title: 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.
authors.affiliation: Ecology and Evolutionary Biology, Faculty of Biomedical and Life Sciences, University of Glasgow, Glasgow, United Kingdom.
authors.forename: Rhona E
authors.initials: RE
authors.lastname: McDonald
authors.forename: Rachel I
authors.initials: RI
authors.lastname: Fleming
authors.forename: John G
authors.initials: JG
authors.lastname: Beeley
authors.forename: Douglas L
authors.initials: DL
authors.lastname: Bovell
authors.forename: Jian R
authors.initials: JR
authors.lastname: Lu
authors.forename: Xiubo
authors.initials: X
authors.lastname: Zhao
authors.forename: Alan
authors.initials: A
authors.lastname: Cooper
authors.forename: Malcolm W
authors.initials: MW
authors.lastname: Kennedy
mesh_terms: D000485:Allergens; D000595:Amino Acid Sequence; D000818:Animals; D055592:Biophysical Phenomena; D050556:Fatty Acid-Binding Proteins; D005453:Fluorescence; D006736:Horses / Q000378:metabolism*; D008969:Molecular Sequence Data; D009502:Neutrons; D011506:Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D012463:Saliva / Q000378:metabolism*; D020539:Sequence Analysis, Protein; D017386:Sequence Homology, Amino Acid; D013500:Surface Tension; D013501:Surface-Active Agents / Q000737:chemistry / Q000378:metabolism*; D013542:Sweat / Q000378:metabolism*; D014158:Transcription, Genetic; D014364:Tryptophan / Q000378:metabolism
chemical_list: D000485:Allergens; D050556:Fatty Acid-Binding Proteins; D011506:Proteins; D011994:Recombinant Proteins; D013501:Surface-Active Agents; C049912:latherin protein, Equus caballus; D014364:Tryptophan