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  • 1995-1999  (3)
  • Key words: BMP-2 — BMP-3 — BMP-4 — mRNA expression — Paracrine — Bone cell differentiation.  (1)
  • Key words: osteoclasts  (1)
  • Life and Medical Sciences  (1)
  • 1
    ISSN: 1432-0827
    Keywords: Key words: BMP-2 — BMP-3 — BMP-4 — mRNA expression — Paracrine — Bone cell differentiation.
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Abstract. Normal bone formation is a prolonged process that is carefully regulated and involves sequential expression of growth regulatory factors by osteoblasts as they proliferate and ultimately differentiate. Since this orderly sequence of gene expression by osteoblasts suggests a cascade effect, and BMP-2 is capable of initiating and maintaining this effect, we examined the effects of BMP-2 on expression of other BMPs and compared these effects with the expression pattern of bone cell differentiation marker genes in primary cultures of fetal rat calvarial (FRC) osteoblasts. To examine the gene expression profile during bone cell differentiation and bone formation, we also examined the effects of rBMP-2 on bone formation in vivo and in vitro. rBMP-2 stimulated bone formation on the periosteal surface of mice when 500 ng/day rBMP-2 was injected subcutaneously. When rBMP-2 was added to primary cultures of FRC osteoblasts, it accelerated mineralized nodule formation in a time and concentration-dependent manner (10–40 ng/ml). rBMP-2 (40 ng/ml) enhanced BMP-3 and -4 mRNA expression during the mineralization phase of primary cultures of FRC osteoblasts. Enhancement of BMP-3 and -4 mRNA expression by rBMP-2 was associated with increased expression of bone cell differentiation marker genes, alkaline phosphatase (ALP), type I collagen, osteocalcin (OC), osteopontin (OP), and bone sialoprotein (BSP). These results suggest that BMP-2 enhances expression of other BMP genes during bone cell differentiation. BMP-2 may act in a paracrine fashion in concert with other BMPs it induces to stimulate bone cell differentiation and bone formation during remodeling.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1435-5604
    Keywords: Key words: osteoclasts ; resorption ; assay ; bacterial surface-associated proteins ; osteomyelitis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract: Staphylococcus aureus infection of bone causes severe bone damage but the mechanisms responsible remain to be established. We used the protein-rich fraction released by saline extraction of Staphylococcus aureus (SAM) to test the hypothesis that the surface-associated proteins promote bone breakdown by directly activating osteoclasts. Isolated chick osteoclasts were incubated on dentine slices with or without the surface protein fraction from S. aureus. The resulting osteoclastic excavations were measured using confocal reflection microscopic surface mapping. SAM both stimulated the formation of resorption pits and induced the production of pits with larger volume : area ratios..
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 57 (1995), S. 351-361 
    ISSN: 0730-2312
    Keywords: cell cycle ; cell division ; protein phosphorylation ; phosphotyrosine ; caffeine ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Changes in protein tyrosine phosphorylation are known to be important for regulating cell cycle progression. With the aim of identifying new proteins involved in the regulation of mitosis, we used an antibody against phosphotyrosine to analyze proteins from synchronized human and hamster cells. At least seven proteins were found that displayed mitosis-specific tyrosine phosphorylation in HeLa cells (pp165, 205, 240, 250, 270, 290, and ∼ 400) and one such protein in hamster BHK cells (pp155). In synchronized HeLa and BHK cells, all proteins except HeLa pp165, pp205, and pp250 were readily detectable only in mitosis. Tyrosine phosphorylation of pp165, pp205, and pp250 was apparent during arrest in S phase, suggesting that cell cycle perturbations can affect the phosphorylation state of some of these proteins. In a related finding in BHK cells, pp155 underwent tyrosine phosphorylation when cells were forced into premature mitosis by caffeine treatment. Only one protein (pp135 in HeLa cells) was found to be dephosphorylated on tyrosine during mitosis. The above findings may prove helpful for isolating new cell cycle proteins that are important for both the normal regulation of mitosis and the mitotic aberrations associated with cell cycle perturbations and chemical treatments.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
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