About this Abstract |
| Meeting |
2024 TMS Annual Meeting & Exhibition
|
| Symposium
|
Bio-Nano Interfaces and Engineering Applications
|
| Presentation Title |
Enamel Formation: Bioinspired Interfacial Design |
| Author(s) |
Malcolm L. Snead |
| On-Site Speaker (Planned) |
Malcolm L. Snead |
| Abstract Scope |
Enamel composed by thousands of hydroxyapatite crystallites aligned in parallel within boundaries fabricated by a single ameloblast cell. This hardest tissue in the vertebrate body starts development as a self-organizing assembly of matrix proteins that control cell to interface interactions, as well as crystallite habit. Here, we examine ameloblastin, a protein that is initially distributed uniformly across the cell boundary interface which redistributes to the lateral margins of the extracellular matrix following secretion thus producing cell-defined boundaries within the matrix and the mineral phase. The yeast two-hybrid assay identified proteasome subunit alpha type 3 (Psma3) interaction with ameloblastin. Confocal microscopy confirmed Psma3 co-distribution with ameloblastin at the ameloblast-extracellular interface. Co-immunoprecipitation assays identified interactions with each reciprocal protein partner. Protein engineering demonstrated preferential ameloblastin interaction with Psma3. These findings suggest a novel pathway participating in control of protein distribution within the extracellular space which serves to regulate the protein-mineral interactions. |
| Proceedings Inclusion? |
Planned: |