A comparative study of two chemical models for creating subsurface caries lesions on aprismatic and prismatic enamel.

PURPOSE: To investigate the mineral density and lesion depth of artificial caries lesions on aprismatic enamel and prismatic enamel created by lactic acid and acetic acid buffers. METHODS: Forty bovine enamel blocks were allocated to: aprismatic enamel (Group A) and prismatic enamel (Group C) in acetic acid buffer for 192 h and aprismatic enamel (Group B) and prismatic enamel (Group D) in lactic acid buffer for 96 h. The mineral loss and lesion depth were measured using micro-computed tomography. RESULTS: A significant difference (P = 0.01) was observed in the mineral loss (%) in the lesions on aprismatic enamel and prismatic enamel treated with lactic acid buffer while no significant difference (P = 0.51) was observed in the mineral loss (%) in the lesions on aprismatic enamel and prismatic enamel treated with acetic acid buffer. No significant difference was noted in the mean lesion depth of lesions on aprismatic enamel and prismatic enamel treated with acetic acid and lactic acid buffers (P > 0.05). CONCLUSION: Aprismatic enamel and prismatic enamel have similar mineral loss in acetic acid while prismatic enamel showed more mineral loss compared to aprismatic enamel in lactic acid.

Coemergence of the Amphipathic Helix on Ameloblastin With Mammalian Prismatic Enamel.

To investigate correlation between the ameloblastin (Ambn) amino acid sequence and the emergence of prismatic enamel, a notable event in the evolution of ectodermal hard tissues, we analyzed Ambn sequences of 53 species for which enamel microstructures have been previously reported. We found that a potential amphipathic helix (AH) within the sequence encoded by Exon 5 of Ambn appeared in species with prismatic enamel, with a few exceptions. We studied this correlation by investigating synthetic peptides from different species. A blue shift in fluorescence spectroscopy suggested that the peptides derived from mammalian Ambn interacted with liposomes. A downward shift at 222 nm in circular dichroism spectroscopy of the peptides in the presence of liposomes suggested that the peptides of mammals with prismatic enamel underwent a transition from disordered to helical structure. The peptides of species without prismatic enamel did not show similar secondary structural changes in the presence of liposomes. Peptides of mammals with prismatic enamel caused liposome leakage and inhibited LS8 and ALC cell spreading regulated by full-length Ambn. RT-PCR showed that AH is involved in Ambn's regulation of cell polarization genes: Vangl2, Vangl1, Prickle1, ROCK1, ROCK2, and Par3. Our comprehensive sequence analysis clearly demonstrates that AH motif is closely related to the emergence of enamel prismatic structure, providing insight into the evolution of complex enamel microstructure. We speculate that the AH motif evolved in mammals to interact with cell membrane, triggering signaling pathways required for specific changes in cell morphology associated with the formation of enamel prismatic structure.