Abstract: Enamel is the outermost covering of vertebrate teeth and the hardest tissue in the vertebrate body. During tooth development, ectoderm-derived ameloblast cells create enamel by synthesizing a complex protein mixture into the extracellular space where the proteins self-assemble to form a matrix that patterns the woven hydroxyapatite (Wang et al., 2007; Zhu et al., 2006). During enamel biomineralization, the assembly of the protein matrix precedes mineral replacement. The predominant protein of mammalian enamel is amelogenin, which is secreted from ameloblasts. It is a hydrophobic protein that self-assembles to form nanospheres that in turn influence the crystal type, organization, and packing of the crystallites (Du et al., 2005). In contrast to the mesenchyme-controlled biomineralization of bone, which uses collagen and remodels both the organic and the inorganic phases over a lifetime, enamel contains no collagen and does not remodel. The mature enamel composite contains hardly any protein (Smith et al., 1998) and is a tough, crack-tolerant, and abrasion-resistant tissue (White et al., 2001).
Publication Year: 2014
Publication Date: 2014-07-24
Language: en
Type: book-chapter
Indexed In: ['crossref']
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Cited By Count: 1
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