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. 1996 Nov;71(5):2591–2601. doi: 10.1016/S0006-3495(96)79451-1

Molecular mobility in the monolayers of foam films stabilized by porcine lung surfactant.

Z I Lalchev 1, R K Todorov 1, Y T Christova 1, P J Wilde 1, A R Mackie 1, D C Clark 1
PMCID: PMC1233746  PMID: 8913597

Abstract

Certain physical properties of a range of foam film types that are believed to exist in vivo in the lung have been investigated. The contribution of different lung surfactant components found in porcine lung surfactant to molecular surface diffusion in the plane of foam films has been investigated for the first time. The influence of the type and thickness of black foam films, temperature, electrolyte concentration, and extract composition on surface diffusion has been studied using the fluorescence recovery after photobleaching technique. Fluorescent phospholipid probe molecules in foam films stabilized by porcine lung surfactant samples or their hydrophobic extracts consisting of surfactant lipids and hydrophobic lung surfactant proteins, SP-B and SP-C, exhibited more rapid diffusion than observed in films of its principal lipid component alone, L-alpha-phosphatidylcholine dipalmitoyl. This effect appears to be due to contributions from minor lipid components present in the total surfactant lipid extracts. The minor lipid components influence the surface diffusion in foam films both by their negative charge and by lowering the phase transition temperature of lung surfactant samples. In contrast, the presence of high concentrations of the hydrophillic surfactant protein A (SP-A) and non-lung-surfactant proteins in the sample reduced the diffusion coefficient (D) of the lipid analog in the adsorbed layer of the films. Hysteresis behavior of D was observed during temperature cycling, with the cooling curve lying above the heating curve. However, in cases where some surface molecular aggregation and surface heterogeneity were observed during cooling, the films became more rigid and molecules at the interfaces became immobilized. The thickness, size, capillary pressure, configuration, and composition of foam films of lung surfactant prepared in vitro support their investigation as realistic structural analogs of the surface films that exist in vivo in the lung. Compared to other models currently in use, foam films provide new opportunities for studying the properties and function of physiologically important alveolar surface films.

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Selected References

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  1. BLIGH E. G., DYER W. J. A rapid method of total lipid extraction and purification. Can J Biochem Physiol. 1959 Aug;37(8):911–917. doi: 10.1139/o59-099. [DOI] [PubMed] [Google Scholar]
  2. Bangham A. D. "Surface tensions" in the lung. Biophys J. 1995 Apr;68(4):1630–1633. doi: 10.1016/S0006-3495(95)80339-5. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Beers M. F., Bates S. R., Fisher A. B. Differential extraction for the rapid purification of bovine surfactant protein B. Am J Physiol. 1992 Jun;262(6 Pt 1):L773–L778. doi: 10.1152/ajplung.1992.262.6.L773. [DOI] [PubMed] [Google Scholar]
  4. CLEMENTS J. A. Surface phenomena in relation to pulmonary function. Physiologist. 1962 Feb;5:11–28. [PubMed] [Google Scholar]
  5. Cham B. E., Knowles B. R. A solvent system for delipidation of plasma or serum without protein precipitation. J Lipid Res. 1976 Mar;17(2):176–181. [PubMed] [Google Scholar]
  6. Dluhy R. A., Reilly K. E., Hunt R. D., Mitchell M. L., Mautone A. J., Mendelsohn R. Infrared spectroscopic investigations of pulmonary surfactant. Surface film transitions at the air-water interface and bulk phase thermotropism. Biophys J. 1989 Dec;56(6):1173–1181. doi: 10.1016/S0006-3495(89)82764-X. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Enhorning G. Pulsating bubble technique for evaluating pulmonary surfactant. J Appl Physiol Respir Environ Exerc Physiol. 1977 Aug;43(2):198–203. doi: 10.1152/jappl.1977.43.2.198. [DOI] [PubMed] [Google Scholar]
  8. FOLCH J., LEES M., SLOANE STANLEY G. H. A simple method for the isolation and purification of total lipides from animal tissues. J Biol Chem. 1957 May;226(1):497–509. [PubMed] [Google Scholar]
  9. Hall S. B., Venkitaraman A. R., Whitsett J. A., Holm B. A., Notter R. H. Importance of hydrophobic apoproteins as constituents of clinical exogenous surfactants. Am Rev Respir Dis. 1992 Jan;145(1):24–30. doi: 10.1164/ajrccm/145.1.24. [DOI] [PubMed] [Google Scholar]
  10. Hawgood S., Clements J. A. Pulmonary surfactant and its apoproteins. J Clin Invest. 1990 Jul;86(1):1–6. doi: 10.1172/JCI114670. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Hills B. A. What is the true role of surfactant in the lung? Thorax. 1981 Jan;36(1):1–4. doi: 10.1136/thx.36.1.1. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Kahovcová J., Odavić R. A simple method for the quantitative analysis of phospholipids separated by thin layer chromatography. J Chromatogr. 1969 Mar 11;40(1):90–96. doi: 10.1016/s0021-9673(01)96622-1. [DOI] [PubMed] [Google Scholar]
  13. 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]
  14. Kuroki Y., Voelker D. R. Pulmonary surfactant proteins. J Biol Chem. 1994 Oct 21;269(42):25943–25946. [PubMed] [Google Scholar]
  15. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  16. Naydenova S., Lalchev Z., Petrov A. G., Exerowa D. Pure and mixed lipid black foam films as models of membrane fusion. Eur Biophys J. 1990;17(6):343–347. doi: 10.1007/BF00258383. [DOI] [PubMed] [Google Scholar]
  17. Ng V. L., Herndon V. L., Mendelson C. R., Snyder J. M. Characterization of rabbit surfactant-associated proteins. Biochim Biophys Acta. 1983 Nov 29;754(2):218–226. doi: 10.1016/0005-2760(83)90164-9. [DOI] [PubMed] [Google Scholar]
  18. Nikolova A., Exerowa D., Lalchev Z., Tsonev L. Thermal transitions in dimyristoylphosphatidylcholine foam bilayers. Eur Biophys J. 1994;23(2):145–152. doi: 10.1007/BF00208869. [DOI] [PubMed] [Google Scholar]
  19. PATTLE R. E. Properties, function and origin of the alveolar lining layer. Nature. 1955 Jun 25;175(4469):1125–1126. doi: 10.1038/1751125b0. [DOI] [PubMed] [Google Scholar]
  20. Revak S. D., Merritt T. A., Degryse E., Stefani L., Courtney M., Hallman M., Cochrane C. G. Use of human surfactant low molecular weight apoproteins in the reconstitution of surfactant biologic activity. J Clin Invest. 1988 Mar;81(3):826–833. doi: 10.1172/JCI113391. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Scarpelli E. M., Clutario B. C., Traver D. Failure of immature lungs to produce foam and retain air at birth. Pediatr Res. 1979 Nov;13(11):1285–1289. doi: 10.1203/00006450-197911000-00016. [DOI] [PubMed] [Google Scholar]
  22. Scarpelli E. M. Intrapulmonary foam at birth: an adaptational phenomenon. Pediatr Res. 1978 Nov;12(11):1070–1076. doi: 10.1203/00006450-197811000-00009. [DOI] [PubMed] [Google Scholar]
  23. 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]
  24. Schürch S., Bachofen H., Goerke J., Possmayer F. A captive bubble method reproduces the in situ behavior of lung surfactant monolayers. J Appl Physiol (1985) 1989 Dec;67(6):2389–2396. doi: 10.1152/jappl.1989.67.6.2389. [DOI] [PubMed] [Google Scholar]
  25. 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]
  26. Tenchov B. On the reversibility of the phase transitions in lipid-water systems. Chem Phys Lipids. 1991 Mar;57(2-3):165–177. doi: 10.1016/0009-3084(91)90074-l. [DOI] [PubMed] [Google Scholar]

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