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  • 1
    Electronic Resource
    Electronic Resource
    Further characterization of interaction between bone sialoprotein (BSP) and collagen (1995)
    Springer
    Calcified tissue international 56 (1995), S. 140-144 
    Details
    ISSN: 1432-0827
    Keywords: Bone sialoprotein ; Collagen ; Hole zone ; Calcification
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Abstract Bone sialoprotein (BSP) has an affinity to collagen fibrils [25]. A role of carbohydrate chains in the affinity was examined by removing sialic acids of BSP. Neuraminidase treatment of the BSP increased the binding to collagen. Binding sites of BSP on collagen were examined by biochemical and electron-microscopic methods. Purified bovine BSP was labeled with biotin. Collagen α chains or CNBr peptides were separated by electrophoresis and transfered to nitrocellulose membranes. The membranes were incubated with the biotin-labeled BSP, and the bound BSP was visualized with avidin conjugated with alkaline phosphatase. The labeled BSP was preferentially bound to the α 2 chain, and peptides derived from α 2 chain. In another experiment, the labeled BSP was incubated with reconstituted native collagen fibrils. The mixture was put on a copper grid, reacted with avidin conjugated with gold particles, and observed with an electron microscope. The gold particles were seen mainly within hole zones of the fibrils. BSP bound to the α 2 chain within the hole zones may regulate the onset of calcification at hole zones and the cell binding to collagen fibrils.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00296346
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Stimulation by bone sialoprotein of calcification in osteoblast-like MC3T3-E1 cells (1995)
    Springer
    Calcified tissue international 56 (1995), S. 403-407 
    Details
    ISSN: 1432-0827
    Keywords: Bone sialoprotein ; Fibronectin ; Type I colfagen ; MC3T3-E1 cells ; Calcification
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Abstract Bone sialoprotein (BSP) containing an Arg-Gly-Asp cell-binding sequence was purified from bovine bone 4 M guanidine-HCl extract after HCl demineralization by a series of chromatographic procedures. When this protein was coated on culture dishes in the presence of type I collagen, it increased both DNA content and alkaline phosphatase (ALP) activity in osteoblast-like MC3T3-E1 cells, and stimulated calcification in the cells, whereas fibronectin, another cell-binding protein, showed a marked increase in the DNA content but had little effect on the ALP activity. These findings suggest that BSP is mitogenic for preosteoblasts and differentiating the cells into osteoblasts, thereby stimulating bone calcification
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00301610
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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