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Home / Equine Research Bank / PLoS One / Latherin: a surfactant protein of horse sweat and saliva.
PloS one2009; 4(5); e5726; doi: 10.1371/journal.pone.0005726

Latherin: a surfactant protein of horse sweat and saliva.

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.
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Publication Date: 2009-05-29 PubMed ID: 19478940PubMed Central: PMC2684629DOI: 10.1371/journal.pone.0005726Google Scholar: Lookup
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Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

This research focuses on latherin, a protein found in the sweat and saliva of horses, and its role in thermoregulation. The study provides insight into latherin’s ability to decrease water surface tension, and potential in facilitating illustrious cooling in these animals. Moreover, the protein’s sequence remains consistent across multiple equid species and shares similarities with proteins found in other mammals’ oral areas.

Latherin’s Properties & Function

  • The research indicates that latherin, a protein found in horse sweat and saliva, has a key role in regulating body temperature. It is unusual in that it is a surface-active, non-glycosylated protein and is highly conserved across different species.
  • Latherin lowered water surface tension at low concentrations, suggesting it serves as a wetting agent, helping enhance the efficiency of evaporative cooling. Horses, particularly, have a necessity for swift and effective heat dissipation due to their active lifestyle.

Protein Behaviour & Presence in Equids

  • Biophysical characterization unveiled latherin behaves like a standard globular protein in solution, with atypical intrinsic fluorescence characteristics. These characteristics suggest significant conformational change or unfolding of the protein is necessary for forming the air-water interfacial layer.
  • The presence of latherin transcripts were exclusively found in horse skin and salivary glands. Its sequence is identical across geographically diverse equid species, including horses, zebras, onagers, and donkeys.

Relevance to Allergic Reactions & Application in Other Species

  • The research also discovered that recombinantly produced latherin is a target of IgE antibodies from individuals allergic to horses. Hence, latherin likely contributes to allergenic reactions in sensitive individuals.
  • Interestingly, latherin is similar to a family of proteins found in oral cavities and related tissues of other mammals. The researchers propose that these species may have adapted an oral/salivary mucosal protein for facilitating their need for heat dissipation and processing large quantities of dry food.

Cite This Article

APA
McDonald RE, Fleming RI, Beeley JG, Bovell DL, Lu JR, Zhao X, Cooper A, Kennedy MW. (2009). Latherin: a surfactant protein of horse sweat and saliva. PLoS One, 4(5), e5726. https://doi.org/10.1371/journal.pone.0005726

Publication

PloS one
ISSN: 1932-6203
NlmUniqueID: 101285081
Country: United States
Language: English
Volume: 4
Issue: 5
Pages: e5726
PII: e5726

Researcher Affiliations

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

                MeSH Terms

                • Allergens
                • Amino Acid Sequence
                • Animals
                • Biophysical Phenomena
                • Fatty Acid-Binding Proteins
                • Fluorescence
                • Horses / metabolism
                • Molecular Sequence Data
                • Neutrons
                • Proteins / chemistry
                • Proteins / genetics
                • Proteins / metabolism
                • Recombinant Proteins / chemistry
                • Recombinant Proteins / genetics
                • Recombinant Proteins / metabolism
                • Saliva / metabolism
                • Sequence Analysis, Protein
                • Sequence Homology, Amino Acid
                • Surface Tension
                • Surface-Active Agents / chemistry
                • Surface-Active Agents / metabolism
                • Sweat / metabolism
                • Transcription, Genetic
                • Tryptophan / metabolism

                Grant Funding

                • Wellcome Trust
                • GR070994MA / Wellcome Trust

                Conflict of Interest Statement

                The authors have declared that no competing interests exist.

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