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  • 1
    Electronic Resource
    Electronic Resource
    Identification of a bone matrix-derived chemotactic factor (1983)
    Springer
    Calcified tissue international 35 (1983), S. 481-485 
    Details
    ISSN: 1432-0827
    Keywords: Chemotaxis ; Bone ; Osteoblasts ; Bone proteins
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary When demineralized bone matrix powder is implanted subcutaneously in the rat, the early responses involve the appearance and proliferation of mesenchymal cells at the site of implantation, followed by cartilage and bone formation. The ability of cells to migrate to the implant suggests that chemotaxis may be a critical event in this process. Therefore, using the modified Boyden chamber assay, we tested extracts of demineralized bone matrix for chemotactic activity. We have identified and partially purified, on molecular sieve chromatography, a heat labile and trypsin-sensitive protein (Mr=60,000–70,000) that is a potent chemoattractant for mouse calvaria, osteoblast-like cells (MMB-1), but not for monocytes (putative osteoclast precursors). These findings suggest that chemotactic protein(s) have a significant role in the recruitment of osteoprogenitor cells to a site of bone repair.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02405081
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  • 2
    Electronic Resource
    Electronic Resource
    Localization and Expression of Osteopontin in Mineralized and Nonmineralized Tissues of the Periodontium (1995)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 760 (1995), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1995.tb44628.x
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  • 3
    Electronic Resource
    Electronic Resource
    Expression of heat stress proteins by human periodontal ligament cells (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: The purpose of the present report was to document the stress response produced by physical and chemical abuses to human periodontal ligament cells, and to review some of the known functions of stress response proteins produced as a result of such treatments. For these studies human PDL cells were exposed to sublethal challenges of 43°C heat, sodium arsenite and the amino acid analog L-azetidine-2-carboxylic acid (AZC). The cells were labelled with [35S]-methionine and the proteins produced were examined by autofluorography of SDS-PAGE gels. Heat challenges were shown to induce hsps with an apparent mol. wts. of 90K, 68-72K, 41–47K, and 36 K. Arsenite-treated cells produced similar hsps including a 30k protein not produced by other forms of stress. AZC treatment resulted in the production of apparent functionless hsps with apparent molecular weights of 90,000, 72,000, 68,000 and 36,000. The function of these proteins and their possible role in periodontal disease is discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1600-0714.1988.tb01323.x
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  • 4
    Electronic Resource
    Electronic Resource
    Regulation of the attachment and migration of bone cells in vitro (1982)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of periodontal research 17 (1982), S. 0 
    Details
    ISSN: 1600-0765
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1600-0765.1982.tb02047.x
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  • 5
    Electronic Resource
    Electronic Resource
    in vitro attachment of bacteria to extracts of cementum (1985)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of oral pathology & medicine 14 (1985), S. 0 
    Details
    ISSN: 1600-0714
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Cementum is a specialized mineralized tissue providing for the attachment of perio-dontal fibers to the root surface of a tooth. In periodontal disease this connective tissue attachment to the cemental surface is lost. The ability of bacteria to adhere to the root surface, an intial event in the disease process, may be influenced by the organic matrix of cementum. Therefore, an in vitro assay of cell attachment was modified to study bacterial adherence to protein extracts of cementum. Petri dishes coated with the extracts were pre-incubated in culture media and then bacteria were added. Using this assay, Capnocytophaga-like species, a gram negative bacterium implicated in periodontal disease, attached preferentially to dishes coated with cemental extracts when compared with Type I collagen or uncoated dishes. This assay system should prove beneficial for studying the attachment of various microorganisms to protein extracts of both normal and diseased cementum. as well as providing insight into the unique attachment properties of cementum.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1600-0714.1985.tb00469.x
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  • 6
    Electronic Resource
    Electronic Resource
    Expression of mineral-associated proteins by periodontal ligament cells: in vitro vs. ex vivo (1996)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of periodontal research 31 (1996), S. 0 
    Details
    ISSN: 1600-0765
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1600-0765.1996.tb00505.x
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  • 7
    Electronic Resource
    Electronic Resource
    Osteopontin adhesion receptors on gingival fibroblasts (1995)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of periodontal research 30 (1995), S. 0 
    Details
    ISSN: 1600-0765
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Osteopontin (OPN) promotes attachment and spreading of cells in an RGD dependent fashion, suggesting that OPN interacts with integrins on cell surfaces. Here in, we show that LM-609, a monoclonal antibody to the αvβ3 integrin (a vitronectin receptor), inhibited OPN-mediated attachment of gingival fibroblasts. To characterize the cell surface receptors responsible for this interaction, we performed OPN-sepharose affinity chromatography using detergent extracts of 35S-methionine or l25I-surface labeled gingival fibroblasts. Proteins bound to the OPN-matrix were eluted with EDTA and subjected to SDS-PAGE under reducing conditions. EDTA eluates from both 125I-surface labeled and 35Smethionine labeled extracts demonstrated prominent bands in the 90kDa and 50kDa regions, by both autoradiography and fluorography, respectively. These studies suggest that OPN is associated with other cell surface molecules in addition to αvβ3. Furthermore, these as yet to be characterized proteins, may prove to have a stronger affinity for OPN than αvβ3.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1600-0765.1995.tb01250.x
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  • 8
    Electronic Resource
    Electronic Resource
    Protein production by human gingival fibroblasts is enhanced by guanidine EDTA extracts of cementum (1987)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of periodontal research 22 (1987), S. 0 
    Details
    ISSN: 1600-0765
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Nonconfluent cultures of human gingival fibroblasts were exposed to both guanidine and guanidine EDTA extracts of cementum for 48 hours. To compare the effects of cementum extracts on fibroblasts with other mineralized tissue extracts, cells were also exposed to guanidine and guanidine EDTA extracts of dentin and alveolar bone. The cells were radioactively labeled during the last 24 h. Total protein production was measured via the incorporation of radioactive proline. Collagen production was estimated by digestion of the radioactive protein mixture with bacterial collagenase. All guanidine EDTA extracts elicited statistically significant increases in total protein production compared to controls. At 50 μg/ml of extract, the increases in protein production were 340%, 143% and 338% for bone, cementum and dentin, respectively. Similar results were obtained for collagen production. In contrast, the guanidine extracts had no effect on either protein or collagen production by human gingival fibroblasts. These data indicate that the functions of gingival fibroblasts can be altered by proteins from associated mineralized tissues. Identifying such proteins and understanding their biological functions will enhance our knowledge of the mechanisms that regulate connective tissue regeneration.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1600-0765.1987.tb01542.x
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  • 9
    Electronic Resource
    Electronic Resource
    Cell attachment activity of cementum: bone sialoprotein _ identified in cementum (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: Considerable research effort has been directed at preparing root surfaces in a fashion that would promote cell attachment leading to periodontal regeneration; however, no methods have proven to be clinically predictable. Identification of attachment protein(s) associated with the root surface matrix of cementum may prove valuable for developing effective clinical treatments. In this study cementum proteins were extracted from bovine and human teeth by sequential chaotropic extraction using guanidine followed by guanidine/EDTA. The guanidine/EDTA extract, but not guanidine extract, was found to promote attachment of fibroblasts. This attachment activity was inhibitable with synthetic peptide containing the attachment sequence arginine-glycine-aspartic acid (RGD). Fractionation of the guanidine/EDTA extract revealed several fractions with attachment activity. Immunoblot analysis demonstrated that two of these fractions contain the bone-associated RGD containing attachment protein, bone sialoprotein-II (BSP-II). In addition, attachment activity was also noted in other fractions that could not be attributed to BSP-II or fibronectin. These studies indicate that a component of the attachment activity of cementum is likely to be due to BSP-II and that cementum contains additional, as yet undetermined, attachment proteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1600-0765.1991.tb01620.x
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  • 10
    Electronic Resource
    Electronic Resource
    Molecular factors regulating development and regeneration of cementum (1993)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of periodontal research 28 (1993), S. 0 
    Details
    ISSN: 1600-0765
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1600-0765.1993.tb02123.x
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