Evidence map›Paper›PMID 27508436›Full record

ArticleBiophysical journal2016

Human Pulmonary Surfactant Protein SP-A1 Provides Maximal Efficiency of Lung Interfacial Films.

Elena Lopez-Rodriguez, Alicia Pascual, Raquel Arroyo, Joanna Floros, Jesus Perez-Gil

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

25 citing papers in PubMed, 49 citations in OpenAlex.

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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

5 authors at 3 institutions in 3 countries.

Elena Lopez-RodriguezFunctional and Applied Anatomy, Hannover Medical School, Hannover, Germany; Department of Biochemistry, Faculty of Biology, and Hospital 12 Octubre Research Institute, Complutense University of Madrid, Madrid, Spain.
Alicia PascualDepartment of Biochemistry, Faculty of Biology, and Hospital 12 Octubre Research Institute, Complutense University of Madrid, Madrid, Spain.
Raquel ArroyoDepartment of Biochemistry, Faculty of Biology, and Hospital 12 Octubre Research Institute, Complutense University of Madrid, Madrid, Spain.
Joanna FlorosPenn University, Philadelphia, Pennsylvania.
Jesus Perez-GilDepartment of Biochemistry, Faculty of Biology, and Hospital 12 Octubre Research Institute, Complutense University of Madrid, Madrid, Spain. Electronic address: jperezgil@bio.ucm.es.
Research Institute Hospital 12 de Octubre · ESUniversidad Complutense de Madrid · ESPenn Center for AIDS Research · US

Funding

SURFACTANT PROTEINS AND RESPIRATORY DISTRESS SYNDROMER37HL034788 · NHLBI · PENNSYLVANIA STATE UNIV HERSHEY MED CTR · PI FLOROS, JOANNA · 1996 to 2005
$3.2M
SURFACTANT PROTEINS AND RESPIRATORY DISTRESS SYNDROMER01HL034788 · NHLBI · PENNSYLVANIA STATE UNIV HERSHEY MED CTR · PI FLOROS, JOANNA · 1985 to 2011
$3.0M
NHLBI NIH HHS R01 HL034788NHLBI NIH HHS R37 HL034788
6 · The paper itself

Abstract

Pulmonary surfactant is a lipoprotein complex that reduces surface tension to prevent alveolar collapse and contributes to the protection of the respiratory surface from the entry of pathogens. Surfactant protein A (SP-A) is a hydrophilic glycoprotein of the collectin family, and its main function is related to host defense. However, previous studies have shown that SP-A also aids in the formation and biophysical properties of pulmonary surfactant films at the air-water interface. Humans, unlike rodents, have two genes, SFTPA1 and SFTPA2. The encoded proteins, SP-A1 and SP-A2, differ quantitatively or qualitatively in function. It has been shown that both gene products are necessary for tubular myelin formation, an extracellular structural form of lung surfactant. The goal of this study was to investigate potential differences in the biophysical properties of surfactants containing human SP-A1, SP-A2, or both. For this purpose, we have studied for the first time, to our knowledge, the biophysical properties of pulmonary surfactant from individual humanized transgenic mice expressing human SP-A1, SP-A2, or both SP-A1 and SP-A2, in the captive bubble surfactometer. We observed that pulmonary surfactant containing SP-A1 reaches lower surface tension after postexpansion interfacial adsorption than surfactants containing no SP-A or only SP-A2. Under interfacial compression-expansion cycling conditions, surfactant films containing SP-A1 also performed better, particularly with respect to the reorganization of the films that takes place during compression. On the other hand, addition of recombinant SP-A1 to a surfactant preparation reconstituted from the hydrophobic fraction of a porcine surfactant made it more resistant to inhibition by serum than the addition of equivalent amounts of SP-A2. We conclude that the presence of SP-A1 allows pulmonary surfactant to adopt a particularly favorable structure with optimal biophysical properties.

Indexed as

AnimalsGene Knockout TechniquesHumansHydrophobic and Hydrophilic InteractionsLungMiceMice, TransgenicPulmonary Surfactant-Associated Protein ASurface TensionSwinePulmonary Surfactant-Associated Protein ASFTPA1 protein, humanSFTPA2 protein, human

Identifiers

PMID27508436
PMCPMC4982931
OpenAlexW2475730955

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.