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  • cytoskeleton  (1)
  • ionophore  (1)
  • video microscopy  (1)
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  • 1
    Digitale Medien
    Digitale Medien
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 4 (1984), S. 57-71 
    ISSN: 0886-1544
    Schlagwort(e): actin ; calcium ; coelomocytes ; ionophore ; pH ; shape transformation ; video microscopy ; Life and Medical Sciences ; Cell & Developmental Biology
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Biologie , Medizin
    Notizen: We have investigated the ability of the Ca+ + ionophore A23187 to induce the transformation of petaloid sea urchin coleomocytes to the filopodial form. The response of individual cells to different media was observed with time-lapse phasecontrast video microscopy. In the presence of 1 mM CaCl2, isotonic medium containing 1-5 μM A23187 produces a similar shape transformation to that caused by hypotonic shock. Higher concentrations of ionophore (10-20 μM) induce the formation of filopodia that are thinner and less rigid than those generated by hypotonic shock or low doses of ionophore. A23187 also induces shape transformation in highly flattened cells that do not respond fully to hypotonic shock. The induction of cytoplasmic alkalinization by NH4Cl, methylamine-HCl, or the Na+ ionophore monensin does not induce shape transformation, suggesting that increased intracellular pH is not the stimulus for this process. Ultrastructural changes in cytoskeletal organization were examined in negatively stained detergent-extracted cells. Low doses of ionophore produce filopodia that are indistin-guishable from those of hypotonically shocked cells, with actin filament bundles that are straight and cohesive along their entire length. High concentrations of ionophore produce filopodia with filament bundles that branch repeatedly and splay apart near their tips, forming loops and irregular curves. These results suggest that an increase in intracellular free Ca+ + concentration acts as the trigger that stimulates coelomocyte shape transformation, but that abnormally high concentrations of intracellular Ca+ +, produced by high doses of ionophore, interfere with actin filament bundling.
    Zusätzliches Material: 8 Ill.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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  • 2
    Digitale Medien
    Digitale Medien
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 7 (1987), S. 304-314 
    ISSN: 0886-1544
    Schlagwort(e): spectrin-like ; actin-binding protein ; Ca++-regulated ; cytoskeleton ; eggs ; Life and Medical Sciences ; Cell & Developmental Biology
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Biologie , Medizin
    Notizen: Sea urchin egg spectrin has been purified from a homogenate of unfertilized Strongylocentrotus purpuratus eggs using standard biochemical procedures. SDS-PAGE analysis of the molecule revealed a closely spaced, high molecular weight doublet at 237/234 kDa (present in an equimolar ratio). Rotary shadowed images of egg spectrin revealed a double-stranded, elongate, flexible rod-shaped contour, measuring 210 nm in length and ∼ 4-8 nm in width. Additionally, this molecule is shown to be immunologically related to avian erythroid spectrin, since it cross-reacts with antibodies prepared against the chicken erythrocyte α-spectrin/240 kDa subunit. The interaction of egg spectrin with actin was examined by sedimentation and falling-ball viscometry assays. The binding and cross linking properties of spectrin to actin demonstrate a unique Ca++-sensitive regulation at micromolar Ca++ concentrations. This observation provides new insight into the way Ca++ may regulate spectrin-actin interactions in vitro and further suggests possible structural and modulatory roles for egg spectrin in the developing sea urchin embryo.
    Zusätzliches Material: 6 Ill.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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