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Published on: July 10, 2014
Tuft protein: protein cross-linking in enamel development.
Colin Robinson1, Jackie Hudson
1Division of Oral Biology, Leeds Dental Institute, University of Leeds, Leeds, UK. C.Robinson@Leeds.ac.uk
European Journal of Oral Sciences
|January 17, 2012
Summary
Tuft protein, found in dental enamel, is chemically cross-linked. This cross-linking explains its insolubility and may protect it during enamel matrix degradation.
Area of Science:
- Biochemistry
- Dental Enamel Research
- Protein Chemistry
Background:
- Tuft protein is a component of dental enamel, located at the enamel-dentine junction and prism peripheries.
- It is known to be a mixture of proteins, including amelin, but its extreme insolubility has hindered biochemical studies.
- The insolubility in various solvents like acids, EDTA, and detergents raises questions about its chemical nature.
Purpose of the Study:
- To investigate the potential chemical cross-linking of tuft protein.
- To determine if cross-linking could explain the observed insolubility of tuft protein.
- To explore the functional implications of tuft protein cross-linking in dental enamel.
Main Methods:
- Utilized antibodies specific to gamma-glutamyl cross-linking peptides.
- Applied these antibodies to analyze tuft protein samples.
- Examined tuft protein from various sources where it is present.
Main Results:
- Antibody testing showed a positive response for the presence of a cross-linking isopeptide in tuft protein.
- This indicates that tuft protein does indeed undergo chemical cross-linking.
- The presence of cross-linking correlates with the material's known insolubility.
Conclusions:
- Chemical cross-linking is a characteristic feature of tuft protein.
- This cross-linking likely accounts for the extreme insolubility of tuft protein in common solvents.
- Cross-linking may serve a protective role, preventing degradation of tuft protein during amelogenesis at the enamel-dentine junction.
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