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Science 19 July 1996:
Vol. 273. no. 5273, pp. 330 - 332
DOI: 10.1126/science.273.5273.330
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Reports
Role of Lipid Polymorphism in Pulmonary Surfactant
Walter R. Perkins,
Richard B. Dause,
Roberta A. Parente,
*
Sharma R. Minchey,
Keir
C. Neuman,
Sol M. Gruner,
Theodore F. Taraschi,
Andrew S. Janoff
The development of artificial surfactants for the treatment
of respiratory distress syndrome (RDS) requires lipid systems that can
spread rapidly from solution to the air-water interface. Because
hydration-repulsion forces stabilize liposomal bilayers and oppose
spreading, liposome systems that undergo geometric rearrangement from
the bilayer (lamellar) phase to the hexagonal II (HII)
phase could hasten lipid transfer to the air-water interface through
unstable transition intermediates. A liposome system containing
dipalmitoylphosphatidylcholine was designed; the system is stable at
23°C but undergoes transformation to the HII phase as the
temperature increases to 37°C. The spreading of lipid from this
system to the air-water interface was rapid at 37°C but slow at
23°C. When tested in vivo in a neonatal rabbit model, such systems
elicited an onset of action equal to that of native human surfactant.
These findings suggest that lipid polymorphic phase behavior may have a
crucial role in the effective functioning of pulmonary surfactant.
W. R. Perkins, R. B. Dause, R. A. Parente, S. R. Minchey, A. S. Janoff, The Liposome Company, Inc., 1 Research Way, Princeton, NJ
08540, USA.
K. C. Neuman and S. M. Gruner, Department of Physics, Princeton
University, Princeton, NJ 08544, USA.
T. F. Taraschi, Department of Pathology and Cell Biology, Thomas
Jefferson University, Philadelphia, PA 19107, USA.
*
Present address: Ortho Diagnostic Systems, Raritan, NJ 08869, USA.
To whom correspondence should be addressed.
THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
- Differential Effects of Lysophosphatidylcholine on the Adsorption of Phospholipids to an Air/Water Interface.
- S. C. Biswas, S. B. Rananavare, and S. B. Hall (2007)
Biophys. J.
92, 493-501
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- Influence of the Membrane Lipid Structure on Signal Processing via G Protein-Coupled Receptors.
- Q. Yang, R. Alemany, J. Casas, K. Kitajka, S. M. Lanier, and P. V. Escriba (2005)
Mol. Pharmacol.
68, 210-217
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- Membrane Structure Modulation, Protein Kinase C{alpha} Activation, and Anticancer Activity of Minerval.
- J. Martinez, O. Vogler, J. Casas, F. Barcelo, R. Alemany, J. Prades, T. Nagy, C. Baamonde, P. G. Kasprzyk, S. Teres, et al. (2005)
Mol. Pharmacol.
67, 531-540
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- Naturally derived commercial surfactants differ in composition of surfactant lipids and in surface viscosity.
- M. Rudiger, A. Tolle, W. Meier, and B. Rustow (2005)
Am J Physiol Lung Cell Mol Physiol
288, L379-L383
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- The G{beta}{gamma} Dimer Drives the Interaction of Heterotrimeric Gi Proteins with Nonlamellar Membrane Structures.
- O. Vogler, J. Casas, D. Capo, T. Nagy, G. Borchert, G. Martorell, and P. V. Escriba (2004)
J. Biol. Chem.
279, 36540-36545
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- Plasmalogens effectively reduce the surface tension of surfactant-like phospholipid mixtures.
- M. Rudiger, I. Kolleck, G. Putz, R. R. Wauer, P. Stevens, and B. Rustow (1998)
Am J Physiol Lung Cell Mol Physiol
274, L143-L148
| Abstract »
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- Role of lipid polymorphism in G protein-membrane interactions: Nonlamellar-prone phospholipids and peripheral protein binding to membranes.
- P. V. Escriba, A. Ozaita, C. Ribas, A. Miralles, E. Fodor, T. Farkas, and J. A. Garcia-Sevilla (1997)
PNAS
94, 11375-11380
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