Structure and function of enamel gene products

Deutsch, D.

doi:10.1002/ar.1092240209

Cited by 102 publications

(63 citation statements)

References 150 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Control experiments using antigen-absorbed antiserum resulted in no specific staining. Although we have no immunochemical data on the specificity of this antiserum against human enamel proteins, previous immunochemical and immunohistochemical studies have demonstrated an extensive cross-reactivity between amelogenins of a variety of mammalian species (HEROLD et al, 1979;ZEICHNER-DAVID et al, 1987;DEUTSCH, 1989). Sequencing studies have shown that there is a high degree of sequence conservation in amelogenins derived from bovine, porcine and human specimens (FUKAE et al, 1980;FINCHAM et al, 1983;TAKAGI et al, 1984).…”

Section: Discussionmentioning

confidence: 89%

“…Although several biochemical and immunochemical reports have dealt with enamel proteins of the human tooth germ (FINCHAM, 1980;ROBINSON et al, 1981;DEUTSCH et al, 1983DEUTSCH et al, , 1984FINCHAM et al, 1983;ZEICHNER-DAVID et al, 1987), no report has discussed the immunocytochemical localization of enamel proteins, except for a brief description by DEUTSCH (1989) at the light microscopic level. In the present study, we investigated the ultrastructural localization of amelogenin-like immunoreactivity in the deciduous tooth germ of the human fetus.…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Immunocytochemical localization of amelogenins in the deciduous tooth germs of the human fetus.

Uchida

Tanabe

Fukae

1989

Archives of Histology and Cytology

View full text Add to dashboard Cite

Section: Discussionmentioning

confidence: 89%

Section: Discussionmentioning

confidence: 99%

Immunocytochemical localization of amelogenins in the deciduous tooth germs of the human fetus.

Uchida

Tanabe

Fukae

1989

Archives of Histology and Cytology

View full text Add to dashboard Cite

“…They performed a phylogenetic analysis based on the literature data including 10 amelogenin sequences (8 mammals, 1 crocodile, and 1 amphibian). Such a question is based on the assumption that the amelogenin proteins certainly play an important role in enamel deposition and maturation (Deutsch 1989;Diekwisch et al 1993). Mathur and Polly (2000) concluded that amelogenin evolution slows as enamel complexity increases, probably because selective constraints on amelogenin increase as enamel complexity increases.…”

Section: Insertion Of Triplet Repeats and Amino Acid Deletionsmentioning

confidence: 99%

Molecular Evolution of Amelogenin in Mammals

2005

View full text Add to dashboard Cite

Abstract. An evolutionary analysis of mammalian amelogenin, the major protein of forming enamel, was conducted by comparison of 26 sequences (including 14 new ones) representative of the main mammalian lineages. Amelogenin shows highly conserved residues in the hydrophilic N-and C-terminal regions. The central hydrophobic region (most of exon 6) is more variable, but it has conserved a high amount of proline and glutamine located in triplets, PXQ, indicating that these residues play an important role. This region evolves more rapidly, and is less constrained, than the other well-conserved regions, which are subjected to strong constraints. The comparison of the substitution rates in relation to the CpG richness confirmed that the highly conserved regions are subjected to strong selective pressures. The amino acids located at important sites and the residues known to lead to amelogenesis imperfecta when substituted were present in all sequences examined. Evolutionary analysis of the variable region of exon 6 points to a particular zone, rich in either amino acid insertion or deletion. We consider this region a hot spot of mutation for the mammalian amelogenin. In this region, numerous triplet repeats (PXQ) have been inserted recently and independently in five lineages, while most of the hydrophobic exon 6 region probably had its origin in several rounds of triplet insertions, early in vertebrate evolution. The putative ancestral DNA sequence of the mammalian amelogenin was calculated using a maximum likelihood approach. The putative ancestral protein was composed of 177 residues. It already contained all important amino acid positions known to date, its hydrophobic variable region was rich in proline and glutamine, and it contained triplet repeats PXQ as in the modern sequences.

show abstract

“…During development of tooth enamel, ameloblast cells within the enamel organ secrete an organic matrix comprising primarily proteins called amelogenins and enamelins (tuft proteins) (Eastoe, 1979;Deutsch, 1989;Limeback, 1991). Amelogenins constitute approximately 90% of the enamel matrix protein and are relatively easy to extract from developing teeth using 4 M guanidine hydrochloride, while the more acidic enamelins are thought to adhere tightly to enamel mineral crystals, which must be dissolved with 0.5 M EDTA in order for the guanidine extraction to be efficient (Termine et al, 1980).…”

Section: Introductionmentioning

confidence: 99%

Regulation of amelogenin gene expression during tooth development

Chen

Piddington

Decker

et al. 1994

Developmental Dynamics

View full text Add to dashboard Cite

The amelogenins are the predominant matrix proteins in developing enamel and are crucial for proper enamel mineralization. Transgenic mice were constructed in order to identify the segment of the amezogenin gene required for specific expression in enamel organ cells. A 3.5 kb fragment of the bovine X-chromosoma1 amelogenin gene that includes a TATA box, the transcription initiation site, and 32 bp of exon 1 was linked to the pgalactosidase gene and injected into fertilized mouse eggs. Newborn transgene positive mice expressed pgalactosidase activity in developing teeth treated with the chromogenic substrate Xgal. Foci of ameloblasts were positive in newborn mice; stain intensity and number of positive ameloblasts increased in 1-day and 2-day postnatal mice. Some of the adjacent stratum intermedium cells also were positive in the later stages. Targeting of the transgene to the enamel organ was specific; the only other cells observed to be positive were macrophages, which have endogenous pgalactosidase activity.

show abstract

Structure and function of enamel gene products

Cited by 102 publications

References 150 publications

Immunocytochemical localization of amelogenins in the deciduous tooth germs of the human fetus.

Immunocytochemical localization of amelogenins in the deciduous tooth germs of the human fetus.

Molecular Evolution of Amelogenin in Mammals

Regulation of amelogenin gene expression during tooth development

Contact Info

Product

Resources

About