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  • 1
    Electronic Resource
    Electronic Resource
    Cells from Hertwig's epithelial root sheath do not transcribe amelogenin (1991)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of periodontal research 26 (1991), S. 0 
    Details
    ISSN: 1600-0765
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Recent experimental evidence has led to the Interpretation that “enamel-like” material is deposited along the forming mouse molar root surface by cells of Hertwig's epithelial root sheath (HERS cells) and that this material is integral to the developmental program for cementogenesis. The experimental strategy described in this study was to examine selected developmental stages of root formation for mouse first and second mandibular molars in order to localize the cellular sites of amelogenin gene transcripts using high resolution in situ hybridization. Amelogenin is the major structural protein of coronal enamel and is highly conserved among mammalian species at the DNA and amino acid sequence level. Within the limits of sensitivity for in situ hybridization and utilizing either cRNAs or oligodeoxynucleotide probes, we were unable to localize amelogenin transcripts within HERS cells from selected developmental stages associated with mouse molar root formation. In contrast, previous studies using antipeptide antibodies have provided immuno-histochemical localization of amelogenin domains in HERS cell-derived products. For these HERS cell-derived proteins to contain both amelogenin epitopes and yet fail to yield nucleic acid hybridization Signals suggests that either gene rearrangement and/or alternative processing of messenger RNAs from the structural gene locus operate to produce immunologically related motifs sharing insufficient complementarity at the nucleotide level to permit efficient detection by hybridization. It is postulated that HERS cells synthesize proteins which contain amelogenin domains and that these proteins participate during cementogenesis. However, these enamel-related proteins are neither identical to, nor collinear with coronal canonical amelogenin transcripts.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1600-0765.1991.tb01624.x
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    In situ hybridization analysis of keratin gene expression in human ameloblastomas (1988)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of oral pathology & medicine 17 (1988), S. 0 
    Details
    ISSN: 1600-0714
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Complementary DNA (cDNA) clones corresponding to the 55 kDa (K 14) and 59 kDa (K 10) keratins were used as probes for in situ hybridization analysis for the expression of keratin genes in human ameloblastomas and in oral mucosa. Transcripts for either the K 14 keratin or the K 10 keratin were restricted in their spatial distribution within stratified epithelia consistent with the stage of differentiation of the keratinocyte: the K 14 keratin gene transcript was restricted to the basal cell layers of the mucosa, while the K 10 kerattranscript was expressed predominantly in suprabasal cells, within the granular and prickle layers. In contrast, only the K 14 keratin transcript could be indentified within the epithelial cells of human ameloblastomas. The differentiation-specific keratin transcript (K 10) was not present at detectable levels in this type of odontogenic tumors. In an atypical, infiltrating ameloblastoma, either the K 10 nor the K 14 transcript could be identified. Granular cells within one ameloblastoma expressed the K 14 transcript. A detailed examination of the pattern of gene expression in these unique tumors may lead to a better understanding of their pathogenesis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1600-0714.1988.tb01330.x
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Isolation and characterization of a mouse amelogenin expressed in Escherichia coli (1994)
    Springer
    Calcified tissue international 54 (1994), S. 312-319 
    Details
    ISSN: 1432-0827
    Keywords: Amelogenin ; Expression ; Enamel ; Recombinant DNA ; Tooth
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Abstract A mouse cDNA encoding a 180 amino acid amelogenin was subcloned into the pET expression plasmid (Novagen, Madison, WI) for production in Escherichia coli. A simple growth and purification protocol yields 20–50 mg of 95–99% pure recombinant amelogenin from a 4.5-liter culture. This is the first heterologous expression of an enamel protein. The expressed protein was characterized by partial Edman sequencing, amino acid composition analysis, SDS-PAGE, Western blotting, laser desorption mass spectrometry, and hydroxyapatite binding. The recombinant amelogenin is 179 amino acids in length, has a molecular weight of 20,162 daltons, and hydroxyapatite binding properties similar to the porcine 173 residue amelogenin. Solubility analyses showed that the bacterially expressed protein is only sparingly soluble in the pH range of 6.4–8.0 or in solutions 20% saturated with ammonium sulfate. The purified protein was used to generate rabbit polyclonal anti-amelogenin antibodies which show specific reaction to amelogenins in both Western blot analyses of enamel extracts and in immunostaining of developing mouse molars.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00295956
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    Paper (German National Licenses)
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