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Volumn 1801, Issue 9, 2010, Pages 1082-1089

Natural ligand binding and transfer from liver fatty acid binding protein (LFABP) to membranes

Author keywords

Acyl CoA; Enterocyte; Fatty acid; Lipid binding protein; Lipid metabolism; Lipid transfer

Indexed keywords

FATTY ACID BINDING PROTEIN; MUTANT PROTEIN; OLEIC ACID; OLEOYL COENZYME A; PALMITIC ACID; PALMITOYL COENZYME A; ACYL COENZYME A; FATTY ACID; LIGAND; OLEOYL-COENZYME A; PROTEIN BINDING; RECOMBINANT PROTEIN;

EID: 77954656481     PISSN: 13881981     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbalip.2010.05.008     Document Type: Article
Times cited : (17)

References (45)
  • 1
    • 50949128339 scopus 로고    scopus 로고
    • The emerging functions and mechanisms of mammalian fatty acid-binding proteins
    • Storch J., Corsico B. The emerging functions and mechanisms of mammalian fatty acid-binding proteins. Annu. Rev. Nutr. 2008, 28:73-95.
    • (2008) Annu. Rev. Nutr. , vol.28 , pp. 73-95
    • Storch, J.1    Corsico, B.2
  • 2
    • 0030986132 scopus 로고    scopus 로고
    • The crystal structure of the liver fatty acid-binding protein. A complex with two bound oleates
    • Thompson J., Winter N., Terwey D., Bratt J., Banaszak L. The crystal structure of the liver fatty acid-binding protein. A complex with two bound oleates. J. Biol. Chem. 1997, 14:7140-7150.
    • (1997) J. Biol. Chem. , vol.14 , pp. 7140-7150
    • Thompson, J.1    Winter, N.2    Terwey, D.3    Bratt, J.4    Banaszak, L.5
  • 3
    • 35848954991 scopus 로고    scopus 로고
    • Solution-state molecular structure of apo and oleate-liganded liver fatty acid-binding protein
    • He Y., Yang X., Wang H., Estephan R., Francis F., Kodukula S., Storch J., Stark R.E. Solution-state molecular structure of apo and oleate-liganded liver fatty acid-binding protein. Biochemistry 2007, 46:12543-12556.
    • (2007) Biochemistry , vol.46 , pp. 12543-12556
    • He, Y.1    Yang, X.2    Wang, H.3    Estephan, R.4    Francis, F.5    Kodukula, S.6    Storch, J.7    Stark, R.E.8
  • 4
    • 77954656315 scopus 로고
    • Refined apoprotein structure of rat intestinal fatty acid binding protein produced in Escherichia coli
    • Sacchettini J.C., Gordon J.I., Banaszak L.J. Refined apoprotein structure of rat intestinal fatty acid binding protein produced in Escherichia coli. Biochim. Biophys. Acta 1989, 1747:189-194.
    • (1989) Biochim. Biophys. Acta , vol.1747 , pp. 189-194
    • Sacchettini, J.C.1    Gordon, J.I.2    Banaszak, L.J.3
  • 5
    • 0029859741 scopus 로고    scopus 로고
    • Thermodynamic and kinetic properties of fatty acid interactions with rat liver fatty acid-binding protein
    • Richieri G.V., Ogata R.T., Kleinfeld A.M. Thermodynamic and kinetic properties of fatty acid interactions with rat liver fatty acid-binding protein. J. Biol. Chem. 1996, 271:31068-31074.
    • (1996) J. Biol. Chem. , vol.271 , pp. 31068-31074
    • Richieri, G.V.1    Ogata, R.T.2    Kleinfeld, A.M.3
  • 6
    • 0023656293 scopus 로고
    • Studies on fatty acid-binding proteins. The binding properties of rat liver fatty acid-binding protein
    • Wilkinson T.C., Wilton D.C. Studies on fatty acid-binding proteins. The binding properties of rat liver fatty acid-binding protein. Biochem J. 1987, 247:485-488.
    • (1987) Biochem J. , vol.247 , pp. 485-488
    • Wilkinson, T.C.1    Wilton, D.C.2
  • 7
    • 0023662960 scopus 로고
    • Binding of acyl-CoA to liver fatty acid binding protein: effect on acyl-CoA synthesis
    • Burrier R.E., Manson C.R., Brecher P. Binding of acyl-CoA to liver fatty acid binding protein: effect on acyl-CoA synthesis. Biochim. Biophys. Acta 1987, 919:221-230.
    • (1987) Biochim. Biophys. Acta , vol.919 , pp. 221-230
    • Burrier, R.E.1    Manson, C.R.2    Brecher, P.3
  • 8
    • 0028071589 scopus 로고
    • The binding of lysophospholipids to rat liver fatty acid-binding protein and albumin
    • Thumser A.E., Voysey J.E., Wilton D.C. The binding of lysophospholipids to rat liver fatty acid-binding protein and albumin. Biochem. J. 1994, 301:801-806.
    • (1994) Biochem. J. , vol.301 , pp. 801-806
    • Thumser, A.E.1    Voysey, J.E.2    Wilton, D.C.3
  • 9
    • 0023013710 scopus 로고
    • Binding of lysophosphatidylcholine to the rat liver fatty acid binding protein
    • Burrier R.E., Brecher P. Binding of lysophosphatidylcholine to the rat liver fatty acid binding protein. Biochim. Biophys. Acta 1986, 879:229-239.
    • (1986) Biochim. Biophys. Acta , vol.879 , pp. 229-239
    • Burrier, R.E.1    Brecher, P.2
  • 10
    • 0029993073 scopus 로고    scopus 로고
    • Fatty acid transfer from liver and intestinal fatty acid-binding proteins to membranes occurs by different mechanisms
    • Hsu K.T., Storch J. Fatty acid transfer from liver and intestinal fatty acid-binding proteins to membranes occurs by different mechanisms. J. Biol. Chem. 1996, 271:13317-13323.
    • (1996) J. Biol. Chem. , vol.271 , pp. 13317-13323
    • Hsu, K.T.1    Storch, J.2
  • 11
    • 40949143121 scopus 로고    scopus 로고
    • The integrity of the alpha-helical domain of intestinal fatty acid binding protein is essential for the collision-mediated transfer of fatty acids to phospholipid membranes
    • Franchini G.R., Storch J., Corsico B. The integrity of the alpha-helical domain of intestinal fatty acid binding protein is essential for the collision-mediated transfer of fatty acids to phospholipid membranes. Biochim. Biophys. Acta 2008, 1781:192-199.
    • (2008) Biochim. Biophys. Acta , vol.1781 , pp. 192-199
    • Franchini, G.R.1    Storch, J.2    Corsico, B.3
  • 12
    • 12144289741 scopus 로고    scopus 로고
    • The alpha-helical domain of liver fatty acid binding protein is responsible for the diffusion-mediated transfer of fatty acids to phospholipid membranes
    • Córsico B., Liou H.L., Storch J. The alpha-helical domain of liver fatty acid binding protein is responsible for the diffusion-mediated transfer of fatty acids to phospholipid membranes. Biochemistry 2004, 43:3600-3607.
    • (2004) Biochemistry , vol.43 , pp. 3600-3607
    • Córsico, B.1    Liou, H.L.2    Storch, J.3
  • 13
    • 0034004499 scopus 로고    scopus 로고
    • Liver and intestinal fatty acid-binding proteins obtain fatty acids from phospholipid membranes by different mechanisms
    • Thumser A.E., Storch J. Liver and intestinal fatty acid-binding proteins obtain fatty acids from phospholipid membranes by different mechanisms. J. Lipid Res. 2000, 41:647-656.
    • (2000) J. Lipid Res. , vol.41 , pp. 647-656
    • Thumser, A.E.1    Storch, J.2
  • 14
    • 0031043596 scopus 로고    scopus 로고
    • Ligand binding alters the backbone mobility of intestinal fatty acid-binding protein as monitored by 15N NMR relaxation and 1H exchange
    • Hodsdon M.E., Cistola D.P. Ligand binding alters the backbone mobility of intestinal fatty acid-binding protein as monitored by 15N NMR relaxation and 1H exchange. Biochemistry 1997, 36:2278-2290.
    • (1997) Biochemistry , vol.36 , pp. 2278-2290
    • Hodsdon, M.E.1    Cistola, D.P.2
  • 15
    • 0032514695 scopus 로고    scopus 로고
    • The helical domain of intestinal fatty acid binding protein is critical for collisional transfer of fatty acids to phospholipid membranes
    • Corsico B., Cistola D.P., Frieden C., Storch J. The helical domain of intestinal fatty acid binding protein is critical for collisional transfer of fatty acids to phospholipid membranes. Proc. Natl. Acad. Sci. U.S.A. 1998, 95:12174-12178.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 12174-12178
    • Corsico, B.1    Cistola, D.P.2    Frieden, C.3    Storch, J.4
  • 16
    • 12544254957 scopus 로고    scopus 로고
    • Tryptophan insertion mutagenesis of liver fatty acid-binding protein: L28W mutant provides important insights into ligand binding and physiological function
    • Hagan R.M., Worner-Gibbs J., Wilton D.C. Tryptophan insertion mutagenesis of liver fatty acid-binding protein: L28W mutant provides important insights into ligand binding and physiological function. J. Biol. Chem. 2005, 280:1782-1789.
    • (2005) J. Biol. Chem. , vol.280 , pp. 1782-1789
    • Hagan, R.M.1    Worner-Gibbs, J.2    Wilton, D.C.3
  • 17
    • 0141594833 scopus 로고    scopus 로고
    • Ablation of the liver fatty acid binding protein gene decreases fatty acyl CoA binding capacity and alters fatty acyl CoA pool distribution in mouse liver
    • Martin G.G., Huang H., Atshaves B.P., Binas B., Schroeder F. Ablation of the liver fatty acid binding protein gene decreases fatty acyl CoA binding capacity and alters fatty acyl CoA pool distribution in mouse liver. Biochemistry 2003, 42:11520-11532.
    • (2003) Biochemistry , vol.42 , pp. 11520-11532
    • Martin, G.G.1    Huang, H.2    Atshaves, B.P.3    Binas, B.4    Schroeder, F.5
  • 20
    • 0016360614 scopus 로고
    • Preparation of homogeneous, single-walled phosphatidylcholine vesicles
    • Huang C., Thompson T.E. Preparation of homogeneous, single-walled phosphatidylcholine vesicles. Methods Enzymol. 1974, 32:485-489.
    • (1974) Methods Enzymol. , vol.32 , pp. 485-489
    • Huang, C.1    Thompson, T.E.2
  • 21
    • 0022448658 scopus 로고
    • Transfer of long-chain fluorescent free fatty acids between unilamellar vesicles
    • Storch J., Kleinfeld A.M. Transfer of long-chain fluorescent free fatty acids between unilamellar vesicles. Biochemistry 1986, 25:1717-1726.
    • (1986) Biochemistry , vol.25 , pp. 1717-1726
    • Storch, J.1    Kleinfeld, A.M.2
  • 22
    • 0026322079 scopus 로고
    • Expression, purification, and crystallization of the adipocyte lipid binding protein
    • Xu Z., Buelt M.K., Banaszak L.J., Bernlohr D.A. Expression, purification, and crystallization of the adipocyte lipid binding protein. J. Biol. Chem. 1991, 266:14367-14370.
    • (1991) J. Biol. Chem. , vol.266 , pp. 14367-14370
    • Xu, Z.1    Buelt, M.K.2    Banaszak, L.J.3    Bernlohr, D.A.4
  • 23
    • 0030901275 scopus 로고    scopus 로고
    • Spontaneous transfer of monoacyl amphiphiles between lipid and protein surfaces
    • Massey J.B., Bick D.H., Pownall H.J. Spontaneous transfer of monoacyl amphiphiles between lipid and protein surfaces. Biophys. J. 1997, 72:1732-1743.
    • (1997) Biophys. J. , vol.72 , pp. 1732-1743
    • Massey, J.B.1    Bick, D.H.2    Pownall, H.J.3
  • 24
    • 0025160178 scopus 로고
    • A comparison of heart and liver fatty acid-binding proteins: interactions with fatty acids and possible functional differences studied with fluorescent fatty acid analogues
    • Storch J. A comparison of heart and liver fatty acid-binding proteins: interactions with fatty acids and possible functional differences studied with fluorescent fatty acid analogues. Mol. Cell. Biochem. 1990, 98:141-147.
    • (1990) Mol. Cell. Biochem. , vol.98 , pp. 141-147
    • Storch, J.1
  • 25
    • 33744935307 scopus 로고    scopus 로고
    • Protein-membrane interaction and fatty acid transfer from intestinal fatty acid-binding protein to membranes. Support for a multistep process
    • Falomir-Lockhart L.J., Laborde L., Kahn P.C., Storch J., Córsico B. Protein-membrane interaction and fatty acid transfer from intestinal fatty acid-binding protein to membranes. Support for a multistep process. J. Biol. Chem. 2006, 281:13979-13989.
    • (2006) J. Biol. Chem. , vol.281 , pp. 13979-13989
    • Falomir-Lockhart, L.J.1    Laborde, L.2    Kahn, P.C.3    Storch, J.4    Córsico, B.5
  • 26
    • 0036812347 scopus 로고    scopus 로고
    • The effect of charge reversal mutations in the alpha-helical region of liver fatty acid binding protein on the binding of fatty-acyl CoAs, lysophospholipids and bile acids
    • Hagan R.M., Davies J.K., Wilton D.C. The effect of charge reversal mutations in the alpha-helical region of liver fatty acid binding protein on the binding of fatty-acyl CoAs, lysophospholipids and bile acids. Mol. Cell. Biochem. 2002, 239:55-60.
    • (2002) Mol. Cell. Biochem. , vol.239 , pp. 55-60
    • Hagan, R.M.1    Davies, J.K.2    Wilton, D.C.3
  • 27
    • 0032701131 scopus 로고    scopus 로고
    • Liver fatty acid binding protein: species variation and the accommodation of different ligands
    • Thompson J.A., Reese-Wagoner A., Banaszak L. Liver fatty acid binding protein: species variation and the accommodation of different ligands. Biochim. Biophys. Acta 1999, 1441:117-130.
    • (1999) Biochim. Biophys. Acta , vol.1441 , pp. 117-130
    • Thompson, J.A.1    Reese-Wagoner, A.2    Banaszak, L.3
  • 28
    • 23244434183 scopus 로고    scopus 로고
    • Fatty acid transfer from intestinal fatty acid binding protein to membranes: electrostatic and hydrophobic interactions
    • Córsico B., Franchini G.R., Hsu K.T., Storch J. Fatty acid transfer from intestinal fatty acid binding protein to membranes: electrostatic and hydrophobic interactions. J. Lipid Res. 2005, 46:1765-1772.
    • (2005) J. Lipid Res. , vol.46 , pp. 1765-1772
    • Córsico, B.1    Franchini, G.R.2    Hsu, K.T.3    Storch, J.4
  • 29
    • 0020368876 scopus 로고
    • Kinetics of transfer of pyrene and rac-1-oleyl-2-[4-(3-pyrenyl)butanoyl]glycerol between human plasma lipoproteins
    • Charlton S.C., Smith L.C. Kinetics of transfer of pyrene and rac-1-oleyl-2-[4-(3-pyrenyl)butanoyl]glycerol between human plasma lipoproteins. Biochemistry 1982, 21:4023-4030.
    • (1982) Biochemistry , vol.21 , pp. 4023-4030
    • Charlton, S.C.1    Smith, L.C.2
  • 30
    • 0021844418 scopus 로고
    • Physical properties of fatty acyl-CoA. Critical micelle concentrations and micellar size and shape
    • Constantinides P.P., Steim J.M. Physical properties of fatty acyl-CoA. Critical micelle concentrations and micellar size and shape. J. Biol. Chem. 1985, 260:7573-7580.
    • (1985) J. Biol. Chem. , vol.260 , pp. 7573-7580
    • Constantinides, P.P.1    Steim, J.M.2
  • 31
    • 0037489430 scopus 로고    scopus 로고
    • Structural and biochemical characterization of toad liver fatty acid-binding protein
    • Di Pietro S.M., Corsico B., Perduca M., Monaco H.L., Santome J.A. Structural and biochemical characterization of toad liver fatty acid-binding protein. Biochemistry 2003, 42:8192-8203.
    • (2003) Biochemistry , vol.42 , pp. 8192-8203
    • Di Pietro, S.M.1    Corsico, B.2    Perduca, M.3    Monaco, H.L.4    Santome, J.A.5
  • 32
    • 0028307429 scopus 로고
    • Regulation of fluorescent fatty acid transfer from adipocyte and heart fatty acid binding proteins by acceptor membrane lipid composition and structure
    • Wootan M.G., Storch J. Regulation of fluorescent fatty acid transfer from adipocyte and heart fatty acid binding proteins by acceptor membrane lipid composition and structure. J. Biol. Chem. 1994, 269:10517-10523.
    • (1994) J. Biol. Chem. , vol.269 , pp. 10517-10523
    • Wootan, M.G.1    Storch, J.2
  • 33
    • 0030033066 scopus 로고    scopus 로고
    • Role of portal region lysine residues in electrostatic interactions between heart fatty acid binding protein and phospholipid membranes
    • Herr F.M., Aronson J., Storch J. Role of portal region lysine residues in electrostatic interactions between heart fatty acid binding protein and phospholipid membranes. Biochemistry 1996, 35:1296-1303.
    • (1996) Biochemistry , vol.35 , pp. 1296-1303
    • Herr, F.M.1    Aronson, J.2    Storch, J.3
  • 34
    • 0034917381 scopus 로고    scopus 로고
    • Collision-mediated transfer of long-chain fatty acids by neural tissue fatty acid-binding proteins (FABP): studies with fluorescent analogs
    • Thumser A.E., Tsai J., Storch J. Collision-mediated transfer of long-chain fatty acids by neural tissue fatty acid-binding proteins (FABP): studies with fluorescent analogs. J. Mol. Neurosci. 2001, 16:143-150.
    • (2001) J. Mol. Neurosci. , vol.16 , pp. 143-150
    • Thumser, A.E.1    Tsai, J.2    Storch, J.3
  • 36
    • 34248145499 scopus 로고    scopus 로고
    • Kinetic mechanism of ligand binding in human ileal bile acid binding protein as determined by stopped-flow fluorescence analysis
    • Toke O., Monsey J.D., Cistola D.P. Kinetic mechanism of ligand binding in human ileal bile acid binding protein as determined by stopped-flow fluorescence analysis. Biochemistry 2007, 46:5427-5436.
    • (2007) Biochemistry , vol.46 , pp. 5427-5436
    • Toke, O.1    Monsey, J.D.2    Cistola, D.P.3
  • 37
    • 0034705067 scopus 로고    scopus 로고
    • Isolation, characterization and binding properties of two rat liver fatty acid-binding protein isoforms
    • Di Pietro S.M., Santomé J.A. Isolation, characterization and binding properties of two rat liver fatty acid-binding protein isoforms. Biochim. Biophys. Acta 2000, 1478:186-200.
    • (2000) Biochim. Biophys. Acta , vol.1478 , pp. 186-200
    • Di Pietro, S.M.1    Santomé, J.A.2
  • 38
    • 0033991851 scopus 로고    scopus 로고
    • Microsomal fatty acyl-CoA transacylation and hydrolysis: fatty acyl-CoA species dependent modulation by liver fatty acyl-CoA binding proteins
    • Jolly C.A., Wilton D.C., Schroeder F. Microsomal fatty acyl-CoA transacylation and hydrolysis: fatty acyl-CoA species dependent modulation by liver fatty acyl-CoA binding proteins. Biochim. Biophys. Acta 2000, 1483:185-197.
    • (2000) Biochim. Biophys. Acta , vol.1483 , pp. 185-197
    • Jolly, C.A.1    Wilton, D.C.2    Schroeder, F.3
  • 39
    • 0035956863 scopus 로고    scopus 로고
    • Fatty acids and hypolipidemic drugs regulate peroxisome proliferator-activated receptors alpha- and gamma-mediated gene expression via liver fatty acid binding protein: a signaling path to the nucleus
    • Wolfrum C., Borrmann C.M., Börchers T., Spener F. Fatty acids and hypolipidemic drugs regulate peroxisome proliferator-activated receptors alpha- and gamma-mediated gene expression via liver fatty acid binding protein: a signaling path to the nucleus. Proc. Natl. Acad. Sci. U.S.A. 2001, 98:2323-2328.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 2323-2328
    • Wolfrum, C.1    Borrmann, C.M.2    Börchers, T.3    Spener, F.4
  • 41
    • 0039250873 scopus 로고    scopus 로고
    • Binding of fatty acid and peroxisome proliferators to orthologous fatty acid binding proteins from human, murine, and bovine liver
    • Wolfrum C., Borchers T., Sacchettini J.C., Spener F. Binding of fatty acid and peroxisome proliferators to orthologous fatty acid binding proteins from human, murine, and bovine liver. Biochemistry 2000, 39:14363.
    • (2000) Biochemistry , vol.39 , pp. 14363
    • Wolfrum, C.1    Borchers, T.2    Sacchettini, J.C.3    Spener, F.4
  • 42
    • 21444456038 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor alpha interacts with high affinity and is conformationally responsive to endogenous ligands
    • Hostetler H.A., Petrescu A.D., Kier A.B., Schroeder F. Peroxisome proliferator-activated receptor alpha interacts with high affinity and is conformationally responsive to endogenous ligands. J. Biol. Chem. 2005, 280:18667-18682.
    • (2005) J. Biol. Chem. , vol.280 , pp. 18667-18682
    • Hostetler, H.A.1    Petrescu, A.D.2    Kier, A.B.3    Schroeder, F.4
  • 43
    • 0033524415 scopus 로고    scopus 로고
    • Ligand selectivity of the peroxisome proliferator-activated receptor alpha
    • Lin Q., Ruuska S.E., Shaw N.S., Dong D., Noy N. Ligand selectivity of the peroxisome proliferator-activated receptor alpha. Biochemistry 1999, 38:185-190.
    • (1999) Biochemistry , vol.38 , pp. 185-190
    • Lin, Q.1    Ruuska, S.E.2    Shaw, N.S.3    Dong, D.4    Noy, N.5
  • 44
    • 0035862979 scopus 로고    scopus 로고
    • Fatty-acyl-CoA thioesters inhibit recruitment of steroid receptor co-activator 1 to alpha and gamma isoforms of peroxisome-proliferator-activated receptors by competing with agonists
    • Murakami K., Ide T., Nakazawa T., Okazaki T., Mochizuki T., Kadowaki T. Fatty-acyl-CoA thioesters inhibit recruitment of steroid receptor co-activator 1 to alpha and gamma isoforms of peroxisome-proliferator-activated receptors by competing with agonists. Biochem. J. 2001, 353:231-238.
    • (2001) Biochem. J. , vol.353 , pp. 231-238
    • Murakami, K.1    Ide, T.2    Nakazawa, T.3    Okazaki, T.4    Mochizuki, T.5    Kadowaki, T.6


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