Evidence map›Paper›PMID 17693477›Full record

ArticleBiophysical journal2007

Surfactant protein A forms extensive lattice-like structures on 1,2-dipalmitoylphosphatidylcholine/rough-lipopolysaccharide-mixed monolayers.

Ignacio García-Verdugo, Olga Cañadas, Svetla G Taneva, Kevin M W Keough, Cristina Casals

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
0.8field-weighted citation impact, top 28% 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

15 citing papers in PubMed, 31 citations in OpenAlex.

  1. Synergistic Action of Antimicrobial Lung Proteins againstInternational journal of molecular sciences · 2021
    Article
  2. Review
  3. Alveolar lipids in pulmonary disease. A review.Lipids in health and disease · 2020
    Review
  4. Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
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  12. Article
  13. Pulmonary surfactant: an immunological perspective.Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology · 2010
    Review
  14. Article
  15. 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

5 authors at 3 institutions in 2 countries.

Ignacio García-VerdugoDepartamento de Bioquímica y Biología Molecular I and CIBER Enfermedades Respiratorias, Complutense University of Madrid, 28040-Madrid, Spain.
Olga Cañadas
Svetla G Taneva
Kevin M W Keough
Cristina Casals
Memorial University of Newfoundland · CAUniversidad Complutense de Madrid · ESCentro de Investigación Biomédica en Red de Enfermedades Respiratorias · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Due to the inhalation of airborne particles containing bacterial lipopolysaccharide (LPS), these molecules might incorporate into the 1,2-dipalmitoylphosphatidylcholine (DPPC)-rich monolayer and interact with surfactant protein A (SP-A), the major surfactant protein component involved in host defense. In this study, epifluorescence microscopy combined with a surface balance was used to examine the interaction of SP-A with mixed monolayers of DPPC/rough LPS (Re-LPS). Binary monolayers of Re-LPS plus DPPC showed negative deviations from ideal behavior of the mean areas in the films consistent with partial miscibility and attractive interaction between the lipids. This interaction resulted in rearrangement and reduction of the size of DPPC-rich solid domains in DPPC/Re-LPS monolayers. The adsorption of SP-A to these monolayers caused expansion in the lipid molecular areas. SP-A interacted strongly with Re-LPS and promoted the formation of DPPC-rich solid domains. Fluorescently labeled Texas red-SP-A accumulated at the fluid-solid boundary regions and formed networks of interconnected filaments in the fluid phase of DPPC/Re-LPS monolayers in a Ca(2+)-independent manner. These lattice-like structures were also observed when TR-SP-A interacted with lipid A monolayers. These novel results deepen our understanding of the specific interaction of SP-A with the lipid A moiety of bacterial LPS.

Indexed as

1,2-DipalmitoylphosphatidylcholineAdsorptionBiophysicsCalciumLipidsLipopolysaccharidesMicroscopy, FluorescenceModels, ChemicalMolecular ConformationPressureProtein BindingPulmonary Surfactant-Associated Protein ASurface Properties1,2-DipalmitoylphosphatidylcholineCalciumLipidsLipopolysaccharidesPulmonary Surfactant-Associated Protein A

Identifiers

PMID17693477
PMCPMC2072082
OpenAlexW2139644134

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.