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  • Human saliva proteome analysis and its potential applications

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Human whole saliva is consisted mainly of secretions derived from three major salivary glands. The protein components are proline-rich proteins, amylase, statherin, histatins, etc. However, detailed understanding of the protein composition of whole saliva is still limited because of the lack of knowledge about the proteins in order of their contributions to whole saliva, such as secretions from minor salivary glands and gingival crevicular fluid. In addition, little is known about modifications that occur in proteins during or after secretion into the oral cavity. Interest in the characterization of the whole salivary proteins has increased during the last decade. This article will review the recent advances in human saliva proteome analysis. Currently, proteomic techniques are state of the art for the analysis of biologic materials, and saliva is no exception. 2D electrophoresis and tryptic digest analysis by mass spectrometry are the typical methodology, but new approaches using CITP/CZE ESI-MS/MS methods have already been introduced for saliva analysis. 1479 proteins have been identified as human saliva proteome, producing the largest catalogue from a single saliva sample. Understanding the proteome of whole saliva in an environment of continuous turnover will be a prerequisite to gain insight into the physiological and pathological processes to oral health, and be crucial for the identification of meaningful biomarkers for oral disease. Human saliva is an attractive body fluid for disease diagnosis and prognosis because saliva testing is simple, safe, low-cost and noninvasive. Comprehensive analysis and identification of the proteomic content in human whole saliva will not only contribute to the understanding of oral health and disease pathogenesis, but also form a foundation for the discovery of saliva protein biomarkers for human disease detection.

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