Related Content
Search Google Scholar for:
|
|
Science 23 July 1993:
Vol. 261. no. 5120, pp. 453 - 456
DOI: 10.1126/science.8332910
|
|
Articles
Science, Vol 261, Issue 5120, 453-456
Copyright © 1993 by American Association for the Advancement of Science
A function of lung surfactant protein SP-B
ML Longo,
AM Bisagno,
JA Zasadzinski,
R Bruni,
and
AJ Waring
Department of Chemical and Nuclear Engineering, University of California, Santa Barbara 93106.
The primary function of lung surfactant is to form monolayers at the alveolar interface capable of lowering the normal surface tension to near zero. To accomplish this process, the surfactant must be capable of maintaining a coherent, tightly packed monolayer that avoids collapse during expiration. The positively charged amino-terminal peptide SP-B1-25 of lung surfactant-specific protein SP-B increases the collapse pressure of an important component of lung surfactant, palmitic acid (PA), to nearly 70 millinewtons per meter. This alteration of the PA isotherms removes the driving force for "squeeze-out" of the fatty acids from the primarily dipalmitoylphosphatidylcholine monolayers of lung surfactant. An uncharged mutant of SP-B1-25 induced little change in the isotherms, suggesting that a specific charge interaction between the cationic peptide and the anionic lipid is responsible for the stabilization. The effect of SP-B1-25 on fatty acid isotherms is remarkably similar to that of simple poly-cations, suggesting that such polymers might be useful as components of replacement surfactants for the treatment of respiratory distress syndrome.
THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
- Molecular Dynamics Simulation Study of a Pulmonary Surfactant Film Interacting with a Carbonaceous Nanoparticle.
- S. Choe, R. Chang, J. Jeon, and A. Violi (2008)
Biophys. J.
95, 4102-4114
| Abstract »
| Full Text »
| PDF »
- The Surfactant Peptide KL4 Sequence Is Inserted with a Transmembrane Orientation into the Endoplasmic Reticulum Membrane.
- L. Martinez-Gil, J. Perez-Gil, and I. Mingarro (2008)
Biophys. J.
95, L36-L38
| Abstract »
| Full Text »
| PDF »
- Comparing Experimental and Simulated Pressure-Area Isotherms for DPPC.
- S. L. Duncan and R. G. Larson (2008)
Biophys. J.
94, 2965-2986
| Abstract »
| Full Text »
| PDF »
- The Surfactant Peptide KL4 in Lipid Monolayers: PHASE BEHAVIOR, TOPOGRAPHY, AND CHEMICAL DISTRIBUTION.
- M. Saleem, M. C. Meyer, D. Breitenstein, and H.-J. Galla (2008)
J. Biol. Chem.
283, 5195-5207
| Abstract »
| Full Text »
| PDF »
- Effects of Hydrophobic Surfactant Proteins on Collapse of Pulmonary Surfactant Monolayers.
- F. Lhert, W. Yan, S. C. Biswas, and S. B. Hall (2007)
Biophys. J.
93, 4237-4243
| Abstract »
| Full Text »
| PDF »
- Critical Structure-Function Determinants within the N-Terminal Region of Pulmonary Surfactant Protein SP-B.
- A. G. Serrano, M. Ryan, T. E. Weaver, and J. Perez-Gil (2006)
Biophys. J.
90, 238-249
| Abstract »
| Full Text »
| PDF »
- Molecular Dynamics Simulations of the Anchoring and Tilting of the Lung-Surfactant Peptide SP-B1-25 in Palmitic Acid Monolayers.
- H. Lee, S. K. Kandasamy, and R. G. Larson (2005)
Biophys. J.
89, 3807-3821
| Abstract »
| Full Text »
| PDF »
- More Than a Monolayer: Relating Lung Surfactant Structure and Mechanics to Composition.
- C. Alonso, T. Alig, J. Yoon, F. Bringezu, H. Warriner, and J. A. Zasadzinski (2004)
Biophys. J.
87, 4188-4202
| Abstract »
| Full Text »
| PDF »
- Electrostatic Barrier to Recovery of Dipalmitoylphosphatidylglycerol Monolayers after Collapse.
- T. F. Alig, H. E. Warriner, L. Lee, and J. A. Zasadzinski (2004)
Biophys. J.
86, 897-904
| Abstract »
| Full Text »
| PDF »
- Location of Structural Transitions in an Isotopically Labeled Lung Surfactant SP-B Peptide by IRRAS.
- C. R. Flach, P. Cai, D. Dieudonne, J. W. Brauner, K. M. W. Keough, J. Stewart, and R. Mendelsohn (2003)
Biophys. J.
85, 340-349
| Abstract »
| Full Text »
| PDF »
- Molecular Dynamics Simulations of a Pulmonary Surfactant Protein B Peptide in a Lipid Monolayer.
- J. A. Freites, Y. Choi, and D. J. Tobias (2003)
Biophys. J.
84, 2169-2180
| Abstract »
| Full Text »
| PDF »
- Effect of Hydrophobic Surfactant Proteins SP-B and SP-C on Binary Phospholipid Monolayers: II. Infrared External Reflectance-Absorption Spectroscopy.
- J. M. Brockman, Z. Wang, R. H. Notter, and R. A. Dluhy (2003)
Biophys. J.
84, 326-340
| Abstract »
| Full Text »
| PDF »
- Focus on proteins, surfaces, et al..
- R. Bruni (2002)
Am J Physiol Lung Cell Mol Physiol
283, L894-L896
| Full Text »
| PDF »
- Function and inhibition sensitivity of the N-terminal segment of surfactant protein B (SP-B1-25) in preterm rabbits.
- M Gupta, J M Hernandez-Juviel, A J Waring, and F J Walther (2001)
Thorax
56, 871-876
| Abstract »
| Full Text »
| PDF »
- SP-B refining of pulmonary surfactant phospholipid films.
- K. Nag, J. G. Munro, K. Inchley, S. Schurch, N. O. Petersen, and F. Possmayer (1999)
Am J Physiol Lung Cell Mol Physiol
277, L1179-L1189
| Abstract »
| Full Text »
| PDF »
- Addition of alpha 1-Antitrypsin to Surfactant Improves Oxygenation in Surfactant-deficient Rats.
- Y. BELAI, J. M. HERNÁNDEZ-JUVIEL, R. BRUNI, A. J. WARING, and F. J. WALTHER (1999)
Am. J. Respir. Crit. Care Med.
159, 917-923
| Abstract »
| Full Text »
- NO2-induced generation of extracellular reactive oxygen is mediated by epithelial lining layer antioxidants.
- L. W. Velsor and E. M. Postlethwait (1997)
Am J Physiol Lung Cell Mol Physiol
273, L1265-L1275
| Abstract »
| Full Text »
| PDF »
- Spiking Survanta with Synthetic Surfactant Peptides Improves Oxygenation in Surfactant-deficient Rats.
- F. J. WALTHER, J. HERNANDEZ-JUVIEL, R. BRUNI, and A. J. WARING (1997)
Am. J. Respir. Crit. Care Med.
156, 855-861
| Abstract »
| Full Text »
| PDF »
- Helping premature lungs breathe easier.
- J Travis (1993)
Science
261, 426
| PDF »
|
|
