Salivary protein profiling in type 1 diabetes using two-dimensional electrophoresis and mass spectrometry

Abstract

Owing to its noninvasive collection, saliva is considered as a potent diagnostic fluid. The goal of this study was to investigate the modification of the salivary proteome occurring in type 1 diabetes to highlight potential biomarkers of the pathology. High-resolution two-dimensional gel electrophoresis and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry were combined to perform a largescale analysis. The proteomic comparison of saliva samples from healthy subjects and poorly controlled type 1 diabetes patients revealed a modulation of 23 proteins. Fourteen isoforms of ?-amylase, one prolactin inducible protein, three isoforms of salivary acidic protein-1, and three isoforms of salivary cystatins SA-1 were detected as under expressed, whereas two isoforms of serotransferrin were over expressed in the pathological condition. The proteins under expressed were all known to be implicated in the oral anti-inflammatory process, suggesting that the pathology induced a decrease of nonimmunological defense of oral cavity. As only particular isoforms of proteins were modulated, type 1 diabetes seemed to differentially affect posttranslational modification. Copyright © 2006 Humana Press Inc.