henry-Berger, F. Caira, G. Veyssiere, D.J. Mangelsdorf, and J.M. Lobaccaro Regulation of the aldo-keto reductase gene AKR1B7 by the nuclear oxysterol receptor LXRα (liver X receptor-α) in the mouse intestine: putative role of LXRs in lipid detoxification processes Mol. Endocrinol. 18 2004 888 898 (Pubitemid 38435328)
19. M.J. Liu, Y. Takahashi, T. Wada, J. He, J. Gao, Y. Tian, S. Li, and W. Xie The aldo-keto reductase Akr1b7 gene is a common transcriptional target of xenobiotic receptors pregnane X receptor and constitutive androstane receptor Mol. Pharmacol. 76 2009 604 611
20. M.C. Battista, C. Roberge, A. Martinez, and N. Gallo-Payet 24-dehydrocholesterol reductase/seladin-1: a key protein differentially involved in adrenocorticotropin effects observed in human and rat adrenal cortex Endocrinology 150 2009 4180 4190
21. P. Kotokorpi, C. Gardmo, C.S. Nyström, and A. Mode Activation of the glucocorticoid receptor or liver X receptors interferes with growth hormone-induced akr1b7 gene expression in rat hepatocytes Endocrinology 145 2004 5704 5713 (Pubitemid 39571715)
22. G. Jia, R. Takahashi, Z. Zhang, Y. Tsuji, and H. Sone Aldo-keto reductase 1 family B7 is the gene induced in response to oxidative stress in the livers of Long-Evans Cinnamon rats Int. J. Oncol. 29 2006 829 838
23. S. Lambert-Langlais, J.C. Pointud, A.M. Lefranois-Martinez, F. Volat, M. Manin, F. Coudoré, P. Val, I. Sahut-Barnola, B. Ragazzon, E. Louiset, C. Delarue, H. Lefebvre, Y. Urade, and A. Martinez Aldo keto reductase 1B7 and prostaglandin F2alpha are regulators of adrenal endocrine functions PLoS One 4 2009 e7309
24. S. Endo, T. Matsunaga, H. Mamiya, C. Ohta, M. Soda, Y. Kitade, K. Tajima, H.T. Zhao, O. El-Kabbani, and A. Hara Kinetic studies of AKR1B10, human aldose reductase-like protein: endogenous substrates and inhibition by steroids Arch. Biochem. Biophys. 487 2009 1 9
25. C.C. Doughty, and S.M. Conrad A reaction mechanism for aldose reductase from lens Biochim. Biophys. Acta 708 1982 358 364
26. R. Chung, S. Endo, A. Hara, and O. El-Kabbani Crystallization and preliminary X-ray analysis of a rat aldose reductase-like protein (AKR1B14) Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 65 2009 395 397
27. K. Sundaram, U. Dhagat, S. Endo, R. Chung, T. Matsunaga, A. Hara, and O. El-Kabbani Structure of rat aldose reductase-like protein AKR1B14 holoenzyme: probing the role of His269 in coenzyme binding by site-directed mutagenesis Bioorg. Med. Chem. Lett. 21 2011 801 804
28. W.W. Cleland Statistical analysis of enzyme kinetic data Meth. Enzymol. 63 1979 103 138
29. I.H. Segel Enzyme Kinetics 1975 John Wiley and Sons New York 227 272
30. R.A. Friesner, J.L. Banks, R.B. Murphy, T.A. Halgren, J.J. Klicic, D.T. Mainz, M.P. Repasky, E.H. Knoll, M. Shelley, J.K. Perry, D.E. Shaw, P. Francis, and P.S. Shenkin Glide: a new approach for rapid, accurate docking and scoring. 1. Method and assessment of docking accuracy J. Med. Chem. 47 2004 1739 1749 (Pubitemid 38380917)
31. H. Sakakura, M. Suzuki, N. Kimura, H. Takeda, S. Nagata, and M. Maeda Simultaneous determination of bile acids in rat bile and serum by high-performance liquid chromatography J. Chromatogr. 621 1993 123 131
32. D.R. Bauman, S.I. Rudnick, L.M. Szewczuk, Y. Jin, S. Gopishetty, and T.M. Penning Development of nonsteroidal anti-inflammatory drug analogs and steroid carboxylates selective for human aldo-keto reductase isoforms: potential antineoplastic agents that work independently of cyclooxygenase isozymes Mol. Pharmacol. 67 2005 60 68 (Pubitemid 40069966)
33. J.A. Doorn, E. Maser, A. Blum, D.J. Claffey, and D.R. Petersen Human carbonyl reductase catalyzes reduction of 4-oxonon-2-enal Biochemistry 43 2004 13106 13114 (Pubitemid 39366059)
34. L.M. Sayre, D. Lin, Q. Yuan, X. Zhu, and X. Tang Protein adducts generated from products of lipid oxidation: focus on HNE and one Drug Metab. Rev. 38 2006 651 675 (Pubitemid 44903261)
35. A. Fini, and A. Roda Chemical properties of bile acids. IV. Acidity constants of glycine-conjugated bile acids J. Lipid Res. 28 1987 755 759
36. K.M. Bohren, C.E. Grimshaw, C.J. Lai, D.H. Harrison, D. Ringe, G.A. Petsko, and K.H. Gabbay 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 1994 2021 2032 (Pubitemid 24099596)
37. C.E. Grimshaw, K.M. Bohren, C.J. Lai, and K.H. Gabbay Human aldose reductase: rate constants for a mechanism including interconversion of ternary complexes by recombinant wild-type enzyme Biochemistry 34 1995 14356 14365
38. D.R. Schmidt, S. Schmidt, S.R. Holmstrom, M. Makishima, R.T. Yu, C.L. Cummins, D.J. Mangelsdorf, and S.A. Kliewer AKR1B7 is induced by the farnesoid X receptor and metabolizes bile acids J. Biol. Chem. 286 2011 2425 2432
39. P.B. Hylemon, H. Zhou, W.M. Pandak, S. Ren, G. Gil, and P. Dent Bile acids as regulatory molecules J. Lipid Res. 50 2009 1509 1520
40. S.M. Houten, M. Watanabe, and J. Auwerx Endocrine functions of bile acids EMBO J. 25 2006 1419 1425
41. E. Aubert-Jousset, V. Sbarra, and D. Lombardo Site-directed mutagenesis of the distal basic cluster of pancreatic bile salt-dependent lipase J. Biol. Chem. 279 2004 39697 39704 (Pubitemid 39258238)
42. 2: regulation of fat and cholesterol homeostasis Biochim. Biophys. Acta 1768 2007 2478 2490 (Pubitemid 47532028)
43. G.M. Hanozet, M. Simonetta, and G. Gerola Activation of rat liver alcohol dehydrogenase by deoxycholic acid FEBS Lett. 65 1976 120 122
44. J.H. Schlattjan, C. Winter, and J. Greven Regulation of renal tubular bile acid transport in the early phase of an obstructive cholestasis in the rat Nephron Physiol. 95 2003 49 56
45. M. Trauner, and J.L. Boyer Bile salt transporters: molecular characterization, function, and regulation Physiol. Rev. 83 2003 633 671 (Pubitemid 36378680)
46. P.A. Dawson, M.L. Hubbert, and A. Rao Getting the mOST from OST: role of organic solute transporter, OSTα-OSTβ, in bile acid and steroid metabolism Biochim. Biophys. Acta 1801 2010 994 1004