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Volumn 132, Issue , 2017, Pages 143-149

Oxidative metabolism of curcumin-glucuronide by peroxidases and isolated human leukocytes

Author keywords

Autoxidation; Bicyclopentadione; Curcumin; Glucuronide; Myeloperoxidase; Peroxidase

Indexed keywords

CURCUMIN; GLUCURONIDE; HORSERADISH PEROXIDASE; PEROXIDASE;

EID: 85014780846     PISSN: 00062952     EISSN: 18732968     Source Type: Journal    
DOI: 10.1016/j.bcp.2017.03.002     Document Type: Article
Times cited : (25)

References (48)
  • 1
    • 0032926620 scopus 로고    scopus 로고
    • Biotransformation of curcumin through reduction and glucuronidation in mice
    • [1] Pan, M.H., Huang, T.M., Lin, J.K., Biotransformation of curcumin through reduction and glucuronidation in mice. Drug Metab. Dispos. 27 (1999), 486–494.
    • (1999) Drug Metab. Dispos. , vol.27 , pp. 486-494
    • Pan, M.H.1    Huang, T.M.2    Lin, J.K.3
  • 2
    • 34548065533 scopus 로고    scopus 로고
    • Glucuronidation of curcuminoids by human microsomal and recombinant UDP-glucuronosyltransferases
    • [2] Hoehle, S.I., Pfeiffer, E., Metzler, M., Glucuronidation of curcuminoids by human microsomal and recombinant UDP-glucuronosyltransferases. Mol. Nutr. Food Res. 51 (2007), 932–938.
    • (2007) Mol. Nutr. Food Res. , vol.51 , pp. 932-938
    • Hoehle, S.I.1    Pfeiffer, E.2    Metzler, M.3
  • 3
    • 0018222291 scopus 로고
    • The metabolism and excretion of curcumin (1,7-bis-(4-hydroxy-3-methoxyphenyl)-1,6-heptadiene-3,5-dione) in the rat
    • [3] Holder, G.M., Plummer, J.L., Ryan, A.J., The metabolism and excretion of curcumin (1,7-bis-(4-hydroxy-3-methoxyphenyl)-1,6-heptadiene-3,5-dione) in the rat. Xenobiotica 8 (1978), 761–768.
    • (1978) Xenobiotica , vol.8 , pp. 761-768
    • Holder, G.M.1    Plummer, J.L.2    Ryan, A.J.3
  • 7
    • 4544236324 scopus 로고    scopus 로고
    • Modulation of arachidonic acid metabolism by curcumin and related beta-diketone derivatives: effects on cytosolic phospholipase A(2), cyclooxygenases and 5-lipoxygenase
    • [7] Hong, J., Bose, M., Ju, J., Ryu, J.H., Chen, X., Sang, S., Lee, M.J., Yang, C.S., Modulation of arachidonic acid metabolism by curcumin and related beta-diketone derivatives: effects on cytosolic phospholipase A(2), cyclooxygenases and 5-lipoxygenase. Carcinogenesis 25 (2004), 1671–1679.
    • (2004) Carcinogenesis , vol.25 , pp. 1671-1679
    • Hong, J.1    Bose, M.2    Ju, J.3    Ryu, J.H.4    Chen, X.5    Sang, S.6    Lee, M.J.7    Yang, C.S.8
  • 8
    • 34247646955 scopus 로고    scopus 로고
    • Inhibition of human recombinant cytochrome P450s by curcumin and curcumin decomposition products
    • [8] Appiah-Opong, R., Commandeur, J.N., van Vugt-Lussenburg, B., Vermeulen, N.P., Inhibition of human recombinant cytochrome P450s by curcumin and curcumin decomposition products. Toxicology 235 (2007), 83–91.
    • (2007) Toxicology , vol.235 , pp. 83-91
    • Appiah-Opong, R.1    Commandeur, J.N.2    van Vugt-Lussenburg, B.3    Vermeulen, N.P.4
  • 9
    • 84858072552 scopus 로고    scopus 로고
    • The pharmacology of curcumin: is it the degradation products?
    • [9] Shen, L., Ji, H.F., The pharmacology of curcumin: is it the degradation products?. Trends Mol. Med. 18 (2012), 138–144.
    • (2012) Trends Mol. Med. , vol.18 , pp. 138-144
    • Shen, L.1    Ji, H.F.2
  • 10
    • 78651401023 scopus 로고    scopus 로고
    • Autoxidative and cyclooxygenase-2 catalyzed transformation of the dietary chemopreventive agent curcumin
    • [10] Griesser, M., Pistis, V., Suzuki, T., Tejera, N., Pratt, D.A., Schneider, C., Autoxidative and cyclooxygenase-2 catalyzed transformation of the dietary chemopreventive agent curcumin. J. Biol. Chem. 286 (2011), 1114–1124.
    • (2011) J. Biol. Chem. , vol.286 , pp. 1114-1124
    • Griesser, M.1    Pistis, V.2    Suzuki, T.3    Tejera, N.4    Pratt, D.A.5    Schneider, C.6
  • 11
    • 84863090612 scopus 로고    scopus 로고
    • Vanillin and ferulic acid: not the major degradation products of curcumin
    • author reply 363–364
    • [11] Gordon, O.N., Schneider, C., Vanillin and ferulic acid: not the major degradation products of curcumin. Trends Mol. Med. 18 (2012), 361–363 author reply 363–364.
    • (2012) Trends Mol. Med. , vol.18 , pp. 361-363
    • Gordon, O.N.1    Schneider, C.2
  • 12
    • 84872119769 scopus 로고    scopus 로고
    • Oxidative metabolites of curcumin poison human type II topoisomerases
    • [12] Ketron, A.C., Gordon, O.N., Schneider, C., Osheroff, N., Oxidative metabolites of curcumin poison human type II topoisomerases. Biochemistry 52 (2013), 221–227.
    • (2013) Biochemistry , vol.52 , pp. 221-227
    • Ketron, A.C.1    Gordon, O.N.2    Schneider, C.3    Osheroff, N.4
  • 14
    • 84890100019 scopus 로고    scopus 로고
    • Comparison of the effects of curcumin and curcumin glucuronide in human hepatocellular carcinoma HepG2 cells
    • [14] Shoji, M., Nakagawa, K., Watanabe, A., Tsuduki, T., Yamada, T., Kuwahara, S., Kimura, F., Miyazawa, T., Comparison of the effects of curcumin and curcumin glucuronide in human hepatocellular carcinoma HepG2 cells. Food Chem. 151 (2014), 126–132.
    • (2014) Food Chem. , vol.151 , pp. 126-132
    • Shoji, M.1    Nakagawa, K.2    Watanabe, A.3    Tsuduki, T.4    Yamada, T.5    Kuwahara, S.6    Kimura, F.7    Miyazawa, T.8
  • 15
    • 0035114277 scopus 로고    scopus 로고
    • Characterization of metabolites of the chemopreventive agent curcumin in human and rat hepatocytes and in the rat in vivo, and evaluation of their ability to inhibit phorbol ester-induced prostaglandin E2 production
    • [15] Ireson, C., Orr, S., Jones, D.J., Verschoyle, R., Lim, C.K., Luo, J.L., Howells, L., Plummer, S., Jukes, R., Williams, M., Steward, W.P., Gescher, A., Characterization of metabolites of the chemopreventive agent curcumin in human and rat hepatocytes and in the rat in vivo, and evaluation of their ability to inhibit phorbol ester-induced prostaglandin E2 production. Cancer Res. 61 (2001), 1058–1064.
    • (2001) Cancer Res. , vol.61 , pp. 1058-1064
    • Ireson, C.1    Orr, S.2    Jones, D.J.3    Verschoyle, R.4    Lim, C.K.5    Luo, J.L.6    Howells, L.7    Plummer, S.8    Jukes, R.9    Williams, M.10    Steward, W.P.11    Gescher, A.12
  • 16
    • 82955170666 scopus 로고    scopus 로고
    • Tetrahydrocurcumin is more effective than curcumin in preventing azoxymethane-induced colon carcinogenesis
    • [16] Lai, C.S., Wu, J.C., Yu, S.F., Badmaev, V., Nagabhushanam, K., Ho, C.T., Pan, M.H., Tetrahydrocurcumin is more effective than curcumin in preventing azoxymethane-induced colon carcinogenesis. Mol. Nutr. Food Res. 55 (2011), 1819–1828.
    • (2011) Mol. Nutr. Food Res. , vol.55 , pp. 1819-1828
    • Lai, C.S.1    Wu, J.C.2    Yu, S.F.3    Badmaev, V.4    Nagabhushanam, K.5    Ho, C.T.6    Pan, M.H.7
  • 17
    • 80155194987 scopus 로고    scopus 로고
    • Tetrahydrocurcumin, a major metabolite of curcumin, induced autophagic cell death through coordinative modulation of PI3K/Akt-mTOR and MAPK signaling pathways in human leukemia HL-60 cells
    • [17] Wu, J.C., Lai, C.S., Badmaev, V., Nagabhushanam, K., Ho, C.T., Pan, M.H., Tetrahydrocurcumin, a major metabolite of curcumin, induced autophagic cell death through coordinative modulation of PI3K/Akt-mTOR and MAPK signaling pathways in human leukemia HL-60 cells. Mol. Nutr. Food Res. 55 (2011), 1646–1654.
    • (2011) Mol. Nutr. Food Res. , vol.55 , pp. 1646-1654
    • Wu, J.C.1    Lai, C.S.2    Badmaev, V.3    Nagabhushanam, K.4    Ho, C.T.5    Pan, M.H.6
  • 18
    • 84859722015 scopus 로고    scopus 로고
    • Tetrahydrocurcumin ameliorates homocysteinylated cytochrome-c mediated autophagy in hyperhomocysteinemia mice after cerebral ischemia
    • [18] Tyagi, N., Qipshidze, N., Munjal, C., Vacek, J.C., Metreveli, N., Givvimani, S., Tyagi, S.C., Tetrahydrocurcumin ameliorates homocysteinylated cytochrome-c mediated autophagy in hyperhomocysteinemia mice after cerebral ischemia. J. Mol. Neurosci. 47 (2012), 128–138.
    • (2012) J. Mol. Neurosci. , vol.47 , pp. 128-138
    • Tyagi, N.1    Qipshidze, N.2    Munjal, C.3    Vacek, J.C.4    Metreveli, N.5    Givvimani, S.6    Tyagi, S.C.7
  • 19
    • 72549092899 scopus 로고    scopus 로고
    • Contribution of degradation products to the anticancer activity of curcumin
    • [19] Shen, L., Ji, H.-F., Contribution of degradation products to the anticancer activity of curcumin. Clin. Cancer Res., 15, 2009, 7108.
    • (2009) Clin. Cancer Res. , vol.15 , pp. 7108
    • Shen, L.1    Ji, H.-F.2
  • 20
    • 0030839940 scopus 로고    scopus 로고
    • Stability of curcumin in buffer solutions and characterization of its degradation products
    • [20] Wang, Y.J., Pan, M.H., Cheng, A.L., Lin, L.I., Ho, Y.S., Hsieh, C.Y., Lin, J.K., Stability of curcumin in buffer solutions and characterization of its degradation products. J. Pharm. Biomed. Anal. 15 (1997), 1867–1876.
    • (1997) J. Pharm. Biomed. Anal. , vol.15 , pp. 1867-1876
    • Wang, Y.J.1    Pan, M.H.2    Cheng, A.L.3    Lin, L.I.4    Ho, Y.S.5    Hsieh, C.Y.6    Lin, J.K.7
  • 21
    • 84929096317 scopus 로고    scopus 로고
    • Unraveling curcumin degradation. Autoxidation proceeds through spiroepoxide and vinylether intermediates en route to the main bicyclopentadione
    • [21] Gordon, O.N., Luis, P.B., Sintim, H.O., Schneider, C., Unraveling curcumin degradation. Autoxidation proceeds through spiroepoxide and vinylether intermediates en route to the main bicyclopentadione. J. Biol. Chem. 290 (2015), 4817–4828.
    • (2015) J. Biol. Chem. , vol.290 , pp. 4817-4828
    • Gordon, O.N.1    Luis, P.B.2    Sintim, H.O.3    Schneider, C.4
  • 22
    • 84940999062 scopus 로고    scopus 로고
    • Degradation of curcumin: from mechanism to biological implications
    • [22] Schneider, C., Gordon, O.N., Edwards, R.L., Luis, P.B., Degradation of curcumin: from mechanism to biological implications. J. Agric. Food Chem. 63 (2015), 7606–7614.
    • (2015) J. Agric. Food Chem. , vol.63 , pp. 7606-7614
    • Schneider, C.1    Gordon, O.N.2    Edwards, R.L.3    Luis, P.B.4
  • 23
    • 84982364659 scopus 로고
    • A synthesis of curcumin and related compounds
    • [23] Pabon, H.J.J., A synthesis of curcumin and related compounds. Recl. Trav. Chim. Pays-Bas 83 (1964), 379–386.
    • (1964) Recl. Trav. Chim. Pays-Bas , vol.83 , pp. 379-386
    • Pabon, H.J.J.1
  • 24
    • 84890560570 scopus 로고    scopus 로고
    • Facile synthesis of deuterated and [(14) C]labeled analogs of vanillin and curcumin for use as mechanistic and analytical tools
    • [24] Gordon, O.N., Graham, L.A., Schneider, C., Facile synthesis of deuterated and [(14) C]labeled analogs of vanillin and curcumin for use as mechanistic and analytical tools. J. Labelled Comp. Radiopharm. 56 (2013), 696–699.
    • (2013) J. Labelled Comp. Radiopharm. , vol.56 , pp. 696-699
    • Gordon, O.N.1    Graham, L.A.2    Schneider, C.3
  • 25
    • 0035370769 scopus 로고    scopus 로고
    • Identification of quercetin 3-O-beta-D-glucuronide as an antioxidative metabolite in rat plasma after oral administration of quercetin
    • [25] Moon, J.H., Tsushida, T., Nakahara, K., Terao, J., Identification of quercetin 3-O-beta-D-glucuronide as an antioxidative metabolite in rat plasma after oral administration of quercetin. Free Radic. Biol. Med. 30 (2001), 1274–1285.
    • (2001) Free Radic. Biol. Med. , vol.30 , pp. 1274-1285
    • Moon, J.H.1    Tsushida, T.2    Nakahara, K.3    Terao, J.4
  • 26
  • 28
    • 0024297764 scopus 로고
    • Mechanism-based inactivation of horseradish-peroxidase by sodium-azide – formation of meso-azidoprotoporphyrin-IX
    • [28] Ortiz de Montellano, P.R., David, S.K., Ator, M.A., Tew, D., Mechanism-based inactivation of horseradish-peroxidase by sodium-azide – formation of meso-azidoprotoporphyrin-IX. Biochemistry 27 (1988), 5470–5476.
    • (1988) Biochemistry , vol.27 , pp. 5470-5476
    • Ortiz de Montellano, P.R.1    David, S.K.2    Ator, M.A.3    Tew, D.4
  • 29
    • 4344694589 scopus 로고    scopus 로고
    • Abnormal solvent effects on hydrogen atom abstraction. 2. Resolution of the curcumin antioxidant controversy. The role of sequential proton loss electron transfer
    • [29] Litwinienko, G., Ingold, K.U., Abnormal solvent effects on hydrogen atom abstraction. 2. Resolution of the curcumin antioxidant controversy. The role of sequential proton loss electron transfer. J. Org. Chem. 69 (2004), 5888–5896.
    • (2004) J. Org. Chem. , vol.69 , pp. 5888-5896
    • Litwinienko, G.1    Ingold, K.U.2
  • 30
    • 34247143185 scopus 로고    scopus 로고
    • Solvent effects on the rates and mechanisms of reaction of phenols with free radicals
    • [30] Litwinienko, G., Ingold, K.U., Solvent effects on the rates and mechanisms of reaction of phenols with free radicals. Acc. Chem. Res. 40 (2007), 222–230.
    • (2007) Acc. Chem. Res. , vol.40 , pp. 222-230
    • Litwinienko, G.1    Ingold, K.U.2
  • 31
    • 84929590403 scopus 로고    scopus 로고
    • Oxidative transformation of demethoxy- and bisdemethoxycurcumin: products, mechanism of formation, and poisoning of human topoisomerase IIalpha
    • [31] Gordon, O.N., Luis, P.B., Ashley, R.E., Osheroff, N., Schneider, C., Oxidative transformation of demethoxy- and bisdemethoxycurcumin: products, mechanism of formation, and poisoning of human topoisomerase IIalpha. Chem. Res. Toxicol. 28 (2015), 989–996.
    • (2015) Chem. Res. Toxicol. , vol.28 , pp. 989-996
    • Gordon, O.N.1    Luis, P.B.2    Ashley, R.E.3    Osheroff, N.4    Schneider, C.5
  • 32
    • 84989685027 scopus 로고
    • Enzymatic generation of triplet biacetyl
    • [32] Soares, C.H.L., Bechara, E.J.H., Enzymatic generation of triplet biacetyl. Photochem. Photobiol. 36 (1982), 117–119.
    • (1982) Photochem. Photobiol. , vol.36 , pp. 117-119
    • Soares, C.H.L.1    Bechara, E.J.H.2
  • 33
    • 0032902307 scopus 로고    scopus 로고
    • Chemical studies on antioxidant mechanism of curcuminoid: analysis of radical reaction products from curcumin
    • [33] Masuda, T., Hidaka, K., Shinohara, A., Maekawa, T., Takeda, Y., Yamaguchi, H., Chemical studies on antioxidant mechanism of curcuminoid: analysis of radical reaction products from curcumin. J. Agric. Food Chem. 47 (1999), 71–77.
    • (1999) J. Agric. Food Chem. , vol.47 , pp. 71-77
    • Masuda, T.1    Hidaka, K.2    Shinohara, A.3    Maekawa, T.4    Takeda, Y.5    Yamaguchi, H.6
  • 34
    • 84928639308 scopus 로고    scopus 로고
    • A three-enzyme-system to degrade curcumin to natural vanillin
    • [34] Esparan, V., Krings, U., Struch, M., Berger, R.G., A three-enzyme-system to degrade curcumin to natural vanillin. Molecules 20 (2015), 6640–6653.
    • (2015) Molecules , vol.20 , pp. 6640-6653
    • Esparan, V.1    Krings, U.2    Struch, M.3    Berger, R.G.4
  • 35
    • 18244390487 scopus 로고    scopus 로고
    • Myeloperoxidase: friend and foe
    • [35] Klebanoff, S.J., Myeloperoxidase: friend and foe. J. Leukoc. Biol. 77 (2005), 598–625.
    • (2005) J. Leukoc. Biol. , vol.77 , pp. 598-625
    • Klebanoff, S.J.1
  • 37
    • 84899416857 scopus 로고    scopus 로고
    • Involvement of myeloperoxidase and NADPH oxidase in the covalent binding of amodiaquine and clozapine to neutrophils: implications for drug-induced agranulocytosis
    • [37] Lobach, A.R., Uetrecht, J., Involvement of myeloperoxidase and NADPH oxidase in the covalent binding of amodiaquine and clozapine to neutrophils: implications for drug-induced agranulocytosis. Chem. Res. Toxicol. 27 (2014), 699–709.
    • (2014) Chem. Res. Toxicol. , vol.27 , pp. 699-709
    • Lobach, A.R.1    Uetrecht, J.2
  • 38
    • 43049173503 scopus 로고    scopus 로고
    • Mammalian heme peroxidases: from molecular mechanisms to health implications
    • [38] Davies, M.J., Hawkins, C.L., Pattison, D.I., Rees, M.D., Mammalian heme peroxidases: from molecular mechanisms to health implications. Antioxid. Redox Signal. 10 (2008), 1199–1234.
    • (2008) Antioxid. Redox Signal. , vol.10 , pp. 1199-1234
    • Davies, M.J.1    Hawkins, C.L.2    Pattison, D.I.3    Rees, M.D.4
  • 39
    • 84929639716 scopus 로고    scopus 로고
    • Mode of action of lactoperoxidase as related to its antimicrobial activity: a review
    • Article ID 517164
    • [39] Bafort, E., Parisi, O., Perraudin, J.P., Jijakli, M.H., Mode of action of lactoperoxidase as related to its antimicrobial activity: a review. Enzyme Res., 2014 Article ID 517164.
    • (2014) Enzyme Res.
    • Bafort, E.1    Parisi, O.2    Perraudin, J.P.3    Jijakli, M.H.4
  • 40
    • 84897972480 scopus 로고    scopus 로고
    • Tyrosinase: the four oxidation states of the active site and their relevance to enzymatic activation, oxidation and inactivation
    • [40] Ramsden, C.A., Riley, P.A., Tyrosinase: the four oxidation states of the active site and their relevance to enzymatic activation, oxidation and inactivation. Bioorg. Med. Chem. 22 (2014), 2388–2395.
    • (2014) Bioorg. Med. Chem. , vol.22 , pp. 2388-2395
    • Ramsden, C.A.1    Riley, P.A.2
  • 41
    • 84934436223 scopus 로고    scopus 로고
    • Regulation of COX and LOX by curcumin
    • [41] Rao, C.V., Regulation of COX and LOX by curcumin. Adv. Exp. Med. Biol. 595 (2007), 213–226.
    • (2007) Adv. Exp. Med. Biol. , vol.595 , pp. 213-226
    • Rao, C.V.1
  • 42
    • 44949262935 scopus 로고    scopus 로고
    • Mammalian xanthine oxidoreductase – mechanism of transition from xanthine dehydrogenase to xanthine oxidase
    • [42] Nishino, T., Okamoto, K., Eger, B.T., Pai, E.F., Nishino, T., Mammalian xanthine oxidoreductase – mechanism of transition from xanthine dehydrogenase to xanthine oxidase. FEBS J. 275 (2008), 3278–3289.
    • (2008) FEBS J. , vol.275 , pp. 3278-3289
    • Nishino, T.1    Okamoto, K.2    Eger, B.T.3    Pai, E.F.4    Nishino, T.5
  • 43
    • 0027930688 scopus 로고
    • Inhibitory effect of curcumin on xanthine dehydrogenase/oxidase induced by phorbol-12-myristate-13-acetate in NIH3T3 cells
    • [43] Lin, J.K., Shih, C.A., Inhibitory effect of curcumin on xanthine dehydrogenase/oxidase induced by phorbol-12-myristate-13-acetate in NIH3T3 cells. Carcinogenesis 15 (1994), 1717–1721.
    • (1994) Carcinogenesis , vol.15 , pp. 1717-1721
    • Lin, J.K.1    Shih, C.A.2
  • 44
    • 65649103461 scopus 로고    scopus 로고
    • Inhibition studies of bovine xanthine oxidase by luteolin, silibinin, quercetin, and curcumin
    • [44] Pauff, J.M., Hille, R., Inhibition studies of bovine xanthine oxidase by luteolin, silibinin, quercetin, and curcumin. J. Nat. Prod. 72 (2009), 725–731.
    • (2009) J. Nat. Prod. , vol.72 , pp. 725-731
    • Pauff, J.M.1    Hille, R.2
  • 46
    • 0041307025 scopus 로고    scopus 로고
    • Quenching of quercetin quinone/quinone methides by different thiolate scavengers: stability and reversibility of conjugate formation
    • [46] Awad, H.M., Boersma, M.G., Boeren, S., Van Bladeren, P.J., Vervoort, J., Rietjens, I.M., Quenching of quercetin quinone/quinone methides by different thiolate scavengers: stability and reversibility of conjugate formation. Chem. Res. Toxicol. 16 (2003), 822–831.
    • (2003) Chem. Res. Toxicol. , vol.16 , pp. 822-831
    • Awad, H.M.1    Boersma, M.G.2    Boeren, S.3    Van Bladeren, P.J.4    Vervoort, J.5    Rietjens, I.M.6
  • 47
    • 0025990221 scopus 로고
    • Interaction of curcumin with glutathione
    • [47] Mathews, S., Rao, M.N.A., Interaction of curcumin with glutathione. Int. J. Pharm. 76 (1991), 257–259.
    • (1991) Int. J. Pharm. , vol.76 , pp. 257-259
    • Mathews, S.1    Rao, M.N.A.2


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