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Volumn 85, Issue 4, 2003, Pages 2397-2405

Interaction of pulmonary surfactant protein SP-A with DPPC/Egg-PG bilayers

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM ION; DIPALMITOYLPHOSPHATIDYLCHOLINE; PHOSPHATIDYLGLYCEROL; SURFACTANT PROTEIN A;

EID: 0141642124     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(03)74663-3     Document Type: Article
Times cited : (9)

References (53)
  • 2
    • 70449246528 scopus 로고
    • Phosphorus assay in column chromatography
    • Bartlett, G. R. 1959. Phosphorus assay in column chromatography. J. Biol. Chem. 234:466-468.
    • (1959) J. Biol. Chem. , vol.234 , pp. 466-468
    • Bartlett, G.R.1
  • 4
    • 0346213760 scopus 로고
    • Direct determination of the oriented sample NMR spectrum from the powder spectrum for systems with local axial symmetry
    • Bloom, M., J. H. Davis, and A. L. MacKay. 1981. Direct determination of the oriented sample NMR spectrum from the powder spectrum for systems with local axial symmetry. Chem. Phys. Lett. 80:198-202.
    • (1981) Chem. Phys. Lett. , vol.80 , pp. 198-202
    • Bloom, M.1    Davis, J.H.2    MacKay, A.L.3
  • 5
    • 0002075860 scopus 로고
    • Observation of surface undulations on the mesoscopic length scale by NMR
    • L. Peliti, editor. Plenum Press, New York
    • Bloom, M., and E. Evans. 1991. Observation of surface undulations on the mesoscopic length scale by NMR. In Biologically Inspired Physics. L. Peliti, editor. Plenum Press, New York. 137-147.
    • (1991) Biologically Inspired Physics , pp. 137-147
    • Bloom, M.1    Evans, E.2
  • 6
    • 0000510171 scopus 로고
    • Transverse nuclear spin relaxation in phospholipid bilayer membranes
    • Bloom, M., and E. Sternin. 1987. Transverse nuclear spin relaxation in phospholipid bilayer membranes. Biochemistry. 26:2101-2105.
    • (1987) Biochemistry , vol.26 , pp. 2101-2105
    • Bloom, M.1    Sternin, E.2
  • 8
    • 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., J. Johansson, P. Persson, A. Eklund, B. Robertson B. Löwenadler, and H. Jörnvall. 1990. 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. USA. 87:2985-2989.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 2985-2989
    • Curstedt, T.1    Johansson, J.2    Persson, P.3    Eklund, A.4    Robertson, B.5    Löwenadler, B.6    Jörnvall, H.7
  • 9
    • 0000745176 scopus 로고
    • Quadrupole echo deuteron magnetic resonance spectroscopy in ordered hydrocarbon chains
    • Davis, J. H., K. R. Jeffrey, M. Bloom M. I. Valic and T. P. Higgs. 1976. Quadrupole echo deuteron magnetic resonance spectroscopy in ordered hydrocarbon chains. Chem. Phys. Lett. 42:390-394.
    • (1976) Chem. Phys. Lett. , vol.42 , pp. 390-394
    • Davis, J.H.1    Jeffrey, K.R.2    Bloom, M.3    Valic, M.I.4    Higgs, T.P.5
  • 11
    • 0030894592 scopus 로고    scopus 로고
    • Pulmonary surfactant protein SP-B interacts similarly with dipalmitoylphosphatidylglycerol and dipalmitoylphosphatidylcholine in phosphatidylcholine/phosphatidylglycerol mixture
    • Dico, A. S., J. Hancock, M. R. Morrow, J. Stewart, S. Harris, and K. M. W. Keough. 1997. Pulmonary surfactant protein SP-B interacts similarly with dipalmitoylphosphatidylglycerol and dipalmitoylphosphatidylcholine in phosphatidylcholine/phosphatidylglycerol mixture. Biochemistry. 36:4172-4177.
    • (1997) Biochemistry , vol.36 , pp. 4172-4177
    • Dico, A.S.1    Hancock, J.2    Morrow, M.R.3    Stewart, J.4    Harris, S.5    Keough, K.M.W.6
  • 12
    • 0022844505 scopus 로고
    • Mannose-binding proteins isolated from rat liver contain carbohydrate-recognition domains linked to collagenous tails. Complete primary structures and homology with pulmonary surfactant apoprotein
    • Drickamer, K., M. S. Dordal, and L. Reynolds. 1986. Mannose-binding proteins isolated from rat liver contain carbohydrate-recognition domains linked to collagenous tails. Complete primary structures and homology with pulmonary surfactant apoprotein. J. Biol. Chem. 261:6878-6887.
    • (1986) J. Biol. Chem. , vol.261 , pp. 6878-6887
    • Drickamer, K.1    Dordal, M.S.2    Reynolds, L.3
  • 13
    • 0016757551 scopus 로고
    • Conformation and motion of the choline head group in bilayers of dipalmitoyl-3-sn-phosphatidylcholine
    • Gally, H.-U., W. Niederberger, and J. Seelig. 1975. Conformation and motion of the choline head group in bilayers of dipalmitoyl-3-sn-phosphatidylcholine. Biochemistry. 14:3647-3652.
    • (1975) Biochemistry , vol.14 , pp. 3647-3652
    • Gally, H.-U.1    Niederberger, W.2    Seelig, J.3
  • 14
    • 0015894118 scopus 로고
    • Isolation and characterization of lamellar bodies and tubular myelin from rat lung homogenates
    • Gil, J., and O. K. Reiss. 1973. Isolation and characterization of lamellar bodies and tubular myelin from rat lung homogenates. J. Cell Biol. 58:152-171.
    • (1973) J. Cell Biol. , vol.58 , pp. 152-171
    • Gil, J.1    Reiss, O.K.2
  • 15
    • 0031740674 scopus 로고    scopus 로고
    • Pulmonary surfactant: Functions and molecular composition
    • Goerke, J. 1998. Pulmonary surfactant: functions and molecular composition. Biochim. Biophys. Acta. 1408:79-89.
    • (1998) Biochim. Biophys. Acta , vol.1408 , pp. 79-89
    • Goerke, J.1
  • 19
    • 0022376675 scopus 로고
    • Chemical characterization of lung surfactant apoproteins: Amino acid composition. N-terminal sequence and enzymic digestion
    • Hawgood, S., H. Efrati, J. Schilling, and B. J. Benson. 1985. Chemical characterization of lung surfactant apoproteins: amino acid composition, N-terminal sequence and enzymic digestion. Biochem. Soc. Trans. 13:1092-1096.
    • (1985) Biochem. Soc. Trans. , vol.13 , pp. 1092-1096
    • Hawgood, S.1    Efrati, H.2    Schilling, J.3    Benson, B.J.4
  • 20
    • 0031796861 scopus 로고    scopus 로고
    • Structure and properties of surfactant protein B
    • Hawgood, S., M. Derrick, and F. Poulain. 1998. Structure and properties of surfactant protein B. Biochim. Biophys. Acta. 1408:150-160.
    • (1998) Biochim. Biophys. Acta , vol.1408 , pp. 150-160
    • Hawgood, S.1    Derrick, M.2    Poulain, F.3
  • 21
    • 0031740469 scopus 로고    scopus 로고
    • Structure and properties of surfactant protein C
    • Johansson, J. 1998. Structure and properties of surfactant protein C. Biochim. Biophys. Acta. 1408:161-172.
    • (1998) Biochim. Biophys. Acta , vol.1408 , pp. 161-172
    • Johansson, J.1
  • 22
    • 0023647323 scopus 로고
    • Differential scanning calorimetric studies of aqueous dispersions of phosphatidylcholines containing two polyenoic chains
    • Keough, K. M. W., and N. Kariel. 1987. Differential scanning calorimetric studies of aqueous dispersions of phosphatidylcholines containing two polyenoic chains. Biochim. Biophys. Acta. 902:11-18.
    • (1987) Biochim. Biophys. Acta , vol.902 , pp. 11-18
    • Keough, K.M.W.1    Kariel, N.2
  • 23
    • 0015401048 scopus 로고
    • Surface active material from dog lung. I. Method of isolation
    • King, R. J., and J. A. Clements. 1972. Surface active material from dog lung. I. Method of isolation. Am. J. Physiol. 223:707-714.
    • (1972) Am. J. Physiol. , vol.223 , pp. 707-714
    • King, R.J.1    Clements, J.A.2
  • 25
    • 0025759056 scopus 로고
    • Response of phosphatidylcholine in the gel and liquid-crystalline states to membrane surface charges
    • Macdonald, P. M., J. Leisen, and F. M. Marassi. 1991. Response of phosphatidylcholine in the gel and liquid-crystalline states to membrane surface charges. Biochemistry. 30:3558-3566.
    • (1991) Biochemistry , vol.30 , pp. 3558-3566
    • Macdonald, P.M.1    Leisen, J.2    Marassi, F.M.3
  • 26
    • 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
  • 27
    • 0027331636 scopus 로고
    • 2H NMR studies of the effect of pulmonary surfactant SP-C on the 1,2-dipalmitoyl-sn-glycero-3-phosphocholine headgroup: A model for transbilayer peptides in surfactant and biological membranes
    • 2H NMR studies of the effect of pulmonary surfactant SP-C on the 1,2-dipalmitoyl-sn-glycero-3-phosphocholine headgroup: a model for transbilayer peptides in surfactant and biological membranes. Biochemistry. 32:11338-11344.
    • (1993) Biochemistry , vol.32 , pp. 11338-11344
    • Morrow, M.R.1    Taneva, S.2    Simatos, G.A.3    Allwood, L.A.4    Keough, K.M.W.5
  • 28
    • 0031663381 scopus 로고    scopus 로고
    • Structural changes of surfactant protein A induced by cations reorient the protein on lipid bilayers
    • Palaniyar, N., R. A. Ridsdale, C. F. Holterman, K. Inchley, F. Possmayer, and G. Harauz. 1998. Structural changes of surfactant protein A induced by cations reorient the protein on lipid bilayers. J. Struct. Biol. 122:297-310.
    • (1998) J. Struct. Biol. , vol.122 , pp. 297-310
    • Palaniyar, N.1    Ridsdale, R.A.2    Holterman, C.F.3    Inchley, K.4    Possmayer, F.5    Harauz, G.6
  • 30
    • 0038064658 scopus 로고    scopus 로고
    • Interfacial properties of surfactant proteins
    • Pérez-Gil, J., and K. M. W. Keough. 1998. Interfacial properties of surfactant proteins. Biochim. Biophys. Acta. 1408:203-217.
    • (1998) Biochim. Biophys. Acta , vol.1408 , pp. 203-217
    • Pérez-Gil, J.1    Keough, K.M.W.2
  • 31
    • 0026634092 scopus 로고
    • Effects of surfactant apolipoproteins on liposome structure: Implications for tubular myelin formation
    • Poulain, F. R., L. Allen, M. C. Williams, R. L. Hamilton, and S. Hawgood. 1992. Effects of surfactant apolipoproteins on liposome structure: implications for tubular myelin formation. Am. J. Physiol. 262:L730-L739.
    • (1992) Am. J. Physiol. , vol.262
    • Poulain, F.R.1    Allen, L.2    Williams, M.C.3    Hamilton, R.L.4    Hawgood, S.5
  • 33
    • 0029854027 scopus 로고    scopus 로고
    • Surface properties, morphology and protein composition of pulmonary surfactant subtypes
    • Putman, E., L. A. J. M. Creuwels, L. M. G. van Golde, and H. P. Haagsman. 1996. Surface properties, morphology and protein composition of pulmonary surfactant subtypes. Biochem. J. 320:599-605.
    • (1996) Biochem. J. , vol.320 , pp. 599-605
    • Putman, E.1    Creuwels, L.A.J.M.2    Van Golde, L.M.G.3    Haagsman, H.P.4
  • 34
    • 0019287284 scopus 로고
    • Isolation of lung lamellar bodies and their conversion to tubular myelin figures in vitro
    • Sanders, D. L., R. J. Hassett, and A. E. Vatter. 1980. Isolation of lung lamellar bodies and their conversion to tubular myelin figures in vitro. Anat. Rec. 198:485-501.
    • (1980) Anat. Rec. , vol.198 , pp. 485-501
    • Sanders, D.L.1    Hassett, R.J.2    Vatter, A.E.3
  • 35
    • 0024974068 scopus 로고
    • Electric charge effects on phospholipids headgroups. Phosphatidylcholine in mixtures with cationic and anionic amphiphiles
    • Scherer, P. G., and J. Seelig. 1989. Electric charge effects on phospholipids headgroups. Phosphatidylcholine in mixtures with cationic and anionic amphiphiles. Biochemistry. 28:7720-7728.
    • (1989) Biochemistry , vol.28 , pp. 7720-7728
    • Scherer, P.G.1    Seelig, J.2
  • 36
    • 0023473837 scopus 로고
    • Phospholipid head groups as sensors of electric charge in membranes. 1987
    • Seelig, J., P. M. Macdonald, and P. G. Scherer. 1987. Phospholipid head groups as sensors of electric charge in membranes. 1987. Biochemistry. 26:7535-7541.
    • (1987) Biochemistry , vol.26 , pp. 7535-7541
    • Seelig, J.1    Macdonald, P.M.2    Scherer, P.G.3
  • 37
    • 0001616247 scopus 로고
    • Localization of lipid exchange sites between bulk lung surfactants and surface monolayer: Freeze fracture study
    • Sen, A., S.-W. Hui, M. Mosgrober-Anthony, B. A. Holm, and E. A. Egan. 1988. Localization of lipid exchange sites between bulk lung surfactants and surface monolayer: freeze fracture study. J. Colloid Interface Sci. 126:355-360.
    • (1988) J. Colloid Interface Sci. , vol.126 , pp. 355-360
    • Sen, A.1    Hui, S.-W.2    Mosgrober-Anthony, M.3    Holm, B.A.4    Egan, E.A.5
  • 38
    • 0025301145 scopus 로고
    • Interaction between perdeuterated bimyristoylphosphatidylcholine and low molecular weight pulmonary surfactant protein SP-C
    • Simatos, G. A., K. B. Forward, M. R. Morrow, and K. M. W. Keough. 1990. Interaction between perdeuterated bimyristoylphosphatidylcholine and low molecular weight pulmonary surfactant protein SP-C. Biochemistry. 29:5807-5814.
    • (1990) Biochemistry , vol.29 , pp. 5807-5814
    • Simatos, G.A.1    Forward, K.B.2    Morrow, M.R.3    Keough, K.M.W.4
  • 39
    • 0020729244 scopus 로고
    • Headgroup interactions in mixed phopholipid bilayers
    • Sixl, F., and A. Watts. 1983. Headgroup interactions in mixed phopholipid bilayers. Proc. Natl. Acad. Sci. USA. 80:1613-1615.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 1613-1615
    • Sixl, F.1    Watts, A.2
  • 41
    • 0001569362 scopus 로고
    • Collective lipid motions in bilayer membranes studied by transverse deuteron spin relaxation
    • Stohrer, J., G. Gröbner, D. Reimer, K. Weisz, C. Mayer, and G. Kothe. 1991. Collective lipid motions in bilayer membranes studied by transverse deuteron spin relaxation. J. Chem. Phys. 95:672-678.
    • (1991) J. Chem. Phys. , vol.95 , pp. 672-678
    • Stohrer, J.1    Gröbner, G.2    Reimer, D.3    Weisz, K.4    Mayer, C.5    Kothe, G.6
  • 42
    • 0024333716 scopus 로고
    • Reconstitution of tubular myelin from synthetic lipids and proteins associated with pig pulmonary surfactant
    • Suzuki, Y., Y. Fujita, and K. Kogishi. 1989. Reconstitution of tubular myelin from synthetic lipids and proteins associated with pig pulmonary surfactant. Am. Rev. Respir. Dis. 140:75-81.
    • (1989) Am. Rev. Respir. Dis. , vol.140 , pp. 75-81
    • Suzuki, Y.1    Fujita, Y.2    Kogishi, K.3
  • 43
    • 0033798421 scopus 로고    scopus 로고
    • Differential effects of surfactant protein A on regional organization of monolayers containing surfactant protein B or C
    • Taneva, S., and K. M. W. Keough. 2000. Differential effects of surfactant protein A on regional organization of monolayers containing surfactant protein B or C. Biophys. J. 79:2010-2023.
    • (2000) Biophys. J. , vol.79 , pp. 2010-2023
    • Taneva, S.1    Keough, K.M.W.2
  • 44
    • 0029093059 scopus 로고
    • Pulmonary surfactant protein SP-A with phospholipids in spread monolayers at the air-water interface
    • Taneva, S., T. McEachern, S. Stewart, and K. M. W. 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    McEachern, T.2    Stewart, S.3    Keough, K.M.W.4
  • 45
    • 0015522277 scopus 로고
    • Fluorescamine: A reagent for assay of amino acids, peptides, and primary amines in the picomole range
    • Udenfriend, S., S. Stein, P. Bohlen, W. Dairman, W. Loimgrukes, and M. Weigele. 1972. Fluorescamine: a reagent for assay of amino acids, peptides, and primary amines in the picomole range. Science. 178:871-872.
    • (1972) Science , vol.178 , pp. 871-872
    • Udenfriend, S.1    Stein, S.2    Bohlen, P.3    Dairman, W.4    Loimgrukes, W.5    Weigele, M.6
  • 48
    • 0000455402 scopus 로고
    • Neue auffassungen über einen grundebeguff der atemmechancik. Die tetrakionskraft der lunge, abhängig von des oberflächenspannung in den alveolen
    • Von Neergaard, K. 1929. Neue Auffassungen über einen Grundebeguff der Atemmechancik. Die Tetrakionskraft der Lunge, Abhängig von des Oberflächenspannung in den Alveolen. Z. Gesamte Exp. Med. 66:373-394.
    • (1929) Z. Gesamte Exp. Med. , vol.66 , pp. 373-394
    • Von Neergaard, K.1
  • 49
    • 0023890913 scopus 로고
    • Macromolecular organization of natural and recombinant lung surfactant protein SP 28-36. Structural homology with the complement factor Clq
    • Voss, T., H. Eistetter, K. P. Schäfer, and J. Engel. 1988. Macromolecular organization of natural and recombinant lung surfactant protein SP 28-36. Structural homology with the complement factor Clq. J. Mol. Biol. 201:219-227.
    • (1988) J. Mol. Biol. , vol.201 , pp. 219-227
    • Voss, T.1    Eistetter, H.2    Schäfer, K.P.3    Engel, J.4
  • 50
    • 36348965087 scopus 로고
    • Time- and frequency-domain "DePakeing" using inverse theory
    • Whittall, K. P., E. Sternin, M. Bloom, and A. L. MacKay. 1989. Time- and frequency-domain "DePakeing" using inverse theory. J. Magn. Reson. 84:64-71.
    • (1989) J. Magn. Reson. , vol.84 , pp. 64-71
    • Whittall, K.P.1    Sternin, E.2    Bloom, M.3    MacKay, A.L.4
  • 51
    • 0026197257 scopus 로고
    • Changes in lipid structure produced by surfactant proteins SP-A, SP-B, and SP-C
    • Williams, M. C., S. Hawgood, and R. L. Hamilton. 1991. Changes in lipid structure produced by surfactant proteins SP-A, SP-B, and SP-C. Am. J. Respir. Cell Mol. Biol. 5:41-50.
    • (1991) Am. J. Respir. Cell Mol. Biol. , vol.5 , pp. 41-50
    • Williams, M.C.1    Hawgood, S.2    Hamilton, R.L.3
  • 52
    • 0033729383 scopus 로고    scopus 로고
    • Pulmonary surfactant protein A interacts with gel-like regions in monolayers of pulmonary surfactant lipid extract
    • Worthman, L.-A. D., K. Nag, N. Rich, M. L. F. Ruano, C. Casals, J. Pérez-Gil, and K. M. W. 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.D.1    Nag, K.2    Rich, N.3    Ruano, M.L.F.4    Casals, C.5    Pérez-Gil, J.6    Keough, K.M.W.7
  • 53
    • 0020960354 scopus 로고
    • Bovine pulmonary surfactant: Chemical composition and physical properties
    • Yu, S. H., N. Smith, P. G. R. Harding, and F. Possmayer. 1983. Bovine pulmonary surfactant: chemical composition and physical properties. Lipids. 18:522-529.
    • (1983) Lipids , vol.18 , pp. 522-529
    • Yu, S.H.1    Smith, N.2    Harding, P.G.R.3    Possmayer, F.4


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