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Volumn 40, Issue 4, 1999, Pages 708-714

Phytanic acid is ligand and transcriptional activator of murine liver fatty acid binding protein

Author keywords

Isothermal titration calorimetry; L FABP; Peroxisome proliferation; Peroxisome proliferator activated receptor; SCP2 SCPx deficient knock out mice; Sterol carrier protein 2; Sterol carrier protein x

Indexed keywords

FATTY ACID BINDING PROTEIN; LIGAND; PEROXISOME PROLIFERATOR; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR; PHYTANIC ACID; PHYTOL; TRANSACTIVATOR PROTEIN;

EID: 0032957086     PISSN: 00222275     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (115)

References (46)
  • 1
    • 0030569533 scopus 로고    scopus 로고
    • Phytanoyl-CoA hydroxylase is present in human liver, located in peroxisomes and deficient in Zellweger syndrome: Direct, unequivocal evidence for the new, revised pathway of phytanic acid α-oxidation in humans
    • Jansen, G. A., S. J. Mihalik, P. A. Watkins, H. W. Mosel, C. Jakobs, S. Denis, and R. J. A. Wanders. 1996. Phytanoyl-CoA hydroxylase is present in human liver, located in peroxisomes and deficient in Zellweger syndrome: direct, unequivocal evidence for the new, revised pathway of phytanic acid α-oxidation in humans. Biochem. Biophys. Res. Commun. 229: 205-210.
    • (1996) Biochem. Biophys. Res. Commun. , vol.229 , pp. 205-210
    • Jansen, G.A.1    Mihalik, S.J.2    Watkins, P.A.3    Mosel, H.W.4    Jakobs, C.5    Denis, S.6    Wanders, R.J.A.7
  • 2
    • 0022516905 scopus 로고
    • Characterization of phytol-phytanate conversion activity in rat liver
    • Muralidharan, F. N., and V. B. Muralidharan. 1986. Characterization of phytol-phytanate conversion activity in rat liver. Biochim. Biophys. Acta. 883: 54-62.
    • (1986) Biochim. Biophys. Acta , vol.883 , pp. 54-62
    • Muralidharan, F.N.1    Muralidharan, V.B.2
  • 4
    • 0029017096 scopus 로고
    • Phytanic acid oxidation: Topographical localization of phytanoyl-CoA ligase and transport of phytanic acid into human peroxisomes
    • Pahan, K., and I. Singh. 1995. Phytanic acid oxidation: topographical localization of phytanoyl-CoA ligase and transport of phytanic acid into human peroxisomes. J. Lipid Res. 36: 986-997.
    • (1995) J. Lipid Res. , vol.36 , pp. 986-997
    • Pahan, K.1    Singh, I.2
  • 5
    • 0002575617 scopus 로고
    • Refsum disease
    • C. Scriver, A. L. Beaudet, W. S. Sly, and D. Valle, editors. McGraw-Hill Book Co., New York, NY
    • Steinberg, D. 1989. Refsum disease. In The Metabolic Basis of Inherited Disease. 6th ed. C. Scriver, A. L. Beaudet, W. S. Sly, and D. Valle, editors. McGraw-Hill Book Co., New York, NY. 1533-1550.
    • (1989) The Metabolic Basis of Inherited Disease. 6th Ed. , pp. 1533-1550
    • Steinberg, D.1
  • 8
    • 0021963729 scopus 로고
    • Human liver fatty acid binding protein. Isolation of a full length cDNA and comparative sequence analyses of orthologous and paralogous proteins
    • Lowe, J. B., M. S. Boguski, D. A. Sweetser, N. A. Elshourbagy, J. M. Taylor, and J. I. Gordon. 1985. Human liver fatty acid binding protein. Isolation of a full length cDNA and comparative sequence analyses of orthologous and paralogous proteins. J. Biol. Chem. 260: 3413-3417.
    • (1985) J. Biol. Chem. , vol.260 , pp. 3413-3417
    • Lowe, J.B.1    Boguski, M.S.2    Sweetser, D.A.3    Elshourbagy, N.A.4    Taylor, J.M.5    Gordon, J.I.6
  • 9
    • 0021719156 scopus 로고
    • Expression of a mammalian fatty acid-binding protein in Escherichia coli
    • Lowe, J. B., A. W. Strauss, and J. I. Gordon. 1984. Expression of a mammalian fatty acid-binding protein in Escherichia coli. J. Biol. Chem. 259: 12696-12704.
    • (1984) J. Biol. Chem. , vol.259 , pp. 12696-12704
    • Lowe, J.B.1    Strauss, A.W.2    Gordon, J.I.3
  • 10
    • 0030188330 scopus 로고    scopus 로고
    • Evaluation and characterization of a porcine small intestine cDNA
    • Wintero, A. K., M. Fredholm, and W. Davies. 1996. Evaluation and characterization of a porcine small intestine cDNA. Mamm, Genome. 7: 509-517.
    • (1996) Mamm, Genome , vol.7 , pp. 509-517
    • Wintero, A.K.1    Fredholm, M.2    Davies, W.3
  • 12
    • 0021275901 scopus 로고
    • Fatty-acid-binding proteins. Occurrence of two fatty-acid-binding proteins in bovine liver cytosol and their binding of fatty acids, cholesterol, and other lipophilic ligands
    • Haunerland, N., G. Jagschies, H. Schulenberg, and F. Spener. 1984. Fatty-acid-binding proteins. Occurrence of two fatty-acid-binding proteins in bovine liver cytosol and their binding of fatty acids, cholesterol, and other lipophilic ligands. Hoppe Seyler's Z. Physiol. Chem. 365: 365-376.
    • (1984) Hoppe Seyler's Z. Physiol. Chem. , vol.365 , pp. 365-376
    • Haunerland, N.1    Jagschies, G.2    Schulenberg, H.3    Spener, F.4
  • 13
    • 0028896925 scopus 로고
    • Cytoplasmic fatty acid-binding proteins: Their structure and genes
    • Veerkamp, J. H., and R. G. Maatman. 1995. Cytoplasmic fatty acid-binding proteins: their structure and genes. Prog. Lipid Res. 34: 17-52.
    • (1995) Prog. Lipid Res. , vol.34 , pp. 17-52
    • Veerkamp, J.H.1    Maatman, R.G.2
  • 14
    • 0030986132 scopus 로고    scopus 로고
    • The crystal structure of the liver fatty acid-binding protein. A complex with two bound oleales
    • Thompson, J., N. Winter, D. Terwey, J. Bratt, and L. Banaszak. 1997. The crystal structure of the liver fatty acid-binding protein. A complex with two bound oleales. J. Biol. Chem. 272: 7140-7150.
    • (1997) J. Biol. Chem. , vol.272 , pp. 7140-7150
    • Thompson, J.1    Winter, N.2    Terwey, D.3    Bratt, J.4    Banaszak, L.5
  • 15
    • 0030718556 scopus 로고    scopus 로고
    • Lipid specificity and location of the sterol carrier protein-2 fatty acid-binding site: A fluorescence displacment and energy transfer study
    • Frolov, A., M. Kimberly, J. T. Billheimer, T. Cho, and F. Schroeder. 1997. Lipid specificity and location of the sterol carrier protein-2 fatty acid-binding site: a fluorescence displacment and energy transfer study. Lipids. 32: 1201-1209.
    • (1997) Lipids , vol.32 , pp. 1201-1209
    • Frolov, A.1    Kimberly, M.2    Billheimer, J.T.3    Cho, T.4    Schroeder, F.5
  • 16
    • 0022401009 scopus 로고
    • A protein of the Z class of liver cytosolic proteins in the rat that preferentially binds heme
    • Vincent, S. H., and U. Muller-Eberhard. 1985. A protein of the Z class of liver cytosolic proteins in the rat that preferentially binds heme. J. Biol. Chem. 260: 14521-14528.
    • (1985) J. Biol. Chem. , vol.260 , pp. 14521-14528
    • Vincent, S.H.1    Muller-Eberhard, U.2
  • 17
    • 0027257417 scopus 로고
    • Involvement of arginine in the binding of heme and fatty acids to fatty acid-binding protein from bovine liver
    • Börchers, T., and F. Spener. 1993. Involvement of arginine in the binding of heme and fatty acids to fatty acid-binding protein from bovine liver. Mol. Cell. Biochem. 123: 23-27.
    • (1993) Mol. Cell. Biochem. , vol.123 , pp. 23-27
    • Börchers, T.1    Spener, F.2
  • 18
    • 0026611046 scopus 로고
    • Regulation of mitochondrial and microsomal phospholipid synthesis by liver fatty acid-binding protein
    • Vancura, A., and D. Haldar. 1992. Regulation of mitochondrial and microsomal phospholipid synthesis by liver fatty acid-binding protein. J. Biol. Chem. 267: 14353-14359.
    • (1992) J. Biol. Chem. , vol.267 , pp. 14353-14359
    • Vancura, A.1    Haldar, D.2
  • 19
    • 0024340893 scopus 로고
    • Specific high affinity binding of lipoxygenase metabolites of arachidonic acid by liver fatty acid binding protein
    • Raza, H., J. R. Pougubala, and S. Sorof. 1989. Specific high affinity binding of lipoxygenase metabolites of arachidonic acid by liver fatty acid binding protein. Biochem. Biophys. Res. Commun. 161: 448-455.
    • (1989) Biochem. Biophys. Res. Commun. , vol.161 , pp. 448-455
    • Raza, H.1    Pougubala, J.R.2    Sorof, S.3
  • 20
    • 0025688143 scopus 로고
    • Preferential binding of growth inhibitory prostaglandins by the target protein of a carcinogen
    • Khan, S. H., and S. Sorof. 1990. Preferential binding of growth inhibitory prostaglandins by the target protein of a carcinogen. Proc. Natl. Acad. Sci. USA. 87: 9401-9405.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 9401-9405
    • Khan, S.H.1    Sorof, S.2
  • 21
    • 0029994543 scopus 로고    scopus 로고
    • Role of the peroxisome proliferator-activated receptor (PPAR) in mediating the effects of fibrates and fatty acids on gene expression
    • Schoonjans, K., B. Staels, and J. Auwerx. 1996. Role of the peroxisome proliferator-activated receptor (PPAR) in mediating the effects of fibrates and fatty acids on gene expression. J. Lipid Res. 37: 907-925.
    • (1996) J. Lipid Res. , vol.37 , pp. 907-925
    • Schoonjans, K.1    Staels, B.2    Auwerx, J.3
  • 22
    • 0021051308 scopus 로고
    • Carcinogenesis by hepatic peroxisome proliferators: Evaluation of the risk of hypolipidemic drugs and industrial plasticizers to humans
    • Reddy, J. K., and N. D. Lalwai. 1983. Carcinogenesis by hepatic peroxisome proliferators: evaluation of the risk of hypolipidemic drugs and industrial plasticizers to humans. Crit. Rev. Toxicol. 12: 1-58.
    • (1983) Crit. Rev. Toxicol. , vol.12 , pp. 1-58
    • Reddy, J.K.1    Lalwai, N.D.2
  • 23
    • 0027300498 scopus 로고
    • Toxicity of peroxisome proliferators
    • Bieri, F., and J. C. Lhuguenot. 1993. Toxicity of peroxisome proliferators. Biochimie. 75: 263-268.
    • (1993) Biochimie , vol.75 , pp. 263-268
    • Bieri, F.1    Lhuguenot, J.C.2
  • 24
    • 0028997684 scopus 로고
    • Targeted disruption of the α isoform of the peroxisome proliferator-activated receptor gene in mice results in abolishment of the pleiotropic effects of peroxisome proliferators
    • Lee, S. S., T. Pineau, J. Drago, E. J. Lee, J. W. Owens, D. L. Kroety, P. M. Fernandez-Salguero, H. Westphal, and F. J Gonzalez. 1995. Targeted disruption of the α isoform of the peroxisome proliferator-activated receptor gene in mice results in abolishment of the pleiotropic effects of peroxisome proliferators. Mol. Cell. Biol. 15: 3012-3022.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 3012-3022
    • Lee, S.S.1    Pineau, T.2    Drago, J.3    Lee, E.J.4    Owens, J.W.5    Kroety, D.L.6    Fernandez-Salguero, P.M.7    Westphal, H.8    Gonzalez, F.J.9
  • 25
    • 0026545711 scopus 로고
    • A role for fatty acids and liver fatty acid binding protein in peroxisome proliferation?
    • Issemann, I., R. Prince, J. Tugwood, and S. Green. 1992. A role for fatty acids and liver fatty acid binding protein in peroxisome proliferation? Biochem. Soc. Trans. 20: 824-827.
    • (1992) Biochem. Soc. Trans. , vol.20 , pp. 824-827
    • Issemann, I.1    Prince, R.2    Tugwood, J.3    Green, S.4
  • 26
    • 0025209859 scopus 로고
    • Induction of fatty acid binding protein by peroxisome proliferators in primary hepatocyte cultures and its relationship to the induction of peroxisomal beta-oxidation
    • Brandes, R., R. M. Kaikaus, N. Lysenko, R. K. Ockner, and N. M. Bass. 1990. Induction of fatty acid binding protein by peroxisome proliferators in primary hepatocyte cultures and its relationship to the induction of peroxisomal beta-oxidation. Biochim. Biophys. Acta. 1034: 53-61.
    • (1990) Biochim. Biophys. Acta , vol.1034 , pp. 53-61
    • Brandes, R.1    Kaikaus, R.M.2    Lysenko, N.3    Ockner, R.K.4    Bass, N.M.5
  • 27
    • 0027327275 scopus 로고
    • Transcriptional induction of the fatty acid binding protein gene in mouse liver by bezafibrate
    • Besnard, P., A. Mallordy, and H. Carlier. 1993. Transcriptional induction of the fatty acid binding protein gene in mouse liver by bezafibrate. FEBS Lett. 327: 219-223.
    • (1993) FEBS Lett. , vol.327 , pp. 219-223
    • Besnard, P.1    Mallordy, A.2    Carlier, H.3
  • 29
    • 0027166062 scopus 로고
    • Amino acid exchange and covalent modification by cysteine and glutathione explain isoforms of fatty acid-binding protein occurring in bovine liver
    • Dörmann, P., T. Börchers, U. Korf, P. Højrup, P. Roepstorff, and F. Spener. 1993. Amino acid exchange and covalent modification by cysteine and glutathione explain isoforms of fatty acid-binding protein occurring in bovine liver. J. Biol. Chem. 268: 16286-16292.
    • (1993) J. Biol. Chem. , vol.268 , pp. 16286-16292
    • Dörmann, P.1    Börchers, T.2    Korf, U.3    Højrup, P.4    Roepstorff, P.5    Spener, F.6
  • 30
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 31
    • 70449158340 scopus 로고
    • A simple method for the isolation and purification of total lipids from animal tissue
    • Folch, J., M. Lees, and G. H. Sloane Stanley. 1957. A simple method for the isolation and purification of total lipids from animal tissue. J. Biol. Chem. 226: 497-509.
    • (1957) J. Biol. Chem. , vol.226 , pp. 497-509
    • Folch, J.1    Lees, M.2    Stanley, G.H.S.3
  • 33
    • 0028950445 scopus 로고
    • Smith-Lemli-Opitz Syndrome diagnosed by using time-of-flight secondary-ion mass spectrometry
    • Seedorf, U., M. Fobker, R. Voss, K. Meyer, F. Kannenberg, and D. Meschede. 1995. Smith-Lemli-Opitz Syndrome diagnosed by using time-of-flight secondary-ion mass spectrometry. Clin. Chem. 41: 548-552.
    • (1995) Clin. Chem. , vol.41 , pp. 548-552
    • Seedorf, U.1    Fobker, M.2    Voss, R.3    Meyer, K.4    Kannenberg, F.5    Meschede, D.6
  • 34
    • 0024356301 scopus 로고
    • Rapid measurement of binding constants and heats of binding using a new titration calorimeter
    • Wiseman, T., S. Williston, J. F. Brandts, and L. N. Lin. 1989. Rapid measurement of binding constants and heats of binding using a new titration calorimeter. Anal. Biochem. 179: 131-137.
    • (1989) Anal. Biochem. , vol.179 , pp. 131-137
    • Wiseman, T.1    Williston, S.2    Brandts, J.F.3    Lin, L.N.4
  • 35
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill, S. C., and P. H. von Hippel. 1989. Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 182: 319-326.
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 36
    • 0027282014 scopus 로고
    • Titration calorimetry as a binding assay for lipid-binding proteins
    • Miller, K. R., and D. P. Cistola. 1993. Titration calorimetry as a binding assay for lipid-binding proteins. Mol. Cell Biochem. 123: 29-37.
    • (1993) Mol. Cell Biochem. , vol.123 , pp. 29-37
    • Miller, K.R.1    Cistola, D.P.2
  • 37
    • 0024374909 scopus 로고
    • A 14-kilodalton selenium-binding protein in mouse liver is fatty acid-binding protein
    • Bansal, M. P., R. G. Cook, K. G. Danielson, and D. Medina. 1989. A 14-kilodalton selenium-binding protein in mouse liver is fatty acid-binding protein. J. Biol. Chem. 264: 13780-13784.
    • (1989) J. Biol. Chem. , vol.264 , pp. 13780-13784
    • Bansal, M.P.1    Cook, R.G.2    Danielson, K.G.3    Medina, D.4
  • 38
    • 0030771852 scopus 로고    scopus 로고
    • DNA binding properties of peroxisome proliferator-activated receptor subtypes on various natural peroxisome proliferator response elements
    • Juge-Aubry, C., A. Pernin, T. Favez, A. G. Burger, W. Wahli, C. A. Meier, and B. Desvergne. 1997. DNA binding properties of peroxisome proliferator-activated receptor subtypes on various natural peroxisome proliferator response elements. J. Biol. Chem. 272: 25252-25259.
    • (1997) J. Biol. Chem. , vol.272 , pp. 25252-25259
    • Juge-Aubry, C.1    Pernin, A.2    Favez, T.3    Burger, A.G.4    Wahli, W.5    Meier, C.A.6    Desvergne, B.7
  • 39
    • 0028900972 scopus 로고
    • The analysis of modified peroxisome proliferator responsive elements of the peroxisomal bifunctional enzyme in transfected HepG2 cells reveals two regulatory motifs
    • Bardot, O., M. C. Clemencet, P. Passilly, and N. Latruffe. 1995. The analysis of modified peroxisome proliferator responsive elements of the peroxisomal bifunctional enzyme in transfected HepG2 cells reveals two regulatory motifs. FEBS. Lett. 360: 183-186.
    • (1995) FEBS. Lett. , vol.360 , pp. 183-186
    • Bardot, O.1    Clemencet, M.C.2    Passilly, P.3    Latruffe, N.4
  • 40
    • 0029859741 scopus 로고    scopus 로고
    • Thermodynamic and kinetic properties of fatty acid interactions with rat liver fatty acid-binding protein
    • Richieri, G. V., R. T. Ogata, and A. M. Kleinfeld. 1996. Thermodynamic and kinetic properties of fatty acid interactions with rat liver fatty acid-binding protein. J. Biol. Chem. 271: 31068-31074.
    • (1996) J. Biol. Chem. , vol.271 , pp. 31068-31074
    • Richieri, G.V.1    Ogata, R.T.2    Kleinfeld, A.M.3
  • 41
    • 0030896007 scopus 로고    scopus 로고
    • Peroxisome proliferation and β-oxidation in Fao and MH1C1 rat hepatoma cells, HepG2 human hepatoblastoma cells and cultured human hepatocytes: Effect of cipofibrate
    • Duclos, S., J. Bride, L. C. Ramirez, and P. Bournot. 1997. Peroxisome proliferation and β-oxidation in Fao and MH1C1 rat hepatoma cells, HepG2 human hepatoblastoma cells and cultured human hepatocytes: effect of cipofibrate. Eur. J. Cell Biol. 72: 314-323.
    • (1997) Eur. J. Cell Biol. , vol.72 , pp. 314-323
    • Duclos, S.1    Bride, J.2    Ramirez, L.C.3    Bournot, P.4
  • 42
    • 0027176127 scopus 로고
    • Metabolic pathways in mammalian peroxisomes
    • Mannaerts, G. P., and P. P van Veldhoven. 1993. Metabolic pathways in mammalian peroxisomes. Biochimie, 75: 147-158.
    • (1993) Biochimie , vol.75 , pp. 147-158
    • Mannaerts, G.P.1    Van Veldhoven, P.P.2
  • 43
    • 0026098687 scopus 로고
    • Structural and functional features of different types of cytoplasmic fatty acid-binding proteins
    • Veerkamp, J. H., R. A. Peeters, and R. G. Maatman. 1991. Structural and functional features of different types of cytoplasmic fatty acid-binding proteins. Biochim. Biophys. Acta. 1081: 1-24.
    • (1991) Biochim. Biophys. Acta , vol.1081 , pp. 1-24
    • Veerkamp, J.H.1    Peeters, R.A.2    Maatman, R.G.3
  • 44
    • 0030996072 scopus 로고    scopus 로고
    • Phospholipid transfer proteins revisited
    • Wirtz, K. W. A. 1997. Phospholipid transfer proteins revisited. Biochem. J. 324: 353-360.
    • (1997) Biochem. J. , vol.324 , pp. 353-360
    • Wirtz, K.W.A.1
  • 45
    • 0026506986 scopus 로고
    • Sterol carrier protein 2 (non-specific lipid transfer protein) is localized in membranous fractions of Leydig cells and Sertoli cells but not in germ cells
    • van Haren, L., K. J. Teerds, B. C. Ossendorp, G. P. van Heusden, J. Orly, D. M. Stocco, K. W. Wirtz, and F. F. Rommerts. 1992 Sterol carrier protein 2 (non-specific lipid transfer protein) is localized in membranous fractions of Leydig cells and Sertoli cells but not in germ cells. Biochim. Biophys. Acta. 1124: 288-296.
    • (1992) Biochim. Biophys. Acta , vol.1124 , pp. 288-296
    • Van Haren, L.1    Teerds, K.J.2    Ossendorp, B.C.3    Van Heusden, G.P.4    Orly, J.5    Stocco, D.M.6    Wirtz, K.W.7    Rommerts, F.F.8
  • 46
    • 0030060358 scopus 로고    scopus 로고
    • Expression of the peroxisome proliferator-activated receptor a gene is stimulated by stress and follows a diurnal rhythm
    • Lemberger, T., R. Saladin, M. Vazquez, F. Assimacopoulos, B. Staels, B. Desvergne, W. Wahli, and J. Auwerx. 1996. Expression of the peroxisome proliferator-activated receptor a gene is stimulated by stress and follows a diurnal rhythm. J. Biol. Chem. 271: 1764-1769.
    • (1996) J. Biol. Chem. , vol.271 , pp. 1764-1769
    • Lemberger, T.1    Saladin, R.2    Vazquez, M.3    Assimacopoulos, F.4    Staels, B.5    Desvergne, B.6    Wahli, W.7    Auwerx, J.8


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