Abstract
A melogenesis imperfecta (AI) is a group of inherited defects of dental enamel formation that show both clinical and genetic heterogeneity. Enamel findings in AI are highly variable, ranging from deficient enamel formation to defects in the mineral and protein content. Enamel formation requires the expression of multiple genes that transcribes matrix proteins and proteinases needed to control the complex process of crystal growth and mineralization. The AI phenotypes depend on the specific gene involved, the location and type of mutation, and the corresponding putative change at the protein level. Different inheritance patterns such as X-linked, autosomal dominant and autosomal recessive types have been reported. Mutations in the amelogenin, enamelin, and kallikrein-4 genes have been demonstrated to result in different types of AI and a number of other genes critical to enamel formation have been identified and proposed as candidates for AI. The aim of this article was to present an evaluation of the literature regarding role of proteins and proteinases important to enamel formation and mutation associated with AI.
Highlights
Dental enamel, the most highly mineralized structure in the human body, is formed within a unique, extracellular matrix derived through the synthesis and secretion of proteins by the ameloblast cells
The arrangement of ions in dental enamel crystals closely approximates that of THE GENETICS OF AMELOGENESIS IMPERFECTA
It is not difficult to understand that changes in enzymatic protein degradation by the genetic defects of proteins or proteinases can result in the pathological changes during the enamel formation[39]
Summary
The most highly mineralized structure in the human body, is formed within a unique, extracellular matrix derived through the synthesis and secretion of proteins by the ameloblast cells. Dental enamel formation is divided into secretory, transition, and maturation stages[56]. Mineral is deposited exclusively on the sides of the crystallites, which grow in width and thickness to coalesce with adjacent crystals. The main structural proteins in forming enamel are amelogenin, ameloblastin, and enamelin. These proteins are proteolytically cleaved following their secretion. During the transition stage there is an increase in proteolytic activity, and in maturation stage the accumulated enamel proteins nearly disappear from the matrix. It is not difficult to understand that changes in enzymatic protein degradation by the genetic defects of proteins or proteinases can result in the pathological changes during the enamel formation[39]
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