Evidence map›Paper›PMID 26270023›Full record

ArticleBiochemistry2015

Environmental Pollutant Ozone Causes Damage to Lung Surfactant Protein B (SP-B).

Joanna M Hemming, Brian R Hughes, Adrian R Rennie, Salvador Tomas, Richard A Campbell, Arwel V Hughes, Thomas Arnold, Stanley W Botchway, Katherine C Thompson

Open access · hybridAbstract read
In one paragraph

Article in Biochemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
4.4field-weighted citation impact, top 6% 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

17 citing papers in PubMed, 32 citations in OpenAlex.

  1. Trial
  2. Parenchymal and inflammatory responses to ozone exposure in the aging healthy and surfactant protein C mutant lung.American journal of physiology. Lung cellular and molecular physiology · 2025
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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

9 authors at 2 institutions in 2 countries.

Joanna M HemmingDepartment of Biological Sciences and Institute of Structural and Molecular Biology, Birkbeck College, University of London , Malet Street, London WC1E 7HX, U.K.
Brian R HughesDepartment of Biological Sciences and Institute of Structural and Molecular Biology, Birkbeck College, University of London , Malet Street, London WC1E 7HX, U.K.
Adrian R RennieMaterials Physics, Department of Physics and Astronomy, Uppsala University , 75120 Uppsala, Sweden.
Salvador TomasDepartment of Biological Sciences and Institute of Structural and Molecular Biology, Birkbeck College, University of London , Malet Street, London WC1E 7HX, U.K.
Richard A CampbellInstitut Laue-Langevin , 71 Avenue des Martyrs, CS20156, 38042 Grenoble Cedex 09, France.
Arwel V HughesISIS Pulsed Neutron and Muon Source, STFC Rutherford Appleton Laboratory , Harwell Oxford, Didcot, Oxfordshire OX11 0QX, U.K.
Thomas ArnoldDiamond Light Source , Harwell Science and Innovation Campus, Didcot OX11 0DE, U.K.
Stanley W BotchwaySTFC, Lasers for Science Facility, Central Laser Facility, Research Complex at Harwell, STFC Rutherford Appleton Laboratory , Harwell Oxford, Didcot, Oxfordshire OX11 0FA, U.K.
Katherine C ThompsonDepartment of Biological Sciences and Institute of Structural and Molecular Biology, Birkbeck College, University of London , Malet Street, London WC1E 7HX, U.K.
Institut Laue-Langevin · FRUppsala University · SE

Funding

Wellcome Trust 093468/Z/10/Z
6 · The paper itself

Abstract

Lung surfactant protein B (SP-B) is an essential protein found in the surfactant fluid at the air-water interface of the lung. Exposure to the air pollutant ozone could potentially damage SP-B and lead to respiratory distress. We have studied two peptides, one consisting of the N-terminus of SP-B [SP-B(1-25)] and the other a construct of the N- and C-termini of SP-B [SP-B(1-25,63-78)], called SMB. Exposure to dilute levels of ozone (~2 ppm) of monolayers of each peptide at the air-water interface leads to a rapid reaction, which is evident from an increase in the surface tension. Fluorescence experiments revealed that this increase in surface tension is accompanied by a loss of fluorescence from the tryptophan residue at the interface. Neutron and X-ray reflectivity experiments show that, in contrast to suggestions in the literature, the peptides are not solubilized upon oxidation but rather remain at the interface with little change in their hydration. Analysis of the product material reveals that no cleavage of the peptides occurs, but a more hydrophobic product is slowly formed together with an increased level of oligomerization. We attributed this to partial unfolding of the peptides. Experiments conducted in the presence of phospholipids reveal that the presence of the lipids does not prevent oxidation of the peptides. Our results strongly suggest that exposure to low levels of ozone gas will damage SP-B, leading to a change in its structure. The implication is that the oxidized protein will be impaired in its ability to interact at the air-water interface with negatively charged phosphoglycerol lipids, thus compromising what is thought to be its main biological function.

Indexed as

1,2-DipalmitoylphosphatidylcholineAirAmino Acid SequenceEnvironmental PollutantsLungModels, MolecularMolecular Sequence DataOzonePeptide FragmentsPhosphatidylglycerolsPressureProtein Structure, SecondaryPulmonary Surfactant-Associated Protein B1,2-Dipalmitoylphosphatidylcholine1-palmitoyl-2-oleoylglycero-3-phosphoglycerolEnvironmental PollutantsOzonePeptide FragmentsPhosphatidylglycerolsPulmonary Surfactant-Associated Protein B

Identifiers

PMID26270023
PMCPMC4571829
OpenAlexW2137459214

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.