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Volumn 1781, Issue 6-7, 2008, Pages 314-320

Activation of PPARγ reverses a defect of surfactant synthesis in mice lacking two types of fatty acid binding protein

Author keywords

Fatty acid binding protein; Fatty acid signaling; Lung compliance; Phospholipid synthesis; Surfactant organisation

Indexed keywords

FATTY ACID BINDING PROTEIN; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA; PIOGLITAZONE; SURFACTANT; 2,4 THIAZOLIDINEDIONE DERIVATIVE; ANTIDIABETIC AGENT; LUNG SURFACTANT; PRIMER DNA;

EID: 48749109440     PISSN: 13881981     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbalip.2008.04.010     Document Type: Article
Times cited : (11)

References (44)
  • 1
    • 0036283121 scopus 로고    scopus 로고
    • PPARs: transcriptional effectors of fatty acids and their derivatives
    • Hihi A.K., Michalik L., and Wahli W. PPARs: transcriptional effectors of fatty acids and their derivatives. Cell. Mol. Life Sci. 59 (2002) 790-798
    • (2002) Cell. Mol. Life Sci. , vol.59 , pp. 790-798
    • Hihi, A.K.1    Michalik, L.2    Wahli, W.3
  • 2
    • 0037396839 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptors beta/delta: emerging roles for a previously neglected third family member
    • Michalik L., Desvergne B., and Wahli W. Peroxisome proliferator-activated receptors beta/delta: emerging roles for a previously neglected third family member. Curr. Opin. Lipidol. 14 (2003) 129-135
    • (2003) Curr. Opin. Lipidol. , vol.14 , pp. 129-135
    • Michalik, L.1    Desvergne, B.2    Wahli, W.3
  • 3
    • 0037900979 scopus 로고    scopus 로고
    • Minireview: lipid metabolism, metabolic diseases, and peroxisome proliferator-activated receptors
    • Lee C.H., Olson P., and Evans R.M. Minireview: lipid metabolism, metabolic diseases, and peroxisome proliferator-activated receptors. Endocrinology 144 (2003) 2201-2207
    • (2003) Endocrinology , vol.144 , pp. 2201-2207
    • Lee, C.H.1    Olson, P.2    Evans, R.M.3
  • 4
    • 3242669109 scopus 로고    scopus 로고
    • Fatty acid-binding proteins - insights from genetic manipulations
    • Haunerland N.H., and Spener F. Fatty acid-binding proteins - insights from genetic manipulations. Prog. Lipid Res. 43 (2004) 328-349
    • (2004) Prog. Lipid Res. , vol.43 , pp. 328-349
    • Haunerland, N.H.1    Spener, F.2
  • 5
    • 0030239495 scopus 로고    scopus 로고
    • Cellular fatty acid-binding proteins: their function and physiological significance
    • Glatz J.F., and van der Vusse G.J. Cellular fatty acid-binding proteins: their function and physiological significance. Prog. Lipid Res. 35 (1996) 243-282
    • (1996) Prog. Lipid Res. , vol.35 , pp. 243-282
    • Glatz, J.F.1    van der Vusse, G.J.2
  • 6
    • 0034717896 scopus 로고    scopus 로고
    • The fatty acid transport function of fatty acid-binding proteins
    • Storch J., and Thumser A.E. The fatty acid transport function of fatty acid-binding proteins. Biochim. Biophys. Acta 1486 (2000) 28-44
    • (2000) Biochim. Biophys. Acta , vol.1486 , pp. 28-44
    • Storch, J.1    Thumser, A.E.2
  • 7
    • 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., and 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. 98 (2001) 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
  • 8
    • 0036291635 scopus 로고    scopus 로고
    • Selective cooperation between fatty acid binding proteins and peroxisome proliferator-activated receptors in regulating transcription
    • Tan N.S., Shaw N.S., Vinckenbosch N., Liu P., Yasmin R., Desvergne B., Wahli W., and Noy N. Selective cooperation between fatty acid binding proteins and peroxisome proliferator-activated receptors in regulating transcription. Mol. Cell. Biol. 22 (2002) 5114-5127
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 5114-5127
    • Tan, N.S.1    Shaw, N.S.2    Vinckenbosch, N.3    Liu, P.4    Yasmin, R.5    Desvergne, B.6    Wahli, W.7    Noy, N.8
  • 9
    • 33645974312 scopus 로고    scopus 로고
    • Adipocyte-type fatty acid-binding protein as inter-compartmental shuttle for peroxisome proliferator activated receptor gamma agonists in cultured cell
    • Adida A., and Spener F. Adipocyte-type fatty acid-binding protein as inter-compartmental shuttle for peroxisome proliferator activated receptor gamma agonists in cultured cell. Biochim. Biophys. Acta 1761 (2006) 172-181
    • (2006) Biochim. Biophys. Acta , vol.1761 , pp. 172-181
    • Adida, A.1    Spener, F.2
  • 10
    • 2942689824 scopus 로고    scopus 로고
    • Phenotype of palmitic acid transport and of signalling in alveolar type II cells from E/H-FABP double-knockout mice: contribution of caveolin-1 and PPARγ
    • Guthmann F., Schachtrup C., Tolle A., Wissel H., Binas B., Kondo H., Owada Y., Spener F., and Rüstow B. Phenotype of palmitic acid transport and of signalling in alveolar type II cells from E/H-FABP double-knockout mice: contribution of caveolin-1 and PPARγ. Biochim. Biophys. Acta 1636 (2004) 196-204
    • (2004) Biochim. Biophys. Acta , vol.1636 , pp. 196-204
    • Guthmann, F.1    Schachtrup, C.2    Tolle, A.3    Wissel, H.4    Binas, B.5    Kondo, H.6    Owada, Y.7    Spener, F.8    Rüstow, B.9
  • 11
    • 0023896553 scopus 로고
    • The pulmonary surfactant system: biochemical aspects and functional significance
    • Van Golde L.M., Batenburg J.J., and Robertson B. The pulmonary surfactant system: biochemical aspects and functional significance. Physiol. Rev. 68 (1988) 374-455
    • (1988) Physiol. Rev. , vol.68 , pp. 374-455
    • Van Golde, L.M.1    Batenburg, J.J.2    Robertson, B.3
  • 12
    • 0033918285 scopus 로고    scopus 로고
    • Analysis of lung surfactant model systems with time-of-flight secondary ion mass spectrometry
    • Bourdos N., Kollmer F., Benninghoven A., Ross M., Sieber M., and Galla H.J. Analysis of lung surfactant model systems with time-of-flight secondary ion mass spectrometry. Biophys. J. 79 (2000) 357-369
    • (2000) Biophys. J. , vol.79 , pp. 357-369
    • Bourdos, N.1    Kollmer, F.2    Benninghoven, A.3    Ross, M.4    Sieber, M.5    Galla, H.J.6
  • 13
  • 15
    • 0037763970 scopus 로고    scopus 로고
    • Liquid-crystalline collapse of pulmonary surfactant monolayers
    • Schief W.R., Antia M., Discher B.M., Hall S.B., and Vogel V. Liquid-crystalline collapse of pulmonary surfactant monolayers. Biophys. J. 84 (2003) 3792-3806
    • (2003) Biophys. J. , vol.84 , pp. 3792-3806
    • Schief, W.R.1    Antia, M.2    Discher, B.M.3    Hall, S.B.4    Vogel, V.5
  • 17
    • 51649179265 scopus 로고
    • Quantitative analysis of phospholipid by thin-layer chromatography and phosphorus analysis of spots
    • Rouser G., Siakotos A.N., and Fleisher S. Quantitative analysis of phospholipid by thin-layer chromatography and phosphorus analysis of spots. Lipids 1 (1966)
    • (1966) Lipids , vol.1
    • Rouser, G.1    Siakotos, A.N.2    Fleisher, S.3
  • 18
    • 0015522277 scopus 로고
    • Fluorescamine: a reagent for assay of amino acids, peptides, proteins, and primary amines in the picomole range
    • Udenfriend S., Stein S., Bohlen P., Dairman W., Leimgruber W., and Weigele M. Fluorescamine: a reagent for assay of amino acids, peptides, proteins, and primary amines in the picomole range. Science 178 (1972) 871-872
    • (1972) Science , vol.178 , pp. 871-872
    • Udenfriend, S.1    Stein, S.2    Bohlen, P.3    Dairman, W.4    Leimgruber, W.5    Weigele, M.6
  • 19
    • 0030842893 scopus 로고    scopus 로고
    • The phase behavior of lipid monolayers containing pulmonary surfactant protein C studied by fluorescence light microscopy
    • von Nahmen A., Post A., Galla H.J., and Sieber M. The phase behavior of lipid monolayers containing pulmonary surfactant protein C studied by fluorescence light microscopy. Eur. Biophys. J. 26 (1997) 359-369
    • (1997) Eur. Biophys. J. , vol.26 , pp. 359-369
    • von Nahmen, A.1    Post, A.2    Galla, H.J.3    Sieber, M.4
  • 20
    • 0036520974 scopus 로고    scopus 로고
    • Kinetics of phospholipid insertion into monolayers containing the lung surfactant proteins SP-B or SP-C
    • Ross M., Krol S., Janshoff A., and Galla H.J. Kinetics of phospholipid insertion into monolayers containing the lung surfactant proteins SP-B or SP-C. Eur. Biophys. J. 31 (2002) 52-61
    • (2002) Eur. Biophys. J. , vol.31 , pp. 52-61
    • Ross, M.1    Krol, S.2    Janshoff, A.3    Galla, H.J.4
  • 21
    • 0022527271 scopus 로고
    • An improved method for isolating type II cells in high yield and purity
    • Dobbs L.G., Gonzalez R., and Williams M.C. An improved method for isolating type II cells in high yield and purity. Am. Rev. Respir. Dis. 134 (1986) 141-145
    • (1986) Am. Rev. Respir. Dis. , vol.134 , pp. 141-145
    • Dobbs, L.G.1    Gonzalez, R.2    Williams, M.C.3
  • 23
    • 17144388958 scopus 로고    scopus 로고
    • Expression of liver-type fatty acid-binding protein in murine lung and its release into serum upon challenge of lung with lipopolysaccharide.
    • Piumngam P., Schachtrup C., Owada Y., Kondo H., Promptmas C., and Spener F. Expression of liver-type fatty acid-binding protein in murine lung and its release into serum upon challenge of lung with lipopolysaccharide. Eur. J. Lipid Sci. Technol. 107 (2005) 145-152
    • (2005) Eur. J. Lipid Sci. Technol. , vol.107 , pp. 145-152
    • Piumngam, P.1    Schachtrup, C.2    Owada, Y.3    Kondo, H.4    Promptmas, C.5    Spener, F.6
  • 25
    • 0032011545 scopus 로고    scopus 로고
    • Suppression of acute lung injury in mice by an inhibitor of phosphodiesterase type 4
    • Miotla J.M., Teixeira M.M., and Hellewell P.G. Suppression of acute lung injury in mice by an inhibitor of phosphodiesterase type 4. Am. J. Respir. Cell. Mol. Biol. 18 (1998) 411-420
    • (1998) Am. J. Respir. Cell. Mol. Biol. , vol.18 , pp. 411-420
    • Miotla, J.M.1    Teixeira, M.M.2    Hellewell, P.G.3
  • 26
    • 2942532731 scopus 로고    scopus 로고
    • L-FABP is exclusively expressed in alveolar macrophages within the myeloid lineage: evidence for a PPARalpha-independent expression
    • Schachtrup C., Scholzen T.E., Grau V., Luger T.A., Sorg C., Spener F., and Kerkhoff C. L-FABP is exclusively expressed in alveolar macrophages within the myeloid lineage: evidence for a PPARalpha-independent expression. Int. J. Biochem. Cell Biol. 36 (2004) 2042-2053
    • (2004) Int. J. Biochem. Cell Biol. , vol.36 , pp. 2042-2053
    • Schachtrup, C.1    Scholzen, T.E.2    Grau, V.3    Luger, T.A.4    Sorg, C.5    Spener, F.6    Kerkhoff, C.7
  • 28
    • 0027185340 scopus 로고
    • Use of transgenic mice to map cis-acting elements in the liver fatty acid-binding protein gene (Fabpl) that regulate its cell lineage-specific, differentiation-dependent, and spatial patterns of expression in the gut epithelium and in the liver acinus
    • Simon T.C., Roth K.A., and Gordon J.I. Use of transgenic mice to map cis-acting elements in the liver fatty acid-binding protein gene (Fabpl) that regulate its cell lineage-specific, differentiation-dependent, and spatial patterns of expression in the gut epithelium and in the liver acinus. J. Biol. Chem. 268 (1993) 18345-18358
    • (1993) J. Biol. Chem. , vol.268 , pp. 18345-18358
    • Simon, T.C.1    Roth, K.A.2    Gordon, J.I.3
  • 29
    • 17744410109 scopus 로고    scopus 로고
    • Insights into binding of fatty acids by fatty acid binding proteins
    • Hanhoff T., Lücke C., and Spener F. Insights into binding of fatty acids by fatty acid binding proteins. Mol. Cell Biochem. 239 (2002) 45-54
    • (2002) Mol. Cell Biochem. , vol.239 , pp. 45-54
    • Hanhoff, T.1    Lücke, C.2    Spener, F.3
  • 30
    • 0032502246 scopus 로고    scopus 로고
    • Bovine epidermal fatty acid-binding protein: determination of ligand specificity and cellular localization in retina and testis
    • Kingma P.B., Bok D., and Ong D.E. Bovine epidermal fatty acid-binding protein: determination of ligand specificity and cellular localization in retina and testis. Biochemistry 37 (1998) 3250-3257
    • (1998) Biochemistry , vol.37 , pp. 3250-3257
    • Kingma, P.B.1    Bok, D.2    Ong, D.E.3
  • 31
    • 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., and Kleinfeld A.M. Thermodynamic and kinetic properties of fatty acid interactions with rat liver fatty acid-binding protein. J. Biol. Chem. 271 (1996) 31068-31074
    • (1996) J. Biol. Chem. , vol.271 , pp. 31068-31074
    • Richieri, G.V.1    Ogata, R.T.2    Kleinfeld, A.M.3
  • 32
    • 0013991183 scopus 로고
    • A stereologic electron microscope study of "tubular myelin figures" in alveolar fluids of rat lungs
    • Weibel E.R., Kistler G.S., and Tondury G. A stereologic electron microscope study of "tubular myelin figures" in alveolar fluids of rat lungs. Z. Zellforsch. Mikrosk. Anat. 69 (1966) 418-427
    • (1966) Z. Zellforsch. Mikrosk. Anat. , vol.69 , pp. 418-427
    • Weibel, E.R.1    Kistler, G.S.2    Tondury, G.3
  • 33
    • 0344765518 scopus 로고    scopus 로고
    • Formation and structure of surface films: captive bubble surfactometry
    • Schurch S., Green F.H., and Bachofen H. Formation and structure of surface films: captive bubble surfactometry. Biochim. Biophys. Acta 1408 (1998) 180-202
    • (1998) Biochim. Biophys. Acta , vol.1408 , pp. 180-202
    • Schurch, S.1    Green, F.H.2    Bachofen, H.3
  • 34
    • 0031019895 scopus 로고    scopus 로고
    • The structure of a model pulmonary surfactant as revealed by scanning force microscopy
    • von Nahmen A., Schenk M., Sieber M., and Amrein M. The structure of a model pulmonary surfactant as revealed by scanning force microscopy. Biophys. J. 72 (1997) 463-469
    • (1997) Biophys. J. , vol.72 , pp. 463-469
    • von Nahmen, A.1    Schenk, M.2    Sieber, M.3    Amrein, M.4
  • 35
    • 0030762136 scopus 로고    scopus 로고
    • A scanning force- and fluorescence light microscopy study of the structure and function of a model pulmonary surfactant
    • Amrein M., von Nahmen A., and Sieber M. A scanning force- and fluorescence light microscopy study of the structure and function of a model pulmonary surfactant. Eur. Biophys. J. 26 (1997) 349-357
    • (1997) Eur. Biophys. J. , vol.26 , pp. 349-357
    • Amrein, M.1    von Nahmen, A.2    Sieber, M.3
  • 36
    • 0036217150 scopus 로고    scopus 로고
    • Scanning force microscopy at the air-water interface of an air bubble coated with pulmonary surfactant
    • Knebel D., Sieber M., Reichelt R., Galla H.J., and Amrein M. Scanning force microscopy at the air-water interface of an air bubble coated with pulmonary surfactant. Biophys. J. 82 (2002) 474-480
    • (2002) Biophys. J. , vol.82 , pp. 474-480
    • Knebel, D.1    Sieber, M.2    Reichelt, R.3    Galla, H.J.4    Amrein, M.5
  • 37
    • 0034033144 scopus 로고    scopus 로고
    • Distribution of the surfactant-associated protein C within a lung surfactant model film investigated by near-field optical microscopy
    • Kramer A., Wintergalen A., Sieber M., Galla H.J., Amrein M., and Guckenberger R. Distribution of the surfactant-associated protein C within a lung surfactant model film investigated by near-field optical microscopy. Biophys. J. 78 (2000) 458-465
    • (2000) Biophys. J. , vol.78 , pp. 458-465
    • Kramer, A.1    Wintergalen, A.2    Sieber, M.3    Galla, H.J.4    Amrein, M.5    Guckenberger, R.6
  • 38
    • 0038680737 scopus 로고    scopus 로고
    • Molecular organization revealed by time-of-flight secondary ion mass spectrometry of a clinically used extracted pulmonary surfactant
    • Harbottel R.R., Nag K., McIntyre N.S., Possmayer F., and Petersen N.O. Molecular organization revealed by time-of-flight secondary ion mass spectrometry of a clinically used extracted pulmonary surfactant. Langmuir 19 (2003) 3698-3704
    • (2003) Langmuir , vol.19 , pp. 3698-3704
    • Harbottel, R.R.1    Nag, K.2    McIntyre, N.S.3    Possmayer, F.4    Petersen, N.O.5
  • 39
    • 0035950761 scopus 로고    scopus 로고
    • Morphology and collapse transitions in binary phospholipid monolayers
    • Gopal A., and Lee E.J. Morphology and collapse transitions in binary phospholipid monolayers. J. Phys. Chem. B 105 (2001) 10348-10354
    • (2001) J. Phys. Chem. B , vol.105 , pp. 10348-10354
    • Gopal, A.1    Lee, E.J.2
  • 40
    • 2342592703 scopus 로고    scopus 로고
    • Alterations in SP-B and SP-C expression in neonatal lung disease
    • Nogee L.M. Alterations in SP-B and SP-C expression in neonatal lung disease. Annu. Rev. Physiol. 66 (2004) 601-623
    • (2004) Annu. Rev. Physiol. , vol.66 , pp. 601-623
    • Nogee, L.M.1
  • 41
    • 48749122155 scopus 로고    scopus 로고
    • Analysis of surface topology and chemical composition of microstructures formed in planar surfactant films under compression
    • Nag K. (Ed), Taylor & Francis Group, Boca Raton FL
    • Malcharek S., Bourdos N., and Galla H.J. Analysis of surface topology and chemical composition of microstructures formed in planar surfactant films under compression. In: Nag K. (Ed). Lung Surfactant Function and Disorder (2005), Taylor & Francis Group, Boca Raton FL 251-274
    • (2005) Lung Surfactant Function and Disorder , pp. 251-274
    • Malcharek, S.1    Bourdos, N.2    Galla, H.J.3
  • 42
    • 10344252269 scopus 로고    scopus 로고
    • The lung collectins, SP-A and SP-D, modulate pulmonary innate immunity
    • Sano H., and Kuroki Y. The lung collectins, SP-A and SP-D, modulate pulmonary innate immunity. Mol. Immunol. 42 (2005) 279-287
    • (2005) Mol. Immunol. , vol.42 , pp. 279-287
    • Sano, H.1    Kuroki, Y.2
  • 43
    • 22144462143 scopus 로고    scopus 로고
    • Multilayer structures in lipid monolayer films containing surfactant protein C: effects of cholesterol and POPE
    • Malcharek S., Hinz A., Hilterhaus L., and Galla H.J. Multilayer structures in lipid monolayer films containing surfactant protein C: effects of cholesterol and POPE. Biophys. J. 88 (2005) 2638-2649
    • (2005) Biophys. J. , vol.88 , pp. 2638-2649
    • Malcharek, S.1    Hinz, A.2    Hilterhaus, L.3    Galla, H.J.4


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