Spatiotemporal expression of ameloblastin isoforms during murine tooth development.

Ameloblasts synthesize and secrete the enamel matrix proteins (amelogenin, ameloblastin, and enamelin). This investigation examined the profiles of ameloblastin in the ameloblasts and in the enamel matrix during different postnatal (PN) days (days 0-9) of development of mouse molar, using an antibody specific for C-terminal sequence of ameloblastin (Ct; GNKVHQPQVHNAWRF). Ameloblastin is found in three different molecular sizes (37, 55, and 66 kDa) in both ameloblasts and enamel matrix during PN development.

Localization of sulfated sialic acids in the dentinal tubules during tooth formation in mice.

Lectin-like properties of the major enamel protein amelogenin suggest that it binds to glycoconjugates in dentinal tubules released at the dentin-enamel junction (DEJ) during enamel formation. Therefore, a detailed mapping of glycosylation in dentinal tubules during tooth formation was undertaken using histochemistry and lectin-binding assays. The tubular content exhibited sialidase-susceptible gamma-metachromasia with Toluidine Blue (pH 2.

Interaction between the enamel matrix proteins amelogenin and ameloblastin.

Enamel matrix consists of amelogenin and non-amelogenins. Though amelogenin is not involved in nucleation of minerals, the enamel mineralization is impaired when amelogenin or other matrix protein (ameloblastin/enamelin) genes are mutated. We hypothesize that amelogenin may promote enamel mineralization by interacting with the calcium-binding matrix proteins.

Amelogenin interacts with cytokeratin-5 in ameloblasts during enamel growth.

The enamel protein amelogenin binds to GlcNAc (Ravindranath, R. M. H.