Identification of novel amelogenin-binding proteins by proteomics analysis

釉原蛋白是釉基质衍生物（Straumann® Emdogain）的主要成分，是一种建议用于促进骨和牙周组织再生的生物活性候选物质。在这项研究中，我们结合亲和层析和蛋白质组学分析，以表征成骨细胞系中的釉原蛋白结合蛋白。在鉴定的釉原蛋白相互作用蛋白中，我们验证了釉原蛋白与Grp 78的生物学相互作用，Grp 78在细胞溶质和膜富集组分中均被鉴定。我们发现釉原蛋白与Grp 78的相互作用促进了SaOS-2细胞的增殖，而与成骨无关，这些发现表明釉原蛋白源性成骨细胞活化的差异效应对于理解釉原蛋白诱导牙周组织再生的细胞和分子基础具有潜在的临床意义。

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.