Protein-mediated Enamel Mineralization

Abstract

Enamel is a hard nanocomposite bioceramic with significant resilience that protects the mammalian tooth from external physical and chemical damages. The remarkable mechanical properties of enamel are associated with its hierarchical structural organization and its thorough connection with underlying dentin. This dynamic mineralizing system offers scientists a wealth of information that allows the study of basic principals of organic matrix-mediated biomineralization and can potentially be utilized in the fields of material science and engineering for development and design of biomimetic materials. This chapter will provide a brief overview of enamel hierarchical structure and properties as well as the process and stages of amelogenesis. Particular emphasis is given to current knowledge of extracellular matrix protein and proteinases, and the structural chemistry of the matrix components and their putative functions. The chapter will conclude by discussing the potential of enamel for regrowth.

Chosen single nucleotide polymorphisms (SNPs) of enamel formation genes and dental caries in a population of Polish children

“…15 Amelogenin constitutes more than 90% of the extracellular matrix protein content and is suggested to control the oriented growth and organization of enamel crystals. 14,16 This protein is expressed from genes on the Y and X chromosomes, however, approx. 90% of all RNA transcripts are from the chromosome X.…”

“…14 Enamelin is involved, in cooperation with amelogenin, in controlling elongated growth and mineral nucleation 14 , whereas tuftelin is proposed to be a potential nucleator of enamel crystallites. 18 It is interesting that currently 2 other enamel matrix proteins were discovered, odontogenic ameloblast-associated (ODAM/APIN) and amelotin.…”

“…14 The extracellular proteins situated between dentin and ameloblasts control the initiation, organization and orientation of crystals in the enamel. 14 Ameloblasts, which are cells producing the enamel, are of epithelial origin and their activity is strictly dependent on the differentiation of odontoblasts, i.e. dentin-making cells of mesenchymal origin.…”

“…15 Ameloblasts secrete also proteinases, such as matrix metalloproteinase-20 and kallikrein-related peptidase-4, which function during different stages of amelogenesis and cause amelogenin and other enamel proteins degradation. 14 The aim of the study was to analyze the genotype and allele frequencies of single nucleotide polymorphisms (SNPs) in AMELX (amelogenin, X isoform), AMBN (ameloblastin), TUFT1 (tuftelin), TFIP11 (tuftelin-interacting protein 11), MMP20 (matrix metalloproteinase-20) and KLK4 (kallikrein-related peptidase-4) genes and to prove their association with dental caries occurrence in a population of Polish children.…”

Expression of Thymosin β4 in Ameloblasts during Mouse Tooth Development

“…Amelogenesis in humans starts at 3 months of pregnancy and the enamel is completely mineralized at postnatal month 6. Ameloblasts differentiate from the inner enamel epithelial cells in the bell stage during tooth development and initiate enamel matrix accumulation on the predentin during the advanced bell stage (Boyde, 1989;Hillson, 1996;Moradian-Oldak, 2012). The morphology and function of ameloblasts undergoes alterations to facilitate various biological functions such as the synthesis and secretion of proteins necessary for enamel matrix formation and the regulation of structure development during amelogenesis (Lacruz et al, 2010).…”