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Volumn 93, Issue 10, 2007, Pages 3529-3540

Surfactant protein A forms extensive lattice-like structures on 1,2-dipalmitoylphosphatidylcholine/rough-lipopolysaccharide-mixed monolayers

Author keywords

[No Author keywords available]

Indexed keywords

DIPALMITOYLPHOSPHATIDYLCHOLINE; LIPOPOLYSACCHARIDE; SURFACTANT PROTEIN A;

EID: 36549078275     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.107.109793     Document Type: Article
Times cited : (27)

References (36)
  • 1
    • 0026062620 scopus 로고
    • Gram-negative endotoxin: An extraordinary lipid with profound effects on eukaryotic signal transduction
    • Raetz, C. R., R. J. Ulevitch, S. D. Wright, C. H. Sibley, A. Ding, and C. F. Nathan. 1991. Gram-negative endotoxin: an extraordinary lipid with profound effects on eukaryotic signal transduction. FASEB J. 5:2653-2660.
    • (1991) FASEB J , vol.5 , pp. 2653-2660
    • Raetz, C.R.1    Ulevitch, R.J.2    Wright, S.D.3    Sibley, C.H.4    Ding, A.5    Nathan, C.F.6
  • 2
    • 85031438961 scopus 로고    scopus 로고
    • Nikaido, H., and M. Vaara. 1987. Outer membrane. In Escherichia coli and Salmonella typhimurium. Cellular and Molecular Biology. C. Neidhardt, J. L. Ingraham, K. Brooks Low, B. Magasanik, M. Schaechter, and H. E. Umbarger, editors. American Society for Microbiology, Washington, DC. 7-22.
    • Nikaido, H., and M. Vaara. 1987. Outer membrane. In Escherichia coli and Salmonella typhimurium. Cellular and Molecular Biology. C. Neidhardt, J. L. Ingraham, K. Brooks Low, B. Magasanik, M. Schaechter, and H. E. Umbarger, editors. American Society for Microbiology, Washington, DC. 7-22.
  • 3
    • 0032754292 scopus 로고    scopus 로고
    • Chemical structure, molecular conformation and bioreactivity of endotoxins
    • R. S. Jack, editor. Karger, Basel, Switzerland
    • Seydel, U., A. B. Schormm, R. Blunck, and K. Brandenburg. 2000. Chemical structure, molecular conformation and bioreactivity of endotoxins. In Chemical Immunology: CD14 in the Inflammatory Response, vol. 74. R. S. Jack, editor. Karger, Basel, Switzerland. 5-24.
    • (2000) Chemical Immunology: CD14 in the Inflammatory Response , vol.74 , pp. 5-24
    • Seydel, U.1    Schormm, A.B.2    Blunck, R.3    Brandenburg, K.4
  • 4
    • 0034820507 scopus 로고    scopus 로고
    • Bacterial lipopolysaccharides and innate immunity
    • Alexander, C., and E. T. Rietschel. 2001. Bacterial lipopolysaccharides and innate immunity. J. Endotoxin Res. 7:197-202.
    • (2001) J. Endotoxin Res , vol.7 , pp. 197-202
    • Alexander, C.1    Rietschel, E.T.2
  • 6
    • 26844480960 scopus 로고    scopus 로고
    • Interaction of SP-A (surfactant protein A) with bacterial rough lipopolysaccharide (Re-LPS), and effects of SP-A on the binding of Re-LPS to CD14 and LPS-binding protein
    • García-Verdugo, I., F. Sánchez-Barbero, K. Soldau, P. S. Tobias, and C. Casals. 2005. Interaction of SP-A (surfactant protein A) with bacterial rough lipopolysaccharide (Re-LPS), and effects of SP-A on the binding of Re-LPS to CD14 and LPS-binding protein. Biochem. J. 391:115-124.
    • (2005) Biochem. J , vol.391 , pp. 115-124
    • García-Verdugo, I.1    Sánchez-Barbero, F.2    Soldau, K.3    Tobias, P.S.4    Casals, C.5
  • 7
    • 0037189590 scopus 로고    scopus 로고
    • Structural basis for interactions between lung surfactant protein C and bacterial lipopolysaccharide
    • Augusto, L. A., J. Li, M. Synguelakis, J. Johansson, and R. Chaby. 2002. Structural basis for interactions between lung surfactant protein C and bacterial lipopolysaccharide. J. Biol. Chem. 277:23484-23492.
    • (2002) J. Biol. Chem , vol.277 , pp. 23484-23492
    • Augusto, L.A.1    Li, J.2    Synguelakis, M.3    Johansson, J.4    Chaby, R.5
  • 8
    • 0026696318 scopus 로고
    • Interactions of surfactant protein D with bacterial lipopolysaccharides. Surfactant protein D is an Escherichia coli-binding protein in bronchoalveolar lavage
    • Kuan, S. F., K. Rust, and E. Crouch. 1992. Interactions of surfactant protein D with bacterial lipopolysaccharides. Surfactant protein D is an Escherichia coli-binding protein in bronchoalveolar lavage. J. Clin. Invest. 90:97-106.
    • (1992) J. Clin. Invest , vol.90 , pp. 97-106
    • Kuan, S.F.1    Rust, K.2    Crouch, E.3
  • 9
    • 0031740744 scopus 로고    scopus 로고
    • Structure, processing and properties of surfactant protein A
    • McCormack, F. X. 1998. Structure, processing and properties of surfactant protein A. Biochim. Biophys. Acta. 1408:109-131.
    • (1998) Biochim. Biophys. Acta , vol.1408 , pp. 109-131
    • McCormack, F.X.1
  • 11
    • 0000625518 scopus 로고
    • Nucleotide and amino acid sequences of pulmonary surfactant protein SP 18 and evidence for cooperation between SP 18 and SP 28-36 in surfactant lipid adsorption
    • Hawgood, S., B. J. Benson, J. Schilling, D. Damm, J. A. Clements, and R. T. White. 1987. Nucleotide and amino acid sequences of pulmonary surfactant protein SP 18 and evidence for cooperation between SP 18 and SP 28-36 in surfactant lipid adsorption. Proc. Natl. Acad. Sci. USA. 84:66-70.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 66-70
    • Hawgood, S.1    Benson, B.J.2    Schilling, J.3    Damm, D.4    Clements, J.A.5    White, R.T.6
  • 12
    • 0025111649 scopus 로고
    • Pulmonary surfactant-associated protein A enhances the surface activity of lipid extract surfactant and reverses inhibition by blood proteins in vitro
    • Cockshutt, A. M., J. Weitz, and F. Possmayer. 1990. Pulmonary surfactant-associated protein A enhances the surface activity of lipid extract surfactant and reverses inhibition by blood proteins in vitro. Biochemistry. 29:8424-8429.
    • (1990) Biochemistry , vol.29 , pp. 8424-8429
    • Cockshutt, A.M.1    Weitz, J.2    Possmayer, F.3
  • 13
    • 0031951412 scopus 로고    scopus 로고
    • Differential partitioning of pulmonary surfactant protein SP-A into regions of monolayers of dipalmitoylphosphatidylcholine and dipalmitoylphosphatidylcholine/dipalmitoylphosphatidylglycerol
    • Ruano, M. L. F., K. Nag, L. A. Worthman, C. Casals, J. Pérez-Gil, and K. M. W. Keough. 1998. Differential partitioning of pulmonary surfactant protein SP-A into regions of monolayers of dipalmitoylphosphatidylcholine and dipalmitoylphosphatidylcholine/dipalmitoylphosphatidylglycerol. Biophys. J. 74:1101-1109.
    • (1998) Biophys. J , vol.74 , pp. 1101-1109
    • Ruano, M.L.F.1    Nag, K.2    Worthman, L.A.3    Casals, C.4    Pérez-Gil, J.5    Keough, K.M.W.6
  • 14
    • 0032839458 scopus 로고    scopus 로고
    • Interactions of pulmonary surfactant protein A with phospholipid monolayers change with pH
    • Ruano, M. L., K. Nag, C. Casals, J. Pérez-Gil, and K. M. Keough. 1999. Interactions of pulmonary surfactant protein A with phospholipid monolayers change with pH. Biophys. J. 77:1469-1476.
    • (1999) Biophys. J , vol.77 , pp. 1469-1476
    • Ruano, M.L.1    Nag, K.2    Casals, C.3    Pérez-Gil, J.4    Keough, K.M.5
  • 15
    • 0033729383 scopus 로고    scopus 로고
    • Pulmonary surfactant protein A interacts with gel-like regions in monolayers of pulmonary surfactant lipid extract
    • Worthman, L. A., K. Nag, N. Rich, M. L. Ruano, C. Casals, J. Pérez-Gil, and K. M. Keough. 2000. Pulmonary surfactant protein A interacts with gel-like regions in monolayers of pulmonary surfactant lipid extract. Biophys. J. 79:2657-2666.
    • (2000) Biophys. J , vol.79 , pp. 2657-2666
    • Worthman, L.A.1    Nag, K.2    Rich, N.3    Ruano, M.L.4    Casals, C.5    Pérez-Gil, J.6    Keough, K.M.7
  • 16
    • 0041525581 scopus 로고    scopus 로고
    • Effect of hydroxylation and N187-linked glycosylation on molecular and functional properties of recombinant human surfactant protein A
    • García-Verdugo, I., F. Sánchez-Barbero, F. U. Bosch, W. Steinhilber, and C. Casals. 2003. Effect of hydroxylation and N187-linked glycosylation on molecular and functional properties of recombinant human surfactant protein A. Biochemistry. 42:9532-9542.
    • (2003) Biochemistry , vol.42 , pp. 9532-9542
    • García-Verdugo, I.1    Sánchez-Barbero, F.2    Bosch, F.U.3    Steinhilber, W.4    Casals, C.5
  • 17
    • 14844297019 scopus 로고    scopus 로고
    • Role of the degree of oligomerization in the structure and function of human surfactant protein A
    • Sánchez-Barbero, F., J. Strassner, R. García-Cañero, W. Steinhilber, and C. Casals. 2005. Role of the degree of oligomerization in the structure and function of human surfactant protein A. J. Biol. Chem. 580:7659-7670.
    • (2005) J. Biol. Chem , vol.580 , pp. 7659-7670
    • Sánchez-Barbero, F.1    Strassner, J.2    García-Cañero, R.3    Steinhilber, W.4    Casals, C.5
  • 19
    • 0030033618 scopus 로고    scopus 로고
    • Comparison of lipid aggregation and self-aggregation activities of pulmonary surfactant-associated protein A
    • Ruano, M. L., E. Miguel, J. Pérez-Gil, and C. Casals. 1996. Comparison of lipid aggregation and self-aggregation activities of pulmonary surfactant-associated protein A. Biochem. J. 313:683-689.
    • (1996) Biochem. J , vol.313 , pp. 683-689
    • Ruano, M.L.1    Miguel, E.2    Pérez-Gil, J.3    Casals, C.4
  • 20
    • 0000254521 scopus 로고
    • Design and construction of an epifluorescence microscopic surface balance for the study of lipid monolayer phase transitions
    • Nag, K., N. H. Rich, C. Boland, and K. M. W. Keough. 1990. Design and construction of an epifluorescence microscopic surface balance for the study of lipid monolayer phase transitions. Rev. Sci. Instrum. 61:3425-3430.
    • (1990) Rev. Sci. Instrum , vol.61 , pp. 3425-3430
    • Nag, K.1    Rich, N.H.2    Boland, C.3    Keough, K.M.W.4
  • 21
    • 0025902367 scopus 로고
    • Epifluorescence microscopic observation of monolayers of dipalmitoylphosphatidylcholine: Dependence of domain size on compression rates
    • Nag, K., C. Boland, N. Rich, and K. M. Keough. 1991. Epifluorescence microscopic observation of monolayers of dipalmitoylphosphatidylcholine: dependence of domain size on compression rates. Biochim. Biophys. Acta. 1068:157-160.
    • (1991) Biochim. Biophys. Acta , vol.1068 , pp. 157-160
    • Nag, K.1    Boland, C.2    Rich, N.3    Keough, K.M.4
  • 22
    • 0026630978 scopus 로고
    • Pulmonary surfactant protein SP-C causes packing rearrangements of dipalmitoylphosphatidylcholine in spread monolayers
    • Pérez-Gil, J., K. Nag, S. Taneva, and K. M. W. Keough. 1992. Pulmonary surfactant protein SP-C causes packing rearrangements of dipalmitoylphosphatidylcholine in spread monolayers. Biophys. J. 63:197-204.
    • (1992) Biophys. J , vol.63 , pp. 197-204
    • Pérez-Gil, J.1    Nag, K.2    Taneva, S.3    Keough, K.M.W.4
  • 23
    • 0029093059 scopus 로고
    • Pulmonary surfactant protein SP-A with phospholipids in spread monolayers at the air-water interface
    • Taneva, S., T. McEachren, J. Stewart, and K. M. Keough. 1995. Pulmonary surfactant protein SP-A with phospholipids in spread monolayers at the air-water interface. Biochemistry. 34:10279-10289.
    • (1995) Biochemistry , vol.34 , pp. 10279-10289
    • Taneva, S.1    McEachren, T.2    Stewart, J.3    Keough, K.M.4
  • 24
    • 0001323381 scopus 로고
    • Intermolecular interaction in some mixed polymer monolayers at the air water interface
    • Wu, S., and J. R. Huntsberger. 1969. Intermolecular interaction in some mixed polymer monolayers at the air water interface. J. Colloid Interface Sci. 29:138-147.
    • (1969) J. Colloid Interface Sci , vol.29 , pp. 138-147
    • Wu, S.1    Huntsberger, J.R.2
  • 25
    • 0031354553 scopus 로고    scopus 로고
    • A close look at domain formation in DPPC monolayers
    • McColongue, C. W., and T. K. Vanderlick. 1997. A close look at domain formation in DPPC monolayers. Langmuir. 13:7158-7164.
    • (1997) Langmuir , vol.13 , pp. 7158-7164
    • McColongue, C.W.1    Vanderlick, T.K.2
  • 26
    • 22044441448 scopus 로고    scopus 로고
    • Interaction of the N-terminal segment of pulmonary surfactant protein SP-C with interfacial phospholipid films
    • Plasencia, I., K. M. W. Keough, and J. Pérez-Gil. 2005. Interaction of the N-terminal segment of pulmonary surfactant protein SP-C with interfacial phospholipid films. Biochim. Biophys. Acta. 1713:118-128.
    • (2005) Biochim. Biophys. Acta , vol.1713 , pp. 118-128
    • Plasencia, I.1    Keough, K.M.W.2    Pérez-Gil, J.3
  • 27
    • 23144458847 scopus 로고    scopus 로고
    • Probing the properties of lipopolysaccharide monolayers and their interaction with the antimicrobial peptide polymyxin B by atomic force microscopy
    • Roes, S., U. Seydel, and T. Gutsmann. 2005. Probing the properties of lipopolysaccharide monolayers and their interaction with the antimicrobial peptide polymyxin B by atomic force microscopy. Langmuir. 21:6970-6978.
    • (2005) Langmuir , vol.21 , pp. 6970-6978
    • Roes, S.1    Seydel, U.2    Gutsmann, T.3
  • 28
    • 0022875852 scopus 로고
    • Interaction between the 35 kDa apolipoprotein of pulmonary surfactant and saturated phosphatidylcholines. Effects of temperature
    • King, R. J., M. C. Phillips, P. M. Horowitz, and S. C. Dang. 1986. Interaction between the 35 kDa apolipoprotein of pulmonary surfactant and saturated phosphatidylcholines. Effects of temperature. Biochim. Biophys. Acta. 879:1-13.
    • (1986) Biochim. Biophys. Acta , vol.879 , pp. 1-13
    • King, R.J.1    Phillips, M.C.2    Horowitz, P.M.3    Dang, S.C.4
  • 29
    • 0027765632 scopus 로고
    • Tryptophan fluorescence study on the interaction of pulmonary surfactant protein A with phospholipid vesicles
    • Casals, C., E. Miguel, and J. Pérez-Gil. 1993. Tryptophan fluorescence study on the interaction of pulmonary surfactant protein A with phospholipid vesicles. Biochem. J. 296:585-593.
    • (1993) Biochem. J , vol.296 , pp. 585-593
    • Casals, C.1    Miguel, E.2    Pérez-Gil, J.3
  • 32
    • 0018702835 scopus 로고
    • Interaction of divalent cations and polymyxin B with lipopolysaccharide
    • Schindler, M., and M. J. Osborn. 1979. Interaction of divalent cations and polymyxin B with lipopolysaccharide. Biochemistry. 18:4425-4430.
    • (1979) Biochemistry , vol.18 , pp. 4425-4430
    • Schindler, M.1    Osborn, M.J.2
  • 33
    • 85047690807 scopus 로고    scopus 로고
    • Surfactant proteins A and D inhibit the growth of Gram-negative bacteria by increasing membrane permeability
    • Wu, H., A. Kuzmenko, S. Wan, L. Schaffer, A. Weiss, J. H. Fisher, K. S. Kim, and F. X. McCormack. 2003. Surfactant proteins A and D inhibit the growth of Gram-negative bacteria by increasing membrane permeability. J. Clin. Invest. 111:1589-1602.
    • (2003) J. Clin. Invest , vol.111 , pp. 1589-1602
    • Wu, H.1    Kuzmenko, A.2    Wan, S.3    Schaffer, L.4    Weiss, A.5    Fisher, J.H.6    Kim, K.S.7    McCormack, F.X.8
  • 34
    • 33644503860 scopus 로고    scopus 로고
    • Pulmonary collectins selectively permeabilize model bacterial membranes containing rough lipopolysaccharide
    • Kuzmenko, A. I., H. Wu, and F. X. McCormack. 2006. Pulmonary collectins selectively permeabilize model bacterial membranes containing rough lipopolysaccharide. Biochemistry. 45:2679-2685.
    • (2006) Biochemistry , vol.45 , pp. 2679-2685
    • Kuzmenko, A.I.1    Wu, H.2    McCormack, F.X.3
  • 35
    • 0033150550 scopus 로고    scopus 로고
    • Correlated atomic force and transmission electron microscopy of nanotubular structures in pulmonary surfactant
    • Nag, K., J. G. Munro, S. A. Hearn, J. Rasmusson, N. O. Petersen, and F. X. Possmayer. 1999. Correlated atomic force and transmission electron microscopy of nanotubular structures in pulmonary surfactant. J. Struct. Biol. 126:1-15.
    • (1999) J. Struct. Biol , vol.126 , pp. 1-15
    • Nag, K.1    Munro, J.G.2    Hearn, S.A.3    Rasmusson, J.4    Petersen, N.O.5    Possmayer, F.X.6
  • 36
    • 0032924918 scopus 로고    scopus 로고
    • Formation of membrane lattice structures and their specific interactions with surfactant protein A
    • Palaniyar, N., R. A. Ridsdale, S. A. Hearn, F. Possmayer, and G. Harauz. 1999. Formation of membrane lattice structures and their specific interactions with surfactant protein A. Am. J. Physiol. 276:L642-L649.
    • (1999) Am. J. Physiol , vol.276
    • Palaniyar, N.1    Ridsdale, R.A.2    Hearn, S.A.3    Possmayer, F.4    Harauz, G.5


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