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Volumn 1682, Issue 1-3, 2004, Pages 18-27

ω-Hydroxylation of farnesol by mammalian cytochromes P450

Author keywords

, prenyl dicarboxylic acids; (2E, 6E, 10E) 12 hydroxyfarnesol; CID; collision induced dissociation; CYP2C19; CYP2E1; Ethanol; farnesyl pyrophosphate; FPP; lipoprotein deficient serum; LPDS; thin layer chromatography; TLC; ZA; zaragozic acid

Indexed keywords

ACETONE; ALPHA,OMEGA PRENYL DICARBOXYLIC ACID; CARBON 14; CYTOCHROME P450 2C19; CYTOCHROME P450 2E1; DICARBOXYLIC ACID DERIVATIVE; FARNESOL; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; UNCLASSIFIED DRUG;

EID: 2442688821     PISSN: 13881981     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbalip.2004.01.003     Document Type: Article
Times cited : (37)

References (41)
  • 2
    • 0028035383 scopus 로고
    • Characterization of two distinct allyl pyrophosphatase activities from rat liver microsomes
    • Bansal V.S., Vaidya S. Characterization of two distinct allyl pyrophosphatase activities from rat liver microsomes. Arch. Biochem. Biophys. 315:1994;393-399
    • (1994) Arch. Biochem. Biophys. , vol.315 , pp. 393-399
    • Bansal, V.S.1    Vaidya, S.2
  • 3
    • 0031239831 scopus 로고    scopus 로고
    • Farnesol as a regulator of HMG-CoA reductase degradation: Characterization and role of farnesyl pyrophosphatase
    • Meigs T.E., Simoni R.D. Farnesol as a regulator of HMG-CoA reductase degradation: characterization and role of farnesyl pyrophosphatase. Arch. Biochem. Biophys. 345:1997;1-9
    • (1997) Arch. Biochem. Biophys. , vol.345 , pp. 1-9
    • Meigs, T.E.1    Simoni, R.D.2
  • 4
    • 0000248311 scopus 로고
    • Studies on the biosynthesis of cholesterol: XIV. the origin of prenoic acids from allyl pyrophosphates in liver enzyme systems
    • Christophe J., Popjak G. Studies on the biosynthesis of cholesterol: XIV. the origin of prenoic acids from allyl pyrophosphates in liver enzyme systems. J. Lipid Res. 2:1961;244-257
    • (1961) J. Lipid Res. , vol.2 , pp. 244-257
    • Christophe, J.1    Popjak, G.2
  • 5
    • 0030660267 scopus 로고    scopus 로고
    • Ubiquitin-mediated regulation of 3-hydroxy-3-methylglutaryl-CoA reductase
    • Hampton R.Y., Bhakta H. Ubiquitin-mediated regulation of 3-hydroxy-3-methylglutaryl-CoA reductase. Proc. Natl. Acad. Sci. U. S. A. 94:1997;12944-12948
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 12944-12948
    • Hampton, R.Y.1    Bhakta, H.2
  • 6
    • 0000812012 scopus 로고    scopus 로고
    • Farnesol is not the nonsterol regulator mediating degradation of HMG-CoA reductase in rat liver
    • Keller R.K., Zhao Z., Chambers C., Ness G.C. Farnesol is not the nonsterol regulator mediating degradation of HMG-CoA reductase in rat liver. Arch. Biochem. Biophys. 328:1996;324-330
    • (1996) Arch. Biochem. Biophys. , vol.328 , pp. 324-330
    • Keller, R.K.1    Zhao, Z.2    Chambers, C.3    Ness, G.C.4
  • 7
    • 0028307290 scopus 로고
    • Identification of farnesol as the non-sterol derivative of mevalonic acid required for the accelerated degradation of 3-hydroxy-3-methylglutaryl-coenzyme a reductase
    • Correll C.C., Ng L., Edwards P.A. Identification of farnesol as the non-sterol derivative of mevalonic acid required for the accelerated degradation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase. J. Biol. Chem. 269:1994;17390-17393
    • (1994) J. Biol. Chem. , vol.269 , pp. 17390-17393
    • Correll, C.C.1    Ng, L.2    Edwards, P.A.3
  • 8
    • 0029969302 scopus 로고    scopus 로고
    • Regulation of 3-hydroxy-3-methylglutaryl-coenzyme a reductase degradation by the nonsterol mevalonate metabolite farnesol in vivo
    • Meigs T.E., Roseman D.S., Simoni R.D. Regulation of 3-hydroxy-3- methylglutaryl-coenzyme A reductase degradation by the nonsterol mevalonate metabolite farnesol in vivo. J. Biol. Chem. 271:1996;7916-7922
    • (1996) J. Biol. Chem. , vol.271 , pp. 7916-7922
    • Meigs, T.E.1    Roseman, D.S.2    Simoni, R.D.3
  • 9
    • 0028832005 scopus 로고
    • Selective farnesol toxicity and translocation of protein kinase C in neoplastic HeLa-S3K and non-neoplastic CF-3 cells
    • Yazlovitskaya E.M., Melnykovych G. Selective farnesol toxicity and translocation of protein kinase C in neoplastic HeLa-S3K and non-neoplastic CF-3 cells. Cancer Lett. 88:1995;179-183
    • (1995) Cancer Lett. , vol.88 , pp. 179-183
    • Yazlovitskaya, E.M.1    Melnykovych, G.2
  • 10
    • 0028128625 scopus 로고
    • Directed cell killing (apoptosis) in human lymphoblastoid cells incubated in the presence of farnesol: Effect of phosphatidylcholine
    • Haug J.S., Goldner C.M., Yazlovitskaya E.M., Voziyan P.A., Melnykovych G. Directed cell killing (apoptosis) in human lymphoblastoid cells incubated in the presence of farnesol: effect of phosphatidylcholine. Biochim. Biophys. Acta. 1223:1994;133-140
    • (1994) Biochim. Biophys. Acta , vol.1223 , pp. 133-140
    • Haug, J.S.1    Goldner, C.M.2    Yazlovitskaya, E.M.3    Voziyan, P.A.4    Melnykovych, G.5
  • 11
    • 0032476029 scopus 로고    scopus 로고
    • Competitive inhibition of choline phosphotransferase by geranylgeraniol and farnesol inhibits phosphatidylcholine synthesis and induces apoptosis in human lung adenocarcinoma A549 cells
    • Miquel K.A., Pradines A., Terce F., Selmi S., Favre G. Competitive inhibition of choline phosphotransferase by geranylgeraniol and farnesol inhibits phosphatidylcholine synthesis and induces apoptosis in human lung adenocarcinoma A549 cells. J. Biol. Chem. 273:1998;26179-26186
    • (1998) J. Biol. Chem. , vol.273 , pp. 26179-26186
    • Miquel, K.A.1    Pradines, A.2    Terce, F.3    Selmi, S.4    Favre, G.5
  • 15
    • 0023874006 scopus 로고
    • Isopentenoid synthesis in isolated embryonic Drosophila cells. Farnesol catabolism and omega-oxidation
    • Gonzalez-Pacanowska D.B., Arison B., Havel C.M., Watson J.A. Isopentenoid synthesis in isolated embryonic Drosophila cells. Farnesol catabolism and omega-oxidation. J. Biol. Chem. 263:1988;1301-1306
    • (1988) J. Biol. Chem. , vol.263 , pp. 1301-1306
    • Gonzalez-Pacanowska, D.B.1    Arison, B.2    Havel, C.M.3    Watson, J.A.4
  • 16
    • 0032127143 scopus 로고    scopus 로고
    • Massive production of farnesol-derived dicarboxylic acids in mice treated with the squalene synthase inhibitor zaragozic acid a
    • Vaidya S., Bostedor R., Kurtz M.M., Bergstrom J.D., Bansal V.S. Massive production of farnesol-derived dicarboxylic acids in mice treated with the squalene synthase inhibitor zaragozic acid A. Arch. Biochem. Biophys. 355:1998;84-92
    • (1998) Arch. Biochem. Biophys. , vol.355 , pp. 84-92
    • Vaidya, S.1    Bostedor, R.2    Kurtz, M.M.3    Bergstrom, J.D.4    Bansal, V.S.5
  • 18
    • 0031584090 scopus 로고    scopus 로고
    • Metabolism of farnesol: Phosphorylation of farnesol by rat liver microsomal and peroxisomal fractions
    • Westfall D.N., Aboushadi N., Shackelford J.E., Krisans S.K. Metabolism of farnesol: phosphorylation of farnesol by rat liver microsomal and peroxisomal fractions. Biochem. Biophys. Res. Commun. 230:1997;562-568
    • (1997) Biochem. Biophys. Res. Commun. , vol.230 , pp. 562-568
    • Westfall, D.N.1    Aboushadi, N.2    Shackelford, J.E.3    Krisans, S.K.4
  • 19
    • 0032524373 scopus 로고    scopus 로고
    • Phosphorylation of farnesol in rat liver microsomes: Properties of farnesol kinase and farnesyl phosphate kinase
    • Bentinger M.J., Grunler J., Peterson E., Swiezewska E., Dallner G. Phosphorylation of farnesol in rat liver microsomes: properties of farnesol kinase and farnesyl phosphate kinase. Arch. Biochem. Biophys. 353:1998;191-198
    • (1998) Arch. Biochem. Biophys. , vol.353 , pp. 191-198
    • Bentinger, M.J.1    Grunler, J.2    Peterson, E.3    Swiezewska, E.4    Dallner, G.5
  • 20
    • 0025974055 scopus 로고
    • Human liver alcohol dehydrogenases catalyze the oxidation of the intermediary alcohols of the shunt pathway of mevalonate metabolism
    • Keung W.M. Human liver alcohol dehydrogenases catalyze the oxidation of the intermediary alcohols of the shunt pathway of mevalonate metabolism. Biochem. Biophys. Res. Commun. 174:1991;701-707
    • (1991) Biochem. Biophys. Res. Commun. , vol.174 , pp. 701-707
    • Keung, W.M.1
  • 21
    • 0010492263 scopus 로고
    • The fate of branched chain fatty acids in the animal body I. a contribution to the problem of Hildebrandt acid
    • Asano M., Yamakawa T. The fate of branched chain fatty acids in the animal body I. A contribution to the problem of Hildebrandt acid. J. Biochem. 37:1950;321-327
    • (1950) J. Biochem. , vol.37 , pp. 321-327
    • Asano, M.1    Yamakawa, T.2
  • 23
    • 0018196553 scopus 로고
    • Cytochrome P-450LM2 mediated hydroxylation of monoterpene alcohols
    • Licht H.J., Coscia C.J. Cytochrome P-450LM2 mediated hydroxylation of monoterpene alcohols. Biochemistry. 17:1978;5638-5646
    • (1978) Biochemistry , vol.17 , pp. 5638-5646
    • Licht, H.J.1    Coscia, C.J.2
  • 24
  • 26
    • 84982067212 scopus 로고
    • Eine synthese des beta-sinensals
    • Buchi G., Wuest H. Eine synthese des beta-sinensals. Helv. Chim. Acta. 50:1967;2440-2445
    • (1967) Helv. Chim. Acta , vol.50 , pp. 2440-2445
    • Buchi, G.1    Wuest, H.2
  • 27
    • 0021682938 scopus 로고
    • Immunochemical evidence for a role of cytochrome P-450 in liver microsomal ethanol oxidation
    • Koop D.R., Nordblom G.D., Coon M.J. Immunochemical evidence for a role of cytochrome P-450 in liver microsomal ethanol oxidation. Arch. Biochem. Biophys. 235:1984;228-238
    • (1984) Arch. Biochem. Biophys. , vol.235 , pp. 228-238
    • Koop, D.R.1    Nordblom, G.D.2    Coon, M.J.3
  • 28
    • 0037216623 scopus 로고    scopus 로고
    • Analysis of differential substrate selectivities of CYP2B6 and CYP2E1 by site-directed mutagenesis and molecular modeling
    • Spatzenegger M., Liu H., Wang Q., Debarber A.E., Koop D.R., Halpert J.R. Analysis of differential substrate selectivities of CYP2B6 and CYP2E1 by site-directed mutagenesis and molecular modeling. J. Pharmacol. Exp. Ther. 304:2003;477-487
    • (2003) J. Pharmacol. Exp. Ther. , vol.304 , pp. 477-487
    • Spatzenegger, M.1    Liu, H.2    Wang, Q.3    Debarber, A.E.4    Koop, D.R.5    Halpert, J.R.6
  • 29
    • 0028900699 scopus 로고
    • Rabbit P450 2E1 expressed in CHO-K1 cells has a short half-life
    • Barmada S., Kienle E., Koop D.R. Rabbit P450 2E1 expressed in CHO-K1 cells has a short half-life. Biochem. Biophys. Res. Commun. 206:1995;601-607
    • (1995) Biochem. Biophys. Res. Commun. , vol.206 , pp. 601-607
    • Barmada, S.1    Kienle, E.2    Koop, D.R.3
  • 30
    • 0032893473 scopus 로고    scopus 로고
    • Tightly regulated and inducible expression of rabbit CYP2E1 using a tetracycline-controlled expression system
    • Huan J.Y., Koop D.R. Tightly regulated and inducible expression of rabbit CYP2E1 using a tetracycline-controlled expression system. Drug Metab. Dispos. 27:1999;549-554
    • (1999) Drug Metab. Dispos. , vol.27 , pp. 549-554
    • Huan, J.Y.1    Koop, D.R.2
  • 32
    • 0002948745 scopus 로고    scopus 로고
    • CYP2C enzymes
    • R.H. Levy, K.E. Thummel, W.F. Trager, P.D. Hansten, & M. Eichelbaum. Philadelphia, PA: Lippincot-Williams and Wilkins
    • Rettie A.E., Koop D.R., Haining R.L. CYP2C enzymes. Levy R.H., Thummel K.E., Trager W.F., Hansten P.D., Eichelbaum M. Metabolic Drug Interactions. 2000;75-86 Lippincot-Williams and Wilkins, Philadelphia, PA
    • (2000) Metabolic Drug Interactions , pp. 75-86
    • Rettie, A.E.1    Koop, D.R.2    Haining, R.L.3
  • 33
    • 0031918678 scopus 로고    scopus 로고
    • Cytochrome P450-dependent desaturation of lauric acid: Isoform selectivity and mechanism of formation of 11-dodecenoic acid
    • Guan X.M., Fisher M.B., Lang D.H., Zheng Y.M., Koop D.R., Rettie A.E. Cytochrome P450-dependent desaturation of lauric acid: isoform selectivity and mechanism of formation of 11-dodecenoic acid. Chem. Biol. Interact. 110:1998;103-121
    • (1998) Chem. Biol. Interact. , vol.110 , pp. 103-121
    • Guan, X.M.1    Fisher, M.B.2    Lang, D.H.3    Zheng, Y.M.4    Koop, D.R.5    Rettie, A.E.6
  • 34
    • 0027164207 scopus 로고
    • Formation of 19(S)-, 19(R)-, and 18(R)-hydroxyeicosatetraenoic acids by alcohol-inducible cytochrome P450 2E1
    • Laethem R.M., Balazy M., Falck J.R., Laethem C.L., Koop D.R. Formation of 19(S)-, 19(R)-, and 18(R)-hydroxyeicosatetraenoic acids by alcohol-inducible cytochrome P450 2E1. J. Biol. Chem. 268:1993;12912-12918
    • (1993) J. Biol. Chem. , vol.268 , pp. 12912-12918
    • Laethem, R.M.1    Balazy, M.2    Falck, J.R.3    Laethem, C.L.4    Koop, D.R.5
  • 35
    • 0030952937 scopus 로고    scopus 로고
    • Hypolipidemic drugs, polyunsaturated fatty acids, and eicosanoids are ligands for peroxisome proliferator-activated receptors alpha and delta
    • Forman B.M., Chen J., Evans R.M. Hypolipidemic drugs, polyunsaturated fatty acids, and eicosanoids are ligands for peroxisome proliferator-activated receptors alpha and delta. Proc. Natl. Acad. Sci. U. S. A. 94:1997;4312-4317
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 4312-4317
    • Forman, B.M.1    Chen, J.2    Evans, R.M.3
  • 36
    • 0036080081 scopus 로고    scopus 로고
    • P-450 metabolites of arachidonic acid in the control of cardiovascular function
    • Roman R.J. P-450 metabolites of arachidonic acid in the control of cardiovascular function. Physiol. Rev. 82:2002;131-185
    • (2002) Physiol. Rev. , vol.82 , pp. 131-185
    • Roman, R.J.1
  • 39
    • 0036840528 scopus 로고    scopus 로고
    • Squalestatin 1-inducible expression of rat CYP2B: Evidence that an endogenous isoprenoid is an activator of the constitutive androstane receptor
    • Kocarek T.A., Mercer-Haines N.A. Squalestatin 1-inducible expression of rat CYP2B: evidence that an endogenous isoprenoid is an activator of the constitutive androstane receptor. Mol. Pharmacol. 62:2002;1177-1186
    • (2002) Mol. Pharmacol. , vol.62 , pp. 1177-1186
    • Kocarek, T.A.1    Mercer-Haines, N.A.2
  • 40
    • 0013853867 scopus 로고
    • Dehydrogenation of trans-trans farnesol by horse liver alcohol dehydrogenase
    • Waller G.R. Dehydrogenation of trans-trans farnesol by horse liver alcohol dehydrogenase. Nature. 207:1965;1389-1390
    • (1965) Nature , vol.207 , pp. 1389-1390
    • Waller, G.R.1
  • 41
    • 0034792584 scopus 로고    scopus 로고
    • Clinical relevance of genetic polymorphisms in the human CYP2C subfamily
    • Goldstein J.A. Clinical relevance of genetic polymorphisms in the human CYP2C subfamily. Br. J. Clin. Pharmacol. 52:2001;349-355
    • (2001) Br. J. Clin. Pharmacol. , vol.52 , pp. 349-355
    • Goldstein, J.A.1


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