Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2011-7-26
pubmed:abstractText
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.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
1470-8752
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
39
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1017-22
pubmed:meshHeading
pubmed:year
2011
pubmed:articleTitle
Latherin and other biocompatible surfactant proteins.
pubmed:affiliation
Institute of Molecular, Cell and Systems Biology, College of Medical, Veterinary and Life Sciences, Graham Kerr Building, University of Glasgow, Glasgow G12 8QQ, UK. malcolm.kennedy@glasgow.ac.uk
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't