Evidence map›Paper›PMID 28834721›Full record

ArticleBiophysical journal2017

Divide & Conquer: Surfactant Protein SP-C and Cholesterol Modulate Phase Segregation in Lung Surfactant.

Nuria Roldan, Jesús Pérez-Gil, Michael R Morrow, Begoña García-Álvarez

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
2.2field-weighted citation impact, top 11% 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

11 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Purification and membrane interactions of human KCNQ1Biochimica et biophysica acta. Biomembranes · 2022
    Article
  6. Article
  7. Article
  8. Human-Based AdvancedFrontiers in medicine · 2021
    Review
  9. Review
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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 2 institutions in 2 countries.

Nuria RoldanDepartment of Biochemistry, Faculty of Biology, Complutense University, Madrid, Spain; Healthcare Research Institute of Hospital 12 de Octubre, Hospital Universitario 12 de Octubre, Madrid, Spain.
Jesús Pérez-GilDepartment of Biochemistry, Faculty of Biology, Complutense University, Madrid, Spain; Healthcare Research Institute of Hospital 12 de Octubre, Hospital Universitario 12 de Octubre, Madrid, Spain.
Michael R MorrowDepartment of Physics and Physical Oceanography, Memorial University of Newfoundland, St. John's, Newfoundland, Canada.
Begoña García-ÁlvarezDepartment of Biochemistry, Faculty of Biology, Complutense University, Madrid, Spain; Healthcare Research Institute of Hospital 12 de Octubre, Hospital Universitario 12 de Octubre, Madrid, Spain. Electronic address: begoga01@ucm.es.
Universidad Complutense de Madrid · ESMemorial University of Newfoundland · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lung surfactant (LS) is an essential system supporting the respiratory function. Cholesterol can be deleterious for LS function, a condition that is reversed by the presence of the lipopeptide SP-C. In this work, the structure of LS-mimicking membranes has been analyzed under the combined effect of SP-C and cholesterol by deuterium NMR and phosphorus NMR and by electron spin resonance. Our results show that SP-C induces phase segregation at 37°C, resulting in an ordered phase with spectral features resembling an interdigitated state enriched in dipalmitoylphosphatidylcholine, a liquid-crystalline bilayer phase, and an extremely mobile phase consistent with small vesicles or micelles. In the presence of cholesterol, POPC and POPG motion seem to be more hindered by SP-C than dipalmitoylphosphatidylcholine. The use of deuterated cholesterol did not show signs of specific interactions that could be attributed to SP-C or to the other hydrophobic surfactant protein SP-B. Palmitoylation of SP-C had an indirect effect on the extent of protein-lipid perturbations by stabilizing SP-C structure, and seemed to be important to maximize differences among the lipids participating in each phase. These results shed some light on how SP-C-induced lipid perturbations can alter membrane structure to sustain LS functionality at the air-liquid interface.

Indexed as

CholesterolPulmonary Surfactant-Associated Protein BPulmonary Surfactant-Associated Protein CTemperatureCholesterolPulmonary Surfactant-Associated Protein BPulmonary Surfactant-Associated Protein C

Identifiers

PMID28834721
PMCPMC5567427
OpenAlexW2747540653

What OpenQuestion holds

Textmetadata
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.