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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of periodontal research 24 (1989), S. 0 
    ISSN: 1600-0765
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: This study investigated the immunohistochemical localization of chondroitin sulfate (chondroitin, 4-sulfate and 6-sulfate) and dermatan sulfate proteoglycan (PG) in human gingival connective tissue, using monoclonal antibodies. Dermatan sulfate was found to be widespread in connective tissue, with an especially strong response shown in collagen fiber bundles under the epithelial basement membrane. Chondroitin 4-sulfale occurred widely in connective tissue but showed only a weak response. Chondroitin 6-sulfate was located in peripheral blood vessels. Chondroitin was not detected in gingival connective tissue.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of periodontal research 28 (1993), S. 0 
    ISSN: 1600-0765
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The purpose of this study was to develop an ELISA method to detect chondroitin sulfate isomer-linked proteoglycans in gingival crevicular fluid (GCF), and to lelucidate the role played by the glycosaminoglycans (GAGs) in GCF during experimentally-induced periodontitis in dogs. Experimental periodontitis was induced by placement of a silk ligature below the gingival margin of the molar teeth in 3 mongrel dogs. GCF was collected using microcapillary tubes at 0. 7.21 and 60 days after ligature placement. Too compare with GAG in GCF, bovinenasal cartilage proteoglycan monomer, dog's serum and supernatant of homogenized gingival tissuw were prepared. Combination of monoclonal antibodies, 3B3 and 9A2, and specific enzymatic digestion made possible the indentification of chondroitin 4 sulfate (C4S), chondroitin 6 sulfate (C6S) and dermatan sulfate (DS). The ELISA method detected very small amounts of chondroitin sulfate (CS) isomers (15-1000 ng/ml of bovine nasal cartilage proteoglycan). The ELISA value of CS isomers in GCF was lower than that of homogenized gingival tissue but higher than that of the serum. The ELISA value of C4S, C6S and DS, although fluctuating, increased in proportion to the severity of the inflammation.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of periodontal research 24 (1989), S. 0 
    ISSN: 1600-0765
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Using the high iron diamine thiocarbohydrazide silver proteinate (HID-TCH-SP) staining technique, we investigated ultrastructural localization of sulfated glycosaminoglycans (GAGs) in the rat gingiva shortly after eruption, especially those associated with internal and external basal laminae. In the apical portion of the internal basal lamina, HID-TCH-SP stain deposits were distributed mainly in the region of the lamina lucida located between the lamina densa and the distal surface membrane of the junctional epithelium and inside the depression of the distal surface membrane adjacent to the basal lamina. Stain deposits were also detected on the surface membrane of cytoplasmic protrusion. Interestingly, the density of HID-TCH-SP stain deposits in the internal basal lamina was highest in the apical portion of the junctional epithelium and decreased in the coronal direction, finally tending to disappear completely. On the other hand, in the external basal lamina the deposits were localized in the whole region of the basal lamina or at both sites of the lamina densa. HID-TCH-SP stain deposits were also detected external to the lamina densa in the basement membrane associated with capillaries and in the connective tissue where they were distributed in close relation to collagen fibrils. Testicular hyaluronidase digested most HID-TCH-SP stain deposits in the connective tissue, whereas those in the region of basement membranes resisted this enzymatic digestion.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of periodontal research 33 (1998), S. 0 
    ISSN: 1600-0765
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: This study was designed to demonstrate, by use of biotin-labeled hyaluronic acid binding protein (HABP) and an avidin–enzyme system, the localization of hyaluronan (HA) in periodontal tissue of beagle dogs during experimentally induced periodontitis. Experimental periodontitis was induced in the dogs by ligation of the gingival sulcus. Experimental tissue was collected at 0, 3, 7 and 21 days after ligation. HA was revealed by strong staining in the intercellular space around epithelial cells and periodontal ligament, and by light staining in the gingival connective tissue. According to the progression of periodontal tissue breakdown, HA was detected in a small number of leukocytes and monocytes, on the surface of osteoclasts, the surface of alveolar bone, thickened endothelium and in epithelial cells related to rete peg formation. Streptomyces hyaluronidase-treated specimens gave negative staining. This study suggests that HA may be associated with the inflammatory reaction in experimental periodontitis tissue.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of periodontal research 33 (1998), S. 0 
    ISSN: 1600-0765
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: This study was designed to demonstrate, by use of biotin-labeled hyaluronic acid binding protein (HABP) and an avidin-enzyme system, the localization of hyaluronan (HA) in periodontal tissue of beagle dogs during experimentally induced periodontitis. Experimental periodontitis was induced in the dogs by ligation of the gingival sulcus. Experimental tissue was collected at 0, 3, 7 and 21 days after ligation. HA was revealed by strong staining in the intercellular space around epithelial cells and periodontal ligament, and by light staining in the gingival connective tissue. According to the progression of periodontal tissue breakdown, HA was detected in a small number of leukocytes and monocytes, on the surface of osteoclasts, the surface of alveolar bone, thickened endothelium and in epithelial cells related to rete peg formation. Streptomyces hyaluronidase-treated specimens gave negative staining. This study suggests that HA may be associated with the inflammatory reaction in experimental periodontitis tissue.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Hoboken, NJ : Wiley-Blackwell
    Journal of Biomedical Materials Research 39 (1998), S. 603-610 
    ISSN: 0021-9304
    Keywords: sintered carbonate apatite ; osteoclasts ; bioresorption ; bioresorbable bone substitutes ; acid dissolution ; Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine , Technology
    Notes: The dissolution behavior of sintered carbonate apatite was investigated in a 10 mM/L acetic acid solution adjusted to pH 5.0 at 37°C, and compared to that of sintered hydroxyapatite and bone apatite for the purpose of establishing some similarities between the physicochemical dissolution of apatite biomaterials in vitro and their ability to be resorbed by osteoclasts in vivo. Both the sintered carbonate apatite and the bone apatite dissolved to an appreciable extent. Their solution compositions changed in an almost identical manner until toward the end of the reaction. The solution compositions for sintered carbonate apatite at 30 s was comparable with that for sintered hydroxyapatite at 3.8 days with respect to the degree of supersaturation, indicating that the former specimen is much more soluble than the latter specimen. Osteoclasts which were obtained from the long bones of 1-day-old neonatal rabbits resorbed bone and sintered carbonate apatite, but not sintered hydroxyapatite. These findings suggest that sintered carbonate apatites, which have characteristics that can be favorably compared with those of bone, especially with respect to its reactivity to acid media, would be useful as bioresorbable bone substitutes. © 1998 John Wiley & Sons, Inc. J Biomed Mater Res, 39, 603-610, 1998.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Hoboken, NJ : Wiley-Blackwell
    Journal of Biomedical Materials Research 31 (1996), S. 43-49 
    ISSN: 0021-9304
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine , Technology
    Notes: An apatite - collagen complex was prepared in calcium β-glycerophosphate solutions at pH 9.0 and 37°C with the purpose of developing new bone substitutes that more closely resemble bone than currently available materials. Reconstituted type I collagen as well as sheet collagen were crosslinked in the presence of alkaline phosphatase and egg-yolk phosvitin. The crosslinked collagens were immersed in daily renewed calcium β-glycerophosphate solutions for 2 and 4 weeks to induce the deposition of apatite on the collagen fibers. After 2 weeks of reaction, for example, apatites deposited approximately two times the crosslinked collagen in weight. With reconstituted collagen, the complex showed some elasticity but no apatite was visually observed to detach under deformation with fingers and forceps. The complex, moreover, did not disintegrate when immersed in saline or animal blood. Nevertheless, the complex resorbed with no evidence of cytotoxity when implanted in muscle tissues. These findings suggest that the apatite - collagen complex prepared would be useful as bone substitutes, especially for periodontal osseous lesion repair and alveolar ridge augmentation. © 1996 John Wiley & Sons, Inc.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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