Salivary protein changes in response to acute stress in medical residents performing advanced clinical simulations: a pilot proteomics study

Abstract

Context: Quantitative changes of salivary proteins due to acute stress were detected.

Objective: To explore protein markers of stress in saliva of eight medical residents who performed emergency medicine simulations.

Materials and methods: Saliva was collected before the simulations, after the simulations, and following morning upon waking. Proteins were separated by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE), identified by mass spectrometry (MS), and relatively quantified by densitometry.

Results: Salivary alpha-amylase and S–type cystatins significantly increased, while the ∼26 kDa and low-molecular weight (MW) (<10 kDa) SDS-PAGE bands exhibited changes after stress.

Discussion and conclusion: Alpha-amylase and cystatins are potential salivary markers of acute stress, but further validation should be performed using larger sample populations.

Keywords:

• Saliva
• stress
• mass spectrometry
• gel electrophoresis
• amylase
• cystatins

Acknowledgements

The emergency medicine simulations were performed in the Interprofessional Immersive Simulation Center at the University of Toledo College of Medicine. Authors would like to thank Dr. Brent D. Cameron for providing samples of synthetic histatin-3 protein. Also thanked to Dr. White’s and Dr. Liu’s graduate statistics consulting class (MATH 6610, Statistical Consulting) for discussion of statistical data.

Disclosure statement

The authors report no conflicts of interest.

Additional information

Funding

This work was supported by Air Force Office of Scientific Research Award # 13RSL135, NIH/NIDCR grant DE023418, and partial matching funds from the University of Toledo. The MALDI-MS instrument was acquired using funding from NSF-MRI grant 0923184. The ESI-Orbitrap Fusion Tribrid mass spectrometer and nanoHPLC were acquired using funding from the Air Force Office of Scientific Research DURIP 14RT0605 grant.