Identification of novel amelogenin-binding proteins by proteomics analysis

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Amelogenin, the major component of enamel matrix derivative (Straumann® Emdogain), is a suggested bioactive candidate for promoting the regeneration of bone and periodontal tissues. In this study, we combined affinity chromatography and proteomic analysis to characterize amelogenin-binding proteins in an osteoblast cell line. Among the identified amelogenin-interacting proteins, we validated the biological interaction of amelogenin with Grp78, which was identified in both cytosolic and membrane-enriched fractions. We demonstrated that the interaction of amelogenin with Grp78 contributed to cell proliferation, rather than correlate with the osteogenesis in SaOS-2 cells.These findings suggest that the differential effects of amelogenin-derived osteoblast activation could be of potential clinical significance for understanding the cellular and molecular bases of amelogenin-induced periodontal tissue regeneration.