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- W2079752891 abstract "Entamoeba histolytica, and invasive enteric protozoa, kills mammalian target cells by sequential adherence and cytolytic events. Using platinum plate electrodes with an alternating current source placed in a Wheatstone bridge circuit, the impedance (resistance to ion flow) of a cell suspension of axenic amebae (strain HM1-IMSS) was measured. The impedance of the amebic cell suspension, expressed as resistivity (in ohm-cm), was significantly greater than the test solution and increased with decreasing temperature or greater cell packing (P < 0.01), indicating that the resistivity measurements reflected the impedance of the amebic surface membrane. Cytochalasin D (10 μg/ml), a microfilament inhibitor which inhibited amebic in vitro adherence and cytolysis of target Chinese hamster ovary (CHO) cells (P < 0.001), also increased resistivity of the amebic suspension (P < 0.01). Exposure of amebae to bepridil (105 M), a slow-channel blocker, inhibited amebic killing of target cells (P < 0.01) and also increased the resistivity of the amebic suspension (P < 0.01), but both to a lesser degree than cytochalasin D (P < 0.001). In contrast, exposure of amebae to verapamil followed by washing had no effect on amebic killing of target cells or resistivity of the amebic suspension. The increased resistivity measured in cytochalasin D or following exposure to bepridil was not due to a change in cell density of the amebic suspension. These studies indicate that changes in impedance of the amebic surface membrane are produced by bepridil and cytochalasin D. The effect of these agents on membrane impedance may contribute directly to the concurrent observed alteration in amebic cytopathogenic capacity or may serve as a parallel marker for the cell membrane alterations induced by such pharmacologic agents which inhibit amebic microfilament function or calcium flux." @default.
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- W2079752891 title "Entamoeba histolytica: Impedance measurements and cytotoxicity in the presence of bepridil, verapamil, and cytochalasin D" @default.
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- W2079752891 doi "https://doi.org/10.1016/s0014-4894(85)80023-0" @default.
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