Abstract
It is generally, albeit not universally [1,2], accepted that pulmonary surfactant stabilizes the lung by lowering the surface tension at the air-water interface of the alveoli. The requirement for pulmonary surfactant is particularly critical at birth when the newborn infant must clear its lungs of fetal pulmonary fluid and establish regular air breathing. Indeed, as outlined in detail in other chapters of this book, treatment of prematurely delivered infants with extracts of bovine or porcine surfactant leads to a significant reduction in the incidence and in the intensity of the respiratory distress syndrome of the neonate [3–5].
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References
Bangham, A. D. Lung surfactant: how it does and does not work. Lung 1987; 165: 17–25.
Hills, B. A. What is the true role of surfactant in the lung. Thorax 1981; 36: 1–4.
Jobe, A. and Ikegami, M. Surfactant in the treatment of respiratory distress syndrome. Am Rev Resp Dis 1987; 136: 1256–75.
Notter, R. H. and Shapiro, D. L. Lung surfactants for replacement therapy: biochemical, biophysical, and clinical aspects. Clin Perinatol 1987; 14: 433–79.
Robertson, B. and Lachman, B. Experimental evaluation of surfactants for replacement therapy. Exp Lung Res 1988; 14: 279–310.
Yu, S.-H., Harding, P. G. F., Smith, N. and Possmayer, F. Bovine pulmonary surfactant: chemical composition and physical properties. Lipids 1983; 18: 522–9.
Possmayer, F., Yu, S.-H., Weber, J. M. and Harding, P. G. R. Pulmonary surfactant. Biochem Cell Biol 1984; 62: 1121–31.
Beppu, O. S., Clements, J. A. and Goerke, J. Phosphatidylglycerol-deficient lung surfactant has normal properties. J Appl Physiol 1983; 55: 496–502.
Hallman, M., Enhorning, G. and Possmayer, F. Composition and surface activity of normal and phosphatidylglycerol-deficient lung surfactant. Pediatr Res 1985; 19: 286–92.
Egberts, J., Beintema-Dubbeldam, A. and de Boers, A. Phosphatidylinositol and not phosphatidylglycerol is the important minor phospholipid in rhesus-monkey surfactant. Biochim Biophys Acta 1987; 919: 90–2.
Possmayer, F. A proposed nomenclature system for pulmonary surfactant-associated proteins. Resp Dis 1988; 138: 990–8.
Persson, A., Rust, K., Chang, D., Moxley, M., Longmore, W. J. and Crouch, E. CP4: a pneumatocyte-derived collagenous surfactant-associated protein. Evidence for heterogeneity of collagenous surfactant proteins. Biochemistry 1988; 27: 8576–84.
Wright, J. R. and Clements, J. A. Metabolism and turnover of lung surfactant. Am Rev Resp Dis 1987; 135: 426–44.
Hawgood, S. Pulmonary surfactant apoproteins: a review of protein and genomic structure. Am J Physiol 1989; 257: L13–22.
Voss, T., Eistettier, H., Schafer, K. and Engel, J. Macromolecular organization of natural and recombinant lung surfactant protein SP28–36. Structural homology with complement factor CIQ. J Mol Biol 1988; 201: 219–27.
Haagsman, H. P., Hawgood, S., Sargeant, T., Buckley, D., White, R. T., Drickamer, K. and Benson, B. J. The major lung surfactant protein, SP28–36, is a calcium-dependent, carbohydrate-binding protein. J Biol Chem 1987; 262: 13877–80.
Weaver, T. E., Sarin, U. K., Sawtell, N., Hull, W. M. and Whitsett, J. A. Identification of surfactant proteolipid in human surfactant and fetal lung. J. Appl Physiol 1988; 65: 982–7.
Curstedt, T., Johansson, J., Barros-Soderling, Robertson, B., Nilsson, G., Westberg, M. and Jornvall, H. Low-molecular-mass surfactant protein type 1. The primary structure of a hydrophobic 8-kDa polypeptide with eight half-cystine residues. Eur J Biochem 1988; 172: 521–5.
Yu, S.-H., Chung, W., Olafson, R. W., Harding, P. G. R. and Possmayer, F. Characterization of the small hydrophobic proteins associated with pulmonary surfactant. Biochim Biophys Acta 1987; 921: 437–48.
Yu, S.-H. and Possmayer, F. Comparative studies on the biophysical activities of the low molecular weight hydrophobic proteins purified from bovine pulmonary surfactant. Biochim Biophys Acta 1988; 961: 337–50.
Johansson, J., Jornvall, H., Eklund, A., Christensen, N., Robertson, B. and Curstedt, T. Hydrophobic 3.7 kDa surfactant polypeptide: structural characterization of the human and bovine forms. FEBS Lett 1988; 232: 61–4.
Yu, S.-H., Chung, W. and Possmayer, F. Structural relationship between the two small hydrophobic apoproteins in bovine pulmonary surfactant. Biochim Biophys Acta 1989; 1005: 93–6.
Enhorning, G. Pulsating bubble technique for evaluating pulmonary surfactant. J Appl Physiol 1977; 43: 198–203.
Weber, M. J. and Possmayer, F. Calcium interactions in pulmonary surfactant. Biochim Biophys Acta 1984; 796: 83–91.
Chung, J., Yu, S.-H., Whitsett, J. A., Harding, P. G. R. and Possmayer, F. Effect of surfactant-associated protein A (SP-A) on the activity of lipid extract surfactant. Biochim Biophys Acta 1989; 1002: 348–58.
Goerke, J. and Clements, J. A. Alveolar surface tension and lung surfactant. In: Fishman, A. P., Macklem, P. T., Mead, J. and Geiger, S. R., eds. Handbook of Physiology, Section 3, The Respiratory System, Vol.III, part 1, Bethesda: American Physiological Society, 1986; 247–61.
Notter, R. H. Biophysical behavior of lung surfactant: implications for respiratory physiology and pathophysiology. Semin Perinatol 1988; 12: 180–212.
Hawco, M. W., Davis, P. J. and Keough, K. M. W. Lipid fluidity in lung surfactant: monolayers of saturated and unsaturated lecithins. J Appl Physiol 1981; 51: 509–15.
Egberts, J., Sloot, H. and Mazure, A. Minimal surface tension, squeeze-out and transition temperatures of binary mixtures of dipalmitoylphosphatidylcholine and unsaturated phospholipids. Biochim Biophys Acta 1989; 1002: 109–13.
Bachofen, H., Schurch, S., Urbinelli, M. and Weibel, E. R. Relation among alveolar surface tension, surface area, volume and recoil pressure. J. Appl Physiol 1987; 62: 1828–87.
Eisenberg, D., Schwarz, E., Komaromy, M. and Wall, R. Analysis of membrane and surface protein sequences with the hydrophobic moment plot. J Mol Biol 1984; 179: 125–42.
Waring, A. J., Fan, B., Nguyen, T., Amirkhanian, J. and Taeusch, W. Structure—function relationships of surfactant proteins SP-B and SP-C. Prog Resp Sci 1989; 25: 343–6.
Elledge, B. W. and Whitsett, J. Interaction of lung surfactant protein C (SP-C) with phospholipid bilayers: Spectroscopic studies. Am Rev Resp Dis 1989; 139: A285.
Waring, A., Taeusch, W., Bruni, R., Amirkhanian, J., Fan, B., Stevens, R. and Young, J. Synthetic amphipathic sequences of surfactant protein-B mimic several physicochemical and in vivo properties of native pulmonary surfactant proteins. Peptide Res 1989; 2: 308–13.
Hawgood, S., Benson, B. J., Schilling, J., Damm, D., Clements, J. A. and White, R. T. 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 1987; 84: 66–70.
Hawgood, S. Structure function: correlation in reassembled surfactant. Prog Resp Sci 1989; 25: 72–80.
Pison, U., Shiffer, K., Hawgood, S. and Goerke, J. Effects of the surfactant-associated proteins, SP-A, SP-B and SP-C on phospholipid surface film formation. Prog Resp Sci 1989; 25: 271–3.
Suzuki, Y., Fujita, Y. and Kogishi, K. Reconstitution of tubular myelin from synthetic lipids and proteins associated with pig pulmonary surfactant. Am Rev Resp Dis 1989; 140: 75–81.
Goerke, J. Lung surfactant. Biochim Biophys Acta 1974; 344: 241–61.
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© 1991 Macmillan Publishers Limited
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Possmayer, F., Cockshutt, A., Yu, SH. (1991). Pulmonary surfactant-associated proteins: their role in surface tension reduction. In: Cosmi, E.V., Di Renzo, G.C., Anceschi, M.M. (eds) The Surfactant System of the Lung. Palgrave, London. https://doi.org/10.1007/978-1-349-12553-1_2
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DOI: https://doi.org/10.1007/978-1-349-12553-1_2
Publisher Name: Palgrave, London
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