Objective: To investigate the immunolocalization of heat shock protein 70 (hsp 70) during reparative formation and to discuss the role of heat shock response in dental pulp injury and repair.
Methods: A single cavity was prepared in the mesial surface of the first molars of both maxilla and mandible in Wistar rat. The animals were sacrificed at 3, 15, and 30 days post-operation. After the histological process, the paraffin sections were reacted with monoclonal antibodies against rat hsp 70 using the strept-avidin-biotin-peroxidase complex method.
Results: Immunolocalization demonstrated heavy staining for hsp 70 in normal pulp and at different stages of dental pulp repair. In normal pulp, immunoreactivity was visualized in the odontoblasts and the pulp fibroblast. In the group sacrificed at 3 days, heavy staining was located in the odontoblast process and cytoplasm. After 15 days, the newly formed odontoblast-like cells were strongly stained. At 30 days, the same staining intensity was observed in odontoblast-like cells and in pulp cells. No staining was seen in reparative dentin.
Conclusion: These results demonstrated that heat shock protein 70 might play an important role as a molecular chaperone during reparative dentin formation.