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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 24 (1986), S. 0 
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: To shed further light on the induction and characterization of thymus-derived mast cells, we cultured a variety of cell populations from murine thymus tissues (Balb/e) in the presence or absence of interleukin 3 (IL-3). The whole cell population and the nun-adherent T cell-depleted population developed mast cells. The morphological studies revealed granulated cells: the granules were stained with toluidine blue, alcian blue (pH 3.0). and metachromatic dyes. Electron microscope revealed altered mast cell granules. These cells contained relatively low amounts of histamine (- 1700 ng/106 cells), were IL.-3 (but not IL-2)-dependent, and did not possess T-cell. B-cell. or macrophage markers. No phagocytosis was observed. the cells also had 20α-hydroxysteroid dehydrogenase, and both IL-3 and IgE (145,600/cell) high affinity receptors. The frequency analysis showed 17 precursor cells per 106 thymic cells. The results indicate that the thymus indeed contains progenitors of mast cells responsive to IL-3, and that the mast cells are derived from non-T. non-phagocytic. and non-adherent cells of the thymus. Their T-lymphocyte product (IL.-3) dependency, ultrastructural appearance, granular stainability, and low content of histamine may support the view that the mast cells originating from the thymus probably belong to a mucosal must cell lineage.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 5 (1976), S. 0 
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Activated Factor B, incorporated into the cobra venom factor (CVF)-dependent C3/C5 convertase, was inactivated by diisopropylfluorophosphate (DFP). In-activation was time- and dose-dependent and was enhanced by the presence of substrate. Treatment of the zymogen of Factor B with DFP effected significant inactivation. Incorporation of [3H]diisopropylphosphate into the zymogen and into the activated form of Factor B was demonstrated after [3H]DFP treatment and subsequent electrophoresis of the proteins on polyacrylamide gels containing sodium dodecyl sulfate. Inactivation of activated C2 incorporated into the classical c5 convertase was observed on DFP treatment of the enzyme. DFP also reduced the activity of the C2 zymogen. The description of their serine proteinase nature further emphasizes the close structural and functional relationship of C2 and Factor B.
    Type of Medium: Electronic Resource
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