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Volumn 24, Issue 10, 2010, Pages 3662-3673

Fluidizing effects of C-reactive protein on lung surfactant membranes: Protective role of surfactant protein A

Author keywords

Fluorescence; Lipid domains; Lipid protein interaction; Lung injury; Membrane fluidity; Protein protein interaction

Indexed keywords

C REACTIVE PROTEIN; PROTEIN A; SURFACTANT PROTEIN A;

EID: 77957844255     PISSN: 08926638     EISSN: 15306860     Source Type: Journal    
DOI: 10.1096/fj.09-142646     Document Type: Article
Times cited : (26)

References (38)
  • 1
    • 0034869253 scopus 로고    scopus 로고
    • Human C-reactive protein: Expression, structure, and function
    • DOI 10.1016/S0161-5890(01)00042-6, PII S0161589001000426
    • Volanakis, J. E. (2001) Human C-reactive protein: expression, structure, and function. Mol. Immunol. 38, 189-197 (Pubitemid 32786776)
    • (2001) Molecular Immunology , vol.38 , Issue.2-3 , pp. 189-197
    • Volanakis, J.E.1
  • 3
    • 26044483536 scopus 로고    scopus 로고
    • C-reactive protein: Ligands, receptors and role in inflammation
    • DOI 10.1016/j.clim.2005.08.004, PII S1521661605002809
    • Marnell, L., Mold, C., and Du Clos, T. W. (2005) C-reactive protein: ligands, receptors and role in inflammation. Clin. Immunol. 117, 104-111 (Pubitemid 41407719)
    • (2005) Clinical Immunology , vol.117 , Issue.2 , pp. 104-111
    • Marnell, L.1    Mold, C.2    Du Clos, T.W.3
  • 4
    • 51649092992 scopus 로고    scopus 로고
    • C-reactive protein and coronary heart disease: A critical review
    • Casas, J. P., Shah, T., Hingorani, A. D., Danesh, J., and Pepys, M. B. (2008) C-reactive protein and coronary heart disease: a critical review. J. Intern. Med. 264, 295-314
    • (2008) J. Intern. Med. , vol.264 , pp. 295-314
    • Casas, J.P.1    Shah, T.2    Hingorani, A.D.3    Danesh, J.4    Pepys, M.B.5
  • 5
    • 67349231433 scopus 로고    scopus 로고
    • 2+and phosphocholine interactions with C-reactive protein using a surface plasmon resonance biosensor
    • 2+ and phosphocholine interactions with C-reactive protein using a surface plasmon resonance biosensor. Anal. Biochem. 391, 39-44
    • (2009) Anal. Biochem. , vol.391 , pp. 39-44
    • Christopeit, T.1    Gossas, T.2    Danielson, U.H.3
  • 6
    • 57749172475 scopus 로고    scopus 로고
    • Structural recognition and functional activation of FcγR by innate pentraxins
    • Lu, J., Marnell, L. L., Marjon, K. D., Mold, C., Du Clos, T. W., and Sun, P. D. (2008) Structural recognition and functional activation of FcγR by innate pentraxins. Nature 456, 989-992
    • (2008) Nature , vol.456 , pp. 989-992
    • Lu, J.1    Marnell, L.L.2    Marjon, K.D.3    Mold, C.4    Du Clos, T.W.5    Sun, P.D.6
  • 7
    • 43149103164 scopus 로고    scopus 로고
    • The connection between C-reactive protein and atherosclerosis
    • Singh, S. K., Suresh, M. V., Voleti, B., and Agrawal, A. (2008) The connection between C-reactive protein and atherosclerosis. Ann. Med. 40, 110-120
    • (2008) Ann. Med. , vol.40 , pp. 110-120
    • Singh, S.K.1    Suresh, M.V.2    Voleti, B.3    Agrawal, A.4
  • 13
    • 0035115645 scopus 로고    scopus 로고
    • Expression of C-reactive protein in the human respiratory tract
    • Gould, J. M., and Weiser, J. N. (2001) Expression of C-reactive protein in the human respiratory tract. Infect. Immun. 69, 1747-1754
    • (2001) Infect. Immun. , vol.69 , pp. 1747-1754
    • Gould, J.M.1    Weiser, J.N.2
  • 14
    • 3342998326 scopus 로고    scopus 로고
    • Expression of C-reactive protein in human lung epithelial cells and upregulation by cytokines and carbon particles
    • Ramage, L., Proudfoot, L., and Guy, K. (2004) Expression of C-reactive protein in human lung epithelial cells and upregulation by cytokines and carbon particles. Inhal. Toxicol. 16, 607-613
    • (2004) Inhal. Toxicol. , vol.16 , pp. 607-613
    • Ramage, L.1    Proudfoot, L.2    Guy, K.3
  • 15
    • 0029949314 scopus 로고    scopus 로고
    • Expression of C-reactive protein by alveolar macrophages
    • Dong, Q., and Wright, J. R. (1996) Expression of C-reactive protein by alveolar macrophages. J. Immunol. 156, 4815-4820
    • (1996) J. Immunol. , vol.156 , pp. 4815-4820
    • Dong, Q.1    Wright, J.R.2
  • 17
  • 18
    • 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
  • 19
    • 0027505573 scopus 로고
    • Reversible and irreversible inactivation of preformed pulmonary surfactant surface films by changes in subphase constituents
    • Amirkhanian, J. D., and Taeusch, H. W. (1993) Reversible and irreversible inactivation of preformed pulmonary surfactant surface films by changes in subphase constituents. Biochim. Biophys. Acta 1165, 321-326
    • (1993) Biochim. Biophys. Acta , vol.1165 , pp. 321-326
    • Amirkhanian, J.D.1    Taeusch, H.W.2
  • 20
    • 0028840675 scopus 로고
    • Phosphocholine reverses inhibition of pulmonary surfactant adsorption caused by C-reactive protein
    • McEachren, T. M., and Keough, K. M. (1995) Phosphocholine reverses inhibition of pulmonary surfactant adsorption caused by C-reactive protein. Am. J. Physiol. 269, L492-L497
    • (1995) Am. J. Physiol. , vol.269
    • McEachren, T.M.1    Keough, K.M.2
  • 22
    • 14844297019 scopus 로고    scopus 로고
    • Role of the degree of oligomerization in the structure and function of human surfactant protein a
    • DOI 10.1074/jbc.M410266200
    • Sanchez-Barbero, F., Strassner, J., Garcia-Canero, R., Steinhilber, W., and Casals, C. (2005) Role of the degree of oligomerization in the structure and function of human surfactant protein A. J. Biol. Chem. 280, 7659-7670 (Pubitemid 40349659)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.9 , pp. 7659-7670
    • Sanchez-Barbero, F.1    Strassner, J.2    Garcia-Canero, R.3    Steinhilber, W.4    Casals, C.5
  • 23
    • 34548802927 scopus 로고    scopus 로고
    • Structural and functional differences among human surfactant proteins SP-A1, SP-A2 and co-expressed SP-A1/SP-A2: Role of supratrimeric oligomerization
    • DOI 10.1042/BJ20070275
    • Sanchez-Barbero, F., Rivas, G., Steinhilber, W., and Casals, C. (2007) Structural and functional differences among human surfactant proteins SP-A1, SP-A2 and co-expressed SP-A1/SPA2: role of supratrimeric oligomerization. Biochem. J. 406, 479-489 (Pubitemid 47425454)
    • (2007) Biochemical Journal , vol.406 , Issue.3 , pp. 479-489
    • Sanchez-Barbero, F.1    Rivas, G.2    Steinhilber, W.3    Casals, C.4
  • 24
    • 55949101551 scopus 로고    scopus 로고
    • SP-A permeabilizes lipopolysaccharide membranes by forming protein aggregates that extract lipids from the membrane
    • Canadas, O., Garcia-Verdugo, I., Keough, K. M., and Casals, C. (2008) SP-A permeabilizes lipopolysaccharide membranes by forming protein aggregates that extract lipids from the membrane. Biophys. J. 95, 3287-3294
    • (2008) Biophys. J. , vol.95 , pp. 3287-3294
    • Canadas, O.1    Garcia-Verdugo, I.2    Keough, K.M.3    Casals, C.4
  • 25
    • 0003633755 scopus 로고    scopus 로고
    • Institute for Animal Laboratory Research National Academy Press, Washington D.C.
    • Institute for Animal Laboratory Research (1996) Guide for the Care and Use of Laboratory Animals, National Academy Press, Washington D.C.
    • (1996) Guide for the Care and Use of Laboratory Animals
  • 27
    • 33846432384 scopus 로고    scopus 로고
    • Effect of surfactant protein a on the physical properties and surface activity of KL4-surfactant
    • Saenz, A., Canadas, O., Bagatolli, L. A., Sanchez-Barbero, F., Johnson, M. E., and Casals, C. (2007) Effect of surfactant protein 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
  • 28
    • 33749046710 scopus 로고    scopus 로고
    • To see or not to see: Lateral organization of biological membranes and fluorescence microscopy
    • Bagatolli, L. A. (2006) To see or not to see: lateral organization of biological membranes and fluorescence microscopy. Biochim. Biophys. Acta 1758, 1541-1556
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 1541-1556
    • Bagatolli, L.A.1
  • 29
    • 0025742883 scopus 로고
    • Quantitation of lipid phases in phospholipid vesicles by the generalized polarization of Laurdan fluorescence
    • Parasassi, T., De Stasio, G., Ravagnan, G., Rusch, R. M., and Gratton, E. (1991) Quantitation of lipid phases in phospholipid vesicles by the generalized polarization of Laurdan fluorescence. Biophys. J. 60, 179-189
    • (1991) Biophys. J. , vol.60 , pp. 179-189
    • Parasassi, T.1    De Stasio, G.2    Ravagnan, G.3    Rusch, R.M.4    Gratton, E.5
  • 30
    • 67349258550 scopus 로고    scopus 로고
    • Parameters modulating the maximum insertion pressure of proteins and peptides in lipid monolayers
    • Calvez, P., Bussieres, S., Eric, D., and Salesse, C. (2009) Parameters modulating the maximum insertion pressure of proteins and peptides in lipid monolayers. Biochimie (Paris) 91, 718-733
    • (2009) Biochimie (Paris) , vol.91 , pp. 718-733
    • Calvez, P.1    Bussieres, S.2    Eric, D.3    Salesse, C.4
  • 31
    • 0030606012 scopus 로고    scopus 로고
    • Lateral pressure in membranes
    • Marsh, D. (1996) Lateral pressure in membranes. Biochim. Biophys. Acta 1286, 183-223
    • (1996) Biochim. Biophys. Acta , vol.1286 , pp. 183-223
    • Marsh, D.1
  • 32
    • 4644268351 scopus 로고    scopus 로고
    • Cholesterol rules: Direct observation of the coexistence of two fluid phases in native pulmonary surfactant membranes at physiological temperatures
    • Bernardino de la Serna, J., Perez-Gil, J., Simonsen, A. C., and Bagatolli, L. A. (2004) Cholesterol rules: direct observation of the coexistence of two fluid phases in native pulmonary surfactant membranes at physiological temperatures. J. Biol. Chem. 279, 40715-40722
    • (2004) J. Biol. Chem. , vol.279 , pp. 40715-40722
    • De La Bernardino Serna, J.1    Perez-Gil, J.2    Simonsen, A.C.3    Bagatolli, L.A.4
  • 33
    • 0023055343 scopus 로고
    • Differential scanning calorimetric studies of lipid-protein interactions in model membrane systems
    • McElhaney, R. N. (1986) Differential scanning calorimetric studies of lipid-protein interactions in model membrane systems. Biochim. Biophys. Acta 864, 361-421
    • (1986) Biochim. Biophys. Acta , vol.864 , pp. 361-421
    • McElhaney, R.N.1
  • 35
    • 67649306728 scopus 로고    scopus 로고
    • Monomeric C-reactive protein activates endothelial cells via interaction with lipid raft microdomains
    • Ji, S. R., Ma, L., Bai, C. J., Shi, J. M., Li, H. Y., Potempa, L. A., Filep, J. G., Zhao, J., and Wu, Y. (2009) Monomeric C-reactive protein activates endothelial cells via interaction with lipid raft microdomains. FASEB J. 23, 1806-1816
    • (2009) FASEB J. , vol.23 , pp. 1806-1816
    • Ji, S.R.1    Ma, L.2    Bai, C.J.3    Shi, J.M.4    Li, H.Y.5    Potempa, L.A.6    Filep, J.G.7    Zhao, J.8    Wu, Y.9
  • 36
    • 33846001313 scopus 로고    scopus 로고
    • Cell membranes and liposomes dissociate C-reactive protein (CRP) to form a new, biologically active structural intermediate: mCRP(m)
    • Ji, S. R., Wu, Y., Zhu, L., Potempa, L. A., Sheng, F. L., Lu, W., and Zhao, J. (2007) Cell membranes and liposomes dissociate C-reactive protein (CRP) to form a new, biologically active structural intermediate: mCRP(m). FASEB J. 21, 284-294
    • (2007) FASEB J. , vol.21 , pp. 284-294
    • Ji, S.R.1    Wu, Y.2    Zhu, L.3    Potempa, L.A.4    Sheng, F.L.5    Lu, W.6    Zhao, J.7


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