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Volumn 276, Issue 4 20-4, 1999, Pages

Filaments of surfactant protein A specifically interact with corrugated surfaces of phospholipid membranes

Author keywords

Lipid protein interaction; Membrane structure; Pulmonary surfactant; Ripple phase; Tubular myelin

Indexed keywords

DIPALMITOYLPHOSPHATIDYLCHOLINE; LUNG SURFACTANT; MYELIN; PHOSPHATIDYLCHOLINE; PHOSPHOLIPID; SURFACTANT PROTEIN A; URANYL ACETATE;

EID: 0032900459     PISSN: 10400605     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajplung.1999.276.4.l631     Document Type: Article
Times cited : (13)

References (33)
  • 1
    • 0025768804 scopus 로고
    • Confocal laser scanning immunofluorescence microscopy of lamellar bodies and pulmonary surfactant protein A in isolated alveolar type II cells
    • Bakewell, W. E., C. J. Viviano, D. Dixon, G. J. Smith, and G. E. Hook. Confocal laser scanning immunofluorescence microscopy of lamellar bodies and pulmonary surfactant protein A in isolated alveolar type II cells. Lab. Invest. 65: 87-95, 1991.
    • (1991) Lab. Invest. , vol.65 , pp. 87-95
    • Bakewell, W.E.1    Viviano, C.J.2    Dixon, D.3    Smith, G.J.4    Hook, G.E.5
  • 2
    • 0027765632 scopus 로고
    • Tryptophan fluorescence study on the interaction of pulmonary surfactant protein A with phospholipid vesicles
    • Casals, C., E. Miguel, and J. Perez-Gil. Tryptophan fluorescence study on the interaction of pulmonary surfactant protein A with phospholipid vesicles. Biochem. J. 296: 585-593, 1993.
    • (1993) Biochem. J. , vol.296 , pp. 585-593
    • Casals, C.1    Miguel, E.2    Perez-Gil, J.3
  • 3
    • 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. M., J. Weitz, and F. Possmayer. 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.
    • (1990) Biochemistry , vol.29 , pp. 8424-8429
    • Cockshutt, A.M.1    Weitz, J.2    Possmayer, F.3
  • 4
    • 0028842781 scopus 로고
    • Ripple phase in asymmetric unilamellar bilayers with saturated and unsaturated phospholipids
    • Czajkowsky, D. M., C. Huang, and Z. Shao. Ripple phase in asymmetric unilamellar bilayers with saturated and unsaturated phospholipids. Biochemistry 34: 12501-12505, 1995.
    • (1995) Biochemistry , vol.34 , pp. 12501-12505
    • Czajkowsky, D.M.1    Huang, C.2    Shao, Z.3
  • 5
    • 0030278241 scopus 로고    scopus 로고
    • Surfactant protein A and lamellar bodies: A homologous secretory function of peritoneum, synovium, and lung
    • Dobbie, J. W. Surfactant protein A and lamellar bodies: a homologous secretory function of peritoneum, synovium, and lung. Perit. Dial. Int. 16: 574-581, 1996.
    • (1996) Perit. Dial. Int. , vol.16 , pp. 574-581
    • Dobbie, J.W.1
  • 6
    • 0023896772 scopus 로고
    • Rat lung type II cell and lamellar body: Elemental composition in situ
    • Cell Physiol. 23
    • Eckenhoff, R. G., and A. P. Somlyo. Rat lung type II cell and lamellar body: elemental composition in situ. Am. J. Physiol. 254 (Cell Physiol. 23): C614-C620, 1988.
    • (1988) Am. J. Physiol. , vol.254
    • Eckenhoff, R.G.1    Somlyo, A.P.2
  • 7
    • 0025267692 scopus 로고
    • Lamellar bodies of cultured human fetal lung: Content of surfactant protein A (SP-A), surface film formation and structural transformation in vitro
    • Froh, D., P. L. Ballard, M. C. Williams, J. Gonzales, J. Goerke, M. W. Odom, and L. W. Gonzales. Lamellar bodies of cultured human fetal lung: content of surfactant protein A (SP-A), surface film formation and structural transformation in vitro. Biochim. Biophys. Acta 1052: 78-89, 1990.
    • (1990) Biochim. Biophys. Acta , vol.1052 , pp. 78-89
    • Froh, D.1    Ballard, P.L.2    Williams, M.C.3    Gonzales, J.4    Goerke, J.5    Odom, M.W.6    Gonzales, L.W.7
  • 9
    • 0017394120 scopus 로고
    • Lamellar bodies: Isolation from rat lung, stability and conversion to tubular myelin figures
    • Hasset, R. J., R. L. Sanders, A. Vatter, and O. K. Reiss. Lamellar bodies: isolation from rat lung, stability and conversion to tubular myelin figures. Federation Proc. 36: 615-621, 1977.
    • (1977) Federation Proc. , vol.36 , pp. 615-621
    • Hasset, R.J.1    Sanders, R.L.2    Vatter, A.3    Reiss, O.K.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, Jr. Effects of a surfactant-associated protein and calcium ions on the structure and surface activity of lung surfactant lipids. Biochemistry 24: 184-190, 1985.
    • (1985) Biochemistry , vol.24 , pp. 184-190
    • Hawgood, S.1    Benson, B.J.2    Hamilton R.L., Jr.3
  • 11
    • 0031115382 scopus 로고    scopus 로고
    • Ultrastructure of tubular myelin in isolated surfactant and immunogold labelling of surfactant protein A
    • Hearn, S. A., and F. Possmayer, Ultrastructure of tubular myelin in isolated surfactant and immunogold labelling of surfactant protein A. Scanning 19: 234-235, 1997.
    • (1997) Scanning , vol.19 , pp. 234-235
    • Hearn, S.A.1    Possmayer, F.2
  • 12
    • 0030942158 scopus 로고    scopus 로고
    • Molecular structures and interactions of pulmonary surfactant components
    • Johansson, J., and T. Curstedt. Molecular structures and interactions of pulmonary surfactant components. Eur. J. Biochem. 244: 675-693, 1997.
    • (1997) Eur. J. Biochem. , vol.244 , pp. 675-693
    • Johansson, J.1    Curstedt, T.2
  • 13
    • 0028789297 scopus 로고
    • Phosphatidylcholine molecular species of calf lung surfactant
    • Lung Cell. Mol. Physiol 13
    • Kahn, M. C., G. J. Anderson, W. R. Anyan, and S. B. Hall. Phosphatidylcholine molecular species of calf lung surfactant. Am. J. Physiol. 269 (Lung Cell. Mol. Physiol 13): L567-L573, 1995.
    • (1995) Am. J. Physiol. , vol.269
    • Kahn, M.C.1    Anderson, G.J.2    Anyan, W.R.3    Hall, S.B.4
  • 14
    • 0027391733 scopus 로고
    • Internalization of surfactant protein A (SP-A) into lamellar bodies of rat alveolar type II cells in vitro
    • Kalina, M., F. X. McCormack, H. Crowley, D. R. Voelker, and R. J. Mason. Internalization of surfactant protein A (SP-A) into lamellar bodies of rat alveolar type II cells in vitro. J. Histochem. Cytochem. 41: 57-70, 1993.
    • (1993) J. Histochem. Cytochem. , vol.41 , pp. 57-70
    • Kalina, M.1    McCormack, F.X.2    Crowley, H.3    Voelker, D.R.4    Mason, R.J.5
  • 15
    • 0021166902 scopus 로고
    • Lipid-apolipoprotein interactions in surfactant studied by reassembly
    • King, R. J. Lipid-apolipoprotein interactions in surfactant studied by reassembly. Exp. Lung Res. 6: 237-253, 1984.
    • (1984) Exp. Lung Res. , vol.6 , pp. 237-253
    • King, R.J.1
  • 16
    • 0015403914 scopus 로고
    • Surface active materials from dog lung. II. Composition and physiological correlations
    • King, R. J., and J. A. Clements. Surface active materials from dog lung. II. Composition and physiological correlations. Am. J. Physiol. 223: 715-726, 1972.
    • (1972) Am. J. Physiol. , vol.223 , pp. 715-726
    • King, R.J.1    Clements, J.A.2
  • 18
    • 0025845404 scopus 로고
    • Pulmonary surfactant protein A (SP-A) specifically binds dipalmitoylphosphatidylcholine
    • Kuroki, Y., and T. Akino. Pulmonary surfactant protein A (SP-A) specifically binds dipalmitoylphosphatidylcholine. J. Biol. Chem. 266: 3068-3073, 1991.
    • (1991) J. Biol. Chem. , vol.266 , pp. 3068-3073
    • Kuroki, Y.1    Akino, T.2
  • 19
    • 0027295134 scopus 로고
    • Condition for the appearance of the metastable P beta′ phase in fully hydrated phosphatidylcholines as studied by small-angle x-ray diffraction
    • Matuoka, S., H. Yao, S. Kato, and I. Hatta. Condition for the appearance of the metastable P beta′ phase in fully hydrated phosphatidylcholines as studied by small-angle x-ray diffraction. Biophys. J. 64: 1456-1460, 1993.
    • (1993) Biophys. J. , vol.64 , pp. 1456-1460
    • Matuoka, S.1    Yao, H.2    Kato, S.3    Hatta, I.4
  • 20
    • 0030920246 scopus 로고    scopus 로고
    • The structure and function of surfactant protein-A
    • McCormack, F. X. The structure and function of surfactant protein-A. Chest 111: 114S-119S, 1997.
    • (1997) Chest , vol.111
    • McCormack, F.X.1
  • 21
    • 0032924918 scopus 로고    scopus 로고
    • Formation of membrane lattice structures and their specific interactions with surfactant protein A
    • Lung Cell. Mol. Physiol. 20
    • Palaniyar, N., R. A. Ridsdale, S. A. Hearn, F. Possmayer, and G. Harauz. Formation of membrane lattice structures and their specific interactions with surfactant protein A. Am. J. Physiol. 276 (Lung Cell. Mol. Physiol. 20): L642-L649, 1999.
    • (1999) Am. J. Physiol. , vol.276
    • Palaniyar, N.1    Ridsdale, R.A.2    Hearn, S.A.3    Possmayer, F.4    Harauz, G.5
  • 22
    • 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. E. Holterman, K. Inchley, F. Possmayer, and G. Harauz. Structural changes of surfactant protein A induced by cations reorient the protein on lipid bilayers. J. Struct. Biol. 122: 297-310, 1998.
    • (1998) J. Struct. Biol. , vol.122 , pp. 297-310
    • Palaniyar, N.1    Ridsdale, R.A.2    Holterman, C.E.3    Inchley, K.4    Possmayer, F.5    Harauz, G.6
  • 23
    • 0032497304 scopus 로고    scopus 로고
    • Surfactant protein A (SP-A) forms a novel supraquaternary structure in the form of fibers
    • Palaniyar, N., R. A. Ridsdale, F. Possmayer, and G. Harauz. Surfactant protein A (SP-A) forms a novel supraquaternary structure in the form of fibers. Biochem. Biophys. Res. Commun. 250: 131-136, 1998.
    • (1998) Biochem. Biophys. Res. Commun. , vol.250 , pp. 131-136
    • Palaniyar, N.1    Ridsdale, R.A.2    Possmayer, F.3    Harauz, G.4
  • 24
    • 0002501754 scopus 로고    scopus 로고
    • Physico-chemical aspects of pulmonary surfactant
    • edited by R. A. Polin and W. W. Fox. New York: Saunders
    • Possmayer, F. Physico-chemical aspects of pulmonary surfactant. In: Fetal and Neonatal Physiology, edited by R. A. Polin and W. W. Fox. New York: Saunders, 1997, p. 1259-1275.
    • (1997) Fetal and Neonatal Physiology , pp. 1259-1275
    • Possmayer, F.1
  • 26
    • 0017661789 scopus 로고
    • A mode of formation of tubular myelin from lamellar bodies in the lung
    • Sanderson, R. J., and A. E. Vatter. A mode of formation of tubular myelin from lamellar bodies in the lung. J. Cell Biol. 74: 1027-1031, 1977.
    • (1977) J. Cell Biol. , vol.74 , pp. 1027-1031
    • Sanderson, R.J.1    Vatter, A.E.2
  • 27
    • 0018966318 scopus 로고
    • Freeze-fracture study of pulmonary lamellar body membranes in solid crystal phase
    • Schulz, W. W., W. H. McAnally, and R. C. Reynolds. Freeze-fracture study of pulmonary lamellar body membranes in solid crystal phase. J. Ultrastruct. Res. 71: 37-48, 1980.
    • (1980) J. Ultrastruct. Res. , vol.71 , pp. 37-48
    • Schulz, W.W.1    McAnally, W.H.2    Reynolds, R.C.3
  • 28
    • 0024333716 scopus 로고
    • Reconstitution of tubular myelin from synthetic lipids and proteins associated with pig pulmonary surfactant
    • Suzuki, Y., Y. Fujita, and K. Kogishi. Reconstitution of tubular myelin from synthetic lipids and proteins associated with pig pulmonary surfactant. Am. Rev. Respir. Dis. 140: 75-81, 1989.
    • (1989) Am. Rev. Respir. Dis. , vol.140 , pp. 75-81
    • Suzuki, Y.1    Fujita, Y.2    Kogishi, K.3
  • 29
    • 0017336982 scopus 로고
    • Conversion of lamellar body membranes into tubular myelin in alveoli of fetal rat lungs
    • Williams, M. C. Conversion of lamellar body membranes into tubular myelin in alveoli of fetal rat lungs. J. Cell Biol. 72: 260-277, 1977.
    • (1977) J. Cell Biol. , vol.72 , pp. 260-277
    • Williams, M.C.1
  • 30
    • 0002106158 scopus 로고
    • Morphologic aspects of the surfactant system
    • edited by B. Robertson, L. M. G. van Golde, and J. J. Batenburg. Amsterdam, The Netherlands: Elsevier
    • Williams, M. C. Morphologic aspects of the surfactant system. In: Pulmonary Surfactant: From Molecular Biology to Clinical Practice, edited by B. Robertson, L. M. G. van Golde, and J. J. Batenburg. Amsterdam, The Netherlands: Elsevier, 1992, p. 87-107.
    • (1992) Pulmonary Surfactant: From Molecular Biology to Clinical Practice , pp. 87-107
    • Williams, M.C.1
  • 31
    • 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. 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.
    • (1991) Am. J. Respir. Cell Mol. Biol. , vol.5 , pp. 41-50
    • Williams, M.C.1    Hawgood, S.2    Hamilton, R.L.3
  • 32
    • 0020960354 scopus 로고
    • Bovine pulmonary surfactant: Chemical composition and physical properties
    • Yu, S.-H., P. G. R. Harding, N. Smith, and F. Possmayer. Bovine pulmonary surfactant: chemical composition and physical properties. Lipids 18: 522-529, 1983.
    • (1983) Lipids , vol.18 , pp. 522-529
    • Yu, S.-H.1    Harding, P.G.R.2    Smith, N.3    Possmayer, F.4
  • 33
    • 0031920791 scopus 로고    scopus 로고
    • Interaction of pulmonary surfactant protein A (SP-A) with dipalmitoylphosphatidylcholine and cholesterol at the air/water interface
    • Yu, S.-H., and F. Possmayer. Interaction of pulmonary surfactant protein A (SP-A) with dipalmitoylphosphatidylcholine and cholesterol at the air/water interface. J. Lipid Res. 39: 555-568, 1998.
    • (1998) J. Lipid Res. , vol.39 , pp. 555-568
    • Yu, S.-H.1    Possmayer, F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.