The Murine Amelogenin Promoter: Developmentally Regulated Expression in Transgenic Animals

Snead, Malcolm L.; Paine, Michael L.; Chen, Liansong; Luo, Benton Yoshida Wen; Zhou, Dan; Lei, Yaping; Liu, Yi‐Hsin; Maxson, Robert E.

doi:10.3109/03008209609029173

Cited by 42 publications

(50 citation statements)

References 14 publications

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“…3). Similar expression patterns have been seen in all transgenic animal lines that involve the amelogenin promoter, which is regulated in a tissue-specific manner (22,26,32). Using an antibody to amelogenin protein (26), no gross quantitative or qualitative changes to the expression pattern for the endogenous amelogenin gene were observed (data not shown).…”

Section: Resultssupporting

confidence: 66%

“…Concentration and reaction conditions used for these antibodies were as recommended by the manufacturer. Essentially, identical data were obtained from animals bearing each of the transgenes, and this tissue-specific expression pattern has been reported previously for a number of transgenic animal lines (22,26,32). Tissue sections were counterstained with hematoxylin prior to photographing.…”

Section: Methodsmentioning

confidence: 54%

“…The reasons for the use of the amelogenin promoter (22), the inclusion of an intron, the use of the Dspp signal peptide (4), the selection of the epitope tags (either c-myc or VSV-G at the amino-terminal of the gene products) (23)(24)(25), and the use of the Dspp 3Ј untranslated region (4) have been discussed previously (26). However, each of these features is included to ensure the efficient transcription, translation, and secretion of the transgene products to the enamel extracellular space, and at the same time having a foreign peptide to follow the spatiotemporal expression of the transgene product.…”

Section: Methodsmentioning

confidence: 99%

“…Immunolocalization-Tissue sections of four-day post-natal heterozygous transgenic mouse pups, or their normal (non-transgenic) littermates, were prepared as described previously (22). An anti-VSV-G monoclonal antibody (Roche, Indianapolis, IN; catalog number 1667351) was used to demonstrate tissue-specific expression of the introduced VSV-Dsp transgene in secretory ameloblast cells.…”

Section: Methodsmentioning

confidence: 99%

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Dentin Sialoprotein and Dentin Phosphoprotein Overexpression during Amelogenesis

Paine

Luo

Wang

et al. 2005

Journal of Biological Chemistry

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The gene for dentin sialophosphoprotein produces a single protein that is post-translationally modified to generate two distinct extracellular proteins: dentin sialoprotein and dentin phosphoprotein. In teeth, dentin sialophosphoprotein is expressed primarily by odontoblast cells, but is also transiently expressed by presecretory ameloblasts. Because of this expression profile it appears that dentin sialophosphoprotein contributes to the early events of amelogenesis, and in particular to those events that result in the formation of the dentinoenamel junction and the adjacent "aprismatic" enamel. Using a transgenic animal approach we have extended dentin sialoprotein or dentin phosphoprotein expression throughout the developmental stages of amelogenesis. Overexpression of dentin sialoprotein results in an increased rate of enamel mineralization, however, the enamel morphology is not significantly altered. In wildtype animals, the inclusion of dentin sialoprotein in the forming aprismatic enamel may account for its increased hardness properties, when compared with bulk enamel. In contrast, the overexpression of dentin phosphoprotein creates "pitted" and "chalky" enamel of nonuniform thickness that is more prone to wear. Disruptions to the prismatic enamel structure are also a characteristic of the dentin phosphoprotein overexpressing animals. These data support the previous suggestion that dentin sialoprotein and dentin phosphoprotein have distinct functions related to tooth formation, and that the dentino-enamel junction should be viewed as a unique transition zone between enamel and the underlying dentin. These results support the notion that the dentin proteins expressed by presecretory ameloblasts contribute to the unique properties of the dentino-enamel junction.Dentin is an ectomesenchymal derived, collagen containing, calcified tissue that forms the major part of the tooth. Genetic diseases that result in abnormal dentin are classified in a subgrouping of dentinogenesis imperfecta. Dentinogenesis imperfecta type I (DI-I) 1 is always associated with one of the osteogenesis imperfectas, where mutations have been characterized in the following collagens: COL1A1, COL1A2, COL5A1, and COL2A1 (1), whereas dentinogenesis imperfecta type II (DI-II) is a disorder in dentin mineralization. Dentinogenesis imperfecta type III (DI-III) has a more extreme abnormal dental phenotype that impacts beyond dentin to the enamel and the pulps of affected teeth (2, 3).In dentin, two of the noncollagenous dentin matrix proteins are dentin siaolprotein (DSP) and dentin phosphoprotein (DPP). Both DSP and DPP are products of a single gene called dentin sialophosphoprotein (DSPP). Following transcription and translation of DSPP, the resulting product is post-translational cleaved to produce DSP and DPP that are primarily expressed in the dentin matrix (4). DPP (also known as phosphophoryn) is a highly acidic protein and is the major noncollagenous matrix component of dentin (ϳ90% of the dentin matrix is collagen) (5, 6). DSP is a glyco...

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Section: Resultssupporting

confidence: 66%

Section: Methodsmentioning

confidence: 54%

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

See 2 more Smart Citations

Dentin Sialoprotein and Dentin Phosphoprotein Overexpression during Amelogenesis

Paine

Luo

Wang

et al. 2005

Journal of Biological Chemistry

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“…The murine amelogenin promoter has been isolated from the mouse X-chromosome. Based upon transgenic mouse studies, our laboratory has demonstrated that the 2,263 nucleotides upstream of amelogenin start codon fully recapitulate the endogenous amelogenin gene expression profile within time and space (8). Deletion analysis of this 2,263-nucleotide stretch demonstrates that the Ϫ70/ ϩ52-bp minimal promoter is indispensable for maintaining transcriptional activity.…”

mentioning

confidence: 99%

NF-Y and CCAAT/Enhancer-binding Protein α Synergistically Activate the Mouse Amelogenin Gene

Xu¹,

Zhou²,

Luo³

et al. 2006

Journal of Biological Chemistry

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Amelogenin is the major protein component of the forming enamel matrix. In situ hybridization revealed a periodicity for amelogenin mRNA hybridization signals ranging from low to high transcript abundance on serial sections of developing mouse teeth. This in vivo observation led us to examine the amelogenin promoter for the activity of transcription factor(s) that account for this expression aspect of the regulation for the amelogenin gene. We have previously shown that CCAAT/enhancer-binding protein ␣ (C/EBP␣) is a potent transactivator of the mouse X-chromosomal amelogenin gene acting at the C/EBP␣ cis-element located in the ؊70/؉52 minimal promoter. The minimal promoter contains a reversed CCAAT box (؊58/؊54) that is four base pairs downstream from the C/EBP␣ binding site. Similar to the C/EBP␣ binding site, the integrity of the reversed CCAAT box is also required for maintaining the activity of the basal promoter. We therefore focused on transcription factors that interact with the reversed CCAAT box. Using electrophoretic mobility shift assays we demonstrated that NF-Y was directly bound to this reversed CCAAT site. Co-transfection of C/EBP␣ and NF-Y synergistically increased the promoter activity. In contrast, increased expression of NF-Y alone had only marginal effects on the promoter. A dominant-negative DNA binding-deficient NF-Y mutant (NF-YAm29) dramatically decreased the promoter activity both in the absence or presence of exogenous expression of C/EBP␣. We identified protein-protein interactions between C/EBP␣ and NF-Y by a co-immunoprecipitation analysis. These results suggest that C/EBP␣ and NF-Y synergistically activate the mouse amelogenin gene and can contribute to its physiological regulation during amelogenesis.

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Evidence for regulation of amelogenin gene expression by 1,25-dihydroxyvitamin D3 in vivo

Papagerakis¹,

Hotton²,

Lezot³

et al. 2000

J. Cell. Biochem.

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The unique hereditary enamel defect clearly related to the disturbance of one enamel matrix protein is X-linked amelogenesis imperfecta (AI), in which several mutations of amelogenin gene have been identified. The clinical phenotype of many of these subjects shows similarities with enamel defects related to rickets. Therefore, we hypothesized that rachitic dental dysplasia is related to disturbances in the amelogenin pathway. In order to test this hypothesis, combined qualitative and quantitative studies in experimental vitamin D-deficient (-D) rat model systems were performed. First, Western blot analysis of microdissected enamel matrix (secretion and maturation stages) showed no clear evidence of dysregulation of amelogenin protein processing in -D rats as compared with the controls. Second, the ultrastructural investigation permitted identification of the internal tissular defect of rachitic enamel, the irregular absence of intraprismatic enamel observed in -D animals, suggesting a possible link between prism morphogenesis and vitamin D. In addition, the steady-state levels of amelogenin mRNAs measured in microdissected dental cells was decreased in -D rats and up-regulated by an unique injection of 1,25-dihydroxyvitamin D(3) (1,25(OH)(2)D(3)). The present study shows evidences that amelogenin expression is regulated by vitamin D. This is the first study of an hormonal regulation of tooth-specific genes.

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The Murine Amelogenin Promoter: Developmentally Regulated Expression in Transgenic Animals

Cited by 42 publications

References 14 publications

Dentin Sialoprotein and Dentin Phosphoprotein Overexpression during Amelogenesis

Dentin Sialoprotein and Dentin Phosphoprotein Overexpression during Amelogenesis

NF-Y and CCAAT/Enhancer-binding Protein α Synergistically Activate the Mouse Amelogenin Gene

Evidence for regulation of amelogenin gene expression by 1,25-dihydroxyvitamin D3 in vivo

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