Salivary protein profiling in type I diabetes using two-dimensional electrophoresis and mass spectrometry |
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Authors: | Christophe Hirtz François Chevalier Nicolas Sommerer Isabelle Raingeard Jacques Bringer Michel Rossignol Dominique Deville de Périere |
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Institution: | 1. Laboratory of Physiology, UFR d'Odontologie, Université Montpellier 1, Montpellier, France 2. Laboratory of Proteomics, UR 1199, INRA, Montpellier, France 3. Service des Maladies Endocriniennes, H?pital Lapeyronie, Montpellier, France
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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.
Authors have contributed equally to this work. |
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