Latherin: a surfactant protein of horse sweat and saliva

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

doi:10.1371/journal.pone.0005726

Latherin: a surfactant protein of horse sweat and saliva

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

Biological and Biomedical Sciences

Research output: Contribution to journal › Article

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 (=1 mg ml-1), and therefore probably acts as a wetting agent to facilitate evaporative cooling through a waterproofed pelt.

Original language	English
Pages (from-to)	e5726
Journal	PLoS ONE
Volume	4
Issue number	5
DOIs	https://doi.org/10.1371/journal.pone.0005726
Publication status	Published - May 2009

Keywords

latherin
equine physiology

Documents and Links

10.1371/journal.pone.0005726

Publication in Scopus

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McDonald, R. E., Flemming, R. I., Beeley, J. G., Bovell, D. L., Lu, J. R., Zhao, X., Cooper, A., & Kennedy, M. W. (2009). Latherin: a surfactant protein of horse sweat and saliva. PLoS ONE, 4(5), e5726. https://doi.org/10.1371/journal.pone.0005726

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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 (=1 mg ml-1), and therefore probably acts as a wetting agent to facilitate evaporative cooling through a waterproofed pelt.",

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AU - Flemming, Rachel I.

AU - Beeley, John G.

AU - Bovell, Douglas L.

AU - Lu, Jian R.

AU - Zhao, Xiubo

AU - Cooper, Alan

AU - Kennedy, Malcolm W.

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AB - 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 (=1 mg ml-1), and therefore probably acts as a wetting agent to facilitate evaporative cooling through a waterproofed pelt.

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