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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Journal of bone and mineral metabolism 16 (1998), S. 151-157 
    ISSN: 1435-5604
    Keywords: Key words: osteoclast ; fusion ; preosteoclast ; osteoblast ; calcitonin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract: The osteoclasts, which play an essential role in bone resorption, are multinucleated cells (MNCs). They are formed by the fusion of mononuclear preosteoclasts (pOCs). However, because of the difficulty of isolating the pOCs, the process of fusion of pOCs has not been elucidated. To establish a fusion assay system, we succeeded in isolating pOCs that are not contaminated with MNCs and osteoblastic cells from the coculture of mouse bone marrow cells and osteoblastic cells. When pOCs were cultured in the presence of osteoblastic cells, the fusion of pOCs into MNCs took place within 24 h. No MNCs were formed in the absence of osteoblastic cells. The number of MNCs formed by the fusion of pOCs was dependent on the number of both pOCs and osteoblastic cells in the culture. Osteoblastic cells were also required for bone resorption by the osteoclasts that were formed by the fusion of pOCs. Osteotropic hormones, such as 1α,25-dihydroxy vitamin D3 [1α,25(OH)2D3] and parathyroid hormone (PTH), did not affect the fusion and pit formation of pOCs in the absence of osteoblastic cells. Eel calcitonin (eCT), however, significantly inhibited the fusion of pOCs induced by osteoblastic cells. These results suggest that the fusion of pOCs was induced by the direct contact between pOCs and osteoblastic cells..
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1617-4623
    Keywords: F plasmid ; Plasmid stability ; DNA binding protein ; SopB protein
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The mini-F plasmid has the trans-acting sopA, sopB genes and the cis-acting sopC DNA which are essential for plasmid partitioning. In this paper, we report the purification of the sopB gene product from extracts of cells harboring a pBR322 derivative carrying the sopB gene. The purity of the final preparation was more than 95%, as determined by densitometry. The amino acid sequence of the amino-terminal region of the protein for the 17 residues identified was identical to that predicted from the DNA sequence of the sopB gene. Therefore, it was concluded that the protein was the sopB gene product. Using anti-SopB serum, the SopB protein was detected in the cell lysates of F+, F′, and Hfr strains. The SopB protein bound to the plasmid DNA of a pBR322 derivative carrying the sopC DNA segment, but not to the vector plasmid pBR322.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Molecular genetics and genomics 234 (1992), S. 346-352 
    ISSN: 1617-4623
    Keywords: F plasmid ; SopA protein ; ATPase ; Plasmid stability
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The SopA, B, C genes of the F plasmid play an essential role in plasmid partitioning during cell division in Escherichia coli. In this paper, the products of the sopA and sopB genes were isolated and their biochemical activities studied. [α-32P]ATP was cross-linked to the SopA protein by UV irradiation; this cross-linking was observed only in the presence of magnesium ion, and was competitively inhibited in the presence of non-radioactive ATP, ADP and dATP, but not other NTPs or dNTPs. In contrast, no ATP binding activity was detected for the SopB protein. The SopA protein showed a modest magnesium ion-dependent ATPase activity and this activity was stimulated in the presence of DNA. The ATPase activity in the presence of DNA was further stimulated by addition of the SopB protein. However, the SopB protein alone failed to stimulate the ATPase activity.
    Type of Medium: Electronic Resource
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