Evidence map›Paper›PMID 19478940›Full record

ArticlePloS one2009

Latherin: a surfactant protein of horse sweat and saliva.

Rhona E McDonald, Rachel I Fleming, John G Beeley, Douglas L Bovell, Jian R Lu, Xiubo Zhao, Alan Cooper, Malcolm W Kennedy

Abstract read
In one paragraph

Article in PloS one, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
–field-weighted citation impact
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

36 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Levels of horse allergen Equ c 4 in dander and saliva from ten horse breeds.Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology · 2019
    Article
  14. Article
  15. Article
  16. Review
  17. Frog foams and natural protein surfactants.Colloids and surfaces. A, Physicochemical and engineering aspects · 2017
    Article
  18. Tubular lipid binding proteins (TULIPs) growing everywhere.Biochimica et biophysica acta. Molecular cell research · 2017
    Review
  19. Review
  20. Review
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

8 authors.

Rhona E McDonaldEcology and Evolutionary Biology, Faculty of Biomedical and Life Sciences, University of Glasgow, Glasgow, United Kingdom.
Rachel I Fleming
John G Beeley
Douglas L Bovell
Jian R Lu
Xiubo Zhao
Alan Cooper
Malcolm W Kennedy

Funding

Wellcome TrustWellcome Trust GR070994MA
6 · The paper itself

Abstract

Horses are unusual in producing protein-rich sweat for thermoregulation, a major component of which is latherin, a highly surface-active, non-glycosylated protein. The amino acid sequence of latherin, determined from cDNA analysis, is highly conserved across four geographically dispersed equid species (horse, zebra, onager, ass), and is similar to a family of proteins only found previously in the oral cavity and associated tissues of mammals. Latherin produces a significant reduction in water surface tension at low concentrations (< or = 1 mg ml(-1)), and therefore probably acts as a wetting agent to facilitate evaporative cooling through a waterproofed pelt. Neutron reflection experiments indicate that this detergent-like activity is associated with the formation of a dense protein layer, about 10 A thick, at the air-water interface. However, biophysical characterization (circular dichroism, differential scanning calorimetry) in solution shows that latherin behaves like a typical globular protein, although with unusual intrinsic fluorescence characteristics, suggesting that significant conformational change or unfolding of the protein is required for assembly of the air-water interfacial layer. RT-PCR screening revealed latherin transcripts in horse skin and salivary gland but in no other tissues. Recombinant latherin produced in bacteria was also found to be the target of IgE antibody from horse-allergic subjects. Equids therefore may have adapted an oral/salivary mucosal protein for two purposes peculiar to their lifestyle, namely their need for rapid and efficient heat dissipation and their specialisation for masticating and processing large quantities of dry food material.

Indexed as

AllergensAmino Acid SequenceAnimalsBiophysical PhenomenaFatty Acid-Binding ProteinsFluorescenceHorsesMolecular Sequence DataNeutronsProteinsRecombinant ProteinsSalivaSequence Analysis, ProteinSequence Homology, Amino AcidSurface-Active AgentsSurface TensionAllergensFatty Acid-Binding Proteinslatherin protein, Equus caballusProteinsRecombinant ProteinsSurface-Active AgentsTryptophan

Identifiers

PMID19478940
PMCPMC2684629

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Registered trials

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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.