Horses and other equids are unusual in producing protein-rich sweat for thermoregulation, a major component of which is latherin, a highly surface-active, non-glycosylated protein that is a member of the PLUNC (palate, lung and nasal epithelium clone) family. Latherin produces a significant reduction in water surface tension at low concentrations (≤1 mg/ml), and probably acts as a wetting agent to facilitate evaporative cooling through a thick, waterproofed pelt. Latherin binds temporarily to hydrophobic surfaces, and so may also have a disruptive effect on microbial biofilms. It may consequently have a dual role in horse sweat in both evaporative cooling and controlling microbial growth in the pelt that would otherwise be resourced by nutrients in sweat. Latherin is also present at high levels in horse saliva, where its role could be to improve mastication of the fibrous diet of equids, and also to reduce microbial adherence to teeth and oral surfaces. Neutron reflection experiments indicate that latherin adsorbs to the air/water interface, and that the protein undergoes significant conformational change and/or partial unfolding during incorporation into the interfacial layer.
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Conference Article|
July 20 2011
Latherin and other biocompatible surfactant proteins Available to Purchase
Malcolm W. Kennedy
Malcolm W. Kennedy
1
1Institute of Molecular, Cell and Systems Biology, College of Medical, Veterinary and Life Sciences, Graham Kerr Building, University of Glasgow, Glasgow G12 8QQ, U.K.
1email [email protected]
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Publisher: Portland Press Ltd
Received:
February 14 2011
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© The Authors Journal compilation © 2011 Biochemical Society
2011
Biochem Soc Trans (2011) 39 (4): 1017–1022.
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Received:
February 14 2011
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Malcolm W. Kennedy; Latherin and other biocompatible surfactant proteins. Biochem Soc Trans 1 August 2011; 39 (4): 1017–1022. doi: https://doi.org/10.1042/BST0391017
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