Skip to main content
NCBI home page
Biophysical Journal logoLink to Biophysical Journal
. 2000 Jul;79(1):357–369. doi: 10.1016/S0006-3495(00)76297-7

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

N Bourdos 1, F Kollmer 1, A Benninghoven 1, M Ross 1, M Sieber 1, H J Galla 1
PMCID: PMC1300939  PMID: 10866961

Abstract

An often-used model lung surfactant containing dipalmitoylphosphatidylcholine (DPPC), dipalmitoylphosphatidylglycerol (DPPG), and the surfactant protein C (SP-C) was analyzed as Langmuir-Blodgett film by spatially resolved time-of-flight secondary ion mass spectrometry (TOF-SIMS) to directly visualize the formation and composition of domains. Binary lipid and lipid/SP-C systems were probed for comparison. TOF-SIMS spectra revealed positive secondary ions (SI) characteristic for DPPC and SP-C, but not for DPPG. SI mapping results in images with domain structures in DPPC/DPPG and DPPG/SP-C, but not in DPPC/SP-C films. We are able to distinguish between the fluid and condensed areas probably due to a matrix effect. These findings correspond with other imaging techniques, fluorescence light microscopy (FLM), scanning force microscopy (SFM), and silver decoration. The ternary mixture DPPC/DPPG/SP-C transferred from the collapse region exhibited SP-C-rich domains surrounding pure lipid areas. The results obtained are in full accordance with our earlier SFM picture of layered protrusions that serve as a compressed reservoir for surfactant material during expansion. Our study demonstrates once more that SP-C plays a unique role in the respiration process.

Full Text

The Full Text of this article is available as a PDF (769.4 KB).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Amrein M., von Nahmen A., Sieber M. A scanning force- and fluorescence light microscopy study of the structure and function of a model pulmonary surfactant. Eur Biophys J. 1997;26(5):349–357. doi: 10.1007/s002490050089. [DOI] [PubMed] [Google Scholar]
  2. Bangham A. D., Morley C. J., Phillips M. C. The physical properties of an effective lung surfactant. Biochim Biophys Acta. 1979 Jun 21;573(3):552–556. doi: 10.1016/0005-2760(79)90229-7. [DOI] [PubMed] [Google Scholar]
  3. CLEMENTS J. A. Surface phenomena in relation to pulmonary function. Physiologist. 1962 Feb;5:11–28. [PubMed] [Google Scholar]
  4. Cochrane C. G., Revak S. D. Pulmonary surfactant protein B (SP-B): structure-function relationships. Science. 1991 Oct 25;254(5031):566–568. doi: 10.1126/science.1948032. [DOI] [PubMed] [Google Scholar]
  5. Demirev P. A. 252-Californium plasma desorption mass spectrometry of glycerophospholipids. Biomed Environ Mass Spectrom. 1987 May;14(5):241–246. doi: 10.1002/bms.1200140508. [DOI] [PubMed] [Google Scholar]
  6. Discher B. M., Maloney K. M., Schief W. R., Jr, Grainger D. W., Vogel V., Hall S. B. Lateral phase separation in interfacial films of pulmonary surfactant. Biophys J. 1996 Nov;71(5):2583–2590. doi: 10.1016/S0006-3495(96)79450-X. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Harwood J. L. Lung surfactant. Prog Lipid Res. 1987;26(3):211–256. doi: 10.1016/0163-7827(87)90004-x. [DOI] [PubMed] [Google Scholar]
  8. Horowitz A. D., Elledge B., Whitsett J. A., Baatz J. E. Effects of lung surfactant proteolipid SP-C on the organization of model membrane lipids: a fluorescence study. Biochim Biophys Acta. 1992 Jun 11;1107(1):44–54. doi: 10.1016/0005-2736(92)90327-i. [DOI] [PubMed] [Google Scholar]
  9. Johansson J., Curstedt T. Molecular structures and interactions of pulmonary surfactant components. Eur J Biochem. 1997 Mar 15;244(3):675–693. doi: 10.1111/j.1432-1033.1997.00675.x. [DOI] [PubMed] [Google Scholar]
  10. Johansson J., Curstedt T., Robertson B. The proteins of the surfactant system. Eur Respir J. 1994 Feb;7(2):372–391. doi: 10.1183/09031936.94.07020372. [DOI] [PubMed] [Google Scholar]
  11. Johansson J., Szyperski T., Curstedt T., Wüthrich K. The NMR structure of the pulmonary surfactant-associated polypeptide SP-C in an apolar solvent contains a valyl-rich alpha-helix. Biochemistry. 1994 May 17;33(19):6015–6023. doi: 10.1021/bi00185a042. [DOI] [PubMed] [Google Scholar]
  12. King R. J., Clements J. A. Surface active materials from dog lung. II. Composition and physiological correlations. Am J Physiol. 1972 Sep;223(3):715–726. doi: 10.1152/ajplegacy.1972.223.3.715. [DOI] [PubMed] [Google Scholar]
  13. Kramer A., Wintergalen A., Sieber M., Galla H. J., Amrein M., Guckenberger R. Distribution of the surfactant-associated protein C within a lung surfactant model film investigated by near-field optical microscopy. Biophys J. 2000 Jan;78(1):458–465. doi: 10.1016/S0006-3495(00)76608-2. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Krüger P., Schalke M., Wang Z., Notter R. H., Dluhy R. A., Lösche M. Effect of hydrophobic surfactant peptides SP-B and SP-C on binary phospholipid monolayers. I. Fluorescence and dark-field microscopy. Biophys J. 1999 Aug;77(2):903–914. doi: 10.1016/S0006-3495(99)76941-9. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Liu M. Synchronized changing of transinterface pressure, bubble radius and surface tension: a unique feature of lung surfactant. Chem Phys Lipids. 1997 Sep 24;89(1):55–65. doi: 10.1016/s0009-3084(97)00063-7. [DOI] [PubMed] [Google Scholar]
  16. Matsubara T., Hayashi A. FAB/mass spectrometry of lipids. Prog Lipid Res. 1991;30(4):301–322. doi: 10.1016/0163-7827(91)90001-l. [DOI] [PubMed] [Google Scholar]
  17. Nag K., Perez-Gil J., Cruz A., Keough K. M. Fluorescently labeled pulmonary surfactant protein C in spread phospholipid monolayers. Biophys J. 1996 Jul;71(1):246–256. doi: 10.1016/S0006-3495(96)79221-4. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Nag K., Taneva S. G., Perez-Gil J., Cruz A., Keough K. M. Combinations of fluorescently labeled pulmonary surfactant proteins SP-B and SP-C in phospholipid films. Biophys J. 1997 Jun;72(6):2638–2650. doi: 10.1016/S0006-3495(97)78907-0. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Oosterlaken-Dijksterhuis M. A., Haagsman H. P., van Golde L. M., Demel R. A. Characterization of lipid insertion into monomolecular layers mediated by lung surfactant proteins SP-B and SP-C. Biochemistry. 1991 Nov 12;30(45):10965–10971. doi: 10.1021/bi00109a022. [DOI] [PubMed] [Google Scholar]
  20. Oosterlaken-Dijksterhuis M. A., Haagsman H. P., van Golde L. M., Demel R. A. Interaction of lipid vesicles with monomolecular layers containing lung surfactant proteins SP-B or SP-C. Biochemistry. 1991 Aug 20;30(33):8276–8281. doi: 10.1021/bi00247a024. [DOI] [PubMed] [Google Scholar]
  21. Post A., Nahmen A. V., Schmitt M., Ruths J., Riegler H., Sieber M., Galla H. J. Pulmonary surfactant protein C containing lipid films at the air-water interface as a model for the surface of lung alveoli. Mol Membr Biol. 1995 Jan-Mar;12(1):93–99. doi: 10.3109/09687689509038502. [DOI] [PubMed] [Google Scholar]
  22. Pérez-Gil J., Nag K., Taneva S., Keough K. M. Pulmonary surfactant protein SP-C causes packing rearrangements of dipalmitoylphosphatidylcholine in spread monolayers. Biophys J. 1992 Jul;63(1):197–204. doi: 10.1016/S0006-3495(92)81582-5. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Pérez-Gil J., Tucker J., Simatos G., Keough K. M. Interfacial adsorption of simple lipid mixtures combined with hydrophobic surfactant protein from pig lung. Biochem Cell Biol. 1992 May;70(5):332–338. doi: 10.1139/o92-051. [DOI] [PubMed] [Google Scholar]
  24. Scarpelli E. M., Mautone A. J. Surface biophysics of the surface monolayer theory is incompatible with regional lung function. Biophys J. 1994 Sep;67(3):1080–1089. doi: 10.1016/S0006-3495(94)80573-9. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Schürch S., Goerke J., Clements J. A. Direct determination of surface tension in the lung. Proc Natl Acad Sci U S A. 1976 Dec;73(12):4698–4702. doi: 10.1073/pnas.73.12.4698. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Schürch S., Qanbar R., Bachofen H., Possmayer F. The surface-associated surfactant reservoir in the alveolar lining. Biol Neonate. 1995;67 (Suppl 1):61–76. doi: 10.1159/000244207. [DOI] [PubMed] [Google Scholar]
  27. Shelley S. A., Paciga J. E., Balis J. U. Lung surfactant phospholipids in different animal species. Lipids. 1984 Nov;19(11):857–862. doi: 10.1007/BF02534515. [DOI] [PubMed] [Google Scholar]
  28. Taneva S. G., Keough K. M. Dynamic surface properties of pulmonary surfactant proteins SP-B and SP-C and their mixtures with dipalmitoylphosphatidylcholine. Biochemistry. 1994 Dec 13;33(49):14660–14670. doi: 10.1021/bi00253a003. [DOI] [PubMed] [Google Scholar]
  29. Taneva S., Keough K. M. 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. 1994 Apr;66(4):1137–1148. doi: 10.1016/S0006-3495(94)80895-1. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Taneva S., Keough K. M. Pulmonary surfactant proteins SP-B and SP-C in spread monolayers at the air-water interface: II. Monolayers of pulmonary surfactant protein SP-C and phospholipids. Biophys J. 1994 Apr;66(4):1149–1157. doi: 10.1016/S0006-3495(94)80896-3. [DOI] [PMC free article] [PubMed] [Google Scholar]
  31. Tchoreloff P., Gulik A., Denizot B., Proust J. E., Puisieux F. 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. 1991 Sep;59(2):151–165. doi: 10.1016/0009-3084(91)90004-u. [DOI] [PubMed] [Google Scholar]
  32. Wang Z., Gurel O., Baatz J. E., Notter R. H. Differential activity and lack of synergy of lung surfactant proteins SP-B and SP-C in interactions with phospholipids. J Lipid Res. 1996 Aug;37(8):1749–1760. [PubMed] [Google Scholar]
  33. Wang Z., Hall S. B., Notter R. H. Dynamic surface activity of films of lung surfactant phospholipids, hydrophobic proteins, and neutral lipids. J Lipid Res. 1995 Jun;36(6):1283–1293. [PubMed] [Google Scholar]
  34. Wang Z., Hall S. B., Notter R. H. Roles of different hydrophobic constituents in the adsorption of pulmonary surfactant. J Lipid Res. 1996 Apr;37(4):790–798. [PubMed] [Google Scholar]
  35. von Nahmen A., Post A., Galla H. J., Sieber M. The phase behavior of lipid monolayers containing pulmonary surfactant protein C studied by fluorescence light microscopy. Eur Biophys J. 1997;26(5):359–369. doi: 10.1007/s002490050090. [DOI] [PubMed] [Google Scholar]
  36. von Nahmen A., Schenk M., Sieber M., Amrein M. The structure of a model pulmonary surfactant as revealed by scanning force microscopy. Biophys J. 1997 Jan;72(1):463–469. doi: 10.1016/S0006-3495(97)78687-9. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Biophysical Journal are provided here courtesy of The Biophysical Society

RESOURCES