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  • 2000-2004  (3)
  • cell proliferation  (2)
  • 12-O-Tetradecanoyl phorbol 13-acetate (TPA)  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Membrane expression of annexin I is enhanced by calcium and TPA in cultured human keratinocytes (2000)
    Springer
    Archives of dermatological research 292 (2000), S. 496-499 
    Details
    ISSN: 1432-069X
    Keywords: Key words Keratinization ; Cornified envelope ; 12-O-Tetradecanoyl phorbol 13-acetate (TPA) ; Epinephrine
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract  Annexin I plays an important role in the process of keratinization as a component of the cornified envelope. To elucidate the function of annexin I in keratinization, we investigated the effects of calcium, epinephrine, hydrocortisone, and 12-O-tetradecanoyl phorbol 13-acetate (TPA) on the expression and localization of annexin I in cultured human keratinocytes. Normal human keratinocytes were cultured in serum-free culture medium (0.15 mM calcium) until 70% confluence. After incubation with a higher concentration of calcium (1.8 mM), TPA (100 nM), epinephrine (50 ÌM), or hydrocortisone (10 ÌM) for 24 h, the expression of annexin I protein and mRNA was examined using immunofluorescence, Western blot, and Northern blot techniques. Immunofluorescence microscopy showed increased membrane staining of annexin I by calcium, which was inhibited by the addition of epinephrine or hydrocortisone. Western blotting confirmed elevated annexin I on the cell membrane. It was increased in the cell membrane fraction, but not in the cytosol fraction. Interestingly, the mRNA level of annexin I was slightly reduced after incubation with calcium, whereas TPA upregulated both membrane expression and the mRNA level. Secretion of annexin I was increased by TPA but inhibited by calcium. Because calcium and TPA are known to promote keratinization, our data suggest that annexin I expression on the cell membrane is involved in the process of keratinization.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004030000172
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Tissue Factor and Cancer Procoagulant Expressed by Glioma Cells Participate in their Thrombin-mediated Proliferation (2000)
    Springer
    Journal of neuro-oncology 46 (2000), S. 1-9 
    Details
    ISSN: 1573-7373
    Keywords: glioma ; coagulation cascade ; tissue factor ; cancer procoagulant ; thrombin ; cell proliferation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The relationship between coagulation cascade activation and glioma cell proliferation was examined. The human glioma cell lines T98G, TM-1 and normal human astrocyte cell strain (NHA) were examined. Using anti-tissue factor (TF) antibody, immunocytochemical detection of TF antigen was obtained in both cell lines and cell strain. TF antigen in cell lysates was also measured by enzyme linked immunosorbent assay (ELISA). In a one-stage clotting assay, T98G, TM-1 and NHA revealed procoagulant activity (PCA) in normal human plasma and factor VII deficient plasma. PCA in normal human plasma was significantly inhibited by both inhibitory anti-TF antibody and cysteine protease inhibitor HgCl2. This result indicates that T98G, TM-1 and NHA cells express not only TF but also cancer procoagulant (CP) at the same time. In a cell proliferation assay, thrombin induced proliferation in T98G and TM-1 cells in a dose-dependent fashion and in NHA cell in a bell-shaped fashion. This mitogenic stimulant was inhibited by the specific thrombin inhibitor hirudin. The combinations of coagulation factors II, V, and X with or without factor VII induced proliferation in T98G, TM-1, and NHA cells. The maximal mitogenic stimulatory effects were larger in glioma cells than in NHA. These mitogenic stimulatory effects were also inhibited by hirudin. Each coagulation factor on its own or in any other combination of coagulation factors had no proliferative effect. Thus, these mitogenic stimulatory effects were considered to be the effect of thrombin. In conclusion, T98G and TM-1 human glioma cells express two different types of procoagulants TF and CP. In the presence of coagulation factors, these glioma cells can generate thrombin and this thrombin generation is capable of inducing glioma cell proliferation in vitro.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006323200001
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Molecular cloning and characterization of OsPSK, a gene encoding a precursor for phytosulfokine-α, required for rice cell proliferation (2000)
    Springer
    Plant molecular biology 44 (2000), S. 635-647 
    Details
    ISSN: 1573-5028
    Keywords: cell proliferation ; peptide plant growth factor ; phytosulfokine ; promoter ; transcriptional enhancer ; transformed rice cell
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We previously characterized an OsPSK cDNA encoding a precursor of phytosulfokine-α (PSK-α), a peptide plant growth factor. Southern blot analysis suggested that OsPSK is a single-copy gene in rice, which we have isolated and characterized. The OsPSK gene consists of one large intron and two exons. The 5-amino acid PSK-α sequence located close to the COOH-terminus of the precursor is encoded in the second exon. A putative TATA box was found at position −68 with respect to the transcription initiation site. Upstream of this sequence, several potential regulatory elements, including one CAAT-box, three CCAAT-boxes, one enhancer core-like sequence, and three E-boxes could be identified. By constructing plasmids with various lengths of the 5′-upstream regions of the OsPSK gene fused to the coding sequence for bacterial β-glucuronidase (GUS), we demonstrated a region 1.9 kb upstream of the transcription initiation point, which contains most of the putative 5′-regulatory elements, to be sufficient for maximal-level GUS expression in transformed rice Oc cells. The promoter of the OsPSK gene gave significantly higher levels of GUS expression than the CaMV 35S promoter. These results suggest that the OsPSK promoter could be useful for the constitutive expression of a foreign gene at high levels in transformed rice culture cells. Northern blot analyses suggest that the expression of OsPSK is reinforced by auxin and cytokinin.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1026576423870
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    Paper (German National Licenses)
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