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  • 1995-1999  (6)
  • 1990-1994  (2)
  • 1
    Publication Date: 1992-01-01
    Print ISSN: 0142-9612
    Electronic ISSN: 1878-5905
    Topics: Biology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Medicine
    Published by Elsevier
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  • 2
    Publication Date: 1996-07-01
    Print ISSN: 0142-9612
    Electronic ISSN: 1878-5905
    Topics: Biology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Medicine
    Published by Elsevier
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  • 3
    Publication Date: 1997-12-01
    Print ISSN: 0925-4439
    Electronic ISSN: 1879-260X
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Published by Elsevier
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  • 4
    Publication Date: 1995-11-01
    Print ISSN: 0927-7765
    Electronic ISSN: 1873-4367
    Topics: Biology , Chemistry and Pharmacology , Physics
    Published by Elsevier
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Calcified tissue international 64 (1999), S. 234-238 
    ISSN: 1432-0827
    Keywords: Key words: Dentine phosphoproteins — Fluoride — Mineralization.
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Abstract. Dentine phosphoproteins have been proposed to have an important role in mineralization. This study focused on the influence of fluoride on the biochemical composition of dentine phosphoproteins and attempts to relate changes to the altered mineralization witnessed during fluorosis. Wistar rats were rendered fluorotic by the administration of 20 ppm sodium fluoride in their drinking water ad libitum, a nonfluorotic group received double-distilled, deionized water only. After 17 weeks, the teeth showed signs of fluorosis. The incisors were removed, split longitudinally, and the pulps were removed. Teeth were powdered and demineralized in 10% EDTA with protease inhibitors, after which the organic matrix was extracted with 4 M guanidinium chloride. Phosphoproteins were selectively precipitated from the soluble extract by the addition of 1.0 M calcium chloride and further purified by anion exchange chromatography. SDS-PAGE revealed two protein bands with molecular weights of 130 kDa and 66 kDa in the nonfluorotic fraction and 116 kDa and 66 kDa in the fluorotic fraction. Western blotting analysis identified the 66 kDa band as α2-HS glycoprotein which co-precipitated with phosphoproteins. Electroelution of the protein bands was performed with subsequent biochemical analyses. Phosphate content was determined for each protein band and was detectable in the 116 kDa and 130 kDa bands from the fluorotic and nonfluorotic samples, respectively, with a decreased level noted in the 116 kDa band. The presence of phosphate and the amino acid analysis of these bands suggested their identity to be dentine phosphoproteins. No changes in the ratio of amino acids was detected in fluorotic samples. The fluoride-induced alterations to the biochemical structure of dentine phosphoproteins would appear to influence the phosphorylation of these macromolecules only, possibly affecting posttranslational events. Such alterations may play a role in disrupting the patterns of mineralization seen during fluorosis.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Springer
    Calcified tissue international 56 (1995), S. 236-239 
    ISSN: 1432-0827
    Keywords: Proteoglycan ; Glycosaminoglycans ; Dentine ; Fluoride ; Biomineralization
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Abstract Proteoglycans and their spatial arms, the glycosaminoglycans, are known to interact with hydroxyapatite, and are considered to have a role in the regulation of mineralization. This study investigates the interactive mechanisms, with particular attention directed at the influence of fluoride on the adsorption process. Proteoglycans and glycosaminoglycans were adsorbed to hydroxyapatite in the presence of fluoride (1–20 ppm range). The adsorbates included a chondroitin 4-sulfate-rich proteoglycan extracted from rat incisor dentine, hyaluronan, chondroitin 4-sulfate, and dermatan sulfate. The order of glycosaminoglycan in decreasing affinity for hydroxyapatite was chondroitin 4-sulfate, dermatan sulfate, and hyaluronan, and the individual glycosaminoglycans showed different responses to the presence of fluoride. Graded increases in fluoride (1–4 ppm) led to 5–40% reduction of glycosaminoglycan adsorption to hydroxyapatite. The proteoglycan showed less affinity for hydroxyapatite, and demonstrated a reduction in adsorption of up to 22% with 20 ppm fluoride. The inhibitory effect of fluoride indicated an electrostatic mechanism, presumably via the calcium sites in the hydroxyapatite lattice.
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Springer
    Calcified tissue international 52 (1993), S. 392-398 
    ISSN: 1432-0827
    Keywords: Fluoride ; Proteoglycans ; Odontoblasts
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary Using an in vitro rat incisor odontoblast system, the effect of fluoride on proteoglycans was investigated at both the metabolic and structural level. Incisors were removed from 4-week-old rats, split longitudinally, and the pulps removed. Teeth were incubated at 37°C, 5% CO2 in Eagle's Minimum Essential Medium containing 35S-sulfate for 7 hours in the presence of 0 mM, 3 mM, or 6 mM sodium fluoride. Teeth were demineralized in EDTA, proteoglycan was extracted from the residue with 4 M guanidinium chloride, and further purified by anion exchange chromatography. Uptake of radiolabel was monitored by liquid scintillation counting. The resultant products were examined by cellulose acetate electrophoresis, SDS-PAGE, chondroitinase digestion, and amino acid analysis. Differential effects of fluoride were observed in both metabolism and biochemical characterization of proteoglycans following incubation at the two concentrations. Fluoride decreased uptake of the radiolabel but led to an accumulation of glycosaminoglycan within the proteoglycan of the matrix. Chondroitin sulfate was the predominant glycosaminoglycan identified, with the additional presence of dermatan sulfate and heparan sulfate identified. Dermatan sulfate levels increased in 3 mM-treated teeth. Fluoride-treated proteoglycans had a reduced molecular weight (200–90K to 180–79K); this reduction is primarily a result of smaller glycosaminoglycan chains, with limited reduction in the size of the core protein of 6 mM-treated teeth occurring. Such alterations in the biochemical metabolism and hence structure and function of proteoglycan may be implicated in the hypomineralization seen in fluorosis.
    Type of Medium: Electronic Resource
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  • 8
    ISSN: 1573-6865
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract This study used biochemical and immunohistochemical methods to characterize the chondroitin sulphate-rich proteoglycans from human alveolar bone obtained from an oral source. Proteoglycans were extracted from bone by a sequential 4 m guanidine HCl extraction process, and purified by DEAE-ion exchange chromatography. SDS-PAGE and Western blot analysis, using CS-56 monoclonal antibody, demonstrated one major proteoglycan species with a core protein of 58 kDa, glycosaminoglycan chains of 45--66 kDa and a mean molecular weight of 205 kDa. This work confirmed the biochemistry of chondroitin sulphate-rich proteoglycans from a novel source of adult human alveolar bone, and pointed towards a proteoglycan with a high glutamate, glycine, aspartate, alanine, serine and leucine content. Sections of alveolar bone were embedded in LR White resin, labelled with CS-56 antibody and examined with the light and electron microscopes. At the light microscope level, labelling was restricted to the osteocyte lacunae and canaliculi. Ultrastructural observations showed that the labelling was localized to fine filamentous material in the walls of the osteocytes and canaliculi. Sparse labelling was associated with the collagen fibres immediately subjacent to the lamina limitans, but no labelling of the mineralized matrix was observed. These findings also indicated subtle differences in the distribution of chondroitin sulphate compared with previously reported work, which may indicate species or age differences in the samples used in this study. Ultrastructural analysis confirmed and extended observations of glycosaminoglycan localization at the osteocyte cell membrane of mature human alveolar bone
    Type of Medium: Electronic Resource
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