Comparative Proteomics of Mouse Tears and Saliva: Evidence from Large Protein Families for Functional Adaptation
We produced a tear proteome of the genome mouse, C57BL/6, that contained 139 different protein identifications: 110 from a two-dimensional (2D) gel with subsequent trypsin digestion, 19 from a one-dimensional (1D) gel with subsequent trypsin digestion and ten from a 1D gel with subsequent Asp-N digestion. We compared this tear proteome with a C57BL/6 mouse saliva proteome produced previously. Sixteen of the 139 tear proteins are shared between the two proteomes, including six proteins that combat microbial growth. Among the 123 other tear proteins, were members of four large protein families that have no counterparts in humans: Androgen-binding proteins (ABPs) with different members expressed in the two proteomes, Exocrine secreted peptides (ESPs) expressed exclusively in the tear proteome, major urinary proteins (MUPs) expressed in one or both proteomes and the mouse-specific Kallikreins (subfamily b KLKs) expressed exclusively in the saliva proteome. All four families have members with suggested roles in mouse communication, which may influence some aspect of reproductive behavior. We discuss this in the context of functional adaptation involving tear and saliva proteins in the secretions of mouse lacrimal and salivary glands, respectively.
Originally published by MDPI under a Creative Commons Attribution License in Proteomes, 2015, Volume 3.
Karn, Robert C. and Laukaitis, Christina M., "Comparative Proteomics of Mouse Tears and Saliva: Evidence from Large Protein Families for Functional Adaptation" Proteomes / (2015): 283-297.
Available at https://digitalcommons.butler.edu/facsch_papers/734