Ultrastructure Analysis of Primary and Permanent teeth with Generalized Amelogenesis imperfecta; In-vitro study
| Autor: | Ghada Mohammed Said Hamed, Walid El-Sayed |
|---|---|
| Rok vydání: | 2020 |
| Předmět: |
0301 basic medicine
Enamel paint Chemistry 030206 dentistry Amelogenesis medicine.disease Enamel rod stomatognathic diseases 03 medical and health sciences 030104 developmental biology 0302 clinical medicine medicine.anatomical_structure stomatognathic system visual_art Biophysics visual_art.visual_art_medium medicine Deciduous teeth Amelogenesis imperfecta Amelogenin Ameloblast Permanent teeth |
| Zdroj: | Egyptian Dental Journal. 66:1041-1048 |
| ISSN: | 2090-2360 |
| DOI: | 10.21608/edj.2020.24006.1016 |
| Popis: | Amelogenesis or enamel formation is a biomineralization process in which specialized epithelial derived cells, ameloblasts, secrete extracellular matrix which later will be mineralized. amelogenesis can be divided into two main stages: the secretory stage and the maturation stage. Objectives: This work aims to investigate the ultrastructure phenotype of permanent and deciduous teeth with generalized enamel defects. Material and Methods; Teeth whether deciduous or permanent (exfoliated or extracted for clinical reasons), were collected from affected individuals. Scanning Electron Microscopy Energy Dispersive X-Ray Spectroscopy techniques were applied. Enzyme digestions was done by using either α- chymotrypsin (Sigma-UK) or lipase (Sigma-UK). Results: Examination of sections of affected teeth using Scanning Electron Microscopy showed abnormal enamel rods that were covered by amorphous material. This pattern was consistent of both primary and secondary dentitions. Energy Dispersive X-Ray Spectroscopy showed increase carbon contents. α- chymotrypsin enzyme was the only enzyme capable for removing this amorphous material. Conclusion: Ultrastructure analysis of the affected teeth showed typical form of hypomaturation amelogenins imperfecta. The study also proved that this amorphous material is mainly proteinases in nature. |
| Databáze: | OpenAIRE |
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