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In vitro albumin binding on apatite crystals from developing enamel
J Menanteau1, M Gregoire, G Daculsi
1Unité de recherche INSERM U225, U.F.R. D'Odontologie, Nantes, France.
Bone and Mineral
|November 1, 1987
Summary
Serum proteins can bind to enamel crystals, contrary to previous assumptions. This finding suggests that the absence of blood proteins in enamel is not due to crystal properties.
Area of Science:
- Biomineralization
- Dental Research
- Materials Science
Background:
- Serum proteins are found in dentin and bone, bound to apatite.
- Enamel's unique organic/crystal structure was thought to prevent protein binding.
- Previous studies lacked direct evidence on enamel crystal protein interactions.
Purpose of the Study:
- To investigate the in vitro ability of enamel crystals to bind serum albumin.
- To determine if enamel crystallites possess free binding sites for serum proteins.
- To re-evaluate the reasons for the absence of blood proteins in mature enamel.
Main Methods:
- Isolation of crystals from developing bovine enamel.
- In vitro binding assays using gold-labelled serum albumin.
- Transmission Electron Microscopy (TEM) to observe crystal structure.
Main Results:
- Bovine developing enamel crystals, despite being coated with enamelins, demonstrated the ability to bind serum albumin.
- The binding of labelled serum albumin indicates the presence of accessible free binding sites on the enamel crystal surface.
- TEM observations of a 'sheath' around crystals may represent a dynamic binding process in vivo.
Conclusions:
- Enamel crystallites possess the capacity to bind serum proteins.
- The lack of serum proteins in enamel is not attributable to inherent properties of the enamel crystallites.
- A dynamic process in vivo may influence protein presence in enamel.