Reversible and irreversible inactivation of preformed pulmonary surfactant surface films by changes in subphase constituents.

@article{Amirkhanian1993ReversibleAI,
  title={Reversible and irreversible inactivation of preformed pulmonary surfactant surface films by changes in subphase constituents.},
  author={J. D. Amirkhanian and H W Taeusch},
  journal={Biochimica et biophysica acta},
  year={1993},
  volume={1165 3},
  pages={
          321-6
        }
}
View on PubMed
doi.org
33 Citations
Background Citations
11
Methods Citations
1
Results Citations
2

33 Citations

Inactivation of pulmonary surfactant due to serum-inhibited adsorption and reversal by hydrophilic polymers: experimental.
TLDR
Observation that addition of either hyaluronan or polyethylene glycol to subphases containing serum reversed inhibition by restoring the rate of surfactant adsorption to that of the clean interface, thereby allowing surfactants to overcome the serum-induced barrier to adsorb reversibly.
Nonionic polymers reverse inactivation of surfactant by meconium and other substances.
TLDR
Results from rat experiments indicate that total lung capacity is increased when PEG is first added to the Survanta, then mixed with meconium and instilled into the lungs, indicating that polymers are capable of reversing the inactivation of surfactant.
The influence of pH on surface properties of lung surfactants
TLDR
It is demonstrated that natural surfactants maintain their optimal surface activities over a broader pH range than do the commercial products because of a lack of SP-A, and careful monitoring of the pH for optimal surface activity is recommended.
Phase transitions in films of lung surfactant at the air-water interface.
Inhibition of Pulmonary Surfactant Biophysical Activity by Cationic Polyamino Acids
TLDR
It is concluded that the surface activity of pulmonary surfactant is significantly inhibited by the presence of the polycations, possibly by the formation of a mixed lipid/polyamino acid film.
Interactions of fibrinogen with bovine lung surfactant extract in bulk bilayer phases and films
TLDR
Interaction ofbovine lipid extract surfactant (BLES) (a clinical replacement LS) with soluble fibrinogen (Fbg) was studied employing various biophysical techniques in bulk bilayer and monolayer films and found to induce two sets of domains in BLES.
Impairing effect of fibrinogen on the mono-/bi-layer form of bovine lung surfactant
Lung surfactant (LS), a lipid–protein mixture responsible for alveolar stability, is inhibited by serum proteins leaked into the lungs in disease. Interaction of bovine lipid extract surfactant…
Role of lipid ordered/disordered phase coexistence in pulmonary surfactant function.
Effects of cationic liposome-DNA complexes on pulmonary surfactant function in vitro and in vivo
TLDR
Findings indicate that cationic liposomes alone may have deleterious effects on behavior of some surfactants possibly by disrupting charge interactions between negatively charged phospholipids and surfactant proteins.
Fluidizing effects of C‐reactive protein on lung surfactant membranes: protective role of surfactant protein A
TLDR
Results indicate that CRP inserts into surfactant membranes and drastically increases membrane fluidity, resulting in surfactan inactivation, and indicates that SP‐A/CRP interactions might be an important factor in vivo in controlling harmful CRP effects in the alveolus.
...
...

References

SHOWING 1-10 OF 36 REFERENCES
Enhancement of biophysical activity of lung surfactant extracts and phospholipid-apoprotein mixtures by surfactant protein A.
Inactivation of Exogenous Surfactant by Pulmonary Edema Fluid
TLDR
The data suggest that the functional properties of an immature neonatal lung, in which serum proteins tend to leak into the airspaces after the onset of ventilation, depend on the stoichiometric relation between surfactant lipids and inhibitory proteins in the lung liquid.
Surface property changes from interactions of albumin with natural lung surfactant and extracted lung lipids.
Pulmonary surfactant-associated protein A enhances the surface activity of lipid extract surfactant and reverses inhibition by blood proteins in vitro.
Although a monolayer of dipalmitoylphosphatidylcholine, the major component of pulmonary surfactant, is thought to be responsible for the reduction of the surface tension at the air-liquid interface…
A biophysical mechanism by which plasma proteins inhibit lung surfactant activity.
A protein from airways of premature lambs that inhibits surfactant function.
TLDR
The inhibitor affected multiple measurements of surfactant function in vitro and its presence may contribute to a surfactants deficiency state in the immature lung.
Effects of hemoglobin and cell membrane lipids on pulmonary surfactant activity.
TLDR
Data show that molecular components in hemorrhagic pulmonary edema can biophysically inactivate endogenous LS and adversely affect lung mechanics, and exogenous surfactant replacement can reverse this process even in the continued presence of inhibitor molecules and thus has potential utility in therapy for adult as well as neonatal RDS.
Alteration of surfactant function due to protein leakage: special interaction with fibrin monomer.
TLDR
High-permeability edema induced by different means results in alterations of lung mechanics and surface activity of lavaged surfactant, presumably due to protein surfactants interaction.
Artificial pulmonary surfactant inhibited by proteins.
TLDR
It is concluded that proteins present in the airways may seriously interfere with the activity of Surfactant TA.
Interaction of lipid vesicles with monomolecular layers containing lung surfactant proteins SP-B or SP-C.
TLDR
The Wilhelmy plate method was used and found that SP-B and SP-C, present in phospholipid vesicles, were able to induce the formation of a monolayer, as became apparent by an increase in surface pressure.
...
...