메뉴 건너뛰기




Volumn 288, Issue 27, 2013, Pages 19805-19815

Liver fatty acid-binding protein binds monoacylglycerol in vitro and in mouse liver cytosol

Author keywords

[No Author keywords available]

Indexed keywords

EQUILIBRIUM BINDING AFFINITY; FATTY ACID-BINDING PROTEINS; GEL-FILTRATION CHROMATOGRAPHY; INTRACELLULAR TRANSPORT; LOW MOLECULAR WEIGHT; PHOSPHOLIPID MEMBRANE; PHYSIOLOGICAL LIGANDS; SINGLE CHAIN AMPHIPHILES;

EID: 84880067712     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.473579     Document Type: Article
Times cited : (35)

References (52)
  • 1
    • 0035289931 scopus 로고    scopus 로고
    • Intestinal lipid absorption and transport
    • Phan, C. T., and Tso, P. (2001) Intestinal lipid absorption and transport. Front. Biosci. 6, D299-319
    • (2001) Front. Biosci , vol.6
    • Phan, C.T.1    Tso, P.2
  • 4
    • 4544275181 scopus 로고    scopus 로고
    • The endocannabinoid system and its therapeutic exploitation
    • Di Marzo, V., Bifulco, M., and De Petrocellis, L. (2004) The endocannabinoid system and its therapeutic exploitation. Nat. Rev. Drug Discov. 3, 771-784
    • (2004) Nat. Rev. Drug Discov , vol.3 , pp. 771-784
    • Di Marzo, V.1    Bifulco, M.2    De Petrocellis, L.3
  • 6
    • 68349129115 scopus 로고    scopus 로고
    • Peripheral endocannabinoid dysregulation in obesity: Relation to intestinal motility and energy processing induced by food deprivation and re-feeding
    • Izzo, A. A., Piscitelli, F., Capasso, R., Aviello, G., Romano, B., Borrelli, F., Petrosino, S., and Di Marzo, V. (2009) Peripheral endocannabinoid dysregulation in obesity: relation to intestinal motility and energy processing induced by food deprivation and re-feeding. Br. J. Pharmacol. 158, 451-461
    • (2009) Br. J. Pharmacol , vol.158 , pp. 451-461
    • Izzo, A.A.1    Piscitelli, F.2    Capasso, R.3    Aviello, G.4    Romano, B.5    Borrelli, F.6    Petrosino, S.7    Di Marzo, V.8
  • 7
    • 36549015066 scopus 로고    scopus 로고
    • The endocannabinoid system and gut-brain signalling
    • Storr, M. A., and Sharkey, K. A. (2007) The endocannabinoid system and gut-brain signalling. Curr. Opin. Pharmacol. 7, 575-582
    • (2007) Curr. Opin. Pharmacol , vol.7 , pp. 575-582
    • Storr, M.A.1    Sharkey, K.A.2
  • 9
    • 84865469104 scopus 로고    scopus 로고
    • Over-expression of monoacylglycerol lipase (MGL) in small intestine alters endocannabinoid levels and whole body energy balance, resulting in obesity
    • Chon, S. H., Douglass, J. D., Zhou, Y. X., Malik, N., Dixon, J. L., Brinker, A., Quadro, L., and Storch, J. (2012) Over-expression of monoacylglycerol lipase (MGL) in small intestine alters endocannabinoid levels and whole body energy balance, resulting in obesity. PLoS One 7, e43962
    • (2012) PLoS One , vol.7
    • Chon, S.H.1    Douglass, J.D.2    Zhou, Y.X.3    Malik, N.4    Dixon, J.L.5    Brinker, A.6    Quadro, L.7    Storch, J.8
  • 10
    • 0034785683 scopus 로고    scopus 로고
    • Common mechanisms of monoacylglycerol and fatty acid uptake by human intestinal Caco-2 cells
    • Ho, S. Y., and Storch, J. (2001) Common mechanisms of monoacylglycerol and fatty acid uptake by human intestinal Caco-2 cells. Am. J. Physiol. Cell Physiol. 281, C1106-C1117
    • (2001) Am. J. Physiol. Cell Physiol , vol.281
    • Ho, S.Y.1    Storch, J.2
  • 11
    • 22144460188 scopus 로고    scopus 로고
    • Uptake of micellar long-chain fatty acid and sn-2-monoacylglycerol into human intestinal Caco-2 cells exhibits characteristics of protein-mediated transport
    • Murota, K., and Storch, J. (2005) Uptake of micellar long-chain fatty acid and sn-2-monoacylglycerol into human intestinal Caco-2 cells exhibits characteristics of protein-mediated transport. J. Nutr. 135, 1626-1630
    • (2005) J. Nutr , vol.135 , pp. 1626-1630
    • Murota, K.1    Storch, J.2
  • 12
    • 0034717896 scopus 로고    scopus 로고
    • The fatty acid transport function of fatty acid-binding proteins
    • Storch, J., and Thumser, A. E. (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.E.2
  • 13
    • 50949128339 scopus 로고    scopus 로고
    • The emerging functions and mechanisms of mammalian fatty acid-binding proteins
    • Storch, J., and Corsico, B. (2008) The emerging functions and mechanisms of mammalian fatty acid-binding proteins. Annu. Rev. Nutr. 28, 73-95
    • (2008) Annu. Rev. Nutr , vol.28 , pp. 73-95
    • Storch, J.1    Corsico, B.2
  • 15
    • 0030443383 scopus 로고    scopus 로고
    • The binding of cholesterol and bile salts to recombinant rat liver fatty acid-binding protein
    • Thumser, A. E., 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.E.1    Wilton, D.C.2
  • 16
    • 0027323806 scopus 로고
    • Diversity of fatty acid-binding protein structure and function: Studies with fluorescent ligands
    • Storch, J. (1993) Diversity of fatty acid-binding protein structure and function: studies with fluorescent ligands. Mol. Cell. Biochem. 123, 45-53
    • (1993) Mol. Cell. Biochem , vol.123 , pp. 45-53
    • Storch, J.1
  • 17
    • 0034004499 scopus 로고    scopus 로고
    • Liver and intestinal fatty acid-binding proteins obtain fatty acids from phospholipid membranes by different mechanisms
    • Thumser, A. E., and Storch, J. (2000) Liver and intestinal fatty acid-binding proteins obtain fatty acids from phospholipid membranes by different mechanisms. J. Lipid Res. 41, 647-656
    • (2000) J. Lipid Res , vol.41 , pp. 647-656
    • Thumser, A.E.1    Storch, J.2
  • 18
    • 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., and Stark, R. E. (2007) Solution-state molecular structure of apo and oleate-liganded liver fatty acid-binding protein. Biochemistry 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
  • 20
    • 0029997106 scopus 로고    scopus 로고
    • Fatty acid transfer in taurodeoxycholate mixed micelles
    • Narayanan, V. S., and Storch, J. (1996) Fatty acid transfer in taurodeoxycholate mixed micelles. Biochemistry 35, 7466-7473
    • (1996) Biochemistry , vol.35 , pp. 7466-7473
    • Narayanan, V.S.1    Storch, J.2
  • 21
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254
    • (1976) Anal. Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 22
    • 0038498152 scopus 로고    scopus 로고
    • Decreased liver fatty acid binding capacity and altered liver lipid distribution in mice lacking the liver fatty acid-binding protein gene
    • Martin, G. G., Danneberg, H., Kumar, L. S., Atshaves, B. P., Erol, E., Bader, M., Schroeder, F., and Binas, B. (2003) Decreased liver fatty acid binding capacity and altered liver lipid distribution in mice lacking the liver fatty acid-binding protein gene. J. Biol. Chem. 278, 21429-21438
    • (2003) J. Biol. Chem , vol.278 , pp. 21429-21438
    • Martin, G.G.1    Danneberg, H.2    Kumar, L.S.3    Atshaves, B.P.4    Erol, E.5    Bader, M.6    Schroeder, F.7    Binas, B.8
  • 23
    • 0020545022 scopus 로고
    • A radiochemical procedure for the assay of fatty acid binding by proteins
    • Glatz, J. F., 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.F.1    Veerkamp, J.H.2
  • 24
    • 79951870969 scopus 로고    scopus 로고
    • A nuclear magnetic resonance-based structural rationale for contrasting stoichiometry and ligand binding site(s) in fatty acid-binding proteins
    • He, Y., Estephan, R., Yang, X., Vela, A., Wang, H., Bernard, C., and Stark, R. E. (2011) A nuclear magnetic resonance-based structural rationale for contrasting stoichiometry and ligand binding site(s) in fatty acid-binding proteins. Biochemistry 50, 1283-1295
    • (2011) Biochemistry , vol.50 , pp. 1283-1295
    • He, Y.1    Estephan, R.2    Yang, X.3    Vela, A.4    Wang, H.5    Bernard, C.6    Stark, R.E.7
  • 25
    • 0006925492 scopus 로고
    • Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity
    • Kay, L. E., Keifer, P., and Saarinen, T. (1992) Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity. J. Am. Chem. Soc. 114, 10663-10665
    • (1992) J. Am. Chem. Soc , vol.114 , pp. 10663-10665
    • Kay, L.E.1    Keifer, P.2    Saarinen, T.3
  • 26
    • 0028393784 scopus 로고
    • The 13C chemical-shift index: A simple method for the identification of protein secondary structure using 13C chemical-shift data
    • Wishart, D. S., and Sykes, B. D. (1994) The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data. J. Biomol. NMR 4, 171-180
    • (1994) J. Biomol. NMR , vol.4 , pp. 171-180
    • Wishart, D.S.1    Sykes, B.D.2
  • 27
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax, A. (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6, 277-293
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 28
    • 34249765651 scopus 로고
    • NMR View: A computer program for the visualization and analysis ofNMRdata
    • Johnson, B. A., and Blevins, R. A. (1994) NMR View: a computer program for the visualization and analysis ofNMRdata. J. Biomol.NMR4, 603-614
    • (1994) J. Biomol.NMR , vol.4 , pp. 603-614
    • Johnson, B.A.1    Blevins, R.A.2
  • 29
    • 0033543577 scopus 로고    scopus 로고
    • Altered flexibility in the substrate-binding site of related native and engineered highalkaline Bacillus subtilisins
    • Mulder, F. A., Schipper, D., Bott, R., and Boelens, R. (1999) Altered flexibility in the substrate-binding site of related native and engineered highalkaline Bacillus subtilisins. J. Mol. Biol. 292, 111-123
    • (1999) J. Mol. Biol , vol.292 , pp. 111-123
    • Mulder, F.A.1    Schipper, D.2    Bott, R.3    Boelens, R.4
  • 30
    • 0016360614 scopus 로고
    • Preparation of homogeneous, single-walled phosphatidylcholine vesicles
    • Huang, C., and Thompson, T. E. (1974) Preparation of homogeneous, single-walled phosphatidylcholine vesicles. Methods Enzymol. 32, 485-489
    • (1974) Methods Enzymol , vol.32 , pp. 485-489
    • Huang, C.1    Thompson, T.E.2
  • 31
    • 0001022995 scopus 로고
    • A modification of the colorimetric phosphorus determination for use with the photoelectric colorimeter
    • Gomori, G. (1942) A modification of the colorimetric phosphorus determination for use with the photoelectric colorimeter. J. Lab. Clin. Med. 27, 955-960
    • (1942) J. Lab. Clin. Med , vol.27 , pp. 955-960
    • Gomori, G.1
  • 32
    • 33847682952 scopus 로고
    • Correction of fluorescence spectra and measurement of fluorescence quantum efficiency
    • Parker, C. A., and Rees, W. T. (1960) Correction of fluorescence spectra and measurement of fluorescence quantum efficiency. Analyst 85, 587-600
    • (1960) Analyst , vol.85 , pp. 587-600
    • Parker, C.A.1    Rees, W.T.2
  • 33
    • 30244573126 scopus 로고
    • Emission properties of NADH. Studies of fluorescence lifetimes and quantum efficiencies of NADH, AcPyADH, and simplified synthetic models
    • Scott, T. G., Spencer, R. D., Leonard, N. J., and Weber, G. (1970) Emission properties of NADH. Studies of fluorescence lifetimes and quantum efficiencies of NADH, AcPyADH, and simplified synthetic models. J. Am. Chem. Soc. 92, 687-695
    • (1970) J. Am. Chem. Soc , vol.92 , pp. 687-695
    • Scott, T.G.1    Spencer, R.D.2    Leonard, N.J.3    Weber, G.4
  • 34
    • 0022448658 scopus 로고
    • Transfer of long-chain fluorescent free fatty acids between unilamellar vesicles
    • Storch, J., and Kleinfeld, A. M. (1986) Transfer of long-chain fluorescent free fatty acids between unilamellar vesicles. Biochemistry 25, 1717-1726
    • (1986) Biochemistry , vol.25 , pp. 1717-1726
    • Storch, J.1    Kleinfeld, A.M.2
  • 35
    • 0025331970 scopus 로고
    • Transfer of fluorescent fatty acids from liver and heart fatty acid-binding proteins to model membranes
    • Storch, J., and Bass, N. M. (1990) Transfer of fluorescent fatty acids from liver and heart fatty acid-binding proteins to model membranes. J. Biol. Chem. 265, 7827-7831
    • (1990) J. Biol. Chem , vol.265 , pp. 7827-7831
    • Storch, J.1    Bass, N.M.2
  • 36
    • 0027317365 scopus 로고
    • Mechanism of fluorescent fatty acid transfer from adipocyte fatty acid binding protein to membranes
    • Wootan, M. G., Bernlohr, D. A., and Storch, J. (1993) Mechanism of fluorescent fatty acid transfer from adipocyte fatty acid binding protein to membranes. Biochemistry 32, 8622-8627
    • (1993) Biochemistry , vol.32 , pp. 8622-8627
    • Wootan, M.G.1    Bernlohr, D.A.2    Storch, J.3
  • 37
    • 0037197669 scopus 로고    scopus 로고
    • Titration and exchange studies of liver fatty acidbinding protein with 13C-labeled long-chain fatty acids
    • Wang, H., He, Y., Kroenke, C. D., Kodukula, S., Storch, J., Palmer, A. G., and Stark, R. E. (2002) Titration and exchange studies of liver fatty acidbinding protein with 13C-labeled long-chain fatty acids. Biochemistry 41, 5453-5461
    • (2002) Biochemistry , vol.41 , pp. 5453-5461
    • Wang, H.1    He, Y.2    Kroenke, C.D.3    Kodukula, S.4    Storch, J.5    Palmer, A.G.6    Stark, R.E.7
  • 38
    • 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
  • 39
    • 0019401036 scopus 로고
    • Emission wavelength-dependent decay of the 9-anthroyloxy-fatty acid membrane probes
    • Matayoshi, E. D., and Kleinfeld, A. M. (1981) Emission wavelength-dependent decay of the 9-anthroyloxy-fatty acid membrane probes. Biophys. J. 35, 215-235
    • (1981) Biophys. J. , vol.35 , pp. 215-235
    • Matayoshi, E.D.1    Kleinfeld, A.M.2
  • 40
    • 0026556949 scopus 로고
    • Free fatty acid transfer from rat liver fatty acid-binding protein to phospholipid vesicles. Effect of ligand and solution properties
    • Kim, H. K., and Storch, J. (1992) Free fatty acid transfer from rat liver fatty acid-binding protein to phospholipid vesicles. Effect of ligand and solution properties. J. Biol. Chem. 267, 77-82
    • (1992) J. Biol. Chem , vol.267 , pp. 77-82
    • Kim, H.K.1    Storch, J.2
  • 41
    • 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., and Storch, J. (1996) Fatty acid transfer from liver and intestinal fatty acid-binding proteins to membranes occurs by different mechanisms. J. Biol. Chem. 271, 13317-13323
    • (1996) J. Biol. Chem , vol.271 , pp. 13317-13323
    • Hsu, K.T.1    Storch, J.2
  • 43
    • 0023837979 scopus 로고
    • Interactions of oleic acid with liver fatty acid binding protein: A carbon-13 NMR study
    • Cistola, D. P., Walsh, M. T., Corey, R. P., Hamilton, J. A., and Brecher, P. (1988) Interactions of oleic acid with liver fatty acid binding protein: a carbon-13 NMR study. Biochemistry 27, 711-717
    • (1988) Biochemistry , vol.27 , pp. 711-717
    • Cistola, D.P.1    Walsh, M.T.2    Corey, R.P.3    Hamilton, J.A.4    Brecher, P.5
  • 44
    • 0022363731 scopus 로고
    • Spectroscopic investigations on the binding site of bovine hepatic fatty acid binding protein. Evidence for the existence of a single binding site for two fatty acid molecules
    • Keuper, H. J., Klein, R. A., and Spener, F. (1985) Spectroscopic investigations on the binding site of bovine hepatic fatty acid binding protein. Evidence for the existence of a single binding site for two fatty acid molecules. Chem. Phys. Lipids 38, 159-173
    • (1985) Chem. Phys. Lipids , vol.38 , pp. 159-173
    • Keuper, H.J.1    Klein, R.A.2    Spener, F.3
  • 45
    • 0028071589 scopus 로고
    • The binding of lysophospholipids to rat liver fatty acid-binding protein and albumin
    • Thumser, A. E., Voysey, J. E., and Wilton, D. C. (1994) The binding of lysophospholipids to rat liver fatty acid-binding protein and albumin. Biochem. J. 301, 801-806
    • (1994) Biochem. J. , vol.301 , pp. 801-806
    • Thumser, A.E.1    Voysey, J.E.2    Wilton, D.C.3
  • 46
    • 0027943460 scopus 로고
    • Immunological identity of rat liver cytosolic heme-binding protein with purified and recombinant liver fatty acid binding protein by Western blots of two-dimensional gels
    • Epstein, L. F., Bass, N. M., Iwahara, S., Wilton, D. C., and Muller-Eberhard, U. (1994) Immunological identity of rat liver cytosolic heme-binding protein with purified and recombinant liver fatty acid binding protein by Western blots of two-dimensional gels. Biochem. Biophys. Res. Commun. 204, 163-168
    • (1994) Biochem. Biophys. Res. Commun , vol.204 , pp. 163-168
    • Epstein, L.F.1    Bass, N.M.2    Iwahara, S.3    Wilton, D.C.4    Muller-Eberhard, U.5
  • 47
    • 0028793378 scopus 로고
    • Molecular cloning, expression, and characterization of a human intestinal 15-kDa protein
    • Fujita, M., Fujii, H., Kanda, T., Sato, E., Hatakeyama, K., and Ono, T. (1995) Molecular cloning, expression, and characterization of a human intestinal 15-kDa protein. Eur. J. Biochem. 233, 406-413
    • (1995) Eur. J. Biochem , vol.233 , pp. 406-413
    • Fujita, M.1    Fujii, H.2    Kanda, T.3    Sato, E.4    Hatakeyama, K.5    Ono, T.6
  • 49
    • 0026480569 scopus 로고
    • Spontaneous lipid transfer between organized lipid assemblies
    • Brown, R. E. (1992) Spontaneous lipid transfer between organized lipid assemblies. Biochim. Biophys. Acta 1113, 375-389
    • (1992) Biochim. Biophys. Acta , vol.1113 , pp. 375-389
    • Brown, R.E.1
  • 50
    • 0019316919 scopus 로고
    • Mechanism of the spontaneous transfer of phospholipids between bilayers
    • Roseman, M. A., and Thompson, T. E. (1980) Mechanism of the spontaneous transfer of phospholipids between bilayers. Biochemistry 19, 439-444
    • (1980) Biochemistry , vol.19 , pp. 439-444
    • Roseman, M.A.1    Thompson, T.E.2
  • 51
    • 0025164099 scopus 로고
    • Historic overview of studies on fatty acid-binding proteins
    • Ockner, R. K. (1990) Historic overview of studies on fatty acid-binding proteins. Mol. Cell. Biochem. 98, 3-9
    • (1990) Mol. Cell. Biochem , vol.98 , pp. 3-9
    • Ockner, R.K.1
  • 52
    • 65549113847 scopus 로고    scopus 로고
    • Identification of intracellular carriers for the endocannabinoid anandamide
    • Kaczocha, M., Glaser, S. T., and Deutsch, D. G. (2009) Identification of intracellular carriers for the endocannabinoid anandamide. Proc. Natl. Acad. Sci. U.S.A. 106, 6375-6380
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 6375-6380
    • Kaczocha, M.1    Glaser, S.T.2    Deutsch, D.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.