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Potential role of the amelogenin N-terminus in the regulation of calcium phosphate formation in vitro
- Source :
- Cells, tissues, organs. 194(2-4)
- Publication Year :
- 2011
-
Abstract
- N-terminal and C-terminal (CT) domains of amelogenin have been shown to be essential for proper enamel formation. Recent studies have also suggested that although the C-terminus plays an apparent role in protein-mineral interactions, other amelogenin structural domains are involved. The objective was to explore the role of the amelogenin N-terminus in the regulation of calcium phosphate formation in vitro. Spontaneous mineralization studies were carried out using the phosphorylated (+P) and nonphosphorylated (–P) N-terminus of the leucine-rich amelogenin peptide (LRAP) that lacks the hydrophilic CT domain. Mineralization progress was monitored via changes in solution pH. Mineral phases formed were characterized using TEM, selected area electron diffraction, and FT-IR. In controls, amorphous calcium phosphate was initially formed and subsequently transformed to randomly oriented hydroxyapatite (HA) plate-like crystals. In contrast to the control, LRAP(+P)-CT stabilized ACP formation for >1 day, while LRAP(–P)-CT accelerated the transformation of ACP to HA but had little effect on crystal shape or orientation. In conclusion, the N-terminal domain found in LRAP, as in amelogenins, appears to have the capacity to interact with forming calcium phosphate mineral phases. Results suggest that the N-terminal domain of amelogenin may play a direct role in early stages of enamel formation.
- Subjects :
- Calcium Phosphates
Paper
Histology
Time Factors
Molecular Sequence Data
Sus scrofa
chemistry.chemical_element
Peptide
Calcium
Mineralization (biology)
Structure-Activity Relationship
Calcification, Physiologic
stomatognathic system
Dental Enamel Proteins
Spectroscopy, Fourier Transform Infrared
Animals
Amorphous calcium phosphate
Amino Acid Sequence
chemistry.chemical_classification
Enamel paint
Amelogenin
Chemistry
Hydrogen-Ion Concentration
In vitro
Biochemistry
visual_art
visual_art.visual_art_medium
Biophysics
Phosphorylation
Anatomy
Subjects
Details
- ISSN :
- 14226421
- Volume :
- 194
- Issue :
- 2-4
- Database :
- OpenAIRE
- Journal :
- Cells, tissues, organs
- Accession number :
- edsair.doi.dedup.....4169a54e392a2571208b5ec8e8b30383