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Abstract
The mottled enamel variant of amelogenesis imperfecta (MI-M) is characterized by pink to white, opaque, and irregular enamel. The enamel and dentin abnormalities in MI-M are the result of an abnormal synthesis of matrix proteins, such as amelogenins. We used redox proteomics to profile the enamel proteins of teeth with the MI-M variant compared to a control enamel and to the enamel proteins of teeth with hypoplastic enamel defects, including dentinogenesis imperfecta type II, non-hypoplastic MI-M, and Möbius syndrome. We discovered that a sample of amelogenin 1 was significantly lower in the enamel of the teeth with the MI-M variant compared to the controls.
Figures (5)
We also evaluated the proteomic profiles of dental tissues from patients with amelogenesis imperfecta (AI) and identified the differential expression of 11 proteins. Amelogenin 1 was the most elevated protein and confirmed as a marker for the affected enamel.
We are currently working with the development of redox proteomics that will allow us to link the oxidation and reduction of cysteine residues with specific functional consequences such as protein activity, localization, and posttranslational modification.
Our results indicate that cysteine residues, which are vulnerable to oxidation, are differentially expressed in teeth affected with amelogenesis imperfecta. Amelogenin 1, the major enamel matrix protein of teeth, was significantly more abundant in the enamel of teeth affected with MI-M compared to controls, suggesting that the redox proteomics approach we have developed and implemented can allow the identification of enamel proteins and protein functions related to enamel pathologies.
We validated the discovery proteomics results by qPCR for amelogenin 1, osteopontin, enamelin, and two of the groups of proteins identified (nucleophosmin and serotransferrin), and identified that the abundance of these proteins (nucleophosmin and osteopontin) was significantly lower in the enamel of the MI-M variant compared to controls. We confirmed that cysteine residues in amelogenin 1
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