Ameloblastin upstream region contains structural elements regulating transcriptional activity in a stromal cell line derived from bone marrow

Tamburstuen, Margareth V.; Snead, Malcolm L.; Reseland, Janne Elin; Paine, Michael L.; Lyngstadaas, Ståle Petter

doi:10.1111/j.1600-0722.2011.00910.x

Cited by 6 publications

(9 citation statements)

References 32 publications

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“…However, to our knowledge there are no studies of the cis-regulatory elements in the EMP genes demonstrating their role in controling EMP gene expression during amelogenesis. Cis-regulatory elements were identified for AMEL [ 48 ], AMBN [ 49 , 50 ], AMTN [ 51 ] and ENAM [ 52 , 53 ] as well as some transcription factors e.g. Cbfa1 for AMBN [ 54 ].…”

Section: Discussionmentioning

confidence: 99%

Comparative expression of the four enamel matrix protein genes, amelogenin, ameloblastin, enamelin and amelotin during amelogenesis in the lizard Anolis carolinensis

Gasse

Sire²

2015

EvoDevo

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BackgroundIn a recent study, we have demonstrated that amelotin (AMTN) gene structure and its expression during amelogenesis have changed during tetrapod evolution. Indeed, this gene is expressed throughout enamel matrix deposition and maturation in non-mammalian tetrapods, while in mammals its expression is restricted to the transition and maturation stages of amelogenesis. Previous studies of amelogenin (AMEL) gene expression in a lizard and a salamander have shown similar expression pattern to that in mammals, but to our knowledge there are no data regarding ameloblastin (AMBN) and enamelin (ENAM) expression in non-mammalian tetrapods. The present study aims to look at, and compare, the structure and expression of four enamel matrix protein genes, AMEL, AMBN, ENAM and AMTN during amelogenesis in the lizard Anolis carolinensis.ResultsWe provide the full-length cDNA sequence of A. carolinensisAMEL and AMBN, and show for the first time the expression of ENAM and AMBN in a non-mammalian species. During amelogenesis in A. carolinensis, AMEL, AMBN and ENAM expression in ameloblasts is similar to that described in mammals. It is noteworthy that AMEL and AMBN expression is also found in odontoblasts.ConclusionsOur findings indicate that AMTN is the only enamel matrix protein gene that is differentially expressed in ameloblasts between mammals and sauropsids. Changes in AMTN structure and expression could be the key to explain the structural differences between mammalian and reptilian enamel, i.e. prismatic versus non-prismatic.

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Section: Discussionmentioning

confidence: 99%

Comparative expression of the four enamel matrix protein genes, amelogenin, ameloblastin, enamelin and amelotin during amelogenesis in the lizard Anolis carolinensis

Gasse

Sire²

2015

EvoDevo

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“…The transcription start site (TSS) and the promoter region of AMBN were analyzed in the mouse [ 32 ]. This region contains cis-acting elements that function both to enhance and suppress transcription, some of them regulating transcription activity in mesenchymal cells in vitro [ 33 ]. Cbfa1 , the essential transcription factor for osteoblast differentiation, was shown to play an important role in AMBN transcription [ 34 ].…”

Section: Introductionmentioning

confidence: 99%

Evolutionary analysis of selective constraints identifies ameloblastin (AMBN) as a potential candidate for amelogenesis imperfecta

2015

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BackgroundAmeloblastin (AMBN) is a phosphorylated, proline/glutamine-rich protein secreted during enamel formation. Previous studies have revealed that this enamel matrix protein was present early in vertebrate evolution and certainly plays important roles during enamel formation although its precise functions remain unclear. We performed evolutionary analyses of AMBN in order to (i) identify residues and motifs important for the protein function, (ii) predict mutations responsible for genetic diseases, and (iii) understand its molecular evolution in mammals.ResultsIn silico searches retrieved 56 complete sequences in public databases that were aligned and analyzed computationally. We showed that AMBN is globally evolving under moderate purifying selection in mammals and contains a strong phylogenetic signal. In addition, our analyses revealed codons evolving under significant positive selection. Evidence for positive selection acting on AMBN was observed in catarrhine primates and the aye-aye. We also found that (i) an additional translation initiation site was recruited in the ancestral placental AMBN, (ii) a short exon was duplicated several times in various species including catarrhine primates, and (iii) several polyadenylation sites are present.ConclusionsAMBN possesses many positions, which have been subjected to strong selective pressure for 200 million years. These positions correspond to several cleavage sites and hydroxylated, O-glycosylated, and phosphorylated residues. We predict that these conserved positions would be potentially responsible for enamel disorder if substituted. Some motifs that were previously identified as potentially important functionally were confirmed, and we found two, highly conserved, new motifs, the function of which should be tested in the near future. This study illustrates the power of evolutionary analyses for characterizing the functional constraints acting on proteins with yet uncharacterized structure.Electronic supplementary materialThe online version of this article (doi:10.1186/s12862-015-0431-0) contains supplementary material, which is available to authorized users.

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“…Fam50a might also stimulate Ambn transcription by directly interacting with Runx2. of Ambn gene (Dhamija & Krebsbach, 2001;Tamburstuen et al, 2011).…”

Section: Immunofluorescence Microscopy Analysis Provided Evidence Thatmentioning

confidence: 99%

“…For example, Ambn gene contains two Runx2‐binding sites. Its transcription is regulated by its interaction with transcription factor Runx2 and Ambn promoter (Camilleri & McDonald, ; Dhamija & Krebsbach, ; Tamburstuen, Snead, Reseland, Paine, & Lyngstadaas, ). Transcription of Amelx gene is also controlled by several transcriptional regulators such as DLXs, MSX2, and C/EBPα (Zhou & Snead, ).…”

Section: Introductionmentioning

confidence: 99%

The Fam50a positively regulates ameloblast differentiation via interacting with Runx2

Kim

Hur

Jeong

et al. 2017

Journal Cellular Physiology

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Differentiated ameloblasts secret enamel matrix proteins such as amelogenin, ameloblastin, and enamelin. Expression levels of these proteins are regulated by various factors. To find a new regulatory factor for ameloblast differentiation, we performed 2D-PAGE analysis using mouse ameloblast lineage cell line (mALCs) cultured with mineralizing medium. Of identified proteins, family with sequence similarity 50 member A (Fam50a) was significantly increased during differentiation of mALCs. Fam50a protein was also highly expressed in secretory ameloblasts of mouse tooth germs. In mALCs cultures, forced expression of Fam50a up-regulated the expression of enamel matrix protein genes such as amelogenin, ameloblastin, and enamelin. In addition, up-regulation of Fam50a also increased ALP activity and mineralized nodule formation in a dose-dependent manner. In contrast, knockdown of Fam50a decreased expression levels of enamel matrix protein genes, ALP activity, and mineralized nodule formation. By fluorescence microscopy, endogenous Fam50a protein was found to be localized to the nucleus of ameloblasts. In addition, Fam50a synergistically increased Ambn transactivation by Runx2. Moreover, Fam50a increased binding affinity of Runx2 to Ambn promoter by physically interacting with Runx2. Taken together, these results suggest Fam50a might be a new positive regulator of ameloblast differentiation.

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Ameloblastin upstream region contains structural elements regulating transcriptional activity in a stromal cell line derived from bone marrow

Cited by 6 publications

References 32 publications

Comparative expression of the four enamel matrix protein genes, amelogenin, ameloblastin, enamelin and amelotin during amelogenesis in the lizard Anolis carolinensis

Comparative expression of the four enamel matrix protein genes, amelogenin, ameloblastin, enamelin and amelotin during amelogenesis in the lizard Anolis carolinensis

Evolutionary analysis of selective constraints identifies ameloblastin (AMBN) as a potential candidate for amelogenesis imperfecta

The Fam50a positively regulates ameloblast differentiation via interacting with Runx2

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