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  • 1
    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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  • 2
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Gamete Research 13 (1986), S. 115-124 
    ISSN: 0148-7280
    Keywords: oocyte maturation ; glycosaminoglycan ; heparin ; heparan sulfate ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Oocyte maturation-preventing factor (OMPF) was extracted from bovine granulosa cells with a buffer containing 1 M urea and 5 mM EDTA. OMPF was partially purified by gel filtration on Sephadex G25 and by reversed-phase high performance liquid chromatography. The maturation-preventing activity of purified fractions was determined by measuring their capacity to block the spontaneous dissolution of the germinal vesicle (GVBD) of isolated cumulus-enclosed mouse oocytes. Hyaluronic acid, chondroitin sulfate, heparin, heparan sulfate, keratan sulfate, and dextran sulfate at concentrations of 500 μg/ml did not affect the frequency of GVBD of isolated mouse oocytes. Heparin and heparan sulfate, however, blocked the inhibitory effect of OMPF, whereas the inhibition of GVBD induced with dibutyryl cAMP, forskolin, W7 (calmodulin antagonist), and 3-isobutyl-l-methylxanthine (phosphodiesterase inhibitor) was not blocked. OMPF was eluted in the adsorbed fraction when chromatographed on heparin-Agarose, showing interaction of OMPF with heparin. The present results suggest that the glycosaminoglycan matrix may influence OMPF action on oocytes.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: 5′-Methylthioadenosine (MTA) is formed from decarboxylated S-adenosylme-thionine during biosynthesis of polyamines. This nucleoside is cleaved by methylthioadenosine phosphorylase (MTA Pase) to adenine and 5-methyl-thioribose-l-phosphate in mammalian cells. 5′-Difluoromethylthioadenosine (DFMTA), a synthetic analog of MTA, was not a substrate for MTA Pase, but was a strong competitive inhibitor of the enzyme (Ki = 0.48 μM). DFMTA caused marked accumulation of labeled MTA formed from [35S]methionine in Raji cells, which contain MTA Pase, but not in CCRF-CEM cells, which do not contain this enzyme, suggesting that it also inhibits the enzyme in intact cells. DFMTA inhibited the growth of a variety of cultured cells and its cytostatic effect was roughly proportional to the MTA Pase activity of the cells. MTA also depressed the growth of cultured cells but, in contrast with DFMTA, its inhibitory effect was greater in MTA Pase-deficient cells (CCRF-CEM) than MTA Pase-containing cells (Raji). Inhibition of growth of Raji cells by DFMTA was partially reversed by exogenous adenine, a reaction product of MTA Pase. These results suggest that the utilization of adenine formed from MTA was important for proliferation of cells containing MTA Pase under the culture conditions employed, and that DFMTA inhibited cell growth by inhibiting MTA Pase activity.
    Additional Material: 2 Ill.
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  • 4
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Acidic and basic fibroblast growth factors (FGFs) are characterized by their high affinity for heparin and their capacity to stimulate angiogenesis in vivo. While both molecules are structurally distinct they have 53% homology in their primary sequence and exist in similar molecular forms. These heparin-binding growth factors are also characterized by a wide distribution, a characteristic that may be attributable, at least in part, to their production by endothelial cells and their storage in the extracellular matrix. Structure-function studies with synthetic fragments of basic FGF have identified two peptidic sequences that cross-react with FGF receptor and that can modulate the cellular response to basic FGF. Both functional domains bind radiolabeled heparin, inhibit cell growth, and can interfere with stimulation of neurite outgrowth, cell adhesion, and differentiated cell function. The possible application of these antagonists to defining the role of FGF in wound repair, nerve regeneration, and vascularization of the vasovasorum is discussed.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
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