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Possible Interaction: Albumin and Pulmonary Surfactants

Research Papers that Mention the Interaction

However, the mechanism by which PS is inhibited by albumin remains controversial.
Biophysical journal  •  2008  |  View Paper
The albumin and fibrinogen significantly inhibited the adsorption rate and ST-lowering properties of surfactant through increasing STs of adsorption rate, min-ST, and max-ST.
We concluded that albumin and fibrinogen significantly altered surfactant function and its ultrastructural morphology in vitro.
Journal of Korean medical science  •  1998  |  View Paper
If albumin reaches the interface, it creates an energy barrier to subsequent LS adsorption that slows or prevents the adsorption of the necessary amounts of LS required to lower surface tension.
Biochimica et biophysica acta  •  2010  |  View Paper
Albumin competes with lung surfactant for the air-water interface, resulting in decreased surfactant adsorption and increased surface tension.
Biochimica et biophysica acta  •  2008  |  View Paper
With a pulsating bubble surfactometer we assessed the ability of various agents, fibrinogen, human serum, albumin , and a 55,000-dalton serum protein, to interfere with the surface activity of Surfactant TA.
Journal of applied physiology  •  1987  |  View Paper
Albumin at the interface creates an energy barrier to subsequent LS adsorption that can be overcome by the depletion attraction induced by polyethylene glycol (PEG) in solution.
Lung surfactant LS ) and albumin compete for the air-water interface when both are present in solution.
These results confirm that albumin adsorption creates a physical barrier that inhibits LS adsorption, and that PEG in the subphase generates a depletion attraction between the LS aggregates and the interface that enhances LS adsorption without substantially altering the structure or properties of the LS monolayer.
Biophysical journal  •  2009  |  View Paper
Albumin adsorbed to the interface induces an energy barrier to surfactant diffusion of order 5 k(B)T, leading to a reduction in adsorption equivalent to reducing the surfactant concentration by a factor of 100.
Lung surfactant adsorption to an air-water interface is strongly inhibited by an energy barrier imposed by the competitive adsorption of albumin and other surface-active serum proteins that are present in the lung during acute respiratory distress syndrome.
Biophysical journal  •  2007  |  View Paper
We studied the mechanisms by which C16:0 lysophosphatidylcholine (LPC) and albumin inhibit the surface activity of calf lung surfactant extract (CLSE) by using a pulsating bubble apparatus with a specialized hypophase exchange system, plus adsorption and Wilhelmy balance measurements.
Pediatric Research  •  1999  |  View Paper
Surfactant mixed with isolated albumin at a concentration equal to that in 11.2-EF/S decreased the tidal volume to 8.6 ml/kg (NS vs 11.2-EF/S), and with isolated fibrinogen lowered it to 18.1 mg/kg (P < 0.05 vs S-alone).
Respiration physiology  •  1994  |  View Paper
The diameter of bubbles generated in the presence of albumin (4 or 40 mg/ml) or fibrinogen (4 mg/ml) was 4-5 times larger, indicating surfactant inhibition.
Biology of the neonate  •  1992  |  View Paper
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