Åsa Berglund

National Veterinary Institute, Sweden, Uppsala, Uppsala, Sweden

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Publications (4)11.9 Total impact

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    ABSTRACT: We have earlier reported that when a weak 50 Hz MF (magnetic field) was applied, the leukemic T-cell line Jurkat responded with intracellular calcium oscillations [Lindström, et al., J. Cell Physiol., 156 (1993) 395-398]. The result suggested that the MF interfered with the signal transduction, although neither target molecules nor molecular mechanisms are at present known. In this study we found that application of a MF to Jurkat cells resulted in significant increase of inositol 1,4,5-trisphosphate (IP3) levels. Chelation of intracellular calcium ions by BAPTA/AM, did not block the increase of IP3 induced by MF. This result implied that MF-induced Ca2+ oscillations were not due to direct stimulation of the Ca(2+)-dependent phospholipase C-gamma 1 (PLC-gamma 1).
    FEBS Letters 03/1995; 359(2-3):151-4. DOI:10.1016/0014-5793(95)00031-4 · 3.34 Impact Factor
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    Åsa Berglund · Lars Backman · Vithaldas P. Shanbhag
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    ABSTRACT: The binding of the isolated alpha-subunit of human erythrocyte spectrin to calmodulin is demonstrated by partitioning in aqueous two-phase systems. The affinity of the alpha-subunit for calmodulin is slightly higher than that of the spectrin dimer, whereas the beta-subunit interacts only very weakly. The binding is in all cases calcium-dependent and is abolished on addition of chlorpromazine. At an ionic strength close to physiological conditions, about 1 microM free calcium is required to induce maximum binding of calmodulin to spectrin dimer.
    FEBS Letters 07/1986; 201(2):306-10. DOI:10.1016/0014-5793(86)80629-9 · 3.34 Impact Factor
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    Åsa Berglund · Lars Backman · Vithaldas P. Shanbhag
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    ABSTRACT: Calmodulin is shown to interact with human spectrin dimer. The binding was highly calcium-dependent and observed in two different kinds of experiments. Firstly, affinity chromatography of calmodulin on a Sepharose 4B column with immobilized spectrin, and secondly, partition in aqueous two-phase polymer systems. In the column experiments stoichiometric amounts of calmodulin were retained on the spectrin-Sepharose column when micromolar concentrations of calcium were present. The calmodulin bound could be eluted with EGTA. The partition coefficient of calmodulin in an aqueous two-phase polymer system containing calcium was changed upon addition of spectrin, indicating an association between the two proteins. In the absence of calcium, spectrin did not cause any change in the partition behaviour of calmodulin, thus showing that the association requires calcium.
    FEBS Letters 07/1984; 172(1):109-13. DOI:10.1016/0014-5793(84)80884-4 · 3.34 Impact Factor
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    ABSTRACT: Interferon-alpha (IFN-alpha) subtypes bind to the same receptor and are expected to have the same biological functions. Whether or not leukocyte IFN, containing six major IFN-alpha proteins had the same anti-tumor effect as one subtype, recombinant IFN-alpha2b, was investigated. Three melanoma lines were treated with both types of IFN, and the effect on proliferation and survival was estimated both after short-term and prolonged treatment. All the melanoma cell lines were sensitive to the antiproliferative effects of both IFN species during short-term treatment. However, upon prolonged culture, the frequency of resistant colony formation was significantly higher in cultures treated with IFN-alpha2b compared to those treated with leukocyte IFN. There was a qualitative difference between the resistant colonies selected by the two IFN species with respect to morphology, growth rate and sensitivity to apoptosis. The development of resistant clones occurred at a lower rate during long-term treatment with leukocyte IFN containing six major subtypes of IFN-alpha as compared to IFN-alpha2b.
    Anticancer research 27(4B):2109-14. · 1.87 Impact Factor

Publication Stats

72 Citations
11.90 Total Impact Points

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Institutions

  • 1995
    • National Veterinary Institute, Sweden
      Uppsala, Uppsala, Sweden
  • 1984
    • Umeå University
      • Department of Medical Biochemistry and Biophysics
      Umeå, Västerbotten, Sweden