Relationship of phenotype and genotype in X-linked amelogenesis imperfecta

Wright, J. T., Hart, P. S., Aldred, M. J., Seow, K., Crawford, P. J. M., Hong, S. P., Gibson, C. W. and Hart, T. C. (2003) Relationship of phenotype and genotype in X-linked amelogenesis imperfecta. Connective Tissue Research, 44 1: 72-78. doi:10.1080/03008200390152124


Author Wright, J. T.
Hart, P. S.
Aldred, M. J.
Seow, K.
Crawford, P. J. M.
Hong, S. P.
Gibson, C. W.
Hart, T. C.
Title Relationship of phenotype and genotype in X-linked amelogenesis imperfecta
Journal name Connective Tissue Research   Check publisher's open access policy
ISSN 0300-8207
Publication date 2003
Sub-type Article (original research)
DOI 10.1080/03008200390152124
Volume 44
Issue 1
Start page 72
End page 78
Total pages 7
Place of publication Abingdon
Publisher Taylor & Francis Ltd
Language eng
Subject 1103 Clinical Sciences
0903 Biomedical Engineering
Abstract X-linked amelogenesis imperfectas (AI) resulting from mutations in the amelogenin gene (AMELX) are phenotypically and genetically diverse. Amelogenin is the predominant matrix protein in developing enamel and is essential for normal enamel formation. To date, 12 allelic AMELX mutations have been described that purportedly result in markedly different expressed amelogenin protein products. We hypothesize that these AMELX gene mutations result in unique and functionally altered amelogenin proteins that are associated with distinct amelogenesis imperfecta phenotypes. The AMELX mutations and associated phenotypes fall generally into three categories. (1) Mutations (e.g., signal peptide mutations) causing a total of loss of amelogenin protein are associated with a primarily hypoplastic phenotype (though mineralization defects also can occur). (2) Missense mutations affecting the N-terminal region, especially those causing changes in the putative lectin-binding domain and TRAP (tyrosine rich amelogenin protein) region of the amelogenin molecule, result in a predominantly hypomineralization/hypomaturation AI phenotype with enamel that is discolored and has retained amelogenin. (3) Mutations causing loss of the amelogenin C terminus result in a phenotype characterized by hypoplasia. The consistent association of similar hypoplastic or hypomineralization/hypomaturation AI phenotypes with specific AMELX mutations may help identify distinct functional domains of the amelogenin molecule. The phenotype-genotype correlations in this study suggest there are important functional domains of the amelogenin molecule that are critical for the development of normal enamel structure, composition, and thickness.
Keyword Cell Biology
Orthopedics
amelogenin
enamel
hereditary
hypomaturation
hypomineralization
hypoplasia
Enamel-matrix Proteins
Acetyl-d-glucosamine
Nonsense Mutation
Dental Enamel
Gene Amelx
Aih1
Manifestations
Nomenclature
Families
Defects
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collections: Excellence in Research Australia (ERA) - Collection
School of Dentistry Publications
 
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Created: Wed, 17 Oct 2007, 11:58:02 EST