Abstract:
: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.
journal_name
Biochem Soc Transjournal_title
Biochemical Society transactionsauthors
Kennedy MWdoi
10.1042/BST0391017subject
Has Abstractpub_date
2011-08-01 00:00:00pages
1017-22issue
4eissn
0300-5127issn
1470-8752pii
BST0391017journal_volume
39pub_type
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