scholarly journals Distinct Steps in the Adsorption of Pulmonary Surfactant to an Air-Liquid Interface

2000 ◽  
Vol 78 (1) ◽  
pp. 257-266 ◽  
Author(s):  
Robert W. Walters ◽  
Robert R. Jenq ◽  
Stephen B. Hall
1980 ◽  
pp. 57-67
Author(s):  
Fred Possmayer ◽  
I. LeRoy Metcalfe ◽  
Goran Enhorning

2020 ◽  
Vol 118 (3) ◽  
pp. 388a
Author(s):  
Mercedes Echaide ◽  
Sonia Vazquez-Sanchez ◽  
Antonio Cruz ◽  
Jesus Perez-Gil

Physiology ◽  
2003 ◽  
Vol 18 (4) ◽  
pp. 151-157 ◽  
Author(s):  
Christopher B. Daniels ◽  
Sandra Orgeig

Pulmonary surfactant controls the surface tension at the air-liquid interface within the lung. This system had a single evolutionary origin that predates the evolution of the vertebrates and lungs. The lipid composition of surfactant has been subjected to evolutionary selection pressures, particularly temperature, throughout the evolution of the vertebrates.


2010 ◽  
Vol 98 (3) ◽  
pp. 89a
Author(s):  
Mercedes Echaide ◽  
Karen Lu ◽  
Elena Lopez ◽  
H William Taeusch ◽  
Jesus Perez-Gil

1984 ◽  
Vol 62 (11) ◽  
pp. 1121-1133 ◽  
Author(s):  
Fred Possmayer ◽  
Shou-Hwa Yu ◽  
J. Marnie Weber ◽  
Paul G. R. Harding

The mammalian lung is stabilized by a specialized material, the pulmonary surfactant, which acts by reversibly reducing the surface tension at the air–liquid interface of the lung during breathing. Pulmonary surfactant contains approximately 90% lipid and 10% proteins. Dipalmitoyl phosphatidylcholine, the major lipid component, appears to be primarily responsible for the ability to reduce surface tension to near 0 dyn/cm (1 dyn = 10 μN). The other components of pulmonary surfactant promote the adsorption and spreading of this disaturated lecithin at the air–liquid interface. Surfactant activity can be accessed by physical and biological assays. Apparent discrepancies between the results obtained with the Wilhelmy plate surface balance and the pulsating bubble surfactometer have led to the suggestion that separate "protein-facilitated" (catalytic type) and "protein-mediated" (chemical type) processes may be involved in adsorption and (or) spreading at the different surfactant concentrations used with these two techniques. Artificial surfactants, which mimic the essential properties of the natural product with the pulsating bubble surfactometer, can be produced with synthetic lipids. Treatment of prematurely delivered infants suffering from the neonatal respiratory distress syndrome with lipid extracts of pulmonary surfactant leads to a marked improvement in gaseous exchange.


2012 ◽  
Vol 102 (3) ◽  
pp. 647a
Author(s):  
Nina Hobi ◽  
Monika Bachhuber ◽  
Jesus Pérez-Gil ◽  
Thomas Haller

2005 ◽  
Vol 1720 (1-2) ◽  
pp. 59-72 ◽  
Author(s):  
H. Bachofen ◽  
U. Gerber ◽  
P. Gehr ◽  
M. Amrein ◽  
S. Schürch

2013 ◽  
Vol 104 (2) ◽  
pp. 429a
Author(s):  
Konstantin Andreev ◽  
Michael W. Martynowycz ◽  
Stephen B. Hall ◽  
David Gidalevitz

Author(s):  
Cristina García-Mouton ◽  
Alberto Hidalgo ◽  
Raquel Arroyo ◽  
Mercedes Echaide ◽  
Antonio Cruz ◽  
...  

This work is focused on the potential use of pulmonary surfactant to deliver full-length recombinant human surfactant protein SP-D (rhSP-D) using the respiratory air-liquid interface as a shuttle. Surfactant protein D (SP-D) is a collectin protein present in the pulmonary surfactant (PS) system, involved in innate immune defense and surfactant homeostasis. It has been recently suggested as a potential therapeutic to alleviate inflammatory responses and lung diseases in preterm infants suffering from respiratory distress syndrome (RDS) or bronchopulmonary dysplasia (BPD). However, none of the current clinical surfactants used for surfactant replacement therapy (SRT) to treat RDS contain SP-D. The interaction of SP-D with surfactant components, the potential of PS as a respiratory drug delivery system and the possibility to produce recombinant versions of human SP-D, brings the possibility of delivering clinical surfactants supplemented with SP-D. Here, we used an in vitro setup that somehow emulates the respiratory air-liquid interface to explore this novel approach. It consists in two different compartments connected with a hydrated paper bridge forming a continuous interface. We firstly analyzed the adsorption and spreading of rhSP-D alone from one compartment to another over the air-liquid interface, observing low interfacial activity. Then, we studied the interfacial spreading of the protein co-administered with PS, both at different time periods or as a mixed formulation, and which oligomeric forms of rhSP-D better traveled associated with PS. The results presented here demonstrated that PS may transport rhSP-D long distances over air-liquid interfaces, either as a mixed formulation or separately in a close window time, opening the doors to empower the current clinical surfactants and SRT.


Pneumologie ◽  
2011 ◽  
Vol 65 (12) ◽  
Author(s):  
M Selmansberger ◽  
AG Lenz ◽  
M Schmidmeir ◽  
O Eickelberg ◽  
T Stoeger ◽  
...  

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