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  • 1
    Electronic Resource
    Electronic Resource
    Copenhagen : Munksgaard International Publishers
    Journal of periodontal research 36 (2001), S. 0 
    ISSN: 1600-0765
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Osteopontin (OPN) is a major glycosylated phosphoprotein in bone matrix and is produced by several cells including osteoblasts, osteoclasts and macrophages. OPN levels increase in active sites of bone metabolism. Recently, several bone-related proteins were identified in gingival crevicular fluid (GCF) to seek markers of alveolar bone resorption in periodontal disease. In this study, we investigated the existence of OPN in GCF and the correlation between OPN level in GCF and probing depth (PD) of sampling sites in 98 periodontitis patients and 35 healthy subjects. An immunoblotting analysis using 10% polyacrylamide gel showed that two forms of OPN with molecular masses of 54 and 66 kDa and several degraded fragments were detected in most GCF samples from diseased sites (PD ≥4 mm). In GCF samples from healthy sites (PD ≤3 mm), only one form (54 kDa) was observed, but any degraded fragments were not detected. When OPN amounts in GCF samples were determined by ELISA, a weak, but significant correlation was observed between OPN amount in GCF and PD (r=0.32, p=0.0013). These results demonstrate that OPN exists in GCF and that OPN level in GCF increases with the progression of periodontal disease.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1600-0765
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Objectives:  Calprotectin is a cytosolic protein with antibacterial action in leukocytes and its level increases in some inflammatory diseases, including periodontal diseases, rheumatoid arthritis and ulcerative colitis. Recently, we found that the lipopolysaccharide of Porphyromonas gingivalis (P-LPS) induced calprotectin release from human neutrophils. P-LPS, a major virulence factor of periodontal pathogens, is known to induce the production and release of inflammatory cytokines through CD14, Toll-like receptor (TLR) and nuclear factor κB (NF-κB). In the present study, we investigated whether calprotectin release by P-LPS is induced via the CD14–TLR–NF-κB pathway and the cellular mechanism of calprotectin release in human neutrophils.Material and methods:  Human neutrophils were isolated from the peripheral blood of healthy donors and pre-incubated in medium containing antibodies against CD14, TLR2 and TLR4, or several inhibitors of NF-κB, microtubules and microfilaments, and then incubated with P-LPS. The calprotectin amount in the culture medium was determined using ELISA, and the nuclear extracts from cells were used for the examination of NF-κB binding activity using electrophoretic mobility shift assays.Results:  P-LPS increased calprotectin release from neutrophils and its induction was inhibited by anti-CD14 and anti-TLR2 antibodies, but not by two anti-TLR4 antibodies. NF-κB inhibitors suppressed P-LPS-induced NF-κB binding activity and calprotectin release. The inhibitors of microtubule and microfilament polymerization significantly decreased P-LPS-induced calprotectin release.Conclusion:  These results suggest that calprotectin release is induced by P-LPS via the CD14–TLR2–NF-κB signal pathway in human neutrophils and may be dependent on microtubule and microfilament systems.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Oxford, UK : Munksgaard International Publishers
    Journal of periodontal research 38 (2003), S. 0 
    ISSN: 1600-0765
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Objectives:  Cyclosporin A (CsA), an immunosuppressive agent, induces fibrous gingival overgrowth through reduction of collagen phagocytosis by fibroblasts. Distinct receptors are involved in the binding of collagen to fibroblasts in collagen phagocytosis, and α2β1 integrin serves as a specific receptor for type I collagen on fibroblasts. To elucidate the role of α2β1 integrin in CsA-induced gingival overgrowth, we investigated collagen phagocytosis and α2β1 integrin expression in rat gingival fibroblasts.Materials and methods:  Fibroblats were isolated from gingiva of rats fed a powdered diet containing or lacking CsA for 30 d. Flow cytometric analysis were performed to measure the collagen phagocytosis and the α2 integrin expression in fibroblasts. Furthermore, total RNAs were isolated from fibroblasts, and the reverse transcriptase-polymerase chain reaction was employed to investigate the mRNA levels of α2 integrin.Results:  In vitro collagen phagocytosis assay revealed that CsA-treated and control fibroblasts contained a mean of 13.5% and 36.1% phagocytic cells, respectively. CsA-treated fibroblasts had 28% lower expression of α2 integrin than that of control. and mRNA expression of α2 integrin in CsA-treated fibroblasts was apparently lower than in the controls, but the mRNA expression of β1 integrin was not affected.Conclusion:  These findings suggest that one etiological factor of gingival overgrowth may be inhibition of collagen phagocytosis by reducing α2 integrin expression in gingival fibroblasts.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1600-0765
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 1600-051X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract. Clinical and biochemical markers of periodontal disease have been used for precise objective diagnosis of periodontal inflammation. Interleukin 1-β (IL-1β) and prostaglandin E2 (PGE2), inflammatory factors, levels in gingival crevicular fluid (GCF) of patients with periodontal disease are elevated and have been studied as biochemical markers. The levels of calprotectin, a leukocyte protein, in body fluids of patients with some inflammatory diseases are raised. Recently, we detected calprotectin in GCF and its concentrations in periodontal pockets were higher than those in healthy gingival crevices. In this study, we investigated the correlations between GCF calprotectin levels and clinical indicators (probing depth and bleeding on probing, BOP), and the IL-1β or PGE2 levels in GCF. Probing depth and BOP at 130 sites of 110 subjects with periodontal or other oral diseases were examined, then GCF samples were collected and their calprotectin, IL-1β and PGE2 were determined by ELISA. The calprotectin level correlated positively with the probing depth and was significantly higher at BOP-positive than BOP-negative sites. There were significant, positive correlations between the calprotectin and IL-1β or PGE2 concentrations. These results indicate that the calprotectin level in GCF correlates well with clinical and biochemical markers of periodontal disease and suggest that calprotectin may be useful for evaluating the extent of periodontal inflammation.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Springer
    Journal of bone and mineral metabolism 6 (1988), S. 26-31 
    ISSN: 1435-5604
    Keywords: dental pulp ; alkaline phosphatase ; dentinogenesis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The distribution of alkaline phosphatase in dentinogenically active bovine dental pulp tissues was investigated histochemically and biochemically. Histochemical observation showed a high enzyme activity in the subodontoblastic layer, especially in coronal pulp and also in the core of radicular pulp. Biochemical results were well consistent with histochemical findings. Alkaline phosphatase activity in the coronal pulp was twice that in radicular pulp. Most of the enzyme activity in coronal pulp was in the subodontoblastic layer (91%), whereas the activity in the radicular pulp was evenly distributed. Since undifferentiated mesenchymal cells were observed in the areas showing relatively high ALPase activity, it seemed that there were some relations between the inducion of ALPase and the undifferentiated mesenchymal cells.
    Type of Medium: Electronic Resource
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  • 7
    ISSN: 1435-5604
    Keywords: parathyroid hormone ; receptors ; osteoprogenitor cells ; differentiation ; cAMP
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The number of parathyroid hormone (PTH) receptors in rat calvaria (RC) cells increased with culture duration, reached a maximum on day 13 when the cells had not yet differentiated into osteoblasts, and then gradually decreased by day 21. However, short exposure (48h) of RC cells to PTH-(1–34) before day 12, but not after day 15, did not decrease alkaline phosphatase (ALP) activity of the cells. Bone-like nodule (BN) formation was also suppressed only when PTH-(1–34) was present during the late culture period (days 14–21). Pretreating the cells with staurosporine, a protein kinase C inhibitor, on day 7 resulted in augmentation of PTH-(1–34)-induced cyclic adenosine monophosphate (cAMP) accumulation and inhibition of ALP activity. PTH-(7–34), which only activates PKC, however, had no effect on RC cell differentiation under any conditions used.
    Type of Medium: Electronic Resource
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  • 8
    ISSN: 0730-2312
    Keywords: human prostatic cancer cell (PC-3) ; osteoblastic cell differentiation ; bone nodule formation ; alkaline phosphatase activity ; osteocalcin ; osteopontin ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Human prostatic carcinoma frequently metastasizes to bone tissue and activates bone metabolism, especially bone formation, at the site of metastasis. It has been reported that an extract of prostatic carcinoma and conditioned medium (CM) of a human prostatic carcinoma cell line, PC-3, established from a bone metastastic lesion, stimulate osteoblastic cell proliferation. However, there is little information about the effect of PC-3 CM on the differentiation of osteoblastic cells. In this study, we investigated the effect of PC-3 CM on the differentiation of two types of osteoblastic cells, primary fetal rat calvaria (RC) cells containing many undifferentiated osteoprogenitor cells, and ROS 17/2.8, a well-differentiated rat osteosarcoma cell line. PC-3 CM inhibited bone nodule formation and the activity of alkaline phosphatase (ALPase), an osteoblastic marker enzyme, on days 7, 14, and 21 (RC cells) or 3, 6, and 9 (ROS 17/2.8 cells) in a dose-dependent manner (5-30% CM). However, the CM did not affect cell proliferation or cell viability. PC-3 CM was found to markedly block the gene expression of ALPase and osteocalcin (OCN) mRNAs but had no effect on the mRNA expression of osteopontin (OPN), the latter two being noncollagenous proteins related to bone matrix mineralization. These findings suggest that PC-3 CM contains a factor that inhibits osteoblastic cell differentiation and that this factor may be involved in the process of bone metastasis from prostatic carcinoma. J. Cell. Biochem. 67:248-256, 1997. © 1997 Wiley-Liss, Inc.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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