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  • 1
    Electronic Resource
    Electronic Resource
    Collaboration between Collagenous Matrix and Osteogenin Is Required for Bone Induction (1990)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 580 (1990), 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.1749-6632.1990.tb17979.x
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  • 2
    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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  • 3
    Electronic Resource
    Electronic Resource
    Bone morphogenetic proteins induce periodontal regeneration in the baboon (Papio ursinus) (1994)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of periodontal research 29 (1994), 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.1600-0765.1994.tb01246.x
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  • 4
    Electronic Resource
    Electronic Resource
    Periodontal regeneration: potential role of bone morphogenetic proteins (1994)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of periodontal research 29 (1994), S. 0 
    Details
    ISSN: 1600-0765
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Initiation of osteogenesis and cementogenesis is a problem central to periodontal regeneration. A major advance in the understanding of bone formation has been the identification of an entirely new family of protein initiators, the bone morphogenetic proteins, that regulate cartilage and bone differentiation in vivo. The purification, genetic cloning and expression of recombinant human bone morphogenetic proteins (BMPs) have laid the foundation for the cellular and molecular dissection of bone development and regeneration. The striking evolutionary conservation of the BMP genes indicates that they are critical in the normal development and function of animals. In addition to postfetal osteogenesis, the BMPs may play multiple roles in embryonic development and organogenesis, including skeletogenesis and the development of craniofacial and dental tissues. The availability of recombinant human BMPs provides several challenges and opportunities to gain insights into the mechanisms regulating the regeneration of bone and cementum for optimal outcome in the periodontal patient.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1600-0765.1994.tb01216.x
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  • 5
    Electronic Resource
    Electronic Resource
    Identification of endothelin–1 in the pathophysiology of metastatic adenocarcinoma of the prostate (1995)
    [s.l.] : Nature Publishing Group
    Nature medicine 1 (1995), S. 944-949 
    Details
    ISSN: 1546-170X
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] Prostate cancer is the second most common cause of death from cancer in U.S. men, and advanced, hormone–refractory disease is characterized by painful osteoblastic bone metastases. Endothelin–1, more commonly known as a potent vasoconstrictor, is a normal ejaculate protein that also ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/nm0995-944
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  • 6
    Electronic Resource
    Electronic Resource
    Collagenous bone matrix is a local mitogen (1979)
    [s.l.] : Nature Publishing Group
    Nature 278 (1979), S. 855-857 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Demineralised bone matrix powder prepared from rat diaphyses was transplanted subcutaneously in the anterior thoracic region of 28-35-d-old, male rats of Long-Evans strain as described previously4. The day of transplantation was designated as day 0. On different days after transplantation, the rats ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/278855a0
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  • 7
    Electronic Resource
    Electronic Resource
    Hormone-dependent haematopoiesis in fibroblast-transformation ossicles (1976)
    [s.l.] : Nature Publishing Group
    Nature 263 (1976), S. 514-515 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Fig. 1 Photomicrographs of histological sections of transformation ossicles from control (a) and hypophysectomised (b) rats stained with haematoxylin and eosin. a, Haematopoietic cells on day 26 in a control rat. b, Scattered basophilic cells in a hypophysectomised rat. Hypophysectomy on day 0 (x ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/263514a0
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  • 8
    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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  • 9
    Electronic Resource
    Electronic Resource
    Influence of vitamin A on matrix-induced endochondral bone formation (1983)
    Springer
    Calcified tissue international 35 (1983), S. 732-739 
    Details
    ISSN: 1432-0827
    Keywords: Mesenchymol cell proliferation ; Chondrogenesis ; Osteogenesis ; Proteoglycans
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary The influence of retinoic acid on matrix-induced endochondral bone differentiation was determined. Retinoic acid was administered during discrete stages of endochondral bone formation, specifically, mesenchymal cell proliferation, chondrogenesis, bone formation, and mineralization. In retinoic acid-treated rats examined on day 3 following matrix implantation, biochemical markers for mesenchymal cell proliferation were about 50% of the controls. Chondrogenesis on day 7, assessed by35SO4 incorporation into proteoglycans, was 27% of the control. In addition, dissociative extraction of proteoglycans with 4.0 M guanidine-HCl and chromatography on Sepharose CL-2B revealed the synthesis of a smaller molecular weight proteoglycan when compared to controls which exhibited the cartilage-specific type. Osteogenesis and bone mineralization were monitored by alkaline phosphatase activity and45Ca incorporation. On day 11 alkaline phosphatase activity was decreased by 40% and45Ca incorporation was 48% of the control. These results revealed the multiple foci of the actions of excess vitamin A.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02405115
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  • 10
    Electronic Resource
    Electronic Resource
    Changes in proline synthetic and degradative enzymes during matrix-induced cartilage and bone formation (1979)
    Springer
    Calcified tissue international 27 (1979), S. 275-279 
    Details
    ISSN: 1432-0827
    Keywords: Proline ; Cartilage ; Bone
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary Proline biosynthetic and degradative enzymes are unevenly distributed in differentiated mammalian tissues. Activities of the synthetic enzymes are relatively high in collagenous tissues, whereas activities of the degradative enzymes are high in noncollagenous tissues. In order to further characterize tissue-specific proline biosynthesis and degradation, we have determined proline enzyme activities during cartilage and bone formation induced by demineralized bone matrix. We can thus follow temporal changes in enzyme activity in a single tissue as different cell types develop. Ornithine aminotransferase and pyrroline-5-carboxylate reductase have peaks of activity which correlate with maximal type II collagen synthesis by chondrocytes. Both enzymes also are active during bone formation. In contrast, proline oxidase and pyrroline-5-carboxylate dehydrogenase are present at low levels and do not change as new cell types appear. Arginase activity peaks during the first 3 days and then rapidly decreases by the time cartilage and bone formation begin. These observations further substantiate the importance of proline biosynthesis in collagenous tissues. The close correlation between ornithine aminotransferase activity and type II collagen synthesis suggests that the pathway from ornithine to proline may be especially important during formation of type II collagen.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02441197
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