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Volumn 3 APR, Issue , 2012, Pages

Biological role of aldo-keto reductases in retinoic acid biosynthesis and signaling

Author keywords

Aldo keto reductase; Cancer; Retinaldehyde; Retinoic acid; Retinol

Indexed keywords

ALCOHOL DEHYDROGENASE; ALDEHYDE DEHYDROGENASE; ALDO KETO REDUCTASE; ALDO KETO REDUCTASE 1B1; ALDO KETO REDUCTASE 1B10; ALDO KETO REDUCTASE 1B12; ALDO KETO REDUCTASE C1; ALDO KETO REDUCTASE C3; ALDO KETO REDUCTASE INHIBITOR; ALITRETINOIN; BETA CAROTENE; CAROTENOID; CELLULAR RETINOL BINDING PROTEIN 1; ENZYME INHIBITOR; FLUFENAMIC ACID; HORMONE RECEPTOR; LITHOCHOLIC ACID; OXIDOREDUCTASE; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR; PONALRESTAT; RETINAL; RETINALDEHYDE REDUCTASE; RETINOIC ACID; RETINOID X RECEPTOR; RETINOL; TOLRESTAT; UNCLASSIFIED DRUG;

EID: 84865715473     PISSN: None     EISSN: 16639812     Source Type: Journal    
DOI: 10.3389/fphar.2012.00058     Document Type: Article
Times cited : (77)

References (79)
  • 1
    • 0029846857 scopus 로고    scopus 로고
    • The Cterminal loop of aldehyde reductase determines the substrate and inhibitor specificity
    • Barski, O. A., Gabbay, K. H., and Bohren, K. M. (1996). The Cterminal loop of aldehyde reductase determines the substrate and inhibitor specificity. Biochemistry 35, 14276-14280.
    • (1996) Biochemistry , vol.35 , pp. 14276-14280
    • Barski, O.A.1    Gabbay, K.H.2    Bohren, K.M.3
  • 2
    • 54549110136 scopus 로고    scopus 로고
    • The aldo-keto reductase superfamily and its role in drug metabolism and detoxification
    • Barski, O. A., Tipparaju, S. M., and Bhatnagar, A. (2008). The aldo-keto reductase superfamily and its role in drug metabolism and detoxification. Drug Metab. Rev. 40, 553-624.
    • (2008) Drug Metab. Rev. , vol.40 , pp. 553-624
    • Barski, O.A.1    Tipparaju, S.M.2    Bhatnagar, A.3
  • 3
    • 50649118622 scopus 로고    scopus 로고
    • Kinetic analysis of human enzyme RDH10 defines the characteristics of a physiologically relevant retinol dehydrogenase
    • Belyaeva, O. V., Johnson, M. P., and Kedishvili, N. Y. (2008). Kinetic analysis of human enzyme RDH10 defines the characteristics of a physiologically relevant retinol dehydrogenase. J. Biol. Chem. 283, 20299-20308.
    • (2008) J. Biol. Chem. , vol.283 , pp. 20299-20308
    • Belyaeva, O.V.1    Johnson, M.P.2    Kedishvili, N.Y.3
  • 4
    • 0037145930 scopus 로고    scopus 로고
    • Human pancreas protein 2 (PAN2) has a retinal reductase activity and is ubiquitously expressed in human tissues
    • Belyaeva, O. V., and Kedishvili, N. Y. (2002). Human pancreas protein 2 (PAN2) has a retinal reductase activity and is ubiquitously expressed in human tissues. FEBS Lett. 531, 489-493.
    • (2002) FEBS Lett , vol.531 , pp. 489-493
    • Belyaeva, O.V.1    Kedishvili, N.Y.2
  • 5
    • 18244398944 scopus 로고    scopus 로고
    • Biochemical properties of purified human retinol dehydrogenase 12 (RDH12): catalytic efficiency toward retinoids and C9 aldehydes and effects of cellular retinol-binding protein type I (CRBPI) and cellular retinaldehyde-binding protein (CRALBP) on the oxidation and reduction of retinoids
    • Belyaeva, O. V., Korkina, O. V., Stetsenko, A. V., Kim, T., Nelson, P. S., and Kedishvili, N. Y. (2005). Biochemical properties of purified human retinol dehydrogenase 12 (RDH12): catalytic efficiency toward retinoids and C9 aldehydes and effects of cellular retinol-binding protein type I (CRBPI) and cellular retinaldehyde-binding protein (CRALBP) on the oxidation and reduction of retinoids. Biochemistry 44, 7035-7047.
    • (2005) Biochemistry , vol.44 , pp. 7035-7047
    • Belyaeva, O.V.1    Korkina, O.V.2    Stetsenko, A.V.3    Kim, T.4    Nelson, P.S.5    Kedishvili, N.Y.6
  • 6
    • 0346365098 scopus 로고    scopus 로고
    • Properties of short-chain dehydrogenase/reductase RalR1: characterization of purified enzyme, its orientation in the microsomal membrane, and distribution in human tissues and cell lines
    • Belyaeva, O. V., Stetsenko, A. V., Nelson, P., and Kedishvili, N. Y. (2003). Properties of short-chain dehydrogenase/reductase RalR1: characterization of purified enzyme, its orientation in the microsomal membrane, and distribution in human tissues and cell lines. Biochemistry 42, 14838-14845.
    • (2003) Biochemistry , vol.42 , pp. 14838-14845
    • Belyaeva, O.V.1    Stetsenko, A.V.2    Nelson, P.3    Kedishvili, N.Y.4
  • 7
    • 33745387612 scopus 로고    scopus 로고
    • Overview of retinoid metabolism and function
    • Blomhoff, R., and Blomhoff, H. K. (2006). Overview of retinoid metabolism and function. J. Neurobiol. 66, 606-630.
    • (2006) J. Neurobiol. , vol.66 , pp. 606-630
    • Blomhoff, R.1    Blomhoff, H.K.2
  • 8
    • 2642679232 scopus 로고    scopus 로고
    • Identification and characterization of a novel human aldose reductase-like gene
    • Cao, D., Fan, S. T., and Chung, S. S. (1998). Identification and characterization of a novel human aldose reductase-like gene. J. Biol. Chem. 273, 11429-11435.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11429-11435
    • Cao, D.1    Fan, S.T.2    Chung, S.S.3
  • 10
    • 0043069767 scopus 로고    scopus 로고
    • Human aldose reductase and human small intestine aldose reductase are efficient retinal reductases: consequences for retinoid metabolism
    • Crosas, B., Hyndman, D. J., Gallego, O., Martras, S., Parés, X., Flynn, T. G., and Farrés, J. (2003). Human aldose reductase and human small intestine aldose reductase are efficient retinal reductases: consequences for retinoid metabolism. Biochem. J. 373, 973-979.
    • (2003) Biochem. J. , vol.373 , pp. 973-979
    • Crosas, B.1    Hyndman, D.J.2    Gallego, O.3    Martras, S.4    Parés, X.5    Flynn, T.G.6    Farrés, J.7
  • 11
    • 4644249735 scopus 로고    scopus 로고
    • Ubiquitous induction of resistance to platinum drugs in human ovarian, cervical, germ-cell and lung carcinoma tumor cells overexpressing isoforms 1 and 2 of dihydrodiol dehydrogenase
    • Deng, H. B., Adikari, M., Parekh, H. K., and Simpkins, H. (2004). Ubiquitous induction of resistance to platinum drugs in human ovarian, cervical, germ-cell and lung carcinoma tumor cells overexpressing isoforms 1 and 2 of dihydrodiol dehydrogenase. Cancer Chemother. Pharmacol. 54, 301-307.
    • (2004) Cancer Chemother. Pharmacol. , vol.54 , pp. 301-307
    • Deng, H.B.1    Adikari, M.2    Parekh, H.K.3    Simpkins, H.4
  • 12
    • 0037439967 scopus 로고    scopus 로고
    • The aldo-keto reductase AKR1C3 is a novel suppressor of cell differentiation that provides a plausible target for the noncyclooxygenase-dependent antineoplastic actions of nonsteroidal antiinflammatory drugs
    • Desmond, J. C., Mountford, J. C., Drayson, M. T., Walker, E. A., Hewison,M.,Ride,J. P.,Luong,Q. T.,Hayden, R. E., Vanin, E. F., and Bunce, C. M. (2003). The aldo-keto reductase AKR1C3 is a novel suppressor of cell differentiation that provides a plausible target for the noncyclooxygenase-dependent antineoplastic actions of nonsteroidal antiinflammatory drugs. Cancer Res. 63, 505-512.
    • (2003) Cancer Res , vol.63 , pp. 505-512
    • Desmond, J.C.1    Mountford, J.C.2    Drayson, M.T.3    Walker, E.A.4    Hewison, M.5    Ride, J.P.6    Luong, Q.T.7    Hayden, R.E.8    Vanin, E.F.9    Bunce, C.M.10
  • 13
    • 79958856252 scopus 로고    scopus 로고
    • Identification of aldo-keto reductase AKR1B10 as a selective target for modification and inhibition by prostaglandin A(1): implications for antitumoral activity
    • Díez-Dacal, B., Gayarre, J., Gharbi, S., Timms, J. F., Coderch, C., Gago, F., and Pérez-Sala, D. (2011). Identification of aldo-keto reductase AKR1B10 as a selective target for modification and inhibition by prostaglandin A(1): implications for antitumoral activity. Cancer Res. 71, 4161-4171.
    • (2011) Cancer Res , vol.71 , pp. 4161-4171
    • Díez-Dacal, B.1    Gayarre, J.2    Gharbi, S.3    Timms, J.F.4    Coderch, C.5    Gago, F.6    Pérez-Sala, D.7
  • 14
    • 79957569340 scopus 로고    scopus 로고
    • Proteasome inhibitors MG-132 and bortezomib induce AKR1C1, AKR1C3, AKR1B1, and AKR1B10 in human colon cancer cell lines SW-480 and HT-29
    • Ebert, B., Kisiela, M., Wsol, V., and Maser, E. (2011). Proteasome inhibitors MG-132 and bortezomib induce AKR1C1, AKR1C3, AKR1B1, and AKR1B10 in human colon cancer cell lines SW-480 and HT-29. Chem. Biol. Interact. 191, 239-249.
    • (2011) Chem. Biol. Interact. , vol.191 , pp. 239-249
    • Ebert, B.1    Kisiela, M.2    Wsol, V.3    Maser, E.4
  • 15
    • 34447642375 scopus 로고    scopus 로고
    • Selectivity determinants of the aldose and aldehyde reductase inhibitor-binding sites
    • El-Kabbani, O., and Podjarny, A. (2007). Selectivity determinants of the aldose and aldehyde reductase inhibitor-binding sites. Cell. Mol. Life Sci. 64, 1970-1978.
    • (2007) Cell. Mol. Life Sci. , vol.64 , pp. 1970-1978
    • El-Kabbani, O.1    Podjarny, A.2
  • 16
    • 0035812729 scopus 로고    scopus 로고
    • Metabolism of vitamin A affected by prostaglandin F synthase in contractile interstitial cells of bovine lung
    • Endo, K., Fukui, M., Mishima, M., and Watanabe, K. (2001). Metabolism of vitamin A affected by prostaglandin F synthase in contractile interstitial cells of bovine lung. Biochem. Biophys. Res. Commun. 287, 956-961.
    • (2001) Biochem. Biophys. Res. Commun. , vol.287 , pp. 956-961
    • Endo, K.1    Fukui, M.2    Mishima, M.3    Watanabe, K.4
  • 17
    • 78249267861 scopus 로고    scopus 로고
    • Rat aldose reductaselike protein (AKR1B14) efficiently reduces the lipid peroxidation product 4-oxo-2-nonenal
    • Endo, S., Matsunaga, T., Fujita, A., Tajima,K.,El-Kabbani,O.,and Hara, A. (2010a). Rat aldose reductaselike protein (AKR1B14) efficiently reduces the lipid peroxidation product 4-oxo-2-nonenal. Biol. Pharm. Bull. 33, 1886-1890.
    • (2010) Biol. Pharm. Bull. , vol.33 , pp. 1886-1890
    • Endo, S.1    Matsunaga, T.2    Fujita, A.3    Tajima, K.4    El-Kabbani, O.5    Hara, A.6
  • 19
    • 34548020351 scopus 로고    scopus 로고
    • Enzymatic characteristics of an aldo-keto reductase family protein (AKR1C15) and its localization in rat tissues
    • Endo, S., Matsunaga, T., Horie, K., Tajima, K., Bunai, Y., Carbone, V., El-Kabbani, O., and Hara, A. (2007). Enzymatic characteristics of an aldo-keto reductase family protein (AKR1C15) and its localization in rat tissues. Arch. Biochem. Biophys. 465, 136-147.
    • (2007) Arch. Biochem. Biophys. , vol.465 , pp. 136-147
    • Endo, S.1    Matsunaga, T.2    Horie, K.3    Tajima, K.4    Bunai, Y.5    Carbone, V.6    El-Kabbani, O.7    Hara, A.8
  • 20
    • 59049093973 scopus 로고    scopus 로고
    • Characterization of a rat NADPH-dependent aldo-keto reductase (AKR1B13) induced by oxidative stress
    • Endo, S., Matsunaga, T., Mamiya, H., Hara, A., Kitade, Y., Tajima, K., and El-Kabbani, O. (2009). Characterization of a rat NADPH-dependent aldo-keto reductase (AKR1B13) induced by oxidative stress. Chem. Biol. Interact. 178, 151-157.
    • (2009) Chem. Biol. Interact. , vol.178 , pp. 151-157
    • Endo, S.1    Matsunaga, T.2    Mamiya, H.3    Hara, A.4    Kitade, Y.5    Tajima, K.6    El-Kabbani, O.7
  • 21
    • 80052142551 scopus 로고    scopus 로고
    • RDH10 is the primary enzyme responsible for the first step of embryonic Vitamin A metabolism and retinoic acid synthesis
    • Farjo, K. M., Moiseyev, G., Nikolaeva, O., Sandell, L. L., Trainor, P. A., and Ma, J. X. (2011). RDH10 is the primary enzyme responsible for the first step of embryonic Vitamin A metabolism and retinoic acid synthesis. Dev. Biol. 357, 347-355.
    • (2011) Dev. Biol. , vol.357 , pp. 347-355
    • Farjo, K.M.1    Moiseyev, G.2    Nikolaeva, O.3    Sandell, L.L.4    Trainor, P.A.5    Ma, J.X.6
  • 23
    • 0036538288 scopus 로고    scopus 로고
    • Kinetic analysis of mouse retinal dehydrogenase type-2 (RALDH2) for retinal substrates
    • Gagnon, I., Duester, G., and Bhat, P. V. (2002). Kinetic analysis of mouse retinal dehydrogenase type-2 (RALDH2) for retinal substrates. Biochim. Biophys. Acta 1596, 156-162.
    • (2002) Biochim. Biophys. Acta , vol.1596 , pp. 156-162
    • Gagnon, I.1    Duester, G.2    Bhat, P.V.3
  • 28
    • 0032584601 scopus 로고    scopus 로고
    • cDNA cloning and characterization of a new human microsomal NAD+dependent dehydrogenase that oxidizes all-trans-retinol and 3alpha-hydroxysteroids
    • Gough,W. H.,Vanooteghem, S., Sint, T., and Kedishvili, N. Y. (1998). cDNA cloning and characterization of a new human microsomal NAD+dependent dehydrogenase that oxidizes all-trans-retinol and 3alpha-hydroxysteroids. J. Biol. Chem. 273, 19778-19785.
    • (1998) J. Biol. Chem. , vol.273 , pp. 19778-19785
    • Gough, W.H.1    Vanooteghem, S.2    Sint, T.3    Kedishvili, N.Y.4
  • 30
    • 0024590799 scopus 로고
    • Immunoquantitation of aldose reductase in human tissues
    • Grimshaw, C. E., and Mathur, E. J. (1989). Immunoquantitation of aldose reductase in human tissues. Anal. Biochem. 176, 66-71.
    • (1989) Anal. Biochem. , vol.176 , pp. 66-71
    • Grimshaw, C.E.1    Mathur, E.J.2
  • 31
    • 83255187330 scopus 로고    scopus 로고
    • Mechanisms involved in the intestinal absorption of dietary vitamin A and provitamin A carotenoids
    • Harrison, E. H. (2012). Mechanisms involved in the intestinal absorption of dietary vitamin A and provitamin A carotenoids. Biochim. Biophys. Acta 1821, 70-77.
    • (2012) Biochim. Biophys. Acta , vol.1821 , pp. 70-77
    • Harrison, E.H.1
  • 32
    • 0033515649 scopus 로고    scopus 로고
    • Differential mechanisms of retinoid transfer from cellular retinol binding proteins types I and II to phospholipid membranes
    • Herr, F. M., Li, E., Weinberg, R. B., Cook, V. R., and Storch, J. (1999). Differential mechanisms of retinoid transfer from cellular retinol binding proteins types I and II to phospholipid membranes. J. Biol. Chem. 274, 9556-9563.
    • (1999) J. Biol. Chem. , vol.274 , pp. 9556-9563
    • Herr, F.M.1    Li, E.2    Weinberg, R.B.3    Cook, V.R.4    Storch, J.5
  • 33
    • 0017702359 scopus 로고
    • Vitamin A1 intestinal absorption in vivo: influence of luminal factors on transport
    • Hollander, D., and Muralidhara, K. S. (1977). Vitamin A1 intestinal absorption in vivo: influence of luminal factors on transport. Am. J. Physiol. 232, E471-E477.
    • (1977) Am. J. Physiol , vol.232
    • Hollander, D.1    Muralidhara, K.S.2
  • 35
    • 0003836655 scopus 로고    scopus 로고
    • Sequence and expression levels in human tissues of a new member of the aldo-keto reductase family
    • Hyndman, D. J., and Flynn, T. G. (1998). Sequence and expression levels in human tissues of a new member of the aldo-keto reductase family. Biochim. Biophys. Acta 1399, 198-202.
    • (1998) Biochim. Biophys. Acta , vol.1399 , pp. 198-202
    • Hyndman, D.J.1    Flynn, T.G.2
  • 36
    • 0030876351 scopus 로고    scopus 로고
    • A new nomenclature for the aldo-keto reductase superfamily
    • Jez, J. M., Flynn, T. G., and Penning, T. M. (1997). A new nomenclature for the aldo-keto reductase superfamily. Biochem. Pharmacol. 54, 639-647.
    • (1997) Biochem. Pharmacol. , vol.54 , pp. 639-647
    • Jez, J.M.1    Flynn, T.G.2    Penning, T.M.3
  • 37
    • 33751096178 scopus 로고    scopus 로고
    • Multiple steps determine the overall rate of the reduction of 5alpha-dihydrotestosterone catalyzed by human type 3 3alphahydroxysteroid dehydrogenase: implications for the elimination of androgens
    • Jin, Y., and Penning, T. M. (2006). Multiple steps determine the overall rate of the reduction of 5alpha-dihydrotestosterone catalyzed by human type 3 3alphahydroxysteroid dehydrogenase: implications for the elimination of androgens. Biochemistry 45, 13054-13063.
    • (2006) Biochemistry , vol.45 , pp. 13054-13063
    • Jin, Y.1    Penning, T.M.2
  • 38
    • 33847021147 scopus 로고    scopus 로고
    • Aldo-keto reductases and bioactivation/detoxication
    • Jin, Y., and Penning, T. M. (2007). Aldo-keto reductases and bioactivation/detoxication. Annu.Rev.Pharmacol. Toxicol. 47, 263-292.
    • (2007) Annu. Rev. Pharmacol. Toxicol. , vol.47 , pp. 263-292
    • Jin, Y.1    Penning, T.M.2
  • 39
    • 79952523150 scopus 로고    scopus 로고
    • Murine aldoketo reductase family 1 subfamily B: identification of AKR1B8 as an ortholog of human AKR1B10
    • Joshi, A., Rajput, S., Wang, C., Ma, J., and Cao, D. (2010). Murine aldoketo reductase family 1 subfamily B: identification of AKR1B8 as an ortholog of human AKR1B10. Biol. Chem. 391, 1371-1378.
    • (2010) Biol. Chem. , vol.391 , pp. 1371-1378
    • Joshi, A.1    Rajput, S.2    Wang, C.3    Ma, J.4    Cao, D.5
  • 40
    • 83255193970 scopus 로고    scopus 로고
    • Analysis, occurrence, and function of 9-cis-retinoic acid
    • Kane, M. A. (2012). Analysis, occurrence, and function of 9-cis-retinoic acid. Biochim. Biophys. Acta 1821, 10-20.
    • (2012) Biochim. Biophys. Acta , vol.1821 , pp. 10-20
    • Kane, M.A.1
  • 41
    • 79952986460 scopus 로고    scopus 로고
    • Binding affinities of CRBPI and CRBPII for 9-cisretinoids
    • Kane, M. A., Bright, F. V., and Napoli, J. L. (2011). Binding affinities of CRBPI and CRBPII for 9-cisretinoids. Biochim. Biophys. Acta 1810, 514-518.
    • (2011) Biochim. Biophys. Acta , vol.1810 , pp. 514-518
    • Kane, M.A.1    Bright, F.V.2    Napoli, J.L.3
  • 43
  • 44
    • 3543044946 scopus 로고    scopus 로고
    • Human ocular aldehyde dehydrogenase isozymes: distribution and properties as major soluble proteins in cornea and lens
    • King, G., and Holmes, R. (1998). Human ocular aldehyde dehydrogenase isozymes: distribution and properties as major soluble proteins in cornea and lens. J. Exp. Zool. 282, 12-17.
    • (1998) J. Exp. Zool. , vol.282 , pp. 12-17
    • King, G.1    Holmes, R.2
  • 45
    • 83255187861 scopus 로고    scopus 로고
    • Alcohol and aldehyde dehydrogenases: retinoid metabolic effects in mouse knockout models
    • Kumar, S., Sandell, L. L., Trainor, P. A., Koentgen, F., and Duester, G. (2012). Alcohol and aldehyde dehydrogenases: retinoid metabolic effects in mouse knockout models. Biochim. Biophys. Acta 1821, 198-205.
    • (2012) Biochim. Biophys. Acta , vol.1821 , pp. 198-205
    • Kumar, S.1    Sandell, L.L.2    Trainor, P.A.3    Koentgen, F.4    Duester, G.5
  • 46
    • 0034704136 scopus 로고    scopus 로고
    • cDNA cloning and expression of a human aldehyde dehydrogenase (ALDH) active with 9-cis-retinal and identification of a rat ortholog
    • Lin, M., and Napoli, J. L. (2000). cDNA cloning and expression of a human aldehyde dehydrogenase (ALDH) active with 9-cis-retinal and identification of a rat ortholog, ALDH12. J. Biol. Chem. 275, 40106-40112.
    • (2000) ALDH12. J. Biol. Chem. , vol.275 , pp. 40106-40112
    • Lin, M.1    Napoli, J.L.2
  • 47
    • 83255186681 scopus 로고    scopus 로고
    • Mammalian carotenoid-oxygenases: key players for carotenoid function and homeostasis
    • Lobo, G. P.,Amengual, J., Palczewski, G., Babino, D., and Von Lintig, J. (2012). Mammalian carotenoid-oxygenases: key players for carotenoid function and homeostasis. Biochim. Biophys. Acta 1821, 78-87.
    • (2012) Biochim. Biophys. Acta , vol.1821 , pp. 78-87
    • Lobo, G.P.1    Amengual, J.2    Palczewski, G.3    Babino, D.4    Von Lintig, J.5
  • 48
    • 1642357433 scopus 로고    scopus 로고
    • Crystal structures of prostaglandin D(2) 11-ketoreductase (AKR1C3) in complex with the nonsteroidal antiinflammatory drugs flufenamic acid and indomethacin
    • Lovering, A. L., Ride, J. P., Bunce, C. M., Desmond, J. C., Cummings, S. M., and White, S. A. (2004). Crystal structures of prostaglandin D(2) 11-ketoreductase (AKR1C3) in complex with the nonsteroidal antiinflammatory drugs flufenamic acid and indomethacin. Cancer Res. 64, 1802-1810.
    • (2004) Cancer Res , vol.64 , pp. 1802-1810
    • Lovering, A.L.1    Ride, J.P.2    Bunce, C.M.3    Desmond, J.C.4    Cummings, S.M.5    White, S.A.6
  • 49
    • 70249138697 scopus 로고    scopus 로고
    • Characterization of the cancer chemopreventive NRF2dependent gene battery in human keratinocytes: demonstration that the KEAP1-NRF2 pathway, and not the BACH1-NRF2 pathway, controls cytoprotection against electrophiles as well as redox-cycling compounds
    • MacLeod, A. K., Mcmahon, M., Plummer, S. M., Higgins, L. G., Penning, T. M., Igarashi, K., and Hayes, J. D. (2009). Characterization of the cancer chemopreventive NRF2dependent gene battery in human keratinocytes: demonstration that the KEAP1-NRF2 pathway, and not the BACH1-NRF2 pathway, controls cytoprotection against electrophiles as well as redox-cycling compounds. Carcinogenesis 30, 1571-1580.
    • (2009) Carcinogenesis , vol.30 , pp. 1571-1580
    • MacLeod, A.K.1    Mcmahon, M.2    Plummer, S.M.3    Higgins, L.G.4    Penning, T.M.5    Igarashi, K.6    Hayes, J.D.7
  • 50
    • 59049086019 scopus 로고    scopus 로고
    • Role of human aldo-keto-reductase AKR1B10 in the protection against toxic aldehydes
    • Martin, H. J., and Maser, E. (2009). Role of human aldo-keto-reductase AKR1B10 in the protection against toxic aldehydes. Chem. Biol. Interact. 178, 145-150.
    • (2009) Chem. Biol. Interact. , vol.178 , pp. 145-150
    • Martin, H.J.1    Maser, E.2
  • 53
    • 0032831815 scopus 로고    scopus 로고
    • Interactions of retinoid binding proteins and enzymes in retinoid metabolism
    • Napoli, J. L. (1999). Interactions of retinoid binding proteins and enzymes in retinoid metabolism. Biochim. Biophys. Acta 1440, 139-162.
    • (1999) Biochim. Biophys. Acta , vol.1440 , pp. 139-162
    • Napoli, J.L.1
  • 54
    • 56149115318 scopus 로고    scopus 로고
    • Inactivation of the anticancer drugs doxorubicin and oracin by aldo-keto reductase (AKR) 1C3
    • Novotna, R., Wsol, V., Xiong, G., and Maser, E. (2008). Inactivation of the anticancer drugs doxorubicin and oracin by aldo-keto reductase (AKR) 1C3. Toxicol. Lett. 181, 1-6.
    • (2008) Toxicol. Lett. , vol.181 , pp. 1-6
    • Novotna, R.1    Wsol, V.2    Xiong, G.3    Maser, E.4
  • 55
    • 58149141588 scopus 로고    scopus 로고
    • Mediumand short-chain dehydrogenase/reductase gene and protein families: medium-chain and shortchain dehydrogenases/reductases in retinoid metabolism
    • Parés, X., Farrés, J., Kedishvili, N., and Duester, G. (2008). Mediumand short-chain dehydrogenase/reductase gene and protein families: medium-chain and shortchain dehydrogenases/reductases in retinoid metabolism. Cell.Mol.Life Sci. 65, 3936-3949.
    • (2008) Cell. Mol. Life Sci. , vol.65 , pp. 3936-3949
    • Parés, X.1    Farrés, J.2    Kedishvili, N.3    Duester, G.4
  • 56
    • 16444364105 scopus 로고    scopus 로고
    • AKR1B10: a new diagnostic marker of non-small cell lung carcinoma in smokers
    • Penning, T. M. (2005). AKR1B10: a new diagnostic marker of non-small cell lung carcinoma in smokers. Clin. Cancer Res. 11, 1687-1690.
    • (2005) Clin. Cancer Res. , vol.11 , pp. 1687-1690
    • Penning, T.M.1
  • 57
    • 0034287545 scopus 로고    scopus 로고
    • Human 3alpha-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
    • Penning, T. M., Burczynski, M. E., Jez, J. M., Hung, C. F., Lin, H. K., Ma, H., Moore, M., Palackal, N., and Ratnam, K. (2000). Human 3alpha-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.
    • (2000) Biochem. J. , vol.351 , pp. 67-77
    • Penning, T.M.1    Burczynski, M.E.2    Jez, J.M.3    Hung, C.F.4    Lin, H.K.5    Ma, H.6    Moore, M.7    Palackal, N.8    Ratnam, K.9
  • 58
    • 61649103983 scopus 로고    scopus 로고
    • Steroid hormone transforming aldoketo reductases and cancer
    • Penning, T. M., and Byrns, M. C. (2009). Steroid hormone transforming aldoketo reductases and cancer. Ann. N. Y. Acad. Sci. 1155, 33-42.
    • (2009) Ann. N. Y. Acad. Sci. , vol.1155 , pp. 33-42
    • Penning, T.M.1    Byrns, M.C.2
  • 59
    • 34547692874 scopus 로고    scopus 로고
    • Human aldo-keto reductases: function, gene regulation, and single nucleotide polymorphisms
    • Penning, T. M., and Drury, J. E. (2007). Human aldo-keto reductases: function, gene regulation, and single nucleotide polymorphisms. Arch. Biochem. Biophys. 464, 241-250.
    • (2007) Arch. Biochem. Biophys. , vol.464 , pp. 241-250
    • Penning, T.M.1    Drury, J.E.2
  • 61
    • 59049105837 scopus 로고    scopus 로고
    • Genomics of smoking exposure and cessation: lessons for cancer prevention and treatment
    • Penning, T. M., and Lerman, C. (2008). Genomics of smoking exposure and cessation: lessons for cancer prevention and treatment. Cancer Prev. Res. (Phila.) 1, 80-83.
    • (2008) Cancer Prev. Res. (Phila. ) , vol.1 , pp. 80-83
    • Penning, T.M.1    Lerman, C.2
  • 62
    • 19944430311 scopus 로고    scopus 로고
    • Characterization of the interaction between retinoic acid receptor/retinoid X receptor (RAR/RXR) heterodimers and transcriptional coactivators through structural and fluorescence anisotropy studies
    • Pogenberg, V., Guichou, J. F., Vivat-Hannah, V., Kammerer, S., Perez, E., Germain, P., De Lera, A. R., Gronemeyer, H., Royer, C. A., and Bourguet, W. (2005). Characterization of the interaction between retinoic acid receptor/retinoid X receptor (RAR/RXR) heterodimers and transcriptional coactivators through structural and fluorescence anisotropy studies. J. Biol. Chem. 280, 1625-1633.
    • (2005) J. Biol. Chem. , vol.280 , pp. 1625-1633
    • Pogenberg, V.1    Guichou, J.F.2    Vivat-Hannah, V.3    Kammerer, S.4    Perez, E.5    Germain, P.6    De Lera, A.R.7    Gronemeyer, H.8    Royer, C.A.9    Bourguet, W.10
  • 63
    • 0025636513 scopus 로고
    • Vitamin A metabolism in the human intestinal Caco-2 cell line
    • Quick, T. C., and Ong, D. E. (1990). Vitamin A metabolism in the human intestinal Caco-2 cell line. Biochemistry 29, 11116-11123.
    • (1990) Biochemistry , vol.29 , pp. 11116-11123
    • Quick, T.C.1    Ong, D.E.2
  • 64
    • 57449083407 scopus 로고    scopus 로고
    • Oxidation of PAH trans-dihydrodiols by human aldo-keto reductase AKR1B10
    • Quinn, A. M., Harvey, R. G., and Penning, T. M. (2008). Oxidation of PAH trans-dihydrodiols by human aldo-keto reductase AKR1B10. Chem. Res. Toxicol. 21, 2207-2215.
    • (2008) Chem. Res. Toxicol. , vol.21 , pp. 2207-2215
    • Quinn, A.M.1    Harvey, R.G.2    Penning, T.M.3
  • 68
    • 79957571968 scopus 로고    scopus 로고
    • Human aldo-keto reductases 1B1 and 1B10: a comparative study on their enzyme activity toward electrophilic carbonyl compounds
    • Shen, Y., Zhong, L., Johnson, S., and Cao, D. (2011). Human aldo-keto reductases 1B1 and 1B10: a comparative study on their enzyme activity toward electrophilic carbonyl compounds. Chem. Biol. Interact. 191, 192-198.
    • (2011) Chem. Biol. Interact. , vol.191 , pp. 192-198
    • Shen, Y.1    Zhong, L.2    Johnson, S.3    Cao, D.4
  • 70
    • 33750286521 scopus 로고    scopus 로고
    • Aldose reductase regulates growth factor-induced cyclooxygenase-2 expression and prostaglandin E2 production in human colon cancer cells
    • Tammali, R., Ramana, K. V., Singhal, S. S., Awasthi, S., and Srivastava, S. K. (2006). Aldose reductase regulates growth factor-induced cyclooxygenase-2 expression and prostaglandin E2 production in human colon cancer cells. Cancer Res. 66, 9705-9713.
    • (2006) Cancer Res , vol.66 , pp. 9705-9713
    • Tammali, R.1    Ramana, K.V.2    Singhal, S.S.3    Awasthi, S.4    Srivastava, S.K.5
  • 71
    • 78649668597 scopus 로고    scopus 로고
    • Retinoids, retinoic acid receptors, and cancer
    • Tang, X. H., and Gudas, L. J. (2011). Retinoids, retinoic acid receptors, and cancer. Annu. Rev. Pathol. 6, 345-364.
    • (2011) Annu. Rev. Pathol. , vol.6 , pp. 345-364
    • Tang, X.H.1    Gudas, L.J.2
  • 72
    • 77952314065 scopus 로고    scopus 로고
    • From carrot to clinic: an overview of the retinoic acid signaling pathway
    • Theodosiou, M., Laudet, V., and Schubert, M. (2010). From carrot to clinic: an overview of the retinoic acid signaling pathway. Cell. Mol. Life Sci. 67, 1423-1445.
    • (2010) Cell. Mol. Life Sci. , vol.67 , pp. 1423-1445
    • Theodosiou, M.1    Laudet, V.2    Schubert, M.3
  • 73
    • 41249097311 scopus 로고    scopus 로고
    • Inhibiting wild-type and C299S mutant AKR1B10; a homologue of aldose reductase upregulated in cancers
    • Verma, M., Martin, H. J., Haq, W., O'Connor, T. R., Maser, E., and 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.
    • (2008) Eur. J. Pharmacol. , vol.584 , pp. 213-221
    • Verma, M.1    Martin, H.J.2    Haq, W.3    O'Connor, T.R.4    Maser, E.5    Balendiran, G.K.6
  • 74
    • 70350371727 scopus 로고    scopus 로고
    • Aldo-keto reductase family 1 member B10 promotes cell survival by regulating lipid synthesis and eliminating carbonyls
    • Wang, C., Yan, R., Luo, D., Watabe, K., Liao, D. F., and Cao, D. (2009). Aldo-keto reductase family 1 member B10 promotes cell survival by regulating lipid synthesis and eliminating carbonyls. J. Biol. Chem. 284, 26742-26748.
    • (2009) J. Biol. Chem. , vol.284 , pp. 26742-26748
    • Wang, C.1    Yan, R.2    Luo, D.3    Watabe, K.4    Liao, D.F.5    Cao, D.6
  • 76
    • 46749092864 scopus 로고    scopus 로고
    • Expression of RALDHs (ALDH1As) and CYP26s in human tissues and during the neural differentiation of P19 embryonal carcinoma stem cell
    • Xi, J., and Yang, Z. (2008). Expression of RALDHs (ALDH1As) and CYP26s in human tissues and during the neural differentiation of P19 embryonal carcinoma stem cell. Gene Expr. Patterns 8, 438-442.
    • (2008) Gene Expr. Patterns , vol.8 , pp. 438-442
    • Xi, J.1    Yang, Z.2
  • 77
    • 0027058140 scopus 로고
    • Retinal oxidation activity and biological role of human cytosolic aldehyde dehydrogenase
    • Yoshida, A., Hsu, L. C., and Dave, V. (1992). Retinal oxidation activity and biological role of human cytosolic aldehyde dehydrogenase. Enzyme 46, 239-244.
    • (1992) Enzyme , vol.46 , pp. 239-244
    • Yoshida, A.1    Hsu, L.C.2    Dave, V.3
  • 79
    • 79960841454 scopus 로고    scopus 로고
    • AKR1B10 induces cell resistance to daunorubicin and idarubicin by reducing C13 ketonic group
    • Zhong, L., Shen, H., Huang, C., Jing, H., and Cao, D. (2011). AKR1B10 induces cell resistance to daunorubicin and idarubicin by reducing C13 ketonic group. Toxicol. Appl. Pharmacol. 255, 40-47.
    • (2011) Toxicol. Appl. Pharmacol. , vol.255 , pp. 40-47
    • Zhong, L.1    Shen, H.2    Huang, C.3    Jing, H.4    Cao, D.5


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