Towards further defining the proteome of mouse saliva

Anne A Blanchard; Peyman Ezzati; Dmitry Shamshurin; Andreea C Nistor; Etienne Leygue; John A Wilkins; Yvonne Myal

doi:10.1186/s12953-015-0068-3

Towards further defining the proteome of mouse saliva

Proteome Sci. 2015 Feb 25:13:10. doi: 10.1186/s12953-015-0068-3. eCollection 2015.

Authors

Anne A Blanchard¹, Peyman Ezzati², Dmitry Shamshurin², Andreea C Nistor³, Etienne Leygue⁴, John A Wilkins², Yvonne Myal¹

Affiliations

¹ Department of Pathology, Faculty of Health Sciences, University of Manitoba, 770 Bannatyne Avenue, Winnipeg, Manitoba Canada ; Department of Physiology and Pathophysiology, Faculty of Health Sciences, University of Manitoba, Winnipeg, Canada.
² Department of Internal Medicine, Faculty of Health Sciences, University of Manitoba, Winnipeg, Canada.
³ Department of Pathology, Faculty of Health Sciences, University of Manitoba, 770 Bannatyne Avenue, Winnipeg, Manitoba Canada.
⁴ Department of Biochemistry and Medical Genetics, Faculty of Health Sciences, University of Manitoba, Winnipeg, Canada.

Abstract

Background: Knowledge of the mouse salivary proteome is not well documented and as a result, very limited. Currently, several salivary proteins remain unidentified and for some others, their function yet to be determined. The goal of the present study is to utilize mass spectrometry analysis to widen our knowledge of mouse salivary proteins, and through extensive database searches, provide further insight into the array of proteins that can be found in saliva. A comprehensive mouse salivary proteome will also facilitate the development of mouse models to study specific biomarkers of many human diseases.

Results: Individual saliva samples were collected from male and female mice, and later pooled according to sex. Two pools of saliva from female mice (2 samples/pool) and 2 pools of saliva from male mice were used for analysis utilizing high performance liquid chromatograph mass spectrometry (nano-RPLC-MS/MS). The resulting datasets identified 345 proteins: 174 proteins were represented in saliva obtained from both sexes, as well as 82 others that were more female specific and 89 that were more male specific. Of these sex linked proteins, twelve were identified as exclusively sex-limited; 10 unique to males and 2 unique to females. Functional analysis of the 345 proteins identified 128 proteins with catalytic activity characteristics; indicative of proteins involved in digestion, and 35 proteins associated with stress response, host defense, and wound healing functions. Submission of the list of 345 proteins to the BioMart data mining tool in the Ensembl database further allowed us to identify a total of 283 orthologous human genes, of which, 131 proteins were recently reported to be present in the human salivary proteome.

Conclusions: The present study is the most comprehensive list to date of the proteins that constitute the mouse salivary proteome. The data presented can serve as a useful resource for identifying potentially useful biomarkers of human health and disease.

Keywords: Biomarkers; Kallikreins; Mass spectrometry; Mouse salivary proteome; Mouse/Human saliva.