Open Access

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

  • Christophe Hirtz1, 2Email author,
  • François Chevalier1, 2,
  • Nicolas Sommerer2,
  • Isabelle Raingeard3,
  • Jacques Bringer3,
  • Michel Rossignol2 and
  • Dominique Deville de Périere1
Clinical Proteomics2:201117

DOI: 10.1385/CP:2:1:117

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 α-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 non-immunological defense of oral cavity. As only particular isoforms of proteins were modulated, type 1 diabetes seemed to differentially affect posttranslational modification.

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