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Biomedical subjects

P Mark Bartold

Publications and source records attributed to P Mark Bartold.

At least 19 recordsLinked to original sources
PubMed2006

Immunohistochemical study of bone sialoprotein and osteopontin in healthy and diseased root surfaces.

BACKGROUND: Periodontal disease is marked by inflammation and damage to tooth-supporting tissues. In particular, damage occurs to factors present in cementum that are thought to have the ability to influence the regeneration of surrounding tissues. Bone sialoprotein and osteopontin are major non-collagenous proteins in mineralized connective tissues associated with precementoblast chemo-attraction, adhesion to the root surface, and cell differentiation. The purpose of this investigation was to determine whether the expression and distribution of bone sialoprotein and osteopontin on root surfaces affected by periodontitis are altered compared to healthy, non-diseased root surfaces. METHODS: Thirty healthy and 30 periodontitis-affected teeth were collected. Following fixation and demineralization, specimens were embedded in paraffin, sectioned, and exposed to antibodies against bone sialoprotein and osteopontin. Stained sections were assessed using light microscopy. RESULTS: Bone sialoprotein was not detected in the exposed cementum (absence of overlying periodontal ligament) of diseased teeth. In most areas where the periodontal ligament was intact, bone sialoprotein was detected for healthy and diseased teeth. For teeth reactive for bone sialoprotein, the matrix of the cementum just below the periodontal ligament was moderately stained. A similar immunoreactivity pattern for osteopontin was observed. CONCLUSIONS: The absence of bone sialoprotein and osteopontin staining along exposed cementum surfaces may be due to structural and compositional changes in matrix components associated with periodontal disease. This may influence the ability for regeneration and new connective tissue attachment onto previously diseased root surfaces.

Alveolar Process↗
PubMed2005

Production of osteopontin by cultured porcine epithelial cell rests of Malassez.

BACKGROUND: The epithelial cell rests of Malassez (ERM) are derived from Hertwig's epithelial root sheath (HERS). During development the cells of HERS deposit a variety of molecules on the newly forming root surface. The possibility that ERM retain this potential after root development is completed and secrete bone or cementum-related proteins needs to be investigated. The purpose of this study was to determine the expression of the non-collagenous proteins osteopontin (OPN) and bone sialoprotein (BSP) by cells derived from the epithelial cell rests of porcine periodontium. METHODS: ERM and fibroblasts were cultured from porcine periodontal ligament. The cells were identified and characterized using transmission electron microscopy, immunohistochemistry, western blot analysis of proteins, reverse transcription-polymerase chain reaction and ability to form mineralized nodules in culture. In particular the expression of the mineralized tissue-related proteins, BSP and OPN, was studied. RESULTS: Cells from porcine periodontal ligaments were successfully cultured; separated and characterized as being of either an epithelial or fibroblastic phenotype. Although the ERM did not form mineralized nodules in culture, they did express a significant amount of mRNA for OPN. CONCLUSION: The results from this study provide evidence that ERM express mRNA for at least one bone/cementum-related protein. Whether this function would be consistent with a role for ERM in tissue formation, inflammation and regeneration remains to be established.

Alveolar Process↗
PubMed2004

Development and transplantation of a mineralized matrix formed by osteoblasts in vitro for bone regeneration.

The use of extracellular matrix materials as scaffolds for the repair and regeneration of tissues is receiving increased attention. The current study was undertaken to test whether extracellular matrix formed by osteoblasts in vitro could be used as a scaffold for osteoblast transplantation and induce new bone formation in critical size osseous defects in vivo. Human osteoblasts derived from alveolar bone were cultured in six-well plates until confluent and then in mineralization media for a further period of 3 weeks to form an osteoblast--mineralized matrix complex. Histologically, at this time point a tissue structure with a "connective tissue"-like morphology was formed. Type I collagen was the major extracellular component present and appeared to determine the matrix macrostructure. Other bone-related proteins such as alkaline phosphatase (ALP), bone morphogenetic protein (BMP)-2 and -4, bone sialoprotein (BSP), osteopontin (OPN), and osteocalcin (OCN) also accumulated in the matrix. The osteoblasts embedded in this matrix expressed mRNAs for these bone-related proteins very strongly. Nodules of calcification were detected in the matrix and there was a correlation between calcification and the distribution of BSP and OPN. When this matrix was transplanted into a critical size bone defect in skulls of immunodeficient mice (SCID), new bone formation occurred. Furthermore, the cells inside the matrix survived and proliferated in the recipient sites, and were traceable by the human-specific Alu gene sequence using in situ hybridization. It was found that bone-forming cells differentiated from both transplanted human osteoblasts and activated endogenous mesenchymal cells. This study indicates that a mineralized matrix, formed by human osteoblasts in vitro, can be used as a scaffold for osteoblast transplantation, which subsequently can induce new bone formation.

Animals↗