Specific cleavage of a recombinant murine amelogenin at the carboxy-terminal region by a proteinase fraction isolated from developing bovine tooth enamel

Moradian‐Oldak, Janet; Simmer, James P.; Sarte, Patrick; Zeichner‐David, Margarita; Fincham, Alan G.

doi:10.1016/0003-9969(94)90090-6

Cited by 69 publications

(55 citation statements)

References 38 publications

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“…Proteolytic enzymes cleave the amelogenin protein by first removing the C-terminal sequence, followed, at the N-terminal region, by a cleavage between either aa 43-44 or aa 45-46. This produces two peptides that are referred to as TRAP43 and TRAP45 (terminal tyrosine-rich amelogenin peptides) (Fincham et al 1991;Fincham and Moradian-Oldak 1993;Moradian-Oldak et al 1994b). These steps in the degradation of the amelogenin protein are thought to be important for the enamel structure and for its proper mineralization.…”

Section: High Conservation Of Residues In the Hydrophilic Domainsmentioning

confidence: 99%

“…This explains why these regions are so highly conserved in the 26 mammalian sequences examined. The well-conserved hydrophilic C-terminal region is known to play a crucial role in the aggregative properties of the amelogenin by its contribution to stabilize the nanospheres (Moradian-Oldak et al 1994b;Wen et al 2001;Snead 2003).…”

Section: High Conservation Of Residues In the Hydrophilic Domainsmentioning

confidence: 99%

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Molecular Evolution of Amelogenin in Mammals

2005

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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.

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Section: High Conservation Of Residues In the Hydrophilic Domainsmentioning

confidence: 99%

Section: High Conservation Of Residues In the Hydrophilic Domainsmentioning

confidence: 99%

Molecular Evolution of Amelogenin in Mammals

2005

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“…It was suggested that these component proteins must have specific protein-protein self-interactions and co-interactions to assemble into an organized organic matrix. This matrix is then competent to undergo mineral replacement and to form a highly ordered * This work was supported by Grant P302/10/0427 from the Czech Science three-dimensional structure consisting of long, thin hydroxyapatite crystallites (9,(11)(12)(13). Two proteinases, the matrix metalloproteinase 20 (MMP-20, enamelysin) and kallikrein 4, were described to be secreted into the enamel matrix throughout amelogenesis and appear to be important for processing of extracellular matrix proteins (14,15).…”

Section: Intrinsically Disordered Proteins (Idps)mentioning

confidence: 99%

Intrinsically Disordered Enamel Matrix Protein Ameloblastin Forms Ribbon-like Supramolecular Structures via an N-terminal Segment Encoded by Exon 5

Wald

Osičková

Šulc

et al. 2013

Journal of Biological Chemistry

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Background: Ameloblastin plays a key role in the complex biomineralization process that forms tooth enamel, the hardest tissue of the body. Results: Ameloblastin self-associates into ribbon-like supramolecular structures via a short segment encoded by exon 5. Conclusion: Ameloblastin self-association may be essential for correct structural organization and mineralization of the enamel in vivo. Significance: The results provide molecular insight into biology of tooth enamel formation.

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“…More recently, ameloblastin has joined the group of enamel tissue-specific proteins. Another group of enamel proteins, the enamel proteases, appear to play a role in post-translational modification of amelogenins (Moradian-Oldak et al 1994;DenBesten and Heffernan 1989;Suga 1970). …”

mentioning

confidence: 99%

Immunohistochemical Similarities and Differences between Amelogenin and Tuftelin Gene Products During Tooth Development

Diekwisch¹,

Ware²,

Fincham

et al. 1997

J Histochem Cytochem.

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SUMMARYAmelogenins and tuftelins are highly specialized proteins secreted into the developing enamel matrix during mammalian enamel formation. Both tuftelins and amelogenins have been associated with various functions during nucleation and maturation of the developing enamel matrix. In this study we conducted experiments to investigate whether tuftelins and portions of the amelogenin molecule were deposited and processed in spatially distinguished portions of the developing enamel matrix, using antibodies specific against tuftelin or amelogenins. The amelogenin antibodies were raised against recombinant and native amelogenins and also included an antibody against a polypeptide encoded by amelogenin exon 4. To compare spatial expression patterns of enamel protein epitopes, 3-day postnatal mouse molar tooth organs were processed for paraffin histology and cut into serial sections. Adjacent sections were exposed to antibodies against either tuftelin or various amelogenin epitopes. To investigate age-related changes of enamel protein expression, amelogenin and tuftelin antibodies were applied to tooth organs of developmental stages E19 and 1, 3, 5, 7, 9 and 11 postnatal days. Tuftelin was detected within the odontoblast processes during earlier stages of development (E19 and 1 day postnatal), whereas during later stages (3-11 days) it was recognized in a portion of the enamel layer adjacent to the dentine-enamel junction. In contrast, all four antibodies against amelogenins reacted with parts of the ameloblast cytoplasm and the entire enamel layer. Using immunohistochemistry, we were not able to detect any differences in the spatial distribution of the four amelogenin epitopes investigated. The spatial differences in the distribution of amelogenin and tuftelin as observed in this study may be intepreted as an indication of functional differences between both proteins during early enamel biomineralization.

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Specific cleavage of a recombinant murine amelogenin at the carboxy-terminal region by a proteinase fraction isolated from developing bovine tooth enamel

Cited by 69 publications

References 38 publications

Molecular Evolution of Amelogenin in Mammals

Molecular Evolution of Amelogenin in Mammals

Intrinsically Disordered Enamel Matrix Protein Ameloblastin Forms Ribbon-like Supramolecular Structures via an N-terminal Segment Encoded by Exon 5

Immunohistochemical Similarities and Differences between Amelogenin and Tuftelin Gene Products During Tooth Development

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