메뉴 건너뛰기




Volumn 410, Issue 1, 2008, Pages 123-129

The interaction of liver fatty-acid-binding protein (FABP) with anionic phospholipid vesicles: Is there extended phospholipid anchorage under these conditions?

Author keywords

Fatty acid binding protein (FABP); Fluorescence; Liver; Membrane anchorage; Phospholipid; Vesicle

Indexed keywords

BINDING SITES; CELL MEMBRANES; LIGANDS; PHOSPHOLIPIDS; PROTEINS;

EID: 39749170233     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20071109     Document Type: Article
Times cited : (12)

References (37)
  • 1
  • 2
    • 0030239495 scopus 로고    scopus 로고
    • Cellular fatty acid-binding proteins: Their function and physiological significance
    • Glatz, J. F. C. and van der Vusse, G. J. (1996) Cellular fatty acid-binding proteins: their function and physiological significance. Prog. Lipid Res. 35, 243-282
    • (1996) Prog. Lipid Res , vol.35 , pp. 243-282
    • Glatz, J.F.C.1    van der Vusse, G.J.2
  • 3
    • 0034717896 scopus 로고    scopus 로고
    • The fatty acid transport function of fatty acid-binding proteins
    • Storch, J. and Thumser, A. A. (2000) The fatty acid transport function of fatty acid-binding proteins. Biochim. Biophys. Acta 1486, 28-44
    • (2000) Biochim. Biophys. Acta , vol.1486 , pp. 28-44
    • Storch, J.1    Thumser, A.A.2
  • 4
    • 0043253165 scopus 로고    scopus 로고
    • The mammalian fatty acid-binding protein multigene family: Molecular and genetic insights into function
    • Hertzel, A. V. and Bernlohr, D. A. (2000) The mammalian fatty acid-binding protein multigene family: molecular and genetic insights into function. Trends Endocrinol. Metab. 11, 175-180
    • (2000) Trends Endocrinol. Metab , vol.11 , pp. 175-180
    • Hertzel, A.V.1    Bernlohr, D.A.2
  • 6
    • 0032557156 scopus 로고    scopus 로고
    • Physiological properties and functions of intracellular fatty acid-binding proteins
    • Coe, N. R. and Bernlohr, D. A. (1998) Physiological properties and functions of intracellular fatty acid-binding proteins. Biochim. Biophys. Acta 1391, 287-306
    • (1998) Biochim. Biophys. Acta , vol.1391 , pp. 287-306
    • Coe, N.R.1    Bernlohr, D.A.2
  • 7
    • 0034988023 scopus 로고    scopus 로고
    • Unravelling the significance of cellular fatty acid-binding proteins
    • Glatz, J. F. C. and Storch, J. (2001) Unravelling the significance of cellular fatty acid-binding proteins. Curr. Opin. Lipidol. 12, 267-274
    • (2001) Curr. Opin. Lipidol , vol.12 , pp. 267-274
    • Glatz, J.F.C.1    Storch, J.2
  • 8
    • 3242669109 scopus 로고    scopus 로고
    • Fatty acid-binding proteins - insights from genetic manipulations
    • Haunerland, N. H. and Spener, F. (2004) Fatty acid-binding proteins - insights from genetic manipulations. Prog. Lipid Res. 43, 328-349
    • (2004) Prog. Lipid Res , vol.43 , pp. 328-349
    • Haunerland, N.H.1    Spener, F.2
  • 9
    • 0033592916 scopus 로고    scopus 로고
    • Binding of recombinant rat liver fatty acid-binding protein to small anionic phospholipid vesicles results in ligand release: A model for interfacial binding and fatty acid targeting
    • Davies, J. K., Thumser, A. A. and Wilton, D. C. (1999) Binding of recombinant rat liver fatty acid-binding protein to small anionic phospholipid vesicles results in ligand release: a model for interfacial binding and fatty acid targeting. Biochemistry 38, 16932-16940
    • (1999) Biochemistry , vol.38 , pp. 16932-16940
    • Davies, J.K.1    Thumser, A.A.2    Wilton, D.C.3
  • 10
    • 0037073726 scopus 로고    scopus 로고
    • Effect of charge reversal mutations on the ligand- and membrane-binding properties of liver fatty acid-binding protein
    • Davies, J. K., Hagan, R. M. and Wilton, D. C. (2002) Effect of charge reversal mutations on the ligand- and membrane-binding properties of liver fatty acid-binding protein. J. Biol. Chem. 277, 48395-48402
    • (2002) J. Biol. Chem , vol.277 , pp. 48395-48402
    • Davies, J.K.1    Hagan, R.M.2    Wilton, D.C.3
  • 11
    • 0025841667 scopus 로고
    • Membrane-binding induces destabilization of cytochrome-c structure
    • Muga, A., Mantsch, H. H. and Surewicz, W. K. (1991) Membrane-binding induces destabilization of cytochrome-c structure. Biochemistry 30, 7219-7224
    • (1991) Biochemistry , vol.30 , pp. 7219-7224
    • Muga, A.1    Mantsch, H.H.2    Surewicz, W.K.3
  • 12
    • 0027963594 scopus 로고
    • Thermotropic behavior of dimyristoylphosphatidylglycerol and its interaction with cytochrome c
    • Heimburg, T. and Biltonen, R. L. (1994) Thermotropic behavior of dimyristoylphosphatidylglycerol and its interaction with cytochrome c. Biochemistry 33, 9477-9488
    • (1994) Biochemistry , vol.33 , pp. 9477-9488
    • Heimburg, T.1    Biltonen, R.L.2
  • 13
    • 0039178090 scopus 로고    scopus 로고
    • Membrane location of spin-labeled cytochrome c determined by paramagnetic relaxation agents
    • Kostrzewa, A., Pali, T., Froncisz, W. and Marsh, D. (2000) Membrane location of spin-labeled cytochrome c determined by paramagnetic relaxation agents. Biochemistry 39, 6066-6074
    • (2000) Biochemistry , vol.39 , pp. 6066-6074
    • Kostrzewa, A.1    Pali, T.2    Froncisz, W.3    Marsh, D.4
  • 14
    • 0032485854 scopus 로고    scopus 로고
    • Multiple conformations of physiological membrane-bound cytochrome c
    • Cortese, J. D., Voglino, A. L. and Hackenbrock, C. R. (1998) Multiple conformations of physiological membrane-bound cytochrome c. Biochemistry 37, 6402-6409
    • (1998) Biochemistry , vol.37 , pp. 6402-6409
    • Cortese, J.D.1    Voglino, A.L.2    Hackenbrock, C.R.3
  • 15
    • 0033946882 scopus 로고    scopus 로고
    • Unfolding and refolding of cytochrome c driven by the interaction with lipid micelles
    • Sanghera, N. and Pinheiro, T. T. (2000) Unfolding and refolding of cytochrome c driven by the interaction with lipid micelles. Protein Sci. 9, 1194-1202
    • (2000) Protein Sci , vol.9 , pp. 1194-1202
    • Sanghera, N.1    Pinheiro, T.T.2
  • 16
    • 0037088593 scopus 로고    scopus 로고
    • Phospholipid-cytochrome c interaction - evidence for the extended lipid anchorage
    • Tuominen, E. K. J., Wallace, C. J. A. and Kinnunen, P. K. J. (2002) Phospholipid-cytochrome c interaction - evidence for the extended lipid anchorage. J. Biol. Chem. 277, 8822-8826
    • (2002) J. Biol. Chem , vol.277 , pp. 8822-8826
    • Tuominen, E.K.J.1    Wallace, C.J.A.2    Kinnunen, P.K.J.3
  • 18
    • 0345313659 scopus 로고    scopus 로고
    • β-lactoglobulin binds palmitate within its central cavity
    • Wu, S. Y., Perez, M. D., Puyol, P. and Sawyer, L. (1999) β-lactoglobulin binds palmitate within its central cavity. J. Biol. Chem. 274, 170-174
    • (1999) J. Biol. Chem , vol.274 , pp. 170-174
    • Wu, S.Y.1    Perez, M.D.2    Puyol, P.3    Sawyer, L.4
  • 19
    • 33646889069 scopus 로고    scopus 로고
    • Conformational changes of β-lactoglobulin induced by anionic phospholipid
    • Liu, X. H., Shang, L., Jiang, X., Dong, S. J. and Wang, E. K. (2006) Conformational changes of β-lactoglobulin induced by anionic phospholipid. Biophys. Chem. 121, 218-223
    • (2006) Biophys. Chem , vol.121 , pp. 218-223
    • Liu, X.H.1    Shang, L.2    Jiang, X.3    Dong, S.J.4    Wang, E.K.5
  • 20
    • 33745830875 scopus 로고    scopus 로고
    • Lipid-induced conformational transitions of β-lactoglobulin
    • Zhang, X. Q. and Keiderling, T. A. (2006) Lipid-induced conformational transitions of β-lactoglobulin. Biochemistry 45, 8444-8452
    • (2006) Biochemistry , vol.45 , pp. 8444-8452
    • Zhang, X.Q.1    Keiderling, T.A.2
  • 21
    • 34247621709 scopus 로고    scopus 로고
    • Electrostatic and hydrophobic interactions governing the interaction and binding of β-lactoglobulin to membranes
    • Zhang, X. Q., Ge, N. and Keiderling, T. A. (2007) Electrostatic and hydrophobic interactions governing the interaction and binding of β-lactoglobulin to membranes. Biochemistry 46, 5252-5260
    • (2007) Biochemistry , vol.46 , pp. 5252-5260
    • Zhang, X.Q.1    Ge, N.2    Keiderling, T.A.3
  • 22
    • 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. and Wilton, D. C. (2005) Tryptophan insertion mutagenesis of liver fatty acid-binding protein - L28W mutant provides important insights into ligand binding and physiological function. J. Biol. Chem. 280, 1782-1789
    • (2005) J. Biol. Chem , vol.280 , pp. 1782-1789
    • Hagan, R.M.1    Worner-Gibbs, J.2    Wilton, D.C.3
  • 23
    • 0345492016 scopus 로고    scopus 로고
    • Lipid-protein interactions studied by introduction of a tryptophan residue: The mechanosensitive channel MscL
    • Powl, A. M., East, J. M. and Lee, A. G. (2003) Lipid-protein interactions studied by introduction of a tryptophan residue: the mechanosensitive channel MscL. Biochemistry 42, 14306-14317
    • (2003) Biochemistry , vol.42 , pp. 14306-14317
    • Powl, A.M.1    East, J.M.2    Lee, A.G.3
  • 24
    • 0025863749 scopus 로고
    • Synthesis of a gene for rat liver fatty-acid-binding protein and its expression in Escherichia coli
    • Worrall, A. F., Evans, C. and Wilton, D. C. (1991) Synthesis of a gene for rat liver fatty-acid-binding protein and its expression in Escherichia coli. Biochem. J. 278, 365-368
    • (1991) Biochem. J , vol.278 , pp. 365-368
    • Worrall, A.F.1    Evans, C.2    Wilton, D.C.3
  • 25
    • 0028285129 scopus 로고
    • Characterization of binding and structural properties of rat liver fatty-acid-binding protein using tryptophan mutants
    • Thumser, A. A. and Wilton, D. C. (1994) Characterization of binding and structural properties of rat liver fatty-acid-binding protein using tryptophan mutants. Biochem. J. 300, 827-833
    • (1994) Biochem. J , vol.300 , pp. 827-833
    • Thumser, A.A.1    Wilton, D.C.2
  • 26
    • 0020545022 scopus 로고
    • A radiochemical procedure for the assay of fatty acid binding by proteins
    • Glatz, J. C. and Veerkamp, J. H. (1983) A radiochemical procedure for the assay of fatty acid binding by proteins. Anal. Biochem. 132, 89-95
    • (1983) Anal. Biochem , vol.132 , pp. 89-95
    • Glatz, J.C.1    Veerkamp, J.H.2
  • 27
    • 0030443383 scopus 로고    scopus 로고
    • The binding of cholesterol and bile salts to recombinant rat liver fatty acid-binding protein
    • Thumser, A. A. and Wilton, D. C. (1996) The binding of cholesterol and bile salts to recombinant rat liver fatty acid-binding protein. Biochem. J. 320, 729-733
    • (1996) Biochem. J , vol.320 , pp. 729-733
    • Thumser, A.A.1    Wilton, D.C.2
  • 28
    • 0025051457 scopus 로고
    • Quenching of tryptophan fluorescence by brominated phospholipid
    • Bolen, E. J. and Holloway, P. W. (1990) Quenching of tryptophan fluorescence by brominated phospholipid. Biochemistry 29, 9638-9643
    • (1990) Biochemistry , vol.29 , pp. 9638-9643
    • Bolen, E.J.1    Holloway, P.W.2
  • 29
    • 0035899991 scopus 로고    scopus 로고
    • Self-association of model transmembrane alpha-helices is modulated by lipid structure
    • Mall, S., Broadbridge, R., Sharma, R. P., East, J. M. and Lee, A. G. (2001) Self-association of model transmembrane alpha-helices is modulated by lipid structure. Biochemistry 40, 12379-12386
    • (2001) Biochemistry , vol.40 , pp. 12379-12386
    • Mall, S.1    Broadbridge, R.2    Sharma, R.P.3    East, J.M.4    Lee, A.G.5
  • 30
    • 0023111150 scopus 로고
    • Determination of the depth of bromine atoms in bilayers formed from bromolipid probes
    • McIntosh, T. J. and Holloway, P. W. (1987) Determination of the depth of bromine atoms in bilayers formed from bromolipid probes. Biochemistry 26, 1783-1788
    • (1987) Biochemistry , vol.26 , pp. 1783-1788
    • McIntosh, T.J.1    Holloway, P.W.2
  • 31
    • 0000146432 scopus 로고    scopus 로고
    • Distance-dependent fluorescence quenching of p-bis[2-(5- phenyloxazolyl)]benzene by various quenchers
    • Zelent, B., Kusba, J., Gryczynski, I., Johnson, M. L. and Lakowicz, J. R. (1996) Distance-dependent fluorescence quenching of p-bis[2-(5- phenyloxazolyl)]benzene by various quenchers. J. Phys. Chem. 100, 18592-18602
    • (1996) J. Phys. Chem , vol.100 , pp. 18592-18602
    • Zelent, B.1    Kusba, J.2    Gryczynski, I.3    Johnson, M.L.4    Lakowicz, J.R.5
  • 32
    • 0027096161 scopus 로고
    • Refinement of the structure of Escherichia coli-derived rat intestinal fatty-acid binding-protein with bound oleate to 1.75-Å resolution - correlation with the structures of the apoprotein and the protein with bound palmitate
    • Sacchettini, J. C., Scapin, G., Gopaul, D. and Gordon, J. I. (1992) Refinement of the structure of Escherichia coli-derived rat intestinal fatty-acid binding-protein with bound oleate to 1.75-Å resolution - correlation with the structures of the apoprotein and the protein with bound palmitate. J. Biol. Chem. 267, 23534-23545
    • (1992) J. Biol. Chem , vol.267 , pp. 23534-23545
    • Sacchettini, J.C.1    Scapin, G.2    Gopaul, D.3    Gordon, J.I.4
  • 33
    • 0028040301 scopus 로고
    • Equilibrium folding studies of cellular retinoic acid binding protein, a predominantly β-sheet protein
    • Liu, Z. P., Rizo, J. and Gierasch, L. M. (1994) Equilibrium folding studies of cellular retinoic acid binding protein, a predominantly β-sheet protein. Biochemistry 33, 134-142
    • (1994) Biochemistry , vol.33 , pp. 134-142
    • Liu, Z.P.1    Rizo, J.2    Gierasch, L.M.3
  • 34
    • 0029740071 scopus 로고    scopus 로고
    • Non-native alpha-helical intermediate in the refolding of lactoglobulin, a predominantly β-sheet protein
    • Hamada, D., Goto, Y. and Segawa, S. I. (1996) Non-native alpha-helical intermediate in the refolding of lactoglobulin, a predominantly β-sheet protein. Nat. Struct. Biol. 3, 868-873
    • (1996) Nat. Struct. Biol , vol.3 , pp. 868-873
    • Hamada, D.1    Goto, Y.2    Segawa, S.I.3
  • 35
    • 0042667012 scopus 로고    scopus 로고
    • Structural analysis of lipid complexes of GM2-activator protein
    • Wright, C. S., Zhao, Q. and Rastinejad, F. (2003) Structural analysis of lipid complexes of GM2-activator protein. J. Mol. Biol. 331, 951-964
    • (2003) J. Mol. Biol , vol.331 , pp. 951-964
    • Wright, C.S.1    Zhao, Q.2    Rastinejad, F.3
  • 36
    • 0032906887 scopus 로고    scopus 로고
    • The liver fatty acid binding protein - comparison of cavity properties of intracellular lipid binding proteins
    • Thompson, J., Ory, J., Reese-Wagoner, A. and Banaszak, L. (1999) The liver fatty acid binding protein - comparison of cavity properties of intracellular lipid binding proteins. Mol. Cell. Biochem. 192, 9-16
    • (1999) Mol. Cell. Biochem , vol.192 , pp. 9-16
    • Thompson, J.1    Ory, J.2    Reese-Wagoner, A.3    Banaszak, L.4
  • 37
    • 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. and Banaszak, L. (1997) The crystal structure of the liver fatty acid-binding protein - a complex with two bound oleates. 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.