The effect of recombinant mouse amelogenins on the formation and organization of hydroxyapatite crystals in vitro.
Fluoride enhances intracellular degradation of amelogenins during secretory phase of amelogenesis of hamster teeth in organ culture.
On the other hand, the amelogenin takes a higher supramolecular organization (20 nm nanospheres) and works as a "scaffold" that guides the growth of crystals for the formation of prisms.
The process of amelogenesis is a complex and regulated by ameloblasts that requires secretion of certain matrix proteins that includes amelogenins
, amelins, enamelins and tuftelins and the previously formed dentine.
The matrix proteins are a heterogeneous group which are generally separated into amelogenins (major component) and enamelins.
To date, mutations in gene encoding the protein amelogenin have been shown to cause some X-linked recessive forms of AI.
Amelogenins are the major (90%) matrix proteins for forming enamel (Sasaki & Shimokawa, 1995).
Evidence for regulation of amelogenin gene expression by 1,25-dihydroxyvitamin [D.
The amelogenins are mainly hydrophobic, but they do have anionic C-termini that appear to occur at the surface of the nanospheres and interact there with the calcium hydroxyapatite of enamel.
Self-assembly of a recombinant amelogenin protein generates supramolecular structures.
Evidence for amelogenin "nanospheres" as functional components of secretory-stage enamel matrix.
are smaller ([approximately] 20 kD) and more hydrophobic than the typical oyster shell protein.