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Protein characterization of fluorosed human enamel
J T Wright1, S C Chen, K I Hall
1Department of Pediatric Dentistry, School of Dentistry University of North Carolina at Chapel Hill 27599-7450, USA.
Journal of Dental Research
|December 1, 1996
Summary
Dental fluorosis in humans involves higher fluoride and protein content in enamel, but similar amino acid profiles. Mature, moderately fluorosed enamel does not show significant amelogenin retention.
Area of Science:
- Biochemistry
- Dental Research
- Mineral Metabolism
Background:
- Dental fluorosis is a developmental defect of enamel.
- Its exact mechanisms remain unclear, with hypotheses involving enamel protein processing.
- Understanding enamel protein changes is crucial for elucidating fluorosis development.
Purpose of the Study:
- To characterize the protein composition of fluorosed human enamel.
- To compare protein content, amino acid profiles, and amelogenin presence in fluorotic versus normal enamel.
Main Methods:
- Analysis of fluoride concentration, total protein, and amino acid composition in fluorotic and normal human enamel.
- Gel electrophoresis and Western blot analysis using anti-amelogenin antibodies.
Main Results:
- Fluorotic enamel showed significantly higher fluoride (431 ppm vs. 62 ppm) and protein content (0.27% vs. 0.11%) than normal enamel.
- Amino acid profiles were similar between fluorotic and normal enamel.
- Gel electrophoresis revealed greater diversity of low-molecular-weight proteins in fluorotic enamel; Western blot showed no significant amelogenin retention.
Conclusions:
- Fluorotic enamel has increased protein content but similar amino acid composition compared to normal enamel.
- Significant amelogenin retention is not evident in mature, moderately fluorosed human enamel.
- While altered protein removal might contribute to hypomineralization, most matrix proteins are absent in mature fluorotic enamel.