Analysis of lung surfactant model systems with time-of-flight secondary ion mass spectrometry

Biophysical Journal

Volumn 79, Issue 1, 2000, Pages 357-369

  Bourdos, Nikolaus ^a   Kollmer, Felix ^a   Benninghoven, Alfred ^a   Ross, Michaela ^a   Sieber, Manfred ^a   Galla, Hans Joachim ^a  

^a UNIVERSITY OF MÜNSTER   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

DIPALMITOYLPHOSPHATIDYLCHOLINE; DIPALMITOYLPHOSPHATIDYLGLYCEROL; LUNG SURFACTANT; SILVER; SURFACTANT PROTEIN A;

ARTICLE; BREATHING; CHEMICAL COMPOSITION; CONTROLLED STUDY; FILM; FLUORESCENCE MICROSCOPY; LUNG ALVEOLUS SURFACE TENSION; MASS SPECTROMETRY; PRESSURE; SCANNING FORCE MICROSCOPY;

EID: 0033918285     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(00)76297-7     Document Type: Article

References (59)

1. Amrein, M., A. von Nahmen, and M. Sieber. 1997. A scanning force- and fluorescence light microscopy study of the structure and function of a model pulmonary surfactant. Eur. Biophys. J. 26:349-357.
2. Ayanoglu, E., A. Wegmann, O. Pilet, G. D. Marbury, J. R. Hass, and C. Djerassi. 1984. Mass spectrometry of phospholipids. Some applications of desorption chemical ionization and fast atom bombardment. J. Am. Chem. Soc. 106:5246-5251.
3. Bangham, A. D. 1979. The physical properties of an effective lung surfactant. Biochim. Biophys. Acta. 573:552-556.
4. Benninghoven, A. 1994. Chemical analysis of inorganic and organic surfaces and thin films by static time-of-flight secondary ion mass spectrometry (TOP-SIMS). Angew. Chem. Int. Ed. Engl. 33:1023-1044.
5. Benninghoven, A., B. Hagenhoff, and E. Niehues. 1993. Surface MS: probing real-world samples. Anal. Chem. 65: 630A-640A.
6. Bertrand, P., and L. Weng. 1996. Time-of-flight secondary ion mass spectrometry (ToF-SIMS). Mikrochim. Acta. 13:167-182.
7. Bourdos, N., F. Kollmer, A. Benninghoven, M. Sieber, and H.-J. Galla. 2000. Imaging of domain structures in a one-component lipid monolayer by time-of-flight secondary ion mass spectrometry. Langmuir. 16: 1481-1484.
8. Clements, J. A. 1962. Surface phenomena in relation to pulmonary function. Physiologist. 5:11-28.
9. Cochrane, C. G., and S. D. Revak. 1991. Pulmonary surfactant protein B (SP-B): structure-function relationships. Science. 254:566-568.
10. Demirev, P. A. 1987. 252-Californium plasma desorption mass spectrometry of glycerophospholipids. Biomed. Environ. Mass Spectrom. 14: 241-246.
11. Discher, B. M., K. M. Maloney, W. R. Schief, V. Vogel, and S. B. Hall. 1996. Lateral phase separation in interfacial films of pulmonary surfactant. Biophys. J. 71:2583-2590.
12. Galla, H.-J., N. Bourdos, A. von Nahmen, M. Amrein, and M. Sieber. 1998. The role of pulmonary surfactant protein C during the breathing cycle. Thin Solid Films. 329:632-635.
13. Garidel, P., C. Johann, L. Mennicke, and A. Blume. 1997. The mixing behaviour of pseudobinary phosphatidylcholine-phosphatidylglycerol mixtures as a function of pH and chain length. Eur. Biophys. J. 26: 447-459.
14. Gleiche, M., L. F. Chi, and H. Fuchs. 1998. Molecular property related silver decoration on fatty acid Langmuir-Blodgett monolayers. Thin Solid Films. 329:268-272.
15. Hagenhoff, B. 1993. Sekundärionenmassenspektrometrie an Molekularen Oberflächenstrukturen. Ph.D. thesis. Westfälische Wilhelms-Universität, Münster. 178 pp.
16. Hagenhoff, B. 1995. Surface mass spectrometry: application to biosensor characterization. Biosensors and Bioelectronics. 10:885-894.
17. Hagenhoff, B., A. Benninghoven, J. Spinke, M. Liley, and W. Knoll. 1993. Time-of-flight secondary ion mass spectrometry investigations of self-assembled monolayers of organic thiols, sulfides, and disulfides on gold surfaces. Langmuir. 9:1622-1624.
18. Harvey, D. J. 1995. Matrix-assisted laser desorption/ionization mass spectrometry of phospholipids. J. Mass Spectrom. 30:1333-1346.
19. Harwood, J. L. 1987. Lung surfactant. Prog. Lipid. Res. 26:211-256.
20. Horowitz, A. D., B. Elledge, J. A. Whitsett, and J. E. Baatz. 1992. Effects of lung surfactant proteolipid SP-C on the organization of model membrane lipids: a fluorescence study. Biochim. Biophys. Acta. 1107:44-54.
21. Johansson, J., and T. Curstedt. 1997. Molecular structures and interactions of pulmonary surfactant components. Eur. J. Biochem. 244:675-693.
22. Johansson, J., T. Curstedt, and B. Robertson. 1994a. The proteins of the surfactant system. Eur. Respir. J. 7:372-391.
23. Johansson, J., T. Szyperski, T. Curstedt, and K. Wüthrich. 1994b. The NMR structure of the pulmonary surfactant-associated polypeptide SP-C in an apolar solvent contains a valyl-rich a-helix. Biochemistry. 33: 6015-6023.
24. King, R. J., and J. A. Clements. 1972. Surface active material from dog lung. I. Method of isolation. Am. J. Physiol. 223:715-726.
25. 5 ion bombardment. Appl. Surf. Sci. 133:47-57.
26. Kramer, A., A. Wintergalen, M. Sieber, H. J. Galla, M. Amrein, and R. Guckenberger. 2000. Distribution of the surfactant associated protein C within a lung surfactant model film investigated by near-field optical microscopy. Biophys. J. 78:454-465.
27. Krüger, P., M. Schalke, Z. Wang, R. H. Notter, R. A. Dluhy, and M. Lösche. 1999. Effect of Hydrophobic surfactant peptides SP-B and SP-C on binary phospholipid monolayers. I. Fluorescence and dark-field microscopy. Biophys. J. 77:903-914.
28. Leufgen, K. M., H. Rulle, A. Benninghoven, M. Sieber, and H-J. Galla. 1996. Imaging time-of-flight secondary ion mass spectrometry allows visualization and analysis of coexisting phases in Langmuir-Blodgett films. Langmuir. 12:1708-1711.
29. Liu, M. 1997. Synchronized changing of transinterface pressure, bubble radius and surface tension: a unique feature of lung surfactant. Chem. Phys. Lipids. 89:55-65.
30. Matsuhara, T., and A. Hayashi. 1991. FAB/Mass spectrometry of lipids. Prog. Lipid Res. 30:301-322.
31. McLafferty, F. W., and F. Turecek. 1993. Interpretation of Mass Spectra. University Science Books, Mill Valley, CA.
32. Nag, K., J. Pèrez-Gil, A. Cruz, and K. M. W. Keough. 1996. Fluorescently labeled pulmonary surfactant protein C in spread phospholipid monolayers. Biophys. J. 71:246-256.
33. Nag, K., S. G. Taneva, J. Pèrez-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.
34. Oosterlaken-Dijksterhuis, M. A., H. P. Haagsman, L. M. G. van Golde, and R. A. Demel. 1991a. Interaction of lipid vesicles with monomolecular layers containing lung surfactant proteins SP-B or SP-C. Biochemistry. 30:8276-8281.
35. Oosterlaken-Dijksterhuis, M. A., H. P. Haagsman, L. M. G. van Golde, and R. A. Demel. 1991b. Characterization of lipid insertion into monomolecular layers mediated by lung surfactant proteins SP-B and SP-C. Biochemistry. 30:10965-10971.
36. Panaiotov, I., Tz. Ivanova, J. Proust, F. Boury, B. Denizot, K. Keough, and S. Taneva. 1996. Effect of hydrophobic protein SP-C on structure and dilatational properties of the model monolayers of pulmonary surfactant. Colloids Surf. B: Biointerfaces. 6:243-260.
37. Pèrez-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.
38. Pèrez-Gil, J., J. Tucker, G. Simatos, and K. M. W. Keough. 1992b. Interfacial adsorption of simple lipid mixtures combined with hydrophobic surfactant protein from pig lung. Biochem. Cell Biol. 70:332-338.
39. Post, A., A. von Nahmen, M. Schmitt, J. Ruths, H. Riegler, M. Sieber, and H-J. Galla. 1995. Pulmonary surfactant protein C containing lipid films at the air-water interface as a model for the surface of lung alveoli. Mol. Membr. Biol. 12:93-99.
40. Rulle, H. 1996. Hochauflösende Abbildungen Strukturiertet Organischer Oberflächen mit Flugzeit-sekundärionen-Massenspektrometrie (TOF-SIMS). Ph.D. thesis. Westfälische Wilhelms-Universität, Münster. 88 pp.
41. Scarpelli, E. M., and A. J. Mautone. 1994. Surface biophysics of the surface monolayer theory is incompatible with regional lung function. Biophys. J. 67:1080-1089.
42. Schüren, S., J. Goerke, and J. A. Clements. 1976. Direct determination of surface tension in the lung. Proc. Natl. Acad. Sci. U.S.A. 73:4698-4702.
43. Schüren, S., R. Qanbar, H. Bachofen, and F. Possmeyer. 1995. The surface-associated surfactant reservoir in the alveolar lining. Biol. Neonate. 67(Suppl. 1):61-76.
44. Schwieters, J., H. G. Cramer, T. Heller, U. Juergens, E. Niehuis, J. Zehnpfennig, and A. Benninghoven. 1991. High mass resolution surface imaging with a time-of-flight secondary ion mass spectroscopy scanning microprobe. J. Vac. Sci. Technol. A. 9:2864-2871.
45. 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.
46. Shelly, S. A., J. E. Paciga, and J. U. Balius. 1984. Lung surfactant phospholipids in different animal species. Lipids. 19:857-862.
47. 5 primary ion bombardment. Appl. Surf. Sci. 140:156-167.
48. Taneva, S. G., and K. M. W. Keough. 1994a. Dynamic surface properties of pulmonary surfactant proteins SP-B and SP-C and their mixtures with dipalmitoylphosphatidylcholine. Biochemistry. 33:14660-14670.
49. Taneva, S. G., and K. M. W. Keough. 1994b. Pulmonary surfactant proteins SP-B and SP-C in spread monolayers at the air-water interface: I. Monolayers of pulmonary surfactant protein SP-B and phospholipids Biophys. J. 66:1137-1148.
50. Taneva, S. G., and K. M. W. Keough. 1994c. Pulmonary surfactant proteins SP-B and SP-C in spread monolayers at the air-water interface: II. Monolayers of pulmonary surfactant protein Protein SP-C and phospholipids. Biophys. J. 66:1149-1157.
51. Taneva, S. G., and K. M. W. Keough. 1994d. Pulmonary surfactant proteins SP-B and SP-C in spread monolayers at the air-water interface: III. Proteins SP-B plus SP-C with phospholipids in spread monolayers Biophys. J. 66:1158-1166.
52. Tchoreloff, P., A. Gulik, B. Denizot, J. E. Proust, and F. Puisieux. 1991. A structural study of interfacial phospholipid and lung surfactant layers by transmission electron microscopy after Blodgett sampling: influence of surface pressure and temperature. Chem. Phys. Lipids. 59:151-165.
53. van Leyen, D., D. Greifendorf, and A. Benninghoven. 1987. Secondary ion formation from peptides: influence of primary structure and substrates, 6th International Conference on Secondary Ion Mass Spectrometry Versailles, Sept. 13-18, 679-682.
54. von Nahmen, A. 1997. Strukturelle Organisation von Surfactant Protein C haltigen Phospholipid-Monoschichten an der Luft-Wasser-Grenzflä che - Ein Modell des alveolären Surfactant. Ph.D. thesis. Westfälische Wilhelms-Universität, Münster. 139 pp.
55. von Nahmen, A., A. Post, H. J. Galla, and M. Sieber. 1997b. The phase behaviour of lipid monolayers containing pulmonary surfactant protein C studied by fluorescence light microscopy. Eur. Bionhys. J. 26: 359-369.
56. von Nahmen, A., M. Schenk, M. Sieber, and M. Amrein. 1997a. The structure of a model pulmonary surfactant as revealed by scanning force microscopy. Biophys. J. 72:463-469.
57. Wang, Z., O. Gurel, J. E. Baatz, and R. H. Notter. 1996b. Differential activity and lack of synergy of lung surfactant proteins SP-B and SP-C in interactions with phospholipids. J. Lipid Res. 37:1749-1760.
58. Wang, Z., S. B. Hall, and R. H. Notter. 1995. Dynamic surface activity of films of lung surfactant phospholipids. hydrophobic proteins, and neutral lipids. J. Lipid Res. 36:1283-1293.
59. Wang, Z., S. B. Hall, and R. H. Notter. 1996a. Roles of different hydrophobic constituents in the adsorption of pulmonary surfactant. J. Lipid Res. 37:790-798.