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  • 1
    Electronic Resource
    Electronic Resource
    Changes in the solubility of enamel mineral at various stages of porcine amelogenesis (1992)
    Springer
    Calcified tissue international 50 (1992), S. 266-272 
    Details
    ISSN: 1432-0827
    Keywords: Amelogenesis ; Enamel mineral ; Carbonatoapatite ; Solubility
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary The solubility of enamel mineral (a carbonated apatite) formed at various stages of porcine amelogensis was investigated at controlled partial pressures of CO2. Enamel samples were obtained from the outer (young) secretory, inner (old) secretory, early (soft) and late (hard) mature enamel of the permanent dentition of slaughtered piglets. The dissected enamel was pulverized and subjected to a plasma ashing at low temperature to remove organic matter. The composition (Ca, total P, HPO4, and CO3) of the enamel mineral was determined chemically. The enamel mineral contained significant amounts of carbonate and acid phosphate: the model adopted for its stochiometry was [Ca]5-x [HPO4]v[CO3]w[PO4]3-x[OH]1-x. Each enamel sample was equilibrated in dilute phosphoric acid solutions (0.01–1.2 mM) under Pco2=1.86 and 1.75%. Equilibration of the enamel samples usually took 20–25 days; the solution composition (pH, concentrations of Ca, P, Mg, Na, and K, and activity of Ca2+) was determined periodically. The composition of the solution at equilibrium showed that (1) the outer (younger) secretory mineral was the most soluble and the solubility of enamel mineral decreased with advancing developmental stages; (2) the mean activity product in the saturated solutions for the outer secretory enamel was the same as that calculated on the basis of the reported composition of the enamel fluid; and (3) the solubility data obtained with most of the enamel samples were consistent with a model in which the equlibration includes two processes: dissolution of the original enamel mineral and precipitation of a new carbonatoapatite. Analyses of the equilibrated samples, particularly the mature enamel, by electron microscopy, supported the precipitation of carbonatoapatite. The overall results are in good agreement with previous results indicating that significant changes in the composition and structure of porcine enamel mineral occur with the mineralization progress.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00296292
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  • 2
    Electronic Resource
    Electronic Resource
    Common epitopes of mammalian amelogenins at the C-terminus and possible functional roles of the corresponding domain in enamel mineralization (1992)
    Springer
    Calcified tissue international 51 (1992), S. 85-91 
    Details
    ISSN: 1432-0827
    Keywords: Amelogenesis ; Pig, cow, rat, rabbit amelogenins ; Epitopes at the C-terminus ; Adsorption ; Enamel mineralization
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary The present studies were undertaken to investigate the presence of common epitopes of mammalian amelogenins at the C-terminus and the possible functional importance of the conserved C-terminal domain in enamel mineralization during mammalian amelogenesis. Enamel proteins, including the intact amelogenins and their degraded polypeptides, were isolated from the secretory enamel of pig, cow, rat, and rabbit incisors. Rabbit and rat antipeptide sera, as well as rat anti-25 kD and 20 kD pig amelogenin sera, were used to identify the amelogenins among the isolated matrix proteins of each of the animal species. The antipeptide sera were developed previously (Aoba et al. [19]) using as immunogens the two synthetic peptides, C13 and C25, which correspond to the last 12 (plus Cys for KLH-conjugation) and 25 amino acid residues of pig intact amelogenin, respectively. Reactivity of the enamel proteins with each antiserum was examined by Western blot analysis. The results of immunoblotting showed that a few enamel matrix proteins in each of the mammalian species were recognized by the anti-C13 serum, specifically, pig amelogenin at 25 kD (and trace components at 27, 22, and 18 kD), cow amelogenin at 28 kD (trace components at 26, 22, 19, and 14 kD), rat amelogenins at 28 and 26 kD (and a trace component at 20 kD), and rabbit amelogenins at 24 and 21 kD (and a trace at 13 kD). The anti-C25 serum reacted additionally with pig amelogenin at 23 kD, cow amelogenin at 27 kD (a major matrix constituent), and rabbit protein at 19 kD. The anti-pig 20 kD amelogenin (lacking the last 25 amino acid residues at the C-terminus) serum reacted with a large number of pig, cow, and rat amelogenins but, interestingly, with none of the rabbit enamel proteins. Probing of rat enamel proteins with Maclura pomifera lectin showed the heterogeneity of glycosylation of rat amelogenins, particularly between the 28 and 26 kD intact amelogenins. In parallel adsorption studies, part of the enamel protein samples isolated from each of the species was used as adsorbates to investigate the selective adsorption of amelogenins onto hydroxyapatite. Immunoblot analysis of the proteins adsorbed onto the crystals revealed that the mammalian amelogenins having the common epitopes at the C-terminus, in general, adsorb preferentially onto hydroxyapatite. The adsorption affinity of the degraded amelogenins decreased significantly with the loss of reactivity toward the anti-C13 serum. The overall results support the contention that the intact mammalian amelogenins, including rat and rabbit amelogenins, share common epitopes at the C-terminus and that the conserved C-terminal domain plays an important role in setting the molecular structures of the intact amelogenins so as to facilitate the protein-enamel mineral interaction.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00296224
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  • 3
    Electronic Resource
    Electronic Resource
    Competitive adsorption of magnesium and calcium ions onto synthetic and biological apatites (1992)
    Springer
    Calcified tissue international 51 (1992), S. 143-150 
    Details
    ISSN: 1432-0827
    Keywords: Adsorption ; Magnesium ; Calcium ; Apatite crystals ; Enamel ; Dentin ; Bone
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary Magnesium (Mg) is a conspicuous constituent of hard tissues but its possible role in biomineralization is poorly understood. It is possible that Mg2+ adsorbed onto bioapatites may contribute to the modulation of crystal growth as such inhibitory activity has been reported for synthetic apatites. The present study was undertaken to determine the adsorption isotherms of Mg ions onto synthetic apatites and biominerals in tooth and bone tissues in the presence of other ions of natural occurrence. Synthetic crystals used as adsorbents were hydroxyapatite and, as a better prototype for the biomineral, Mg-containing carbonatoapatite. Human enamel and dentin materials were obtained from extracted, caries-free, permanent teeth. Porcine dentin materials at two developmental stages were obtained from erupted deciduous and unerupted permanent teeth of a 6-month-old slaughtered piglet. Porcine bone was obtained from the cortical portion of the mandible of the same animal. All biomineral samples were pulverized and then treated by plasma ashing (deproteination) at about 60°C. Each of the powdered samples was equilibrated in solutions containing various initial concentrations of Mg2+, Ca2+, and Na+ (or K+) as nitrate salts. Following equilibration, concentrations (and activities) of magnesium and calcium ions in the experimental solution were determined. The pH values of the equilibrium solutions were in the range of 6.2–6.5. Experimental data of the Mg adsorption onto hydroxyapatite were interpreted on the basis of a Langmuir-type model for binary systems assuming competition of Mg2+ and Ca2+ for the same adsorption sites on the crystal surfaces of the apatites. According to this model, the adsorbed Mg is expressed as a function of the ionic activity ratio (Mg2+)/(Ca2+) in the equilibrium solution. The model contains two parameters, the adsorption selectivity constant Ks and the maximum number of adsorption sites N (μmol/g). The numerical values of Ks were similar for all adsorbents used (synthetic and biological) and indicated the preferential adsorption of Ca2+ probably due to spacial restrictions extending to the very surface of the crystals. The initial level of Mg2+ in the surface pool was different in the various biominerals, probably reflecting the composition of fluid in which the biominerals were formed. Whereas the surface pool of Mg of human enamel was marginal, only 5% of the total Mg, significant fractions of the total Mg in human and porcine dentins (about 20–30%), and porcine bone (about 40%) existed on the crystal surfaces. There were significant differences in the total Mg and the value of the parameter N between young (unerupted) and mature (erupted) dentin minerals. It was ascertained that the occupancy of adsorption sites by Mg ions became greater with maturation of the dentin tissues. The overall results suggest that the Mg-mineral interaction in tooth and bone tissues may be a highly tissue-specific process, presumably reflecting differences in fluid composition (particularly Ca and Mg activities) responsible for biomineralization.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00298503
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  • 4
    Electronic Resource
    Electronic Resource
    Inhibition of apatite crystal growth by the amino-terminal segment of human salivary acidic proline-rich proteins (1984)
    Springer
    Calcified tissue international 36 (1984), S. 651-658 
    Details
    ISSN: 1432-0827
    Keywords: Salivary proteins ; Hydroxyapatite ; Adsorption ; Precipitation-inhibitor ; Phosphoserine
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary Inhibition of seeded apatitic crystal growth by human salivary acidic proline-rich phosphoproteins (PRP) has been related to their adsorption onto the apatite seeds. The amino-terminal 30-residue segment of the PRP makes an important contribution to this adsorption. This peptide (PRP1(T1)) and its dephosphorylated analogue from PRP3 (PRP3(T1)DP) were prepared. They have identical sequences, except the phosphates at residues 8 and 22 in PRP1(T1) are absent from PRP3(T1)DP. Adsorption of these peptides onto hydroxyapatite and their effect on crystal growth from a defined supersaturated solution was studied. Adsorption behavior was adequately described by the Langmuir adsorption isotherm. The adsorption affinity constant of PRP1(T1) (K=20,200 ml/µmol) was more than 10 times the corresponding value for PRP3(T1)DP (1,800 ml/µmol), and similar to that of the parent protein, PRP1 (26,200 ml/µmol). Inhibition of crystal growth by the peptides was interpreted in terms of the fractional coverage of the maximum number of adsorption sites (as derived from the adsorption isotherms), suggesting that the molecules block, by adsorption, specific growth sites on these surfaces. Comparison of precipitation kinetics showed that PRP1(T1) is a more effective inhibitor than PRP3(T1)DP at the same initial concentration (10−6−10−7 M). However, on the basis of per mol adsorbed, PRP3(T1)DP displays a greater inhibitory activity; such a behavior is consistent with a more open molecular structure which blocks more growth sites per mol adsorbed than PRP1(T1). Because of its high affinity constant, preadsorbed PRP1(T1) remains in the condensed state in the supersaturated solution used, whereas the preadsorbed PRP3(T1)DP molecules desorb to some extent, resulting in a decrease in inhibitory activity. The results show that the amino-terminal segment of the PRP and the two phosphoserine residues present in this segment are particularly important in the function proposed for these proteins in the oral environment.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02405385
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  • 5
    Electronic Resource
    Electronic Resource
    Analysis of paramagnetic centers in X-ray-irradiated enamel, bone, and carbonate-containing hydroxyapatite by electron spin resonance spectroscopy (1979)
    Springer
    Calcified tissue international 28 (1979), S. 107-112 
    Details
    ISSN: 1432-0827
    Keywords: ESR ; Bone ; Enamel ; CO3-Apatite ; Paramagnetism
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary Carbonate-containing hydroxyapatite, enamel, and bone were irradiated by an X-ray and investigated between 77° and 350°K by means of electron spin resonance (ESR) spectroscopy. The ESR spectrum of enamel irradiated at 77°K in vacuum and observed at the same temperature was almost the same as that of the carbonate-containing hydroxyapatite. The temperature dependence of signal intensities confirms a spin-energy exchange between the mineral and organic constituents in bone, but in enamel no or very little spinenergy exchange between the mineral and organic constituents. Considerable similarity among the ESR spectra of enamel, bone, and carbonate-containing apatite was obtained after X-ray irradiation in air at 300°K with both an X-band and a Q-band ESR spectrometer. The Q-band spectrum can be interpreted in terms of two paramagnetic species. One is identified as a CO 3 3− anion radical which has an axial symmetry withg factors of 2.0029 and 1.9972. The other species is found to be centered atg=2.0019.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02441228
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  • 6
    Electronic Resource
    Electronic Resource
    Characterization of the Mineralization Process in Cultures of Rabbit Growth Plate Chondrocytes
    Amsterdam : Elsevier
    Developmental Biology 156 (1993), S. 372-380 
    Details
    ISSN: 0012-1606
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1006/dbio.1993.1084
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  • 7
    Electronic Resource
    Electronic Resource
    Epitaxial overgrowth of apatite crystals on the thin-ribbon precursor at early stages of porcine enamel mineralization (1993)
    Springer
    Calcified tissue international 53 (1993), S. 249-256 
    Details
    ISSN: 1432-0827
    Keywords: Enamel ; Amelogenesis ; Crystal growth ; Calcium phosphates ; Biomineralization
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary The aim of the present work was to investigate changes in cross-sectional morphologies of enamel crystallites as a function of location in secretory porcine enamel. Enamel tissues were obtained from 5- to 6-month-old slaughtered piglets. For examination by electron microscopy, a portion of the secretory enamel was embedded in resin and ultrathin sections were prepared with a diamond knife. In parallel studies, compositional and structural changes of enamel mineral were assessed by chemical analysis and Fourier transform infrared (FTIR) spectroscopy. For this purpose, two consecutive layers of the outer secretory enamel, each approximately 30 μm thick, were separated from the labial side of permanent incisors. Using high-resolution electron microscopy, early events of enamel crystal growth were characterized as the epitaxial growth of small apatite units on the lateral surfaces of the initially precipitated thin ribbon. These apatite units had regular triangle or trapezoid cross-sections. After fusions of those isolated trapezoids on both lateral sides of the platy template, the resulting enamel crystallites had the well-documented flattened-hexagonal shapes in cross-sections. The initially precipitated thin plate was buried inside the overgrown apatite lamella and then retained as a central dark line. Similar morphological evidence for the epitaxial nucleation and overgrowth of carbonatoapatite on the platy template was obtainedin vitro. Chemical and FTIR analyses of the enamel layer samples showed that the characteristics of the youngest enamel mineral were distinct from those of enamel crystals found in older secretory enamel. The overall results support the concept that initial enamel mineralization comprises two events: the initial precipitation of thin ribbons and the subsequent epitaxial growth of apatite crystals on the two-dimensional octacalcium phosphate-like precursor.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01320910
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  • 8
    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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  • 9
    Electronic Resource
    Electronic Resource
    Analysis of electron-excess and electron-deficient centers in x-ray-irradiated tricalcium phosphates by electron spin resonance spectroscopy (1979)
    Springer
    Calcified tissue international 29 (1979), S. 239-244 
    Details
    ISSN: 1432-0827
    Keywords: ESR ; Tricalcium phosphates ; Electron and hole centers
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary After X-ray irradiation, new paramagnetic centers were observed in electron spin resonance (ESR) spectra of amorphous calcium phosphate (ACP) and Mg-containing tricalcium phosphate (Mg-TCP) when they were heated at 900°C for 1 h before irradiation. Heated ACP shows a single resonance signal atg=2.0005 in place of the hyperfine doublet of the PO 4 2− ion radical, which is the dominant species in the ESR spectrum of unheated ACP. A similar signal is observed in the heated Mg-TCP. Treatment with electron scavengers (Pb2+ and Cd2+) and hole scavengers (Ce3+) suggests that the single resonance signal can be ascribed to a trapped electron. Comparison between the ESR spectra before and after annealing indicates that in the case of the heated ACP such a signal is most likely connected with a localized unpaired electron close to the calcium; on the other hand, in the case of the heated Mg-TCP the signal is connected with the localized electron close to the magnesium. In addition, new sets of signals are observed in those heated samples. Their hyperfine splittings are 612 and 713 gauss for the heated ACP, and 589 and 683 gauss for the heated Mg-TCP. Those new sets of signals are found to be ascribed to the trapped holes close to two magnetically distinct sites of phosphorus nuclei in the crystal lattice ofβ-tricalcium phosphate. Treatment with deuterium oxide strongly indicates that hydrogen atoms originate from adsorbed water molecules, although their half-life is a matter of months even at room temperature.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02408086
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  • 10
    Electronic Resource
    Electronic Resource
    Morphology of the enamel organ in the miniature swine (1991)
    New York, NY [u.a.] : Wiley-Blackwell
    The @Anatomical Record 230 (1991), S. 97-113 
    Details
    ISSN: 0003-276X
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: In recent years, the dentition of the pig has been increasingly used as a model for the study of amelogenesis. Indeed, much of our current knowledge on enamel formation derives from biochemical and physicochemical analyses of the organic and inorganic components, respectively, of porcine enamel. As an extension of this previous work, and as the first step in our attempt to correlate known enamel matrix and mineral changes with adjacent enamel organ morphology, the present study was undertaken to provide a description of the morphological events occurring in the enamel organ during porcine amelogenesis. Two-week-old miniature swine (minipigs) were fixed by vascular perfusion with glutaraldehyde, the deciduous teeth present at this age were embedded in Epon resin and sectioned, and the cells of the enamel organ at each of the various developmental stages of amelogenesis were examined by light and transmission electron microscopy. In many respects, the morphology of the porcine enamel organ was similar to that previously described in other mammalian species. On the other hand, several particularities were noted and these are discussed in the context of available data correlating cell ultrastructure with putative function during enamel formation.
    Additional Material: 27 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/ar.1092300110
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