Tuftelin: enamel mineralization and amelogenesis imperfecta.
Ciba Found Symp
; 205: 135-47; discussion 147-155, 1997.
Article
em En
| MEDLINE
| ID: mdl-9189622
ABSTRACT
Tuftelin is a novel acidic enamel protein thought to play a major role in enamel mineralization. Its identity and localization has been confirmed by amino acid composition, enzyme-linked immunosorbant assay, Western blots, indirect immunohistochemistry and high resolution protein-A gold immunocytochemistry. The deduced tuftelin protein (pI 5.2) contains 389 amino acids and has a calculated peptide molecular mass of 43,814 Da. Immunological studies suggest conservation of tuftelin structure between species throughout vertebrate evolution. The cDNA sequence encodes for several putative post-translation sites including one N-glycosylation consensus site, seven O-glycosylation sites and seven phosphorylation sites, as well as an EF-hand calcium-binding domain (with mismatch), localized towards the N-terminal region. At the C-terminal region (residues 252-345) tuftelin contains structurally relevant determinants for self assembly. We recently cloned and partially sequenced the human tuftelin gene (four exons have now been sequenced). These sequences include exon 1 and over 1000 bases of the putative promoter region. Employing fluorescent in situ hybridization, we mapped the human tuftelin gene to chromosome 1q 21-31. Localization of the human tuftelin gene to a well-defined cytogenetic region may be important in understanding the aetiology of autosomally inherited amelogenesis imperfecta, the most common enamel hereditary disease.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Calcificação de Dente
/
Cromossomos Humanos Par 1
/
Proteínas do Esmalte Dentário
/
Amelogênese Imperfeita
Limite:
Animals
/
Humans
Idioma:
En
Revista:
Ciba Found Symp
Ano de publicação:
1997
Tipo de documento:
Article
País de afiliação:
Israel