Research Article
Identification of human whole saliva protein components using proteomics
Article first published online: 6 FEB 2004
DOI: 10.1002/pmic.200300638
Copyright © 2004 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Additional Information
How to Cite
Vitorino, R., Lobo, M. J. C., Ferrer-Correira, A. J., Dubin, J. R., Tomer, K. B., Domingues, P. M. and Amado, F. M. L. (2004), Identification of human whole saliva protein components using proteomics. PROTEOMICS, 4: 1109–1115. doi: 10.1002/pmic.200300638
Publication History
- Issue published online: 23 MAR 2004
- Article first published online: 6 FEB 2004
- Manuscript Received: 3 JUL 2003
- Abstract
- References
- Cited By
Keywords:
- Matrix assisted laser desorption/ionization-time of flight;
- Saliva;
- Two-dimensional gel electrophoresis
Abstract
The determination of salivary biomarkers as a means of monitoring general health and for the early diagnosis of disease is of increasing interest in clinical research. Based on the linkage between salivary proteins and systemic diseases, the aim of this work was the identification of saliva proteins using proteomics. Salivary proteins were separated using two-dimensional (2-D) gel electrophoresis over a pH range between 3–10, digested, and then analyzed by matrix assisted laser desorption/ionization-time of flight (MALDI-TOF)-TOF mass spectrometry (MS) and tandem mass spectrometry (MS/MS). Proteins were identified using automated MS and MS/MS data acquisition. The resulting data were searched against a protein database using an internal Mascot search routine. Ninety spots give identifications with high statistical reliability. Of the identified proteins, 11 were separated and identified in saliva for the first time using proteomics tools. Moreover, three proteins that have not been previously identified in saliva, PLUNC, cystatin A, and cystatin B were identified.

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