Evidence map›Paper›PMID 20026298›Full record

ReviewBiochimica et biophysica acta2010

Overcoming rapid inactivation of lung surfactant: analogies between competitive adsorption and colloid stability.

Joseph A Zasadzinski, Patrick C Stenger, Ian Shieh, Prajna Dhar

Abstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
2.9field-weighted citation impact, top 9% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

31 citing papers in PubMed, 83 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Evolution of interfacial mechanics of lung surfactant mimics progression of acute respiratory distress syndrome.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  6. Article
  7. Polymer Lung Surfactants Attenuate Direct Lung Injury in Mice.ACS biomaterials science & engineering · 2023
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. The POOR Get POORer: A Hypothesis for the Pathogenesis of Ventilator-induced Lung Injury.American journal of respiratory and critical care medicine · 2020
    Review
  14. Review
  15. Article
  16. Article
  17. Evolution and mechanics of mixed phospholipid fibrinogen monolayers.Journal of the Royal Society, Interface · 2018
    Article
  18. Article
  19. Review
  20. Influence of molecular coherence on surface viscosity.Langmuir : the ACS journal of surfaces and colloids · 2014
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Joseph A ZasadzinskiDepartment of Chemical Engineering, University of California, Santa Barbara, California 93106, USA. gorilla@engineering.ucsb.edu
Patrick C Stenger
Ian Shieh
Prajna Dhar
University of California, Santa Barbara · US

Funding

LIPID AND PROTEIN EFFECTS ON MONOLAYER STABILITYR01HL051177 · NHLBI · UNIVERSITY OF MINNESOTA · PI Joseph Anthony Zasadzinski · 1994 to 2026
$9.5M
NHLBI NIH HHS HL-51177NHLBI NIH HHS R01 HL051177
6 · The paper itself

Abstract

Lung surfactant (LS) is a mixture of lipids and proteins that line the alveolar air-liquid interface, lowering the interfacial tension to levels that make breathing possible. In acute respiratory distress syndrome (ARDS), inactivation of LS is believed to play an important role in the development and severity of the disease. This review examines the competitive adsorption of LS and surface-active contaminants, such as serum proteins, present in the alveolar fluids of ARDS patients, and how this competitive adsorption can cause normal amounts of otherwise normal LS to be ineffective in lowering the interfacial tension. LS and serum proteins compete for the air-water interface when both are present in solution either in the alveolar fluids or in a Langmuir trough. Equilibrium favors LS as it has the lower equilibrium surface pressure, but the smaller proteins are kinetically favored over multi-micron LS bilayer aggregates by faster diffusion. 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. This process can be understood in terms of classic colloid stability theory in which an energy barrier to diffusion stabilizes colloidal suspensions against aggregation. This analogy provides qualitative and quantitative predictions regarding the origin of surfactant inactivation. An important corollary is that any additive that promotes colloid coagulation, such as increased electrolyte concentration, multivalent ions, hydrophilic non-adsorbing polymers such as PEG, dextran, etc. added to LS, or polyelectrolytes such as chitosan, also promotes LS adsorption in the presence of serum proteins and helps reverse surfactant inactivation. The theory provides quantitative tools to determine the optimal concentration of these additives and suggests that multiple additives may have a synergistic effect. A variety of physical and chemical techniques including isotherms, fluorescence microscopy, electron microscopy and X-ray diffraction show that LS adsorption is enhanced by this mechanism without substantially altering the structure or properties of the LS monolayer.

Indexed as

AdsorptionAlgorithmsBlood ProteinsBronchoalveolar Lavage FluidColloidsHumansLung DiseasesModels, BiologicalPulmonary SurfactantsSurface PropertiesBlood ProteinsColloidsPulmonary Surfactantsalbumincharge reversalchitosanDebye lengthdepletion attractioninhibitionpolyethylene glycol

Identifiers

PMID20026298
PMCPMC2834873
OpenAlexW2126376506

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.