Human enamel phenotype associated with amelogenesis imperfecta and a kallikrein-4 (g.2142G>A) proteinase mutation

Kallikrein‐4 is known to be highly expressed during the maturation stage of enamel formation and is thought to be critical for the final phase of crystallite growth. The purpose of this study was to evaluate the enamel phenotype in humans with a known KLK‐4 mutation (g.2142G>A). Primary teeth fro...

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Bibliographic Details
Published in:European journal of oral sciences 2006-05, Vol.114 (s1), p.13-17
Main Authors: Wright, J. Tim, Daly, Bill, Simmons, Darrin, Hong, Sung, Hart, Suzanne P., Hart, Tom C., Atsawasuwan, Phimon, Yamauchi, Mitsuo
Format: Article
Language:English
Subjects:
Adenine
amelogenesis imperfecta
Amelogenesis Imperfecta - genetics
Amelogenesis Imperfecta - pathology
crystallite
Crystallization
Crystallography
Dental Enamel - chemistry
Dental Enamel - ultrastructure
Dental Enamel Proteins - analysis
Dental Enamel Proteins - genetics
Dentistry
enamel
Guanine
Humans
hypomaturation
Kallikreins - analysis
Kallikreins - genetics
KLK-4
Microscopy, Electron
Mutation - genetics
Phenotype
Porosity
Sequence Analysis, Protein
Tooth, Deciduous - ultrastructure
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Summary:Kallikrein‐4 is known to be highly expressed during the maturation stage of enamel formation and is thought to be critical for the final phase of crystallite growth. The purpose of this study was to evaluate the enamel phenotype in humans with a known KLK‐4 mutation (g.2142G>A). Primary teeth from two individuals with a known KLK‐4 mutation were evaluated using amino acid analysis and light and electron microscopy. Light microscopy showed the enamel was of normal thickness but opaque throughout its width compared with normal enamel. Electron microscopy showed enamel affected by the KLK‐4 mutation had a normal prismatic structure and generally had a well‐organized and discernable crystallite composition. In some areas, globular structures were present where crystallites were not discernable or appeared to have an altered morphology. The KLK‐4 mutant enamel had an increased protein content compared with normal enamel. Human enamel formed with a lack of functioning KLK‐4 proteinase is altered primarily in the completeness of crystallite growth, while enamel thickness and prism structure remains essentially normal. Collectively, these studies suggest that the KLK‐4 proteinase is essential for the final crystallite growth of enamel but is not critical for crystallite orientation, prism formation or enamel thickness.
ISSN:0909-8836
1600-0722
DOI:10.1111/j.1600-0722.2006.00291.x