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  • Key words: Osteoclast — Monocyte — Macrophage — Differentiation — Bone Resorption.  (1)
  • Oleandomycin  (1)
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  • Springer  (2)
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  • Springer  (2)
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  • 1
    ISSN: 1432-0827
    Keywords: Key words: Osteoclast — Monocyte — Macrophage — Differentiation — Bone Resorption.
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Abstract. Mononuclear precursors of the human osteoclast have been identified in both bone marrow and the circulation in man, but osteoclast membership of the mononuclear phagocyte system (MPS) and its precise cellular ontogeny remain controversial. We isolated human hematopoietic marrow cells, blood monocytes, and peritoneal macrophages and incubated each of these cell populations with UMR106 osteoblast-like cells on glass coverslips and dentine slices in both the presence and absence of 1,25 dihydroxyvitamin D3 (1,25(OH)2D3), macrophage-colony stimulating factor (M-CSF), and dexamethasone. Cells isolated from peripheral blood and peritoneal dialysis fluid were positive only for monocyte/macrophage markers (CD11a, CD11b, CD14, and HLA-DR) and negative for osteoclast markers [tartrate-resistant acid phosphatase (TRAP), vitronectin reception (VNR), and calcitonin (CT) receptors and did not form resorption pits on dentine slices after 24 hours in culture. Similarly marrow cells did not form resorption pits on dentine slices after 24 hours in culture. However, after 14 days in co-culture with UMR106 cells, in the presence of 1,25(OH)2D3 and M-CSF, numerous TRAP, CT receptor, and VNR-positive multinucleated cells capable of extensive lacunar resorption were formed in co-cultures of all these preparations. The presence of 1,25 (OH)2D3, M-CSF, and UMR106 were absolute requirements for osteoclast differentiation. It is concluded that precursor cells capable of osteoclast differentiation are present in the marrow compartment, the monocyte fraction of peripheral blood, and in the macrophage compartment of extraskeletal tissues and that these cells are capable of differentiating into mature functional osteoclasts. These findings argue in favor of osteoclast membership of the human MPS.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Journal of industrial microbiology and biotechnology 6 (1990), S. 295-297 
    ISSN: 1476-5535
    Keywords: Phosphorylation ; Oleandomycin ; Macrolide 2′-phosphotransferase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary An enzyme that catalyzes 2′-O-phosphorylation of oleandomycin and several other macrolide antibiotics has been purified approximately 47-fold from cell-free extracts ofStreptomyces coelicolor Müller, NRRL 3532 (UC™ 5240). The reaction product was verified as being oleandomycin-2′-O-phosphate by mass spectrometry. As a result of purification, the enzyme was separated from two lincosaminide inactivating enzyme activities also present in the cell-free extract.
    Type of Medium: Electronic Resource
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