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Volumn 56, Issue 2, 2012, Pages 241-250

Importance of β,β-carotene 15,15′-monooxygenase 1 (BCMO1) and β,β-carotene 9′,10′-dioxygenase 2 (BCDO2) in nutrition and health

Author keywords

BCDO2; BCMO1; Carotenoids; SNP; Vitamin A

Indexed keywords

ACYL COENZYME A DESATURASE; BCMO1 PROTEIN, HUMAN; BCO2 PROTEIN, HUMAN; BETA CAROTENE 15,15' MONOOXYGENASE; CAROTENOID; RETINOID;

EID: 84858318259     PISSN: 16134125     EISSN: 16134133     Source Type: Journal    
DOI: 10.1002/mnfr.201100387     Document Type: Review
Times cited : (69)

References (87)
  • 2
    • 0036805238 scopus 로고    scopus 로고
    • Carotenoids, mostly the xanthophylls, exchange between plasma lipoproteins
    • Tyssandier, V., Choubert, G., Grolier, P., Borel, P., Carotenoids, mostly the xanthophylls, exchange between plasma lipoproteins. Int. J. Vitam. Nutr. Res. 2002, 72, 300-308.
    • (2002) Int. J. Vitam. Nutr. Res. , vol.72 , pp. 300-308
    • Tyssandier, V.1    Choubert, G.2    Grolier, P.3    Borel, P.4
  • 3
    • 0031844549 scopus 로고    scopus 로고
    • Bioavailability and bioconversion of carotenoids
    • Castenmiller, J. J. M., West, C. E., Bioavailability and bioconversion of carotenoids. Annu. Rev. Nutr. 1998, 18, 19-38.
    • (1998) Annu. Rev. Nutr. , vol.18 , pp. 19-38
    • Castenmiller, J.J.M.1    West, C.E.2
  • 4
    • 77956188489 scopus 로고    scopus 로고
    • Molecular and dietary regulation of β,β-carotene 15, 15′-monooxygenase 1 (BCMO1)
    • Lietz, G., Lange, J., Rimbach, G., Molecular and dietary regulation of β, β-carotene 15, 15′-monooxygenase 1 (BCMO1). Arch. Biochem. Biophys. 2010, 502, 8-16.
    • (2010) Arch. Biochem. Biophys. , vol.502 , pp. 8-16
    • Lietz, G.1    Lange, J.2    Rimbach, G.3
  • 5
    • 75149149494 scopus 로고    scopus 로고
    • Biochemical evidence for the tyrosine involvement in cationic intermediate stabilization in mouse β-carotene 15, 15′-monooxygenase
    • Poliakov, E., Gentleman, S., Chander, P., Cunningham, F. X., Jr. et al., Biochemical evidence for the tyrosine involvement in cationic intermediate stabilization in mouse β-carotene 15, 15′-monooxygenase. BMC Biochem. 2009, 10, 31.
    • (2009) BMC Biochem. , vol.10 , pp. 31
    • Poliakov, E.1    Gentleman, S.2    Chander, P.3    Cunningham Jr., F.X.4
  • 6
    • 0033916427 scopus 로고    scopus 로고
    • β-Carotene is converted primarily to retinoids in rats in vivo
    • Barua, A. B., Olson, J. A., β-Carotene is converted primarily to retinoids in rats in vivo. J. Nutr. 2000, 130, 1996-2001.
    • (2000) J. Nutr. , vol.130 , pp. 1996-2001
    • Barua, A.B.1    Olson, J.A.2
  • 7
    • 0024503034 scopus 로고
    • Provitamin A function of carotenoids: The conversion of β-carotene into vitamin A
    • Olson, J. A., Provitamin A function of carotenoids: The conversion of β-carotene into vitamin A. J. Nutr. 1989, 119, 105-108.
    • (1989) J. Nutr. , vol.119 , pp. 105-108
    • Olson, J.A.1
  • 8
    • 0026603897 scopus 로고
    • Retinoic acid can be produced from excentric cleavage of β-carotene in human intestinal mucosa
    • Wang, X. D., Krinsky, N. I., Tang, G. W., Russell, R. M., Retinoic acid can be produced from excentric cleavage of β-carotene in human intestinal mucosa. Arch. Biochem. Biophys. 1992, 293, 298-304.
    • (1992) Arch. Biochem. Biophys. , vol.293 , pp. 298-304
    • Wang, X.D.1    Krinsky, N.I.2    Tang, G.W.3    Russell, R.M.4
  • 9
    • 0029914087 scopus 로고    scopus 로고
    • β-Oxidation in rabbit liver in vitro and in the perfused ferret liver contributes to retinoic acid biosynthesis from β-apocarotenoic acids
    • Wang, X. D., Russell, R. M., Liu, C., Stickel, F. et al., β-Oxidation in rabbit liver in vitro and in the perfused ferret liver contributes to retinoic acid biosynthesis from β-apocarotenoic acids. J. Biol. Chem. 1996, 271, 26490-26498.
    • (1996) J. Biol. Chem. , vol.271 , pp. 26490-26498
    • Wang, X.D.1    Russell, R.M.2    Liu, C.3    Stickel, F.4
  • 10
    • 0029089710 scopus 로고
    • The enzymatic cleavage of β-carotene - still controversial
    • Wolf, G., Phil, D., The enzymatic cleavage of β-carotene - still controversial. Nutr. Rev. 1995, 53, 134-137.
    • (1995) Nutr. Rev. , vol.53 , pp. 134-137
    • Wolf, G.1    Phil, D.2
  • 11
    • 0347986903 scopus 로고    scopus 로고
    • Carotene oxygenases: A new family of double bond cleavage enzymes
    • Wyss, A., Carotene oxygenases: A new family of double bond cleavage enzymes. J. Nutr. 2004, 134, 246S-250S.
    • (2004) J. Nutr. , vol.134
    • Wyss, A.1
  • 12
    • 36349019877 scopus 로고    scopus 로고
    • CMO1 deficiency abolishes vitamin A production from β-carotene and alters lipid metabolism in mice
    • Hessel, S., Eichinger, A., Isken, A., Amengual, J. et al., CMO1 deficiency abolishes vitamin A production from β-carotene and alters lipid metabolism in mice. J. Biol. Chem. 2007, 282, 33553-33561.
    • (2007) J. Biol. Chem. , vol.282 , pp. 33553-33561
    • Hessel, S.1    Eichinger, A.2    Isken, A.3    Amengual, J.4
  • 13
    • 77957923646 scopus 로고    scopus 로고
    • Hepatic stellate cells are an important cellular site for β-carotene conversion to retinoid
    • Shmarakov, I., Fleshman, M. K., D'Ambrosio, D. N., Piantedosi, R. et al., Hepatic stellate cells are an important cellular site for β-carotene conversion to retinoid. Arch. Biochem. Biophys. 2010, 504, 3-10.
    • (2010) Arch. Biochem. Biophys. , vol.504 , pp. 3-10
    • Shmarakov, I.1    Fleshman, M.K.2    D'Ambrosio, D.N.3    Piantedosi, R.4
  • 15
    • 79954601092 scopus 로고    scopus 로고
    • A mitochondrial enzyme degrades carotenoids and protects against oxidative stress
    • Amengual, J., Lobo, G. P., Golczak, M., Li, H. N. et al., A mitochondrial enzyme degrades carotenoids and protects against oxidative stress. FASEB J. 2011, 25, 948-959.
    • (2011) FASEB J. , vol.25 , pp. 948-959
    • Amengual, J.1    Lobo, G.P.2    Golczak, M.3    Li, H.N.4
  • 16
    • 78751633674 scopus 로고    scopus 로고
    • Enzymatic formation of apo-carotenoids from the xanthophyll carotenoids lutein, zeaxanthin and β-cryptoxanthin by ferret carotene-9′,10′-monooxygenase
    • Mein, J. R., Dolnikowski, G. G., Ernst, H., Russell, R. M., Wang, X. D., Enzymatic formation of apo-carotenoids from the xanthophyll carotenoids lutein, zeaxanthin and β-cryptoxanthin by ferret carotene-9′, 10′-monooxygenase. Arch. Biochem. Biophys. 2011, 506, 109-121.
    • (2011) Arch. Biochem. Biophys. , vol.506 , pp. 109-121
    • Mein, J.R.1    Dolnikowski, G.G.2    Ernst, H.3    Russell, R.M.4    Wang, X.D.5
  • 17
    • 49749133236 scopus 로고    scopus 로고
    • Enzymatic metabolites of lycopene induce Nrf2-mediated expression of phase II detoxifying/antioxidant enzymes in human bronchial epithelial cells
    • Lian, F., Wang, X. D., Enzymatic metabolites of lycopene induce Nrf2-mediated expression of phase II detoxifying/antioxidant enzymes in human bronchial epithelial cells. Int. J. Cancer 2008, 123, 1262-1268.
    • (2008) Int. J. Cancer , vol.123 , pp. 1262-1268
    • Lian, F.1    Wang, X.D.2
  • 18
    • 34547800757 scopus 로고    scopus 로고
    • Apo-10′-lycopenoic acid inhibits lung cancer cell growth in vitro, and suppresses lung tumorigenesis in the A/J mouse model in vivo
    • Lian, F., Smith, D. E., Ernst, H., Russell, R. M., Wang, X. D., Apo-10′-lycopenoic acid inhibits lung cancer cell growth in vitro, and suppresses lung tumorigenesis in the A/J mouse model in vivo. Carcinogenesis 2007, 28, 1567-1574.
    • (2007) Carcinogenesis , vol.28 , pp. 1567-1574
    • Lian, F.1    Smith, D.E.2    Ernst, H.3    Russell, R.M.4    Wang, X.D.5
  • 19
    • 33845996557 scopus 로고    scopus 로고
    • Asymmetric cleavage of β-carotene yields a transcriptional repressor of retinoid X receptor and peroxisome proliferator-activated receptor responses
    • Ziouzenkova, O., Orasanu, G., Sukhova, G., Lau, E. et al., Asymmetric cleavage of β-carotene yields a transcriptional repressor of retinoid X receptor and peroxisome proliferator-activated receptor responses. Mol. Endocrinol. 2007, 21, 77-88.
    • (2007) Mol. Endocrinol. , vol.21 , pp. 77-88
    • Ziouzenkova, O.1    Orasanu, G.2    Sukhova, G.3    Lau, E.4
  • 20
    • 33745828641 scopus 로고    scopus 로고
    • The biochemical characterization of ferret carotene-9′,10′-monooxygenase catalyzing cleavage of carotenoids in vitro and in vivo
    • Hu, K. Q., Liu, C., Ernst, H., Krinsky, N. I. et al., The biochemical characterization of ferret carotene-9′, 10′-monooxygenase catalyzing cleavage of carotenoids in vitro and in vivo. J. Biol. Chem. 2006, 281, 19327-19338.
    • (2006) J. Biol. Chem. , vol.281 , pp. 19327-19338
    • Hu, K.Q.1    Liu, C.2    Ernst, H.3    Krinsky, N.I.4
  • 21
    • 23844477891 scopus 로고    scopus 로고
    • Key role of conserved histidines in recombinant mouse β-carotene 15,15′-monooxygenase-1 activity
    • Poliakov, E., Gentleman, S., Cunningham, F. X., Jr., Miller-Ihli, N. J., Redmond, T. M., Key role of conserved histidines in recombinant mouse β-carotene 15, 15′-monooxygenase-1 activity. J. Biol. Chem. 2005, 280, 29217-29223.
    • (2005) J. Biol. Chem. , vol.280 , pp. 29217-29223
    • Poliakov, E.1    Gentleman, S.2    Cunningham Jr., F.X.3    Miller-Ihli, N.J.4    Redmond, T.M.5
  • 22
    • 33750462411 scopus 로고    scopus 로고
    • Structural and biological aspects of carotenoid cleavage
    • Kloer, D. P., Schulz, G. E., Structural and biological aspects of carotenoid cleavage. Cell. Mol. Life Sci. 2006, 63, 2291-2303.
    • (2006) Cell. Mol. Life Sci. , vol.63 , pp. 2291-2303
    • Kloer, D.P.1    Schulz, G.E.2
  • 23
    • 0035898492 scopus 로고    scopus 로고
    • The reaction mechanism of the enzyme-catalyzed central cleavage of β-carotene to retinal
    • Leuenberger, M. G., Engeloch-Jarret, C., Woggon, W. D., The reaction mechanism of the enzyme-catalyzed central cleavage of β-carotene to retinal. Angew. Chem. (Int. ed. English) 2001, 40, 2613-2617.
    • (2001) Angew. Chem. (Int. ed. English) , vol.40 , pp. 2613-2617
    • Leuenberger, M.G.1    Engeloch-Jarret, C.2    Woggon, W.D.3
  • 24
    • 53849143995 scopus 로고    scopus 로고
    • Reaction mechanism of apocarotenoid oxygenase (ACO): A DFT study
    • Borowski, T., Blomberg, M. R., Siegbahn, P. E., Reaction mechanism of apocarotenoid oxygenase (ACO): A DFT study. Chemistry 2008, 14, 2264-2276.
    • (2008) Chemistry , vol.14 , pp. 2264-2276
    • Borowski, T.1    Blomberg, M.R.2    Siegbahn, P.E.3
  • 25
    • 41049086313 scopus 로고    scopus 로고
    • In vitro and in vivo characterization of retinoid synthesis from β-carotene
    • Fierce, Y., de Morais Vieira, M., Piantedosi, R., Wyss, A. et al., In vitro and in vivo characterization of retinoid synthesis from β-carotene. Arch. Biochem. Biophys. 2008, 472, 126-138.
    • (2008) Arch. Biochem. Biophys. , vol.472 , pp. 126-138
    • Fierce, Y.1    de Morais Vieira, M.2    Piantedosi, R.3    Wyss, A.4
  • 26
    • 65349134706 scopus 로고    scopus 로고
    • Two common single nucleotide polymorphisms in the gene encoding β-carotene 15,15′-monoxygenase alter β-carotene metabolism in female volunteers
    • Leung, W. C., Hessel, S., Meplan, C., Flint, J. et al., Two common single nucleotide polymorphisms in the gene encoding β-carotene 15, 15′-monoxygenase alter β-carotene metabolism in female volunteers. FASEB J. 2009, 23, 1041-1053.
    • (2009) FASEB J. , vol.23 , pp. 1041-1053
    • Leung, W.C.1    Hessel, S.2    Meplan, C.3    Flint, J.4
  • 27
    • 43149089362 scopus 로고    scopus 로고
    • Utilization of the recombinant human β-carotene-15,15′-monooxygenase gene in Escherichia coli and mammalian cells
    • Park, C. S., Lee, S. W., Kim, Y. S., Kim, E. J. et al., Utilization of the recombinant human β-carotene-15, 15′-monooxygenase gene in Escherichia coli and mammalian cells. Biotechnol. Lett. 2008, 30, 735-741.
    • (2008) Biotechnol. Lett. , vol.30 , pp. 735-741
    • Park, C.S.1    Lee, S.W.2    Kim, Y.S.3    Kim, E.J.4
  • 28
    • 0035794153 scopus 로고    scopus 로고
    • Identification, expression, and substrate specificity of a mammalian β-carotene 15,15′-dioxygenase
    • Redmond, T. M., Gentleman, S., Duncan, T., Yu, S. et al., Identification, expression, and substrate specificity of a mammalian β-carotene 15, 15′-dioxygenase. J. Biol. Chem. 2001, 276, 6560-6565.
    • (2001) J. Biol. Chem. , vol.276 , pp. 6560-6565
    • Redmond, T.M.1    Gentleman, S.2    Duncan, T.3    Yu, S.4
  • 29
  • 30
    • 27244447697 scopus 로고    scopus 로고
    • Cell type-specific expression of β-carotene 9′,10′-monooxygenase in human tissues
    • Lindqvist, A., He, Y. G., Andersson, S., Cell type-specific expression of β-carotene 9′, 10′-monooxygenase in human tissues. J. Histochem. Cytochem. 2005, 53, 1403-1412.
    • (2005) J. Histochem. Cytochem. , vol.53 , pp. 1403-1412
    • Lindqvist, A.1    He, Y.G.2    Andersson, S.3
  • 31
    • 20444378911 scopus 로고    scopus 로고
    • Towards a better understanding of carotenoid metabolism in animals
    • von Lintig, J., Hessel, S., Isken, A., Kiefer, C. et al., Towards a better understanding of carotenoid metabolism in animals. Biochim. Biophys. Acta 2005, 1740, 122-131.
    • (2005) Biochim. Biophys. Acta , vol.1740 , pp. 122-131
    • von Lintig, J.1    Hessel, S.2    Isken, A.3    Kiefer, C.4
  • 32
    • 0034795231 scopus 로고    scopus 로고
    • The substrate specificity of β,β-carotene 15,15′-monooxygenase
    • Wirtz, G. M., Bornemann, C., Giger, A., Muller, R. K. et al., The substrate specificity of β, β-carotene 15, 15′-monooxygenase. Helvet. Chim. Acta 2001, 84, 2301-2315.
    • (2001) Helvet. Chim. Acta , vol.84 , pp. 2301-2315
    • Wirtz, G.M.1    Bornemann, C.2    Giger, A.3    Muller, R.K.4
  • 33
    • 59149084071 scopus 로고    scopus 로고
    • Substrate specificity of a recombinant chicken β-carotene 15,15′-monooxygenase that converts β-carotene into retinal
    • Kim, Y. S., Oh, D. K., Substrate specificity of a recombinant chicken β-carotene 15, 15′-monooxygenase that converts β-carotene into retinal. Biotechnol. Lett. 2009, 31, 403-408.
    • (2009) Biotechnol. Lett. , vol.31 , pp. 403-408
    • Kim, Y.S.1    Oh, D.K.2
  • 34
    • 0038412523 scopus 로고    scopus 로고
    • Provitamin A conversion to retinal via the β,β-carotene-15,15′-oxygenase (bcox) is essential for pattern formation and differentiation during zebrafish embryogenesis
    • Lampert, J. M., Holzschuh, J., Hessel, S., Driever, W. et al., Provitamin A conversion to retinal via the β, β-carotene-15, 15′-oxygenase (bcox) is essential for pattern formation and differentiation during zebrafish embryogenesis. Development 2003, 130, 2173-2186.
    • (2003) Development , vol.130 , pp. 2173-2186
    • Lampert, J.M.1    Holzschuh, J.2    Hessel, S.3    Driever, W.4
  • 35
    • 57749108322 scopus 로고    scopus 로고
    • NinaB combines carotenoid oxygenase and retinoid isomerase activity in a single polypeptide
    • Oberhauser, V., Voolstra, O., Bangert, A., von Lintig, J., Vogt, K., NinaB combines carotenoid oxygenase and retinoid isomerase activity in a single polypeptide. Proc. Natl. Acad. Sci. USA 2008, 105, 19000-19005.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 19000-19005
    • Oberhauser, V.1    Voolstra, O.2    Bangert, A.3    von Lintig, J.4    Vogt, K.5
  • 36
    • 0034697178 scopus 로고    scopus 로고
    • Filling the gap in vitamin A research. Molecular identification of an enzyme cleaving β-carotene to retinal
    • von Lintig, J., Vogt, K., Filling the gap in vitamin A research. Molecular identification of an enzyme cleaving β-carotene to retinal. J. Biol. Chem. 2000, 275, 11915-11920.
    • (2000) J. Biol. Chem. , vol.275 , pp. 11915-11920
    • von Lintig, J.1    Vogt, K.2
  • 37
    • 0034770556 scopus 로고    scopus 로고
    • Molecular analysis of vitamin A formation: cloning and characterization of β-carotene 15,15′-dioxygenases
    • von Lintig, J., Wyss, A., Molecular analysis of vitamin A formation: cloning and characterization of β-carotene 15, 15′-dioxygenases. Arch. Biochem. Biophys. 2001, 385, 47-52.
    • (2001) Arch. Biochem. Biophys. , vol.385 , pp. 47-52
    • von Lintig, J.1    Wyss, A.2
  • 38
    • 0035816626 scopus 로고    scopus 로고
    • Characterization of a novel carotenoid cleavage dioxygenase from plants
    • Schwartz, S. H., Qin, X., Zeevaart, J. A., Characterization of a novel carotenoid cleavage dioxygenase from plants. J. Biol. Chem. 2001, 276, 25208-25211.
    • (2001) J. Biol. Chem. , vol.276 , pp. 25208-25211
    • Schwartz, S.H.1    Qin, X.2    Zeevaart, J.A.3
  • 39
    • 45149133700 scopus 로고    scopus 로고
    • The carotenoid cleavage dioxygenase 1 enzyme has broad substrate specificity, cleaving multiple carotenoids at two different bond positions
    • Vogel, J. T., Tan, B. C., McCarty, D. R., Klee, H. J., The carotenoid cleavage dioxygenase 1 enzyme has broad substrate specificity, cleaving multiple carotenoids at two different bond positions. J. Biol. Chem. 2008, 283, 11364-11373.
    • (2008) J. Biol. Chem. , vol.283 , pp. 11364-11373
    • Vogel, J.T.1    Tan, B.C.2    McCarty, D.R.3    Klee, H.J.4
  • 40
    • 77955642541 scopus 로고    scopus 로고
    • Colors with functions: Elucidating the biochemical and molecular basis of carotenoid metabolism
    • von Lintig, J., Colors with functions: Elucidating the biochemical and molecular basis of carotenoid metabolism. Annu. Rev. Nutr. 2010, 30, 35-56.
    • (2010) Annu. Rev. Nutr. , vol.30 , pp. 35-56
    • von Lintig, J.1
  • 41
    • 0029845726 scopus 로고    scopus 로고
    • Rat intestinal β-carotene dioxygenase activity is located primarily in the cytosol of mature jejunal enterocytes
    • Duszka, C., Grolier, P., Azim, E. M., AlexandreGouabau, M. C. et al., Rat intestinal β-carotene dioxygenase activity is located primarily in the cytosol of mature jejunal enterocytes. J. Nutr. 1996, 126, 2550-2556.
    • (1996) J. Nutr. , vol.126 , pp. 2550-2556
    • Duszka, C.1    Grolier, P.2    Azim, E.M.3    AlexandreGouabau, M.C.4
  • 42
    • 0037189569 scopus 로고    scopus 로고
    • Biochemical properties of purified recombinant human β-carotene 15,15′-monooxygenase
    • Lindqvist, A., Andersson, S., Biochemical properties of purified recombinant human β-carotene 15, 15′-monooxygenase. J. Biol. Chem. 2002, 277, 23942-23948.
    • (2002) J. Biol. Chem. , vol.277 , pp. 23942-23948
    • Lindqvist, A.1    Andersson, S.2
  • 43
    • 1842534960 scopus 로고    scopus 로고
    • Cell type-specific expression of β-carotene 15,15′-mono-oxygenase in human tissues
    • Lindqvist, A., Andersson, S., Cell type-specific expression of β-carotene 15, 15′-mono-oxygenase in human tissues. J. Histochem. Cytochem. 2004, 52, 491-499.
    • (2004) J. Histochem. Cytochem. , vol.52 , pp. 491-499
    • Lindqvist, A.1    Andersson, S.2
  • 44
    • 0035943608 scopus 로고    scopus 로고
    • Expression and characterization of a murine enzyme able to cleave β-carotene. The formation of retinoids
    • Paik, J., During, A., Harrison, E. H., Mendelsohn, C. L. et al., Expression and characterization of a murine enzyme able to cleave β-carotene. The formation of retinoids. J. Biol. Chem. 2001, 276, 32160-32168.
    • (2001) J. Biol. Chem. , vol.276 , pp. 32160-32168
    • Paik, J.1    During, A.2    Harrison, E.H.3    Mendelsohn, C.L.4
  • 45
    • 33748641523 scopus 로고    scopus 로고
    • Molecular cloning of the rat β-carotene 15,15′-monooxygenase gene and its regulation by retinoic acid
    • Takitani, K., Zhu, C. L., Inoue, A., Tamai, H., Molecular cloning of the rat β-carotene 15, 15′-monooxygenase gene and its regulation by retinoic acid. Eur. J. Nutr. 2006, 45, 320-326.
    • (2006) Eur. J. Nutr. , vol.45 , pp. 320-326
    • Takitani, K.1    Zhu, C.L.2    Inoue, A.3    Tamai, H.4
  • 46
    • 0034630745 scopus 로고    scopus 로고
    • Cloning and expression of β,β-carotene 15,15′-dioxygenase
    • Wyss, A., Wirtz, G., Woggon, W., Brugger, R. et al., Cloning and expression of β, β-carotene 15, 15′-dioxygenase. Biochem. Biophys. Res. Commun. 2000, 271, 334-336.
    • (2000) Biochem. Biophys. Res. Commun. , vol.271 , pp. 334-336
    • Wyss, A.1    Wirtz, G.2    Woggon, W.3    Brugger, R.4
  • 47
    • 33645509662 scopus 로고    scopus 로고
    • Dietary lycopene downregulates carotenoid 15,15′-monooxygenase and PPAR-gamma in selected rat tissues
    • Zaripheh, S., Nara, T. Y., Nakamura, M. T., Erdman, J. W., Jr., Dietary lycopene downregulates carotenoid 15, 15′-monooxygenase and PPAR-gamma in selected rat tissues. J. Nutr. 2006, 136, 932-938.
    • (2006) J. Nutr. , vol.136 , pp. 932-938
    • Zaripheh, S.1    Nara, T.Y.2    Nakamura, M.T.3    Erdman Jr., J.W.4
  • 48
    • 0035957943 scopus 로고    scopus 로고
    • Identification and characterization of a mammalian enzyme catalyzing the asymmetric oxidative cleavage of provitamin A
    • Kiefer, C., Hessel, S., Lampert, J. M., Vogt, K. et al., Identification and characterization of a mammalian enzyme catalyzing the asymmetric oxidative cleavage of provitamin A. J. Biol. Chem. 2001, 276, 14110-14116.
    • (2001) J. Biol. Chem. , vol.276 , pp. 14110-14116
    • Kiefer, C.1    Hessel, S.2    Lampert, J.M.3    Vogt, K.4
  • 49
    • 79955652875 scopus 로고    scopus 로고
    • β-Carotene and its cleavage enzyme β-carotene-15,15′-oxygenase (CMOI) affect retinoid metabolism in developing tissues
    • Kim, Y. K., Wassef, L., Chung, S., Jiang, H. et al., β-Carotene and its cleavage enzyme β-carotene-15, 15′-oxygenase (CMOI) affect retinoid metabolism in developing tissues. FASEB J. 2011, 25, 1641-1652.
    • (2011) FASEB J. , vol.25 , pp. 1641-1652
    • Kim, Y.K.1    Wassef, L.2    Chung, S.3    Jiang, H.4
  • 50
    • 14244257340 scopus 로고    scopus 로고
    • Adipogenic transcriptional regulation of hepatic stellate cells
    • She, H., Xiong, S., Hazra, S., Tsukamoto, H., Adipogenic transcriptional regulation of hepatic stellate cells. J. Biol. Chem. 2005, 280, 4959-4967.
    • (2005) J. Biol. Chem. , vol.280 , pp. 4959-4967
    • She, H.1    Xiong, S.2    Hazra, S.3    Tsukamoto, H.4
  • 51
    • 4043094220 scopus 로고    scopus 로고
    • Retinoic acid receptor alpha dominant negative form causes steatohepatitis and liver tumors in transgenic mice
    • Yanagitani, A., Yamada, S., Yasui, S., Shimomura, T. et al., Retinoic acid receptor alpha dominant negative form causes steatohepatitis and liver tumors in transgenic mice. Hepatology 2004, 40, 366-375.
    • (2004) Hepatology , vol.40 , pp. 366-375
    • Yanagitani, A.1    Yamada, S.2    Yasui, S.3    Shimomura, T.4
  • 52
    • 34249977327 scopus 로고    scopus 로고
    • Retinaldehyde represses adipogenesis and diet-induced obesity
    • Ziouzenkova, O., Orasanu, G., Sharlach, M., Akiyama, T. E. et al., Retinaldehyde represses adipogenesis and diet-induced obesity. Nat. Med. 2007, 13, 695-702.
    • (2007) Nat. Med. , vol.13 , pp. 695-702
    • Ziouzenkova, O.1    Orasanu, G.2    Sharlach, M.3    Akiyama, T.E.4
  • 53
    • 40949141493 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and oxidative stress in the pathogenesis of alcohol- and obesity-induced fatty liver diseases
    • Mantena, S. K., King, A. L., Andringa, K. K., Eccleston, H. B., Bailey, S. M., Mitochondrial dysfunction and oxidative stress in the pathogenesis of alcohol- and obesity-induced fatty liver diseases. Free Radic. Biol. Med. 2008, 44, 1259-1272.
    • (2008) Free Radic. Biol. Med. , vol.44 , pp. 1259-1272
    • Mantena, S.K.1    King, A.L.2    Andringa, K.K.3    Eccleston, H.B.4    Bailey, S.M.5
  • 54
    • 0033735497 scopus 로고    scopus 로고
    • Amount of dietary fat and type of soluble fiber independently modulate postabsorptive conversion of β-carotene to vitamin A in mongolian gerbils
    • Deming, D. M., Boileau, A. C., Lee, C. M., Erdman, J. W., Jr., Amount of dietary fat and type of soluble fiber independently modulate postabsorptive conversion of β-carotene to vitamin A in mongolian gerbils. J. Nutr. 2000, 130, 2789-2796.
    • (2000) J. Nutr. , vol.130 , pp. 2789-2796
    • Deming, D.M.1    Boileau, A.C.2    Lee, C.M.3    Erdman Jr., J.W.4
  • 55
    • 0029793657 scopus 로고    scopus 로고
    • The effects of dietary taurocholate, fat, protein, and carbohydrate on the distribution and fate of dietary β-carotene in ferrets
    • Lakshman, M. R., Liu, Q. H., Sapp, R., Somanchi, M., Sundaresan, P. R., The effects of dietary taurocholate, fat, protein, and carbohydrate on the distribution and fate of dietary β-carotene in ferrets. Nutr. Cancer 1996, 26, 49-61.
    • (1996) Nutr. Cancer , vol.26 , pp. 49-61
    • Lakshman, M.R.1    Liu, Q.H.2    Sapp, R.3    Somanchi, M.4    Sundaresan, P.R.5
  • 56
    • 0031685583 scopus 로고    scopus 로고
    • β-Carotene 15,15′-dioxygenase activity and cellular retinol-binding protein type ll level are enhanced by dietary unsaturated triacylglycerols in rat intestines
    • During, A., Nagao, A., Terao, J., β-Carotene 15, 15′-dioxygenase activity and cellular retinol-binding protein type ll level are enhanced by dietary unsaturated triacylglycerols in rat intestines. J. Nutr. 1998, 128, 1614-1619.
    • (1998) J. Nutr. , vol.128 , pp. 1614-1619
    • During, A.1    Nagao, A.2    Terao, J.3
  • 57
    • 24744446431 scopus 로고    scopus 로고
    • Effects of dietary protein, fat and β-carotene levels on β-carotene absorption in rats
    • Hosotani, K., Kitagawa, M., Effects of dietary protein, fat and β-carotene levels on β-carotene absorption in rats. Int. J. Vitamin Nutr. Res. 2005, 75, 274-280.
    • (2005) Int. J. Vitamin Nutr. Res. , vol.75 , pp. 274-280
    • Hosotani, K.1    Kitagawa, M.2
  • 58
    • 0038265390 scopus 로고    scopus 로고
    • Identification of β-carotene 15,15′-monooxygenase as a peroxisome proliferator-activated receptor target gene
    • Boulanger, A., McLemore, P., Copeland, N. G., Gilbert, D. J. et al., Identification of β-carotene 15, 15′-monooxygenase as a peroxisome proliferator-activated receptor target gene. FASEB J. 2003, 17, 1304-1306.
    • (2003) FASEB J. , vol.17 , pp. 1304-1306
    • Boulanger, A.1    McLemore, P.2    Copeland, N.G.3    Gilbert, D.J.4
  • 59
    • 33746939839 scopus 로고    scopus 로고
    • Cooperation between MEF2 and PPARgamma in human intestinal β,β-carotene 15,15′-monooxygenase gene expression
    • Gong, X., Tsai, S. W., Yan, B., Rubin, L. P., Cooperation between MEF2 and PPARgamma in human intestinal β, β-carotene 15, 15′-monooxygenase gene expression. BMC Mol. Biol. 2006, 7, 7.
    • (2006) BMC Mol. Biol. , vol.7 , pp. 7
    • Gong, X.1    Tsai, S.W.2    Yan, B.3    Rubin, L.P.4
  • 60
    • 78649564234 scopus 로고    scopus 로고
    • Loss of carotene-9′,10′-monooxygenase expression increases serum and tissue lycopene concentrations in lycopene-fed mice
    • Ford, N. A., Clinton, S. K., von Lintig, J., Wyss, A., Erdman, J. W., Jr., Loss of carotene-9′, 10′-monooxygenase expression increases serum and tissue lycopene concentrations in lycopene-fed mice. J. Nutr. 2010, 140, 2134-2138.
    • (2010) J. Nutr. , vol.140 , pp. 2134-2138
    • Ford, N.A.1    Clinton, S.K.2    von Lintig, J.3    Wyss, A.4    Erdman Jr., J.W.5
  • 61
    • 77958143518 scopus 로고    scopus 로고
    • Chronic alcohol intake upregulates hepatic expression of carotenoid cleavage enzymes and PPAR in rats
    • Luvizotto, R. A., Nascimento, A. F., Veeramachaneni, S., Liu, C., Wang, X. D., Chronic alcohol intake upregulates hepatic expression of carotenoid cleavage enzymes and PPAR in rats. J. Nutr. 2010, 140, 1808-1814.
    • (2010) J. Nutr. , vol.140 , pp. 1808-1814
    • Luvizotto, R.A.1    Nascimento, A.F.2    Veeramachaneni, S.3    Liu, C.4    Wang, X.D.5
  • 62
    • 41949107029 scopus 로고    scopus 로고
    • Isx participates in the maintenance of vitamin A metabolism by regulation of β-carotene 15,15′-monooxygenase (Bcmo1) expression
    • Seino, Y., Miki, T., Kiyonari, H., Abe, T. et al., Isx participates in the maintenance of vitamin A metabolism by regulation of β-carotene 15, 15′-monooxygenase (Bcmo1) expression. J. Biol. Chem. 2008, 283, 4905-4911.
    • (2008) J. Biol. Chem. , vol.283 , pp. 4905-4911
    • Seino, Y.1    Miki, T.2    Kiyonari, H.3    Abe, T.4
  • 63
    • 77953516537 scopus 로고    scopus 로고
    • ISX is a retinoic acid-sensitive gatekeeper that controls intestinal β,β-carotene absorption and vitamin A production
    • Lobo, G. P., Hessel, S., Eichinger, A., Noy, N. et al., ISX is a retinoic acid-sensitive gatekeeper that controls intestinal β, β-carotene absorption and vitamin A production. FASEB J. 2010.
    • (2010) FASEB J.
    • Lobo, G.P.1    Hessel, S.2    Eichinger, A.3    Noy, N.4
  • 64
    • 0033859722 scopus 로고    scopus 로고
    • Intestinal β-carotene 15,15′-dioxygenase activity is markedly enhanced in copper-deficient rats fed on high-iron diets and fructose
    • During, A., Fields, M., Lewis, C. G., Smith, J. C., Intestinal β-carotene 15, 15′-dioxygenase activity is markedly enhanced in copper-deficient rats fed on high-iron diets and fructose. Br. J. Nutr. 2000, 84, 117-124.
    • (2000) Br. J. Nutr. , vol.84 , pp. 117-124
    • During, A.1    Fields, M.2    Lewis, C.G.3    Smith, J.C.4
  • 65
    • 0029813806 scopus 로고    scopus 로고
    • Absorption of β-carotene and other carotenoids in humans and animal models
    • van Vliet, T., Absorption of β-carotene and other carotenoids in humans and animal models. Eur. J. Clin. Nutr. 1996, 50, S32-S37.
    • (1996) Eur. J. Clin. Nutr. , vol.50
    • van Vliet, T.1
  • 66
    • 23744447355 scopus 로고    scopus 로고
    • Rpe65 is the retinoid isomerase in bovine retinal pigment epithelium
    • Jin, M., Li, S., Moghrabi, W. N., Sun, H., Travis, G. H., Rpe65 is the retinoid isomerase in bovine retinal pigment epithelium. Cell 2005, 122, 449-459.
    • (2005) Cell , vol.122 , pp. 449-459
    • Jin, M.1    Li, S.2    Moghrabi, W.N.3    Sun, H.4    Travis, G.H.5
  • 68
    • 26444596185 scopus 로고    scopus 로고
    • Mutation of key residues of RPE65 abolishes its enzymatic role as isomerohydrolase in the visual cycle
    • Redmond, T. M., Poliakov, E., Yu, S., Tsai, J. Y. et al., Mutation of key residues of RPE65 abolishes its enzymatic role as isomerohydrolase in the visual cycle. Proc. Natl. Acad. Sci. USA 2005, 102, 13658-13663.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 13658-13663
    • Redmond, T.M.1    Poliakov, E.2    Yu, S.3    Tsai, J.Y.4
  • 69
    • 25844464185 scopus 로고    scopus 로고
    • Identification of conserved histidines and glutamic acid as key residues for isomerohydrolase activity of RPE65, an enzyme of the visual cycle in the retinal pigment epithelium
    • Takahashi, Y., Moiseyev, G., Chen, Y., Ma, J. X., Identification of conserved histidines and glutamic acid as key residues for isomerohydrolase activity of RPE65, an enzyme of the visual cycle in the retinal pigment epithelium. FEBS Lett. 2005, 579, 5414-5418.
    • (2005) FEBS Lett. , vol.579 , pp. 5414-5418
    • Takahashi, Y.1    Moiseyev, G.2    Chen, Y.3    Ma, J.X.4
  • 70
    • 0042285478 scopus 로고    scopus 로고
    • Genetic defects in vitamin A metabolism of the retinal pigment epithelium
    • Thompson, D. A., Gal, A., Genetic defects in vitamin A metabolism of the retinal pigment epithelium. Dev. Ophthalmol. 2003, 37, 141-154.
    • (2003) Dev. Ophthalmol. , vol.37 , pp. 141-154
    • Thompson, D.A.1    Gal, A.2
  • 71
    • 35848948610 scopus 로고    scopus 로고
    • Loss-of-function mutation in carotenoid 15,15′-monooxygenase identified in a patient with hypercarotenemia and hypovitaminosis A
    • Lindqvist, A., Sharvill, J., Sharvill, D. E., Andersson, S., Loss-of-function mutation in carotenoid 15, 15′-monooxygenase identified in a patient with hypercarotenemia and hypovitaminosis A. J. Nutr. 2007, 137, 2346-2350.
    • (2007) J. Nutr. , vol.137 , pp. 2346-2350
    • Lindqvist, A.1    Sharvill, J.2    Sharvill, D.E.3    Andersson, S.4
  • 72
    • 77950890497 scopus 로고    scopus 로고
    • Genome-wide association study identifies variants at the IL18-BCO2 locus associated with interleukin-18 levels
    • He, M., Cornelis, M. C., Kraft, P., van Dam, R. M. et al., Genome-wide association study identifies variants at the IL18-BCO2 locus associated with interleukin-18 levels. Arterioscler. Thromb. Vasc. Biol. 2010, 30, 885-890.
    • (2010) Arterioscler. Thromb. Vasc. Biol. , vol.30 , pp. 885-890
    • He, M.1    Cornelis, M.C.2    Kraft, P.3    van Dam, R.M.4
  • 73
    • 70349318148 scopus 로고    scopus 로고
    • Mutation in bovine β-carotene oxygenase 2 affects milk color
    • Berry, S. D., Davis, S. R., Beattie, E. M., Thomas, N. L. et al., Mutation in bovine β-carotene oxygenase 2 affects milk color. Genetics 2009, 182, 923-926.
    • (2009) Genetics , vol.182 , pp. 923-926
    • Berry, S.D.1    Davis, S.R.2    Beattie, E.M.3    Thomas, N.L.4
  • 74
    • 77952068017 scopus 로고    scopus 로고
    • Genetic variation in the β, β-carotene-9′,10′-dioxygenase gene and association with fat colour in bovine adipose tissue and milk
    • Tian, R., Pitchford, W. S., Morris, C. A., Cullen, N. G., Bottema, C. D., Genetic variation in the β, β-carotene-9′, 10′-dioxygenase gene and association with fat colour in bovine adipose tissue and milk. Anim. Genet. 2010, 41, 253-259.
    • (2010) Anim. Genet. , vol.41 , pp. 253-259
    • Tian, R.1    Pitchford, W.S.2    Morris, C.A.3    Cullen, N.G.4    Bottema, C.D.5
  • 75
    • 77649110092 scopus 로고    scopus 로고
    • A nonsense mutation in the β-carotene oxygenase 2 (BCO2) gene is tightly associated with accumulation of carotenoids in adipose tissue in sheep (Ovis aries)
    • Vage, D. I., Boman, I. A., A nonsense mutation in the β-carotene oxygenase 2 (BCO2) gene is tightly associated with accumulation of carotenoids in adipose tissue in sheep (Ovis aries). BMC Genet. 2010, 11, 10.
    • (2010) BMC Genet. , vol.11 , pp. 10
    • Vage, D.I.1    Boman, I.A.2
  • 76
    • 40149109370 scopus 로고    scopus 로고
    • Identification of the yellow skin gene reveals a hybrid origin of the domestic chicken
    • Eriksson, J., Larson, G., Gunnarsson, U., Bed'Hom, B. et al., Identification of the yellow skin gene reveals a hybrid origin of the domestic chicken. PLoS Genet. 2008, 4, e1000010.
    • (2008) PLoS Genet. , vol.4
    • Eriksson, J.1    Larson, G.2    Gunnarsson, U.3    Bed'Hom, B.4
  • 77
    • 84858302897 scopus 로고    scopus 로고
    • Do single nucleotide polymorphisms in β-carotene dioxygenase-2 (BCDO2) gene affect the postprandial response?
    • Tourniaire, F., Minihane, A. M., Hesketh, J., Lietz, G., Do single nucleotide polymorphisms in β-carotene dioxygenase-2 (BCDO2) gene affect the postprandial response? Proc. Nutr. Soc. 2008, 67, E187.
    • (2008) Proc. Nutr. Soc. , vol.67
    • Tourniaire, F.1    Minihane, A.M.2    Hesketh, J.3    Lietz, G.4
  • 78
    • 8744286799 scopus 로고    scopus 로고
    • The biochemical characterization of two carotenoid cleavage enzymes from Arabidopsis indicates that a carotenoid-derived compound inhibits lateral branching
    • Schwartz, S. H., Qin, X., Loewen, M. C., The biochemical characterization of two carotenoid cleavage enzymes from Arabidopsis indicates that a carotenoid-derived compound inhibits lateral branching. J. Biol. Chem. 2004, 279, 46940-46945.
    • (2004) J. Biol. Chem. , vol.279 , pp. 46940-46945
    • Schwartz, S.H.1    Qin, X.2    Loewen, M.C.3
  • 79
    • 0035868276 scopus 로고    scopus 로고
    • Expression pattern and localization of β,β-carotene 15,15′-dioxygenase in different tissues
    • Wyss, A., Wirtz, G. M., Woggon, W. D., Brugger, R. et al., Expression pattern and localization of β, β-carotene 15, 15′-dioxygenase in different tissues. Biochem. J. 2001, 354, 521-529.
    • (2001) Biochem. J. , vol.354 , pp. 521-529
    • Wyss, A.1    Wirtz, G.M.2    Woggon, W.D.3    Brugger, R.4
  • 80
    • 34547338564 scopus 로고    scopus 로고
    • Differences in expression and activity of β,β′-carotene-15,15′-oxygenase in liver and duodenum of cattle with yellow or white fat
    • Morales, A., Gonzalez, A., Varela-Echavarria, A., Shimada, A., Mora, O., Differences in expression and activity of β, β′-carotene-15, 15′-oxygenase in liver and duodenum of cattle with yellow or white fat. J. Anim. Physiol. Anim. Nutr. 2007, 91, 341-346.
    • (2007) J. Anim. Physiol. Anim. Nutr. , vol.91 , pp. 341-346
    • Morales, A.1    Gonzalez, A.2    Varela-Echavarria, A.3    Shimada, A.4    Mora, O.5
  • 81
    • 0035280250 scopus 로고    scopus 로고
    • Cloning and characterization of a human β,β-carotene-15,15′-dioxygenase that is highly expressed in the retinal pigment epithelium
    • Yan, W., Jang, G. F., Haeseleer, F., Esumi, N. et al., Cloning and characterization of a human β, β-carotene-15, 15′-dioxygenase that is highly expressed in the retinal pigment epithelium. Genomics 2001, 72, 193-202.
    • (2001) Genomics , vol.72 , pp. 193-202
    • Yan, W.1    Jang, G.F.2    Haeseleer, F.3    Esumi, N.4
  • 82
    • 34648826614 scopus 로고    scopus 로고
    • Effective production of retinal from β-carotene using recombinant mouse β-carotene 15,15′-monooxygenase
    • Kim, Y. S., Kim, N. H., Kim, H. J., Lee, J. K. et al., Effective production of retinal from β-carotene using recombinant mouse β-carotene 15, 15′-monooxygenase. Appl. Microbiol. Biotechnol. 2007, 76, 1339-1345.
    • (2007) Appl. Microbiol. Biotechnol. , vol.76 , pp. 1339-1345
    • Kim, Y.S.1    Kim, N.H.2    Kim, H.J.3    Lee, J.K.4
  • 83
    • 0024326945 scopus 로고
    • Enzymatic conversion of all-trans-β-carotene to retinal by a cytosolic enzyme from rabbit and rat intestinal mucosa
    • Lakshman, M. R., Mychkovsky, I., Attlesey, M., Enzymatic conversion of all-trans-β-carotene to retinal by a cytosolic enzyme from rabbit and rat intestinal mucosa. Proc. Natl. Acad. Sci. USA 1989, 86, 9124-9128.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 9124-9128
    • Lakshman, M.R.1    Mychkovsky, I.2    Attlesey, M.3
  • 84
    • 0015480054 scopus 로고
    • Purification and properties of carotene 15,15′-dioxygenase of rabbit intestine
    • Lakshmanan, M. R., Chansang, H., Olson, J. A., Purification and properties of carotene 15, 15′-dioxygenase of rabbit intestine. J. Lipid Res. 1972, 13, 477-482.
    • (1972) J. Lipid Res. , vol.13 , pp. 477-482
    • Lakshmanan, M.R.1    Chansang, H.2    Olson, J.A.3
  • 85
    • 0001507926 scopus 로고
    • The enzymatic conversion of all-trans β-carotene into retinal
    • Goodman, D. S., Huang, H. S., Kanai, M., Shiratori, T., The enzymatic conversion of all-trans β-carotene into retinal. J. Biol. Chem. 1967, 242, 3543-3554.
    • (1967) J. Biol. Chem. , vol.242 , pp. 3543-3554
    • Goodman, D.S.1    Huang, H.S.2    Kanai, M.3    Shiratori, T.4
  • 86
    • 0031574272 scopus 로고    scopus 로고
    • In vitro and in vivo inhibition of β-carotene dioxygenase activity by canthaxanthin in rat intestine
    • Grolier, P., Duszka, C., Borel, P., AlexandreGouabau, M. C., AzaisBraesco, V., In vitro and in vivo inhibition of β-carotene dioxygenase activity by canthaxanthin in rat intestine. Arch. Biochem. Biophys. 1997, 348, 233-238.
    • (1997) Arch. Biochem. Biophys. , vol.348 , pp. 233-238
    • Grolier, P.1    Duszka, C.2    Borel, P.3    AlexandreGouabau, M.C.4    AzaisBraesco, V.5
  • 87
    • 57349182281 scopus 로고    scopus 로고
    • Lycopene biodistribution is altered in 15,15′-carotenoid monooxygenase knockout mice
    • Lindshield, B. L., King, J. L., Wyss, A., Goralczyk, R. et al., Lycopene biodistribution is altered in 15, 15′-carotenoid monooxygenase knockout mice. J. Nutr. 2008, 138, 2367-2371.
    • (2008) J. Nutr. , vol.138 , pp. 2367-2371
    • Lindshield, B.L.1    King, J.L.2    Wyss, A.3    Goralczyk, R.4


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