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Volumn 6, Issue 5, 2012, Pages 4147-4156

Adsorption of surfactant lipids by single-walled carbon nanotubes in mouse lung upon pharyngeal aspiration

Author keywords

Carbon nanotubes; Macrophages; Surfactant

Indexed keywords

ANIMAL MODEL; AQUEOUS PHASE; BRONCHOALVEOLAR LAVAGE FLUID; HYDROPHOBIC ALKYL CHAIN; IN-VITRO; IN-VIVO; LIQUID CHROMATOGRAPHY-MASS SPECTROMETRY; LUNG CELLS; MOLECULAR SPECIATION; MOUSE LUNG; MOUSE MODELS; PHOSPHATIDYL CHOLINE; PHOSPHATIDYLGLYCEROLS; PHOSPHOLIPID BINDING; POLAR HEADGROUPS; PULMONARY SURFACTANTS; STRUCTURAL ASSESSMENTS; SURFACTANT COATING; SURFACTANT PROTEINS;

EID: 84863766513     PISSN: 19360851     EISSN: 1936086X     Source Type: Journal    
DOI: 10.1021/nn300626q     Document Type: Article
Times cited : (170)

References (48)
  • 1
    • 79952317008 scopus 로고    scopus 로고
    • The influence of pulmonary surfactant on nanoparticulate drug delivery systems
    • Schleh, C.; Rothen-Rutishauser, B.; Kreyling, W. G. The Influence of Pulmonary Surfactant on Nanoparticulate Drug Delivery Systems. Eur. J. Pharm. Biopharm. 2011, 77, 350-352.
    • (2011) Eur. J. Pharm. Biopharm. , vol.77 , pp. 350-352
    • Schleh, C.1    Rothen-Rutishauser, B.2    Kreyling, W.G.3
  • 4
    • 0033071977 scopus 로고    scopus 로고
    • Lung epithelium-specific proteins: Characteristics and potential applications as markers
    • Hermans, C.; Bernard, A. Lung Epithelium-Specific Proteins: Characteristics and Potential Applications as Markers. Am. J. Respir. Crit. Care Med. 1999, 159, 646-678.
    • (1999) Am. J. Respir. Crit. Care Med. , vol.159 , pp. 646-678
    • Hermans, C.1    Bernard, A.2
  • 5
    • 78650061496 scopus 로고    scopus 로고
    • The adsorption of biomolecules to multi-walled carbon nanotubes is influenced by both pulmonary surfactant lipids and surface chemistry
    • Gasser, M.; Rothen-Rutishauser, B.; Krug, H. F.; Gehr, P.; Nelle, M.; Yan, B.; Wick, P. The Adsorption of Biomolecules to Multi-Walled Carbon Nanotubes Is Influenced by Both Pulmonary Surfactant Lipids and Surface Chemistry. J. Nanobiotechnol. 2010, 31.
    • (2010) J. Nanobiotechnol. , pp. 31
    • Gasser, M.1    Rothen-Rutishauser, B.2    Krug, H.F.3    Gehr, P.4    Nelle, M.5    Yan, B.6    Wick, P.7
  • 6
    • 33847789142 scopus 로고    scopus 로고
    • Understanding the nanoparticle-protein corona using methods to quantify exchange rates and affinities of proteins for nanoparticles
    • Cedervall, T.; Lynch, I.; Lindman, S.; Berggard, T.; Thulin, E.; Nilsson, H.; Dawson, K. A.; Linse, S. Understanding the Nanoparticle-Protein Corona Using Methods To Quantify Exchange Rates and Affinities of Proteins for Nanoparticles. Proc. Natl. Acad. Sci. U. S. A. 2007, 104, 2050-2055.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 2050-2055
    • Cedervall, T.1    Lynch, I.2    Lindman, S.3    Berggard, T.4    Thulin, E.5    Nilsson, H.6    Dawson, K.A.7    Linse, S.8
  • 7
    • 55749091647 scopus 로고    scopus 로고
    • Nanoparticle size and surface properties determine the protein corona with possible implications for biological impacts
    • Lundqvist, M.; Stigler, J.; Elia, G.; Lynch, I.; Cedervall, T.; Dawson, K. A. Nanoparticle Size and Surface Properties Determine the Protein Corona with Possible Implications for Biological Impacts. Proc. Natl. Acad. Sci. U. S. A. 2008, 105, 14265-14270.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 14265-14270
    • Lundqvist, M.1    Stigler, J.2    Elia, G.3    Lynch, I.4    Cedervall, T.5    Dawson, K.A.6
  • 10
    • 56449122424 scopus 로고    scopus 로고
    • The influence of protein adsorption on nanoparticle association with cultured endothelial cells
    • Ehrenberg, M. S.; Friedman, A. E.; Finkelstein, J. N.; Oberdorster, G.; McGrath, J. L. The Influence of Protein Adsorption on Nanoparticle Association with Cultured Endothelial Cells. Biomaterials 2009, 30, 603-610.
    • (2009) Biomaterials , vol.30 , pp. 603-610
    • Ehrenberg, M.S.1    Friedman, A.E.2    Finkelstein, J.N.3    Oberdorster, G.4    McGrath, J.L.5
  • 13
    • 73849090193 scopus 로고    scopus 로고
    • Complement and its role in innate and adaptive immune responses
    • Dunkelberger, J. R.; Song, W. C. Complement and Its Role in Innate and Adaptive Immune Responses. Cell Res. 2010, 20, 34-50.
    • (2010) Cell Res. , vol.20 , pp. 34-50
    • Dunkelberger, J.R.1    Song, W.C.2
  • 17
    • 76249088013 scopus 로고    scopus 로고
    • Pulmonary surfactant phosphatidylglycerol inhibits respiratory syncytial virus-induced inflammation and infection
    • Numata, M.; Chu, H. W.; Dakhama, A.; Voelker, D. R. Pulmonary Surfactant Phosphatidylglycerol Inhibits Respiratory Syncytial Virus-Induced Inflammation and Infection. Proc. Natl. Acad. Sci. U. S. A. 2010, 107, 320-325.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 320-325
    • Numata, M.1    Chu, H.W.2    Dakhama, A.3    Voelker, D.R.4
  • 18
    • 0017120797 scopus 로고
    • Phosphatidylglycerol in lung surfactant. III. Possible modifier of surfactant function
    • Hallman, M.; Gluck, L. Phosphatidylglycerol in Lung Surfactant. III. Possible Modifier of Surfactant Function. J. Lipid Res. 1976, 17, 257-262.
    • (1976) J. Lipid Res. , vol.17 , pp. 257-262
    • Hallman, M.1    Gluck, L.2
  • 21
    • 28444454083 scopus 로고    scopus 로고
    • 1-DE MS and 2-D LC-MS analysis of the mouse bronchoalveolar lavage proteome
    • Guo, Y.; Ma, S. F.; Grigoryev, D.; Van Eyk, J.; Garcia, J. G. 1-DE MS and 2-D LC-MS Analysis of the Mouse Bronchoalveolar Lavage Proteome. Proteomics 2005, 5, 4608-4624.
    • (2005) Proteomics , vol.5 , pp. 4608-4624
    • Guo, Y.1    Ma, S.F.2    Grigoryev, D.3    Van Eyk, J.4    Garcia, J.G.5
  • 22
    • 65249097227 scopus 로고    scopus 로고
    • Oxidative stress and asthma: Proteome analysis of chitinase-like proteins and FIZZ1 in lung tissue and bronchoalveolar lavage fluid
    • Zhang, L.; Wang, M.; Kang, X.; Boontheung, P.; Li, N.; Nel, A. E.; Loo, J. A. Oxidative Stress and Asthma: Proteome Analysis of Chitinase-like Proteins and FIZZ1 in Lung Tissue and Bronchoalveolar Lavage Fluid. J. Proteome Res. 2009, 8, 1631-1638.
    • (2009) J. Proteome Res. , vol.8 , pp. 1631-1638
    • Zhang, L.1    Wang, M.2    Kang, X.3    Boontheung, P.4    Li, N.5    Nel, A.E.6    Loo, J.A.7
  • 24
    • 33748167814 scopus 로고    scopus 로고
    • Surfactant protein C; its unique properties and emerging immunomodulatory role in the lung
    • Mulugeta, S.; Meers, M. F. Surfactant Protein C; Its Unique Properties and Emerging Immunomodulatory Role in the Lung. Microbes Infect. 2006, 8, 2317-2323.
    • (2006) Microbes Infect. , vol.8 , pp. 2317-2323
    • Mulugeta, S.1    Meers, M.F.2
  • 26
    • 0031060118 scopus 로고    scopus 로고
    • The pulmonary surfactant system: Biochemical and clinical aspects
    • Creuwels, L. A. J. M.; van Golde, L. M. G.; Haagsman, H. P. The Pulmonary Surfactant System: Biochemical and Clinical Aspects. Lung 1997, 175, 1-39.
    • (1997) Lung , vol.175 , pp. 1-39
    • Creuwels, L.A.J.M.1    Van Golde, L.M.G.2    Haagsman, H.P.3
  • 27
    • 0025239383 scopus 로고
    • Hydrophobic surfactant-associated polypeptides: SP-C is a lipopeptide with two palmitoylated cysteine residues, whereas SP-B lacks covalently linked fatty acyl groups
    • Curstedt, T.; Johansson, J.; Persson, P.; Eklund, A.; Robertson, B.; Lowenadler, B.; Jornvall, H. Hydrophobic Surfactant-Associated Polypeptides: SP-C Is a Lipopeptide with Two Palmitoylated Cysteine Residues, Whereas SP-B Lacks Covalently Linked Fatty Acyl Groups. Proc. Natl. Acad. Sci. U. S. A. 1990, 87, 2985-2989.
    • (1990) Proc. Natl. Acad. Sci. U. S. A. , vol.87 , pp. 2985-2989
    • Curstedt, T.1    Johansson, J.2    Persson, P.3    Eklund, A.4    Robertson, B.5    Lowenadler, B.6    Jornvall, H.7
  • 28
    • 0022970411 scopus 로고
    • Effect of rat surfactant lipids on complement and Fc receptors of macrophages
    • Coonrod, J. D.; Jarrells, M. C.; Yoneda, K. Effect of Rat Surfactant Lipids on Complement and Fc Receptors of Macrophages. Infect. Immun. 1986, 54, 371-378.
    • (1986) Infect. Immun. , vol.54 , pp. 371-378
    • Coonrod, J.D.1    Jarrells, M.C.2    Yoneda, K.3
  • 29
    • 0026649264 scopus 로고
    • The surfactant system of the adult lung: Physiology and clinical perspectives
    • Hamm, H.; Fabel, H.; Bartsch, W. The Surfactant System of the Adult Lung: Physiology and Clinical Perspectives. Clin. Invest. 1992, 70, 637-657.
    • (1992) Clin. Invest. , vol.70 , pp. 637-657
    • Hamm, H.1    Fabel, H.2    Bartsch, W.3
  • 30
    • 84955814602 scopus 로고
    • Pulmonary surfactant: Surface properties and function of alveolar and airway surfactant
    • Schürch, S.; Bachofenb, H.; Possmayer, F. Pulmonary Surfactant: Surface Properties and Function of Alveolar and Airway Surfactant. Pure Appl. Chem. 1992, 64, 1745-1750.
    • (1992) Pure Appl. Chem. , vol.64 , pp. 1745-1750
    • Schürch, S.1    Bachofenb, H.2    Possmayer, F.3
  • 31
    • 76149120388 scopus 로고    scopus 로고
    • Autodock vina: Improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading
    • Trott, O.; Olson, A. J. AutoDock Vina: Improving the Speed and Accuracy of Docking with a New Scoring Function, Efficient Optimization, and Multithreading. J. Comput. Chem. 2010, 31, 455-461.
    • (2010) J. Comput. Chem. , vol.31 , pp. 455-461
    • Trott, O.1    Olson, A.J.2
  • 32
    • 74049137112 scopus 로고    scopus 로고
    • Molecular dynamics study of dipalmitoylphosphatidylcholine lipid layer self-assembly onto a single-walled carbon nanotube
    • Wang, H.; Michielssens, S.; Moors, S.; Ceulemans, A. Molecular Dynamics Study of Dipalmitoylphosphatidylcholine Lipid Layer Self-Assembly onto a Single-Walled Carbon Nanotube. Nano Res. 2009, 2, 945-954.
    • (2009) Nano Res. , vol.2 , pp. 945-954
    • Wang, H.1    Michielssens, S.2    Moors, S.3    Ceulemans, A.4
  • 33
    • 34547602083 scopus 로고    scopus 로고
    • Carbon nanotube/detergent interactions via coarse-grained molecular dynamics
    • Wallace, E. J.; Sansom, M. S. Carbon Nanotube/Detergent Interactions via Coarse-Grained Molecular Dynamics. Nano Lett. 2007, 7, 1923-1928.
    • (2007) Nano Lett. , vol.7 , pp. 1923-1928
    • Wallace, E.J.1    Sansom, M.S.2
  • 34
    • 33751519372 scopus 로고    scopus 로고
    • Oxidized phosphatidylserine-CD36 interactions play an essential role in macrophage-dependent phagocytosis of apoptotic cells
    • Greenberg, M. E.; Sun, M.; Zhang, R.; Febbraio, M.; Silverstein, R.; Hazen, S. L. Oxidized Phosphatidylserine-CD36 Interactions Play an Essential Role in Macrophage-Dependent Phagocytosis of Apoptotic Cells. J. Exp. Med. 2006, 203, 2613-2625.
    • (2006) J. Exp. Med. , vol.203 , pp. 2613-2625
    • Greenberg, M.E.1    Sun, M.2    Zhang, R.3    Febbraio, M.4    Silverstein, R.5    Hazen, S.L.6
  • 35
    • 37049039277 scopus 로고    scopus 로고
    • Structures of T cell immunoglobulin mucin protein 4 show a metal-ion-dependent ligand binding site where phosphatidylserine binds
    • Santiago, C.; Ballesteros, A.; Martinez-Munoz, L.; Mellado, M.; Kaplan, G. G.; Freeman, G. J.; Casasnovas, J. M. Structures of T Cell Immunoglobulin Mucin Protein 4 Show a Metal-Ion-Dependent Ligand Binding Site Where Phosphatidylserine Binds. Immunity 2007, 27, 941-951.
    • (2007) Immunity , vol.27 , pp. 941-951
    • Santiago, C.1    Ballesteros, A.2    Martinez-Munoz, L.3    Mellado, M.4    Kaplan, G.G.5    Freeman, G.J.6    Casasnovas, J.M.7
  • 37
    • 84859133277 scopus 로고    scopus 로고
    • Impaired clearance and enhanced pulmonary inflammatory/fibrotic response to carbon nanotubes in myeloperoxidase-deficient mice
    • 10.1371/journal.pone.0030923
    • Shvedova, A. A.; Kapralov, A. A.; Feng, W.; Kisin, E. R.; Murray, A.; Mercer, R.; St. Croix, C.; Lang, M.; Watkins, S.; Konduru, N.; et al. Impaired Clearance and Enhanced Pulmonary Inflammatory/Fibrotic Response to Carbon Nanotubes in Myeloperoxidase-Deficient Mice. PLoS One 2012, 10.1371/journal. pone.0030923.
    • (2012) PLoS One
    • Shvedova, A.A.1    Kapralov, A.A.2    Feng, W.3    Kisin, E.R.4    Murray, A.5    Mercer, R.6    Croix, S.C.7    Lang, M.8    Watkins, S.9    Konduru, N.10
  • 40
    • 79952302512 scopus 로고    scopus 로고
    • Physical-chemical aspects of protein corona: Relevance to in vitro and in vivo biological impacts of nanoparticles
    • Monopoli, M. P.; Walczyk, D.; Campbell, A.; Elia, G.; Lynch, I.; Bombelli, F. B.; Dawson, K. A. Physical-Chemical Aspects of Protein Corona: Relevance to In Vitro and In Vivo Biological Impacts of Nanoparticles. J. Am. Chem. Soc. 2011, 133, 2525-2534.
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 2525-2534
    • Monopoli, M.P.1    Walczyk, D.2    Campbell, A.3    Elia, G.4    Lynch, I.5    Bombelli, F.B.6    Dawson, K.A.7
  • 41
    • 79959808397 scopus 로고    scopus 로고
    • Proteomic characterization of engineered nanomaterial-protein interactions in relation to surface reactivity
    • Sund, J.; Alenius, H.; Vippola, M.; Savolainen, K.; Puustinen, A. Proteomic Characterization of Engineered Nanomaterial-Protein Interactions in Relation to Surface Reactivity. ACS Nano 2011, 5, 4300-4309.
    • (2011) ACS Nano , vol.5 , pp. 4300-4309
    • Sund, J.1    Alenius, H.2    Vippola, M.3    Savolainen, K.4    Puustinen, A.5
  • 42
    • 67349133162 scopus 로고    scopus 로고
    • Differential proteomics analysis of the surface heterogeneity of dextran iron oxide nanoparticles and the implications for their in vivo clearance
    • Simberg, D.; Park, J. H.; Karmali, P. P.; Zhang, W. M.; Merkulov, S.; McCrae, K.; Bhatia, S. N.; Sailor, M.; Ruoslahti, E. Differential Proteomics Analysis of the Surface Heterogeneity of Dextran Iron Oxide Nanoparticles and the Implications for Their In Vivo Clearance. Biomaterials 2009, 30, 3926-3933.
    • (2009) Biomaterials , vol.30 , pp. 3926-3933
    • Simberg, D.1    Park, J.H.2    Karmali, P.P.3    Zhang, W.M.4    Merkulov, S.5    McCrae, K.6    Bhatia, S.N.7    Sailor, M.8    Ruoslahti, E.9
  • 45
    • 33748329694 scopus 로고    scopus 로고
    • The importance of an endotoxin-free environment during the production of nanoparticles used in medical applications
    • Vallhov, H.; Qin, J.; Johansson, S. M.; Ahlborg, N.; Muhammed, M. A.; Scheynius, A.; Gabrielsson, S. The Importance of an Endotoxin-Free Environment during the Production of Nanoparticles Used in Medical Applications. Nano Lett. 2006, 6, 1682-1686.
    • (2006) Nano Lett. , vol.6 , pp. 1682-1686
    • Vallhov, H.1    Qin, J.2    Johansson, S.M.3    Ahlborg, N.4    Muhammed, M.A.5    Scheynius, A.6    Gabrielsson, S.7
  • 48
    • 70449158340 scopus 로고
    • A simple method for the isolation and purification of total lipides from animal tissues
    • Folch, J.; Lees, M.; Sloane Stanley, G. H. A Simple Method for the Isolation and Purification of Total Lipides from Animal Tissues. J. Biol. Chem. 1957, 226, 497-509.
    • (1957) J. Biol. Chem. , vol.226 , pp. 497-509
    • Folch, J.1    Lees, M.2    Sloane Stanley, G.H.3


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