메뉴 건너뛰기




Volumn 95, Issue 7, 2008, Pages 3287-3294

SP-A permeabilizes lipopolysaccharide membranes by forming protein aggregates that extract lipids from the membrane

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM; LIPOPOLYSACCHARIDE; SURFACTANT PROTEIN A; WATER;

EID: 55949101551     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1529/biophysj.108.137323     Document Type: Article
Times cited : (26)

References (31)
  • 1
    • 34447631692 scopus 로고    scopus 로고
    • Pulmonary collectins in innate immunity of the lung
    • Kuroki, Y., M. Takahashi, and C. Nishitani. 2007. Pulmonary collectins in innate immunity of the lung. Cell. Microbiol. 9:1871-1879.
    • (2007) Cell. Microbiol , vol.9 , pp. 1871-1879
    • Kuroki, Y.1    Takahashi, M.2    Nishitani, C.3
  • 2
    • 11244287371 scopus 로고    scopus 로고
    • Immunoregulatory functions of surfactant proteins
    • Wright, J. R. 2005. Immunoregulatory functions of surfactant proteins. Nat. Rev. Immunol. 5:58-68.
    • (2005) Nat. Rev. Immunol , vol.5 , pp. 58-68
    • Wright, J.R.1
  • 3
    • 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
  • 4
    • 9244262475 scopus 로고    scopus 로고
    • Interactions of pulmonary collectins with Bordetella bronchiseptica and Bordetella pertussis lipopolysaccharide elucidate the structural basis of their antimicrobial activities
    • Schaeffer, L. M., F. X. McCormack, H. Wu, and A. A. Weiss. 2004. Interactions of pulmonary collectins with Bordetella bronchiseptica and Bordetella pertussis lipopolysaccharide elucidate the structural basis of their antimicrobial activities. Infect. Immun. 72:7124-7130.
    • (2004) Infect. Immun , vol.72 , pp. 7124-7130
    • Schaeffer, L.M.1    McCormack, F.X.2    Wu, H.3    Weiss, A.A.4
  • 5
    • 33748655463 scopus 로고    scopus 로고
    • Comparative signature-tagged mutagenesis identifies Pseudomonas factors conferring resistance to the pulmonary collectin SP-A
    • Zhang, S., Y. Chen, E. Potvin, F. Sanschagrin, R. C. Levesque, F. X. McCormack, and G. W. Lau. 2005. Comparative signature-tagged mutagenesis identifies Pseudomonas factors conferring resistance to the pulmonary collectin SP-A. PLoS Pathog. 1:259-268.
    • (2005) PLoS Pathog , vol.1 , pp. 259-268
    • Zhang, S.1    Chen, Y.2    Potvin, E.3    Sanschagrin, F.4    Levesque, R.C.5    McCormack, F.X.6    Lau, G.W.7
  • 7
    • 33644503860 scopus 로고    scopus 로고
    • Pulmonary collectins selectively permeabilize model bacterial membranes containing rough lipopolysaccharide
    • Kuzmenko, A., 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.1    Wu, H.2    McCormack, F.X.3
  • 8
    • 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
  • 9
    • 14844297019 scopus 로고    scopus 로고
    • Role of the degree of oligomerization in the structure and function of human surfactant protein A
    • Sanchez-Barbero, F. J. Strasser, R. Garcia-Canero, 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. 280:7659-7670.
    • (2005) J. Biol. Chem , vol.280 , pp. 7659-7670
    • Sanchez-Barbero, F.1    Strasser, J.2    Garcia-Canero, R.3    Steinhilber, W.4    Casals, C.5
  • 10
    • 34548802927 scopus 로고    scopus 로고
    • Structural and fuctional differences among human surfactant proteins SP-A1, SP-A2, and coexpressed SP-A1/SP-A2. Role of supratrimeric oligomerization
    • Sanchez-Barbero, F., G. Rivas, W. Steinhilber, and C. Casals. 2007. Structural and fuctional differences among human surfactant proteins SP-A1, SP-A2, and coexpressed SP-A1/SP-A2. Role of supratrimeric oligomerization. Biochem. J. 406:479-489.
    • (2007) Biochem. J , vol.406 , pp. 479-489
    • Sanchez-Barbero, F.1    Rivas, G.2    Steinhilber, W.3    Casals, C.4
  • 11
    • 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., K. Nag, L. A. Worthman, C. Casals, J. Perez-Gil, and K. M. 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.1    Nag, K.2    Worthman, L.A.3    Casals, C.4    Perez-Gil, J.5    Keough, K.M.6
  • 12
    • 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
    • Garcia-Verdugo, I., F. Sanchez-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
    • Garcia-Verdugo, I.1    Sanchez-Barbero, F.2    Soldau, K.3    Tobias, P.S.4    Casals, C.5
  • 14
    • 3342893024 scopus 로고    scopus 로고
    • Characterization of liposomal tacrolimus in lung surfactant-like phospholipids and evaluation of its immunosuppressive activity
    • Canadas O., R. Guerrero, R. Garcia-Canero, G. Orellana, M. Menendez, and C. Casals. 2004. Characterization of liposomal tacrolimus in lung surfactant-like phospholipids and evaluation of its immunosuppressive activity. Biochemistry. 43:9926-9938.
    • (2004) Biochemistry , vol.43 , pp. 9926-9938
    • Canadas, O.1    Guerrero, R.2    Garcia-Canero, R.3    Orellana, G.4    Menendez, M.5    Casals, C.6
  • 15
    • 33646694763 scopus 로고    scopus 로고
    • Physical properties and surface activity of surfactant-like membranes containing the cationic and hydrophobic peptide KL4
    • Saenz, A., O. Canadas, L. A. Bagatolli, M. E. Johnson, and C. Casals. 2006. Physical properties and surface activity of surfactant-like membranes containing the cationic and hydrophobic peptide KL4. FEBS J. 273:2515-2527.
    • (2006) FEBS J , vol.273 , pp. 2515-2527
    • Saenz, A.1    Canadas, O.2    Bagatolli, L.A.3    Johnson, M.E.4    Casals, C.5
  • 16
    • 33846432384 scopus 로고    scopus 로고
    • Effect of surfactant protein a (SP-A) on the physical properties and surface activity of KL4-surfactant
    • Saenz, A., O. Canadas, L. A. Bagatolli, F. Sanchez-Barbero, M. E. Johnson, and C. Casals. 2007. Effect of surfactant protein a (SP-A) on the physical properties and surface activity of KL4-surfactant. Biophys. J. 92:482-492.
    • (2007) Biophys. J , vol.92 , pp. 482-492
    • Saenz, A.1    Canadas, O.2    Bagatolli, L.A.3    Sanchez-Barbero, F.4    Johnson, M.E.5    Casals, C.6
  • 17
    • 36849119614 scopus 로고
    • Polarization of the luminescence of phenantrene
    • Azumi, T., and S. P. McGlynn. 1962. Polarization of the luminescence of phenantrene. J. Chem. Phys. 37:2413-2420.
    • (1962) J. Chem. Phys , vol.37 , pp. 2413-2420
    • Azumi, T.1    McGlynn, S.P.2
  • 18
    • 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
  • 19
    • 36549078275 scopus 로고    scopus 로고
    • SP-A forms extensive lattice-like structures on DPPC/rough-lipopolysaccharide mixed monolayers
    • Garcia-Verdugo, I., O. Canadas, S. G. Taneva, K. M. W. Keough, and C. Casals. 2007. SP-A forms extensive lattice-like structures on DPPC/rough-lipopolysaccharide mixed monolayers. Biophys. J. 93:3529-3540.
    • (2007) Biophys. J , vol.93 , pp. 3529-3540
    • Garcia-Verdugo, I.1    Canadas, O.2    Taneva, S.G.3    Keough, K.M.W.4    Casals, C.5
  • 20
    • 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
  • 21
    • 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
  • 22
    • 0021989093 scopus 로고
    • Molecular basis of bacterial outer membrane permeability
    • Nikaido, H., and M. Vaara. 1985. Molecular basis of bacterial outer membrane permeability. Microbiol. Rev. 49:1-32.
    • (1985) Microbiol. Rev , vol.49 , pp. 1-32
    • Nikaido, H.1    Vaara, M.2
  • 23
    • 0027832208 scopus 로고
    • Nucleation and growth in supersaturated monolayers
    • Vollhardt, D. 1993. Nucleation and growth in supersaturated monolayers. Adv. Colloid Interface Sci. 47:1-23.
    • (1993) Adv. Colloid Interface Sci , vol.47 , pp. 1-23
    • Vollhardt, D.1
  • 24
    • 33750526442 scopus 로고    scopus 로고
    • Nucleation in monolayers
    • Vollhardt, D. 2006. Nucleation in monolayers. Adv. Colloid Interface Sci. 123-126:173-188.
    • (2006) Adv. Colloid Interface Sci , vol.123-126 , pp. 173-188
    • Vollhardt, D.1
  • 25
    • 0001217809 scopus 로고
    • The collapse of surfactant monolayers at the air - water interface
    • Smith, R. D., and J. C. Berg. 1980. The collapse of surfactant monolayers at the air - water interface. J. Colloid Interface Sci. 74:273-286.
    • (1980) J. Colloid Interface Sci , vol.74 , pp. 273-286
    • Smith, R.D.1    Berg, J.C.2
  • 26
    • 24044460369 scopus 로고    scopus 로고
    • Divalent cations affect chain mobility and aggregate structure of lipopolysaccharide from Salmonella minnesota reflected in a decrease of its biological activity
    • Garidel, P., M. Rappolt, A. B. Schromm, J. Howe, K. Lohner, J. Andra, M. H. J. Koch, and K. Brandenburg. 2005. Divalent cations affect chain mobility and aggregate structure of lipopolysaccharide from Salmonella minnesota reflected in a decrease of its biological activity. Biochim. Biophys. Acta. 1715:122-131.
    • (2005) Biochim. Biophys. Acta , vol.1715 , pp. 122-131
    • Garidel, P.1    Rappolt, M.2    Schromm, A.B.3    Howe, J.4    Lohner, K.5    Andra, J.6    Koch, M.H.J.7    Brandenburg, K.8
  • 27
    • 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
  • 28
    • 2942753883 scopus 로고    scopus 로고
    • Structure of supported bilayers composed of lipopolysaccharides and bacterial phospholipids: Raft formation and implications for bacterial resistance
    • Tong, J., and T. J. McIntosh. 2004. Structure of supported bilayers composed of lipopolysaccharides and bacterial phospholipids: raft formation and implications for bacterial resistance. Biophys. J. 86:3759-3771.
    • (2004) Biophys. J , vol.86 , pp. 3759-3771
    • Tong, J.1    McIntosh, T.J.2
  • 29
    • 0034718563 scopus 로고    scopus 로고
    • The lipopolysaccharide barrier: Correlation of antibiotic susceptibility with antibiotic permeability and fluorescent probe binding kinetics
    • Snyder, D. S., and T. J. McIntosh. 2000. The lipopolysaccharide barrier: correlation of antibiotic susceptibility with antibiotic permeability and fluorescent probe binding kinetics. Biochemistry. 39:11777-11787.
    • (2000) Biochemistry , vol.39 , pp. 11777-11787
    • Snyder, D.S.1    McIntosh, T.J.2
  • 30
    • 0025218933 scopus 로고
    • Partitioning of hydrophobic probes into lipopolysaccharide bilayers
    • Vaara, M., W. Z. Plachy, and H. Nikaido. 1990. Partitioning of hydrophobic probes into lipopolysaccharide bilayers. Biochim. Biophys. Acta. 1024:152-158.
    • (1990) Biochim. Biophys. Acta , vol.1024 , pp. 152-158
    • Vaara, M.1    Plachy, W.Z.2    Nikaido, H.3
  • 31
    • 0037417761 scopus 로고    scopus 로고
    • Lipopolysaccharides in bacterial membranes act like cholesterol in eukaryotic plasma membranes in providing protection against melittin-induced bilayer lysis
    • Allende, D., and T. J. McIntosh. 2003. Lipopolysaccharides in bacterial membranes act like cholesterol in eukaryotic plasma membranes in providing protection against melittin-induced bilayer lysis. Biochemistry. 42:1101-1108.
    • (2003) Biochemistry , vol.42 , pp. 1101-1108
    • Allende, D.1    McIntosh, T.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.