메뉴 건너뛰기




Volumn 74, Issue 3, 1998, Pages 1101-1109

Differential partitioning of pulmonary surfactant protein SP-A into regions of monolayers of dipalmitoylphosphatidylcholine and dipalmitoylphosphatidylcholine/dipalmitoylphosphatidylglycerol

Author keywords

[No Author keywords available]

Indexed keywords

DIPALMITOYLPHOSPHATIDYLCHOLINE; DIPALMITOYLPHOSPHATIDYLGLYCEROL; LUNG SURFACTANT; SURFACTANT ASSOCIATED PROTEIN;

EID: 0031951412     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(98)77828-2     Document Type: Article
Times cited : (65)

References (47)
  • 1
    • 0025607320 scopus 로고
    • Specific interactions of proteins with functional lipid monolayers - ways of stimulating biomembrane processes
    • Ahlers, M., W. Müller, A. Reichert, H. Ringsdorf, and J. Venzmer. 1990. Specific interactions of proteins with functional lipid monolayers - ways of stimulating biomembrane processes. Angew. Chem. Int. Ed. Engl. 29:1269-1285.
    • (1990) Angew. Chem. Int. Ed. Engl. , vol.29 , pp. 1269-1285
    • Ahlers, M.1    Müller, W.2    Reichert, A.3    Ringsdorf, H.4    Venzmer, J.5
  • 2
    • 0028577922 scopus 로고
    • Surfactant protein a regulates uptake of pulmonary surfactant by lung type II cells on microporous membranes
    • Bates, S. R., C. Dodia, and A. B. Fisher. 1994. Surfactant protein A regulates uptake of pulmonary surfactant by lung type II cells on microporous membranes. Am. J. Physiol. 267:L753-L760.
    • (1994) Am. J. Physiol. , vol.267
    • Bates, S.R.1    Dodia, C.2    Fisher, A.B.3
  • 3
    • 0024359504 scopus 로고
    • Comparison between intra- and extracellular surfactant in respiratory distress induced by oleic acid
    • Casals, C., L. Herrera, E. Miguel, P. García-Barreno, and A. M. Municio. 1989. Comparison between intra-and extracellular surfactant in respiratory distress induced by oleic acid. Biochim. Biophys. Acta. 1003: 201-203.
    • (1989) Biochim. Biophys. Acta. , vol.1003 , pp. 201-203
    • Casals, C.1    Herrera, L.2    Miguel, E.3    García-Barreno, P.4    Municio, A.M.5
  • 4
    • 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
  • 5
    • 0026646199 scopus 로고
    • Specificity of lung surfactant protein SP-A for both the carbohydrate and the lipid moieities of certain neutral glycolipids
    • Childs, R. A., J. R. Wright, G. F. Ross, C. Yuen, A. M. Lawson, W. Chai, K. Drickramer, and T. Feizi. 1992. Specificity of lung surfactant protein SP-A for both the carbohydrate and the lipid moieities of certain neutral glycolipids. J. Biol. Chem. 267:9972-9979.
    • (1992) J. Biol. Chem. , vol.267 , pp. 9972-9979
    • Childs, R.A.1    Wright, J.R.2    Ross, G.F.3    Yuen, C.4    Lawson, A.M.5    Chai, W.6    Drickramer, K.7    Feizi, T.8
  • 6
    • 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., J. I. 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.1    Weitz, J.I.2    Possmayer, F.3
  • 7
    • 0023115493 scopus 로고
    • Pulmonary surfactant and its components inhibit secretion of phosphatidylcholine from cultured rat alveolar type II cells
    • Dobbs, L. J. R. Wright, S. Hawgood, R. Gonzales, K. Venstrom, and J. Nellenbogen. 1987. Pulmonary surfactant and its components inhibit secretion of phosphatidylcholine from cultured rat alveolar type II cells. Proc. Natl. Acad. Sci. USA. 84:1010-1014.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 1010-1014
    • Dobbs1    Wright, L.J.R.2    Hawgood, S.3    Gonzales, R.4    Venstrom, K.5    Nellenbogen, J.6
  • 8
    • 0023710284 scopus 로고
    • Two distinct classes of carbohydrate-recognition domains in animal lectins
    • Drickamer, K. 1988. Two distinct classes of carbohydrate-recognition domains in animal lectins. J. Biol. Chem. 263:9557-9560.
    • (1988) J. Biol. Chem. , vol.263 , pp. 9557-9560
    • Drickamer, K.1
  • 9
    • 0025267451 scopus 로고
    • 2 in monolayers in the phase transition region: Direct observation of enzyme domain formation using fluorescence microscopy
    • 2 in monolayers in the phase transition region: direct observation of enzyme domain formation using fluorescence microscopy. Biochim. Biophys. Acta. 1023:365-379.
    • (1990) Biochim. Biophys. Acta. , vol.1023 , pp. 365-379
    • Grainger, D.W.1    Reichert, A.2    Ringsdorf, H.3    Salesse, C.4
  • 10
    • 0021915287 scopus 로고
    • Effects of a surfactant-associated protein and calcium ions on the structure and surface activity of lung surfactant lipids
    • Hawgood, S., B. J. Benson, and R. L. Hamilton. 1985. Effects of a surfactant-associated protein and calcium ions on the structure and surface activity of lung surfactant lipids. Biochemistry. 24:184-190.
    • (1985) Biochemistry , vol.24 , pp. 184-190
    • Hawgood, S.1    Benson, B.J.2    Hamilton, R.L.3
  • 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
    • 0026029572 scopus 로고
    • Structure and properties of surfactant associated proteins
    • Hawgood, S., and K. Shiffer. 1991. Structure and properties of surfactant associated proteins. Annu. Rev. Physiol. 53:375-394.
    • (1991) Annu. Rev. Physiol. , vol.53 , pp. 375-394
    • Hawgood, S.1    Shiffer, K.2
  • 13
    • 0022406904 scopus 로고
    • Protein/lipid interactions in phospholipid monolayers containing the bacterial antenna protein B800-850
    • Heckl, W. M., M. Lösche, H. Scheer, and H. Möhwald. 1985. Protein/lipid interactions in phospholipid monolayers containing the bacterial antenna protein B800-850. Biochim. Biophys. Acta. 810:73-83.
    • (1985) Biochim. Biophys. Acta. , vol.810 , pp. 73-83
    • Heckl, W.M.1    Lösche, M.2    Scheer, H.3    Möhwald, H.4
  • 15
    • 0029024418 scopus 로고
    • Exclusion of SP-C but not SP-B, by gel phase palmitoyl lipids
    • Horowitz, A. D. 1995. Exclusion of SP-C but not SP-B, by gel phase palmitoyl lipids. Chem. Phys. Lipids. 76:27-39.
    • (1995) Chem. Phys. Lipids , vol.76 , pp. 27-39
    • Horowitz, A.D.1
  • 16
    • 0027438028 scopus 로고
    • Lipid effects on aggregation of pulmonary surfactant protein SP-C studied by fluorescence energy transfer
    • Horowitz, A. D., J. E. Baatz, and J. A. Whitsett. 1993. Lipid effects on aggregation of pulmonary surfactant protein SP-C studied by fluorescence energy transfer. Biochemistry. 32:9513-9523.
    • (1993) Biochemistry , vol.32 , pp. 9513-9523
    • Horowitz, A.D.1    Baatz, J.E.2    Whitsett, J.A.3
  • 18
    • 0002372513 scopus 로고
    • Physical chemistry of pulmonary surfactant in the terminal air spaces
    • B. Robertson, L. M. G. Van Golde, and J. J. Batenburg, editors. Elsevier, Amsterdam
    • Keough, K. M. W. 1992. Physical chemistry of pulmonary surfactant in the terminal air spaces. In Pulmonary Surfactant: From Molecular Biology to Clinical Practice. B. Robertson, L. M. G. Van Golde, and J. J. Batenburg, editors. Elsevier, Amsterdam. 165-192.
    • (1992) Pulmonary Surfactant: from Molecular Biology to Clinical Practice , pp. 165-192
    • Keough, K.M.W.1
  • 19
    • 0021035007 scopus 로고
    • Reassembly of lipid-protein complexes of pulmonary surfactant: Proposed mechanism of interaction
    • King, R. J., M. C. Carmichael, and P. M. Horowitz. 1983. Reassembly of lipid-protein complexes of pulmonary surfactant: proposed mechanism of interaction. J. Biol. Chem. 258:10672-10680.
    • (1983) J. Biol. Chem. , vol.258 , pp. 10672-10680
    • King, R.J.1    Carmichael, M.C.2    Horowitz, P.M.3
  • 20
    • 0022875852 scopus 로고
    • Interactions 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. Interactions 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
  • 22
    • 0025845404 scopus 로고
    • Pulmonary surfactant protein a (SP-A) specifically binds dipalmitoylphosphatidylcholine
    • Kuroki, Y., and T. Akino. 1991. Pulmonary surfactant protein A (SP-A) specifically binds dipalmitoylphosphatidylcholine. J. Biol. Chem. 266: 3068-3073.
    • (1991) J. Biol. Chem. , vol.266 , pp. 3068-3073
    • Kuroki, Y.1    Akino, T.2
  • 23
    • 0027996784 scopus 로고
    • Pulmonary surfactant proteins
    • Kuroki, Y., and D. R. Voelker. 1994. Pulmonary surfactant proteins. J. Biol. Chem. 269:25943-25946.
    • (1994) J. Biol. Chem. , vol.269 , pp. 25943-25946
    • Kuroki, Y.1    Voelker, D.R.2
  • 25
    • 0029070473 scopus 로고
    • Phospholipase A2 domain formation in hydrolyzed asymmetric phospholipid monolayers at the air/water interface
    • Maloney, K. M., M. Grandbois, D. W. Grainger, C. Salesse, K. A. Lewis, and M. F. Roberts. 1995. Phospholipase A2 domain formation in hydrolyzed asymmetric phospholipid monolayers at the air/water interface. Biochim. Biophys. Acta. 1235:395-405.
    • (1995) Biochim. Biophys. Acta. , vol.1235 , pp. 395-405
    • Maloney, K.M.1    Grandbois, M.2    Grainger, D.W.3    Salesse, C.4    Lewis, K.A.5    Roberts, M.F.6
  • 26
    • 0025579948 scopus 로고
    • Phospholipid and phospholipid-protein monolayers at the air/water interface
    • Mohwald, H. 1990. Phospholipid and phospholipid-protein monolayers at the air/water interface. Annu. Rev. Phys. Chem. 41:441-476.
    • (1990) Annu. Rev. Phys. Chem. , vol.41 , pp. 441-476
    • Mohwald, H.1
  • 27
    • 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
  • 28
    • 0025902367 scopus 로고
    • Epifluorescence microscopic observation of monolayers of dipalmitoyl-phosphatidylcholine: Dependence of domain size on compression rates
    • Nag, K., N. H. Rich, C. Boland, and K. M. W. Keough. 1991. Epifluorescence microscopic observation of monolayers of dipalmitoyl-phosphatidylcholine: 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    Rich, N.H.2    Boland, C.3    Keough, K.M.W.4
  • 29
    • 0027217934 scopus 로고
    • Epifluorescence microscopic studies on monolayers containing mixtures of dioleoyl and dipalmitoylphosphatidylcholine
    • Nag, K., and K. M. W. Keough. 1993. Epifluorescence microscopic studies on monolayers containing mixtures of dioleoyl and dipalmitoylphosphatidylcholine. Biophys. J. 65:1019-1026.
    • (1993) Biophys. J. , vol.65 , pp. 1019-1026
    • Nag, K.1    Keough, K.M.W.2
  • 30
    • 0029993251 scopus 로고    scopus 로고
    • Fluorescently labelled pulmonary surfactant protein C (SP-C) in spread phospholipid monolayers
    • Nag, K., J. Pérez-Gil, A. Cruz, and K. M. W. Keough. 1996a. Fluorescently labelled pulmonary surfactant protein C (SP-C) in spread phospholipid monolayers. Biophys. J. 71:246-256.
    • (1996) Biophys. J. , vol.71 , pp. 246-256
    • Nag, K.1    Pérez-Gil, J.2    Cruz, A.3    Keough, K.M.W.4
  • 31
    • 0029762035 scopus 로고    scopus 로고
    • Spontaneous formation of interfacial lipid-protein monolayers during adsorption from vesicles
    • Nag, K., J. Pérez-Gil, A. Cruz, N. R. Rich, and K. M. W. Keough. 1996b. Spontaneous formation of interfacial lipid-protein monolayers during adsorption from vesicles. Biophys. J. 71:1356-1363.
    • (1996) Biophys. J. , vol.71 , pp. 1356-1363
    • Nag, K.1    Pérez-Gil, J.2    Cruz, A.3    Rich, N.R.4    Keough, K.M.W.5
  • 32
    • 0030960208 scopus 로고    scopus 로고
    • Combinations of fluorescently labeled pulmonary surfactant proteins SP-B and SP-C in phospholipid films
    • Nag, K., S. Taneva, J. Pérez-Gil, A. Cruz, and K. M. W. Keough. 1997. Combinations of fluorescently labeled pulmonary surfactant proteins SP-B and SP-C in phospholipid films. Biophys. J. 72:2638-2650.
    • (1997) Biophys. J. , vol.72 , pp. 2638-2650
    • Nag, K.1    Taneva, S.2    Pérez-Gil, J.3    Cruz, A.4    Keough, K.M.W.5
  • 33
    • 0030189525 scopus 로고    scopus 로고
    • Protein adsorption on lipid monolayers at their coexistence region
    • Netz, R. R., D. Andelman, and H. Orland. 1996. Protein adsorption on lipid monolayers at their coexistence region. J. Phys. II. France 6:1023-1047.
    • (1996) J. Phys. II. France , vol.6 , pp. 1023-1047
    • Netz, R.R.1    Andelman, D.2    Orland, H.3
  • 34
    • 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. 1992a. 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
  • 35
    • 0023455555 scopus 로고
    • Cytochrome C interaction with phospholipid monolayers and vesicles
    • Peschke, J., and H. Möhwald. 1987. Cytochrome C interaction with phospholipid monolayers and vesicles. Colloids Surf. 27:305-323.
    • (1987) Colloids Surf. , vol.27 , pp. 305-323
    • Peschke, J.1    Möhwald, H.2
  • 36
    • 0009831826 scopus 로고
    • Effects of surfactant-associated proteins SP-A, SP-B and SP-C, on phospholipid surface film formation
    • Pison, U., K. Shiffer, S. Hawgood, and J. Goerke. 1990. Effects of surfactant-associated proteins SP-A, SP-B and SP-C, on phospholipid surface film formation. Prog. Respir. Res. 25:271-273.
    • (1990) Prog. Respir. Res. , vol.25 , pp. 271-273
    • Pison, U.1    Shiffer, K.2    Hawgood, S.3    Goerke, J.4
  • 37
    • 0030033618 scopus 로고    scopus 로고
    • Comparison of lipid aggregation and self-aggregation activities of pulmonary surfactant-associated protein A
    • Ruano, M. L. F., 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.F.1    Miguel, E.2    Pérez-Gil, J.3    Casals, C.4
  • 38
    • 0026675709 scopus 로고
    • Pulmonary SP-A enhances adsorption and appears to induce surface sorting of lipid extract surfactant
    • Schurch, S., F. Possmayer, S. Cheng, and A. M. Cockshutt. 1992. Pulmonary SP-A enhances adsorption and appears to induce surface sorting of lipid extract surfactant. Am J. Physiol. 263:L210-L218.
    • (1992) Am J. Physiol. , vol.263
    • Schurch, S.1    Possmayer, F.2    Cheng, S.3    Cockshutt, A.M.4
  • 39
    • 0029959007 scopus 로고    scopus 로고
    • Antibody to surfactant protein a increases sensitivity of pulmonary surfactant to inactivation by fibrinogen in vivo
    • Strayer, D. S., E. Herting, B. Sun, and B. Robertson. 1996. Antibody to surfactant protein A increases sensitivity of pulmonary surfactant to inactivation by fibrinogen in vivo. Am. J. Respir. Crit. Care Med. 153:1116-1122.
    • (1996) Am. J. Respir. Crit. Care Med. , vol.153 , pp. 1116-1122
    • Strayer, D.S.1    Herting, E.2    Sun, B.3    Robertson, B.4
  • 40
    • 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
  • 41
    • 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. 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    McEachren, T.2    Stewart, J.3    Keough, K.M.W.4
  • 42
    • 0029033118 scopus 로고
    • Potential role of surfactant proteins a and D in innate lung defense against pathogens
    • Van Golde, L. M. G. 1995. Potential role of surfactant proteins A and D in innate lung defense against pathogens. Biol. Neonate. 67:2-17.
    • (1995) Biol. Neonate. , vol.67 , pp. 2-17
    • Van Golde, L.M.G.1
  • 43
    • 0023890913 scopus 로고
    • Macromolecular organization of natural and recombinant lung surfactant protein SP 28-36
    • Voss, T., H. Eistetter, and K. P. Schafer. 1988. Macromolecular organization of natural and recombinant lung surfactant protein SP 28-36. J. Mol. Biol. 201:219-227.
    • (1988) J. Mol. Biol. , vol.201 , pp. 219-227
    • Voss, T.1    Eistetter, H.2    Schafer, K.P.3
  • 45
    • 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
  • 46
    • 0029031452 scopus 로고
    • Degradation of surfactant lipids and surfactant protein a by alveolar macrophages in vitro
    • Wright, J. R., and D. C. Youmans. 1995. Degradation of surfactant lipids and surfactant protein A by alveolar macrophages in vitro. Am. J. Physiol. 268:L772-L780.
    • (1995) Am. J. Physiol. , vol.268
    • Wright, J.R.1    Youmans, D.C.2
  • 47
    • 0029992874 scopus 로고    scopus 로고
    • Effect of pulmonary surfactant protein a and neutral lipid on accretion and organization of dipalmitoylphosphatidylcholine in surface films
    • Yu, S. H., and F. Possmayer. 1996. Effect of pulmonary surfactant protein A and neutral lipid on accretion and organization of dipalmitoylphosphatidylcholine in surface films. J. Lipid Res. 37:1278-1288.
    • (1996) J. Lipid Res. , vol.37 , pp. 1278-1288
    • Yu, S.H.1    Possmayer, F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.