Search Results - (Author, Cooperation:S. Ivanovski)
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1Latest Papers from Table of Contents or Articles in PressA. Rotundi ; H. Sierks ; V. Della Corte ; M. Fulle ; P. J. Gutierrez ; L. Lara ; C. Barbieri ; P. L. Lamy ; R. Rodrigo ; D. Koschny ; H. Rickman ; H. U. Keller ; J. J. Lopez-Moreno ; M. Accolla ; J. Agarwal ; M. F. A'Hearn ; N. Altobelli ; F. Angrilli ; M. A. Barucci ; J. L. Bertaux ; I. Bertini ; D. Bodewits ; E. Bussoletti ; L. Colangeli ; M. Cosi ; G. Cremonese ; J. F. Crifo ; V. Da Deppo ; B. Davidsson ; S. Debei ; M. De Cecco ; F. Esposito ; M. Ferrari ; S. Fornasier ; F. Giovane ; B. Gustafson ; S. F. Green ; O. Groussin ; E. Grun ; C. Guttler ; M. L. Herranz ; S. F. Hviid ; W. Ip ; S. Ivanovski ; J. M. Jeronimo ; L. Jorda ; J. Knollenberg ; R. Kramm ; E. Kuhrt ; M. Kuppers ; M. Lazzarin ; M. R. Leese ; A. C. Lopez-Jimenez ; F. Lucarelli ; S. C. Lowry ; F. Marzari ; E. M. Epifani ; J. A. McDonnell ; V. Mennella ; H. Michalik ; A. Molina ; R. Morales ; F. Moreno ; S. Mottola ; G. Naletto ; N. Oklay ; J. L. Ortiz ; E. Palomba ; P. Palumbo ; J. M. Perrin ; J. Rodriguez ; L. Sabau ; C. Snodgrass ; R. Sordini ; N. Thomas ; C. Tubiana ; J. B. Vincent ; P. Weissman ; K. P. Wenzel ; V. Zakharov ; J. C. Zarnecki
American Association for the Advancement of Science (AAAS)
Published 2015Staff ViewPublication Date: 2015-01-24Publisher: American Association for the Advancement of Science (AAAS)Print ISSN: 0036-8075Electronic ISSN: 1095-9203Topics: BiologyChemistry and PharmacologyComputer ScienceMedicineNatural Sciences in GeneralPhysicsPublished by: -
2Articles: DFG German National LicensesIvanovski, S. ; Li, H. ; Daley, T. ; Bartold, P. M.
Copenhagen : Munksgaard International Publishers
Published 2000Staff ViewISSN: 1600-0765Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: MedicineNotes: Guided tissue regeneration (GTR) is a clinical procedure developed to facilitate periodontal regeneration by using barrier membranes to selectively promote the repopulation of a periodontal defect by periodontal ligament and bone cells at the expense of epithelial and gingival connective tissue cells. The aim of this study was to gain insight into the biological events occurring during membrane mediated periodontal wound healing by examining the immunohistochemical expression of a number of extracellular matrix components in tissues treated via the GTR technique. Experimental periodontal defects were created around the second premolar tooth in 4 dogs and wound closure was achieved by application of expanded polytetrafluoroethylene membranes around each tooth and flap positioning coronal to the cemento–enamel junction. The dogs were sacrificed after a 4-wk healing period, block dissections of the part of the mandible containing the experimental tooth were obtained and paraffin sections were prepared. Using standard immunohistochemical techniques, the sections were stained with a monoclonal antibody against bone morphogenetic proteins 2 and 4 (BMP-2 and -4) and polyclonal antibodies against collagen I, collagen III, decorin, biglycan, bone sialoprotein, osteopontin and osteocalcin. Collagen I was predominantly localized within the regenerating bone, whereas collagen III staining was more abundant in the soft connective tissues of the defect. Decorin and biglycan staining was faint within the extracellular matrix of the regenerating defect, although both proteoglycans exhibited intense intracellular localization within some of the cells inhabiting the defect. The staining for BMP-2 and -4 was weak within the bone but strong within the extracellular matrix of the regenerating soft tissue. Osteopontin and bone sialoprotein were strongly localized in the regenerating bone and cementum found within the defect. Osteocalcin staining was present in both the regenerating and mature cementum and associated cementoblasts, and it was relatively weaker in the regenerating bone compared to the mature bone. The observed pattern of immunolocalization of the extracellular matrix macromolecules suggests that the heterogeneous cell population filling the GTR wound had created an environment that was conducive to periodontal regeneration.Type of Medium: Electronic ResourceURL: -
3Articles: DFG German National LicensesIvanovski, S. ; Li, H. ; Haase, H. R. ; Bartold, P. M.
Copenhagen : Munksgaard International Publishers
Published 2001Staff ViewISSN: 1600-0765Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: MedicineNotes: The expression of hard tissue associated proteins may be used to identify periodontal fibroblasts with the capability to facilitate periodontal regeneration. The aim of this study was to describe, by immunohistochemistry, the distribution of osteocalcin, osteopontin, bone sialoprotein and bone morphogenic proteins-2 and -4 (BMP-2 and BMP-4) within the human periodontium. Furthermore, the expression of mRNA for the above proteins and alkaline phosphatase by gingival and periodontal ligament fibroblasts in vitro was also assessed by reverse transcriptase polymerase chain reaction (RT-PCR). Localization of osteopontin, osteocalcin, BMP-2 and BMP-4 within sections of human periodontal structures was stronger in the periodontal ligament compared to the gingiva. Bone sialoprotein was not detected in either of the soft tissues but, along with osteopontin and osteocalcin, it was localized in the cementum and bone. In vitro, both the gingival and periodontal ligament fibroblasts expressed mRNA for alkaline phosphatase, BMP-2, BMP-4 and osteopontin. Although there were no differences in the expression of alkaline phosphatase and BMP-4 mRNA between the two cell types, we noted significantly higher mRNA levels of osteopontin in the periodontal ligament and BMP-2 in the gingival fibroblasts. Osteocalcin and bone sialoprotein mRNA expression was only noted in the cultured periodontal ligament fibroblasts. From these results, it can be concluded that distinct differences exist between the two fibroblast populations in terms of the localization and mRNA expression of the majority of the hard tissue associated proteins. Furthermore, the elevated in vitro mRNA expression for osteocalcin, osteopontin and bone sialoprotein may be used to identify cells with the potential to facilitate hard tissue formation and hence periodontal regeneration.Type of Medium: Electronic ResourceURL: -
4Articles: DFG German National LicensesHaase, H. R. ; Ivanovski, S. ; Waters, M. J. ; Bartold, P. M.
Oxford, UK : Munksgaard International Publishers
Published 2003Staff ViewISSN: 1600-0765Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: MedicineNotes: Background: Growth hormone (GH) is a potent regulator of bone formation. The proposed mechanism of GH action is through the stimulation of osteogenic precursor cell proliferation and, following clonal expansion of these cells, promotion of differentiation along the osteogenic lineage.Objectives: We tested this hypothesis by studying the effects of GH on primary cell populations of human periodontal ligament cells (PLC) and alveolar bone cells (ABC), which contain a spectrum of osteogenic precursors.Methods: The cell populations were assessed for mineralization potential after long-term culture in media containing β-glycerophosphate and ascorbic acid, by the demonstration of mineral deposition by Von Kossa staining. The proliferative response of the cells to GH was determined over a 48-h period using a crystal violet dye-binding assay. The profile of the cells in terms of osteogenic marker expression was established using quantitative reverse transcriptase polymerase chain reaction (RT-PCR) for alkaline phosphatase (ALP), osteopontin, osteocalcin, bone sialoprotein (BSP), as well as the bone morphogenetic proteins BMP-2, BMP-4 and BMP-7.Results: As expected, a variety of responses were observed ranging from no mineralization in the PLC populations to dense mineralized deposition observed in one GH-treated ABC population. Over a 48-h period GH was found to be non-mitogenic for all cell populations. Quantitative reverse transcriptase polymerase chain reaction (RT-PCR) BSP mRNA expression correlated well with mineralizing potential of the cells. The change in the mRNA expression of the osteogenic markers was determined following GH treatment of the cells over a 48-h period. GH caused an increase in ALP in most cell populations, and also in BMP expression in some cell populations. However a decrease in BSP, osteocalcin and osteopontin expression in the more highly differentiated cell populations was observed in response to GH.Conclusion: The response of the cells indicates that while long-term treatment with GH may promote mineralization, short-term treatment does not promote proliferation of osteoblast precursors nor induce expression of late osteogenic markers.Type of Medium: Electronic ResourceURL: -
5Articles: DFG German National LicensesIvanovski, S. ; Komaki, M. ; Bartold, P. M. ; Narayanan, A. S.
Oxford, UK : Blackwell Publishing Ltd
Published 1999Staff ViewISSN: 1600-0765Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: MedicineNotes: A specific collagenous cementum attachment protein (CAP) has been identified in human cementum which promotes selective cell migration towards and attachment of various periodontal derived cell populations to root surfaces in vitro. The CAP is known to support attachment of periodontal-derived cell via an RGD motif, which suggests an integrin-mediated mode of attachment. The purpose of the present study was to ascertain which integrin(s) are involved in the attachment of periodontal-derived cells to CAP. The integrins examined comprised subunits of the major receptors for fibronectin (α5) and collagen (α2, α3), as well as the common β1 subunit which is present in many extracellular matrix receptors. The wells of 48-well non-tissue culture treated plates were coated with CAP (2 μg/ml). For negative and positive controls the wells were coated with bovine serum albumin and fibronectin (5 μg/ml), respectively. Human gingival fibroblasts and periodontal ligament fibroblasts were labeled with [3H]-proline, incubated with anti-integrin antibodies and added to the pre-coated wells. Attachment was assessed after incubating the cells for 1 h at 37°C in the presence of the antibodies. Antibodies to α5 and β1 inhibited the attachment of both human gingival fibroblasts and human periodontal ligament fibroblasts to CAP, while anti α2 and α3 antibodies did not affect the attachment. The binding of the fibroblasts to fibronectin was also inhibited by anti-α2 and α3 antibodies, both of which are components of the “classical” fibronectin receptor and remained unaffected by the addition of anti-α2 and α3 antibodies. Proteins migrating in SDS-polyacrylamide gels in positions similar to the α5 and β1 integrin subunits were present in fractions bound to a column of CAP coupled to Sepharose CL-4B. These results indicate that the attachment to CAP of the periodontal-derived cells, human gingival fibroblasts and human periodontal ligament fibroblasts, is mediated primarily via the integrin α5β1.Type of Medium: Electronic ResourceURL: