Abstract
This study aims to identify the proteins in hypomineralized second primary molars (HSPMs) and correlate their function in Amelogenesis. HSPM is a qualitative defect of the enamel of the second primary molars with no clear etiology. Total protein quantification was performed using the Bradford Protein Assay, followed by the electrophoretic separation of samples using 2D-Gel electrophoresis to identify the proteins. The results from the Bradford Protein Assay unveiled a five-fold increase in the protein content in HSPM. Proteins such as Dentin sialo-phosphoprotein (DSPP), Keratin, type I, Serum Albumin, Anti-thrombin III, Alpha-1-Antitrypsin, Histone H3.2, Actin, Heat shock Protein, Vimentin, Desmoglein-3, Glyceraldehyde-3-phosphate dehydrogenase, Inosine-5'-monophosphate dehydrogenase 2, Zinc Alpha 2 glycoprotein, Lysozyme C, Prothrombin, Vit-D binding Protein, Apolipoprotein A-1, Defensin 1, Immunoglobulin Gamma, Immunoglobulin Kappa, and Alpha-Amylase were all upregulated (p < 0.05) in HSPM. This investigation conclusively demonstrates that HSPM-affected teeth have higher protein content than healthy teeth. The study also supports the theory of proteolytic inhibition attributed to reduced protease activity and heightened protease inhibitor activity.
Published Version
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