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Formation of multinuclear cells induced by dimethyl sulfoxide: inhibition of cytokinesis and occurrence of novel nuclear division in dictyostelium cells
Our previous studies showed that 10 percent dimethyl sulfoxide (DMSO) induces the formation of actin microfilament bundles in the cell nucleus together with the dislocation of cortical microfilaments from the plasma membrane. The present study investigated the effects of DMSO on diverse activities m...
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Formato: | Texto |
Lenguaje: | English |
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The Rockefeller University Press
1980
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2110636/ https://www.ncbi.nlm.nih.gov/pubmed/6893450 |
Sumario: | Our previous studies showed that 10 percent dimethyl sulfoxide (DMSO) induces the formation of actin microfilament bundles in the cell nucleus together with the dislocation of cortical microfilaments from the plasma membrane. The present study investigated the effects of DMSO on diverse activities mediated by cellular microfilaments as the second step toward assessing potential differences between nuclear and cytoplasmic actins of dictyostelium mucoroides. DMSO was found to reversibly inhibit cell-to- glass as well as cell-to-cell adhesion, cell locomotion, and cell multiplication, whereas cytoplasmic streaming and phagocytosis were not obviously inhibited. Also, 5 percent DMSO inhibited cytokinesis but did not totally inhibit cell growth thus leading to the development of giant cells more than 10 times larger than normal cells. Transmission electron microscopy using serial thin sections showed the occurrence of multinucleation in the DMSO- induced giant cells. After the removal of DMSO, the giant multinuclear cells underwent multiple cytoplasmic cleavage producing normal-sized mononuclear cells. The nuclear division in the DMSO-induced giant cells was unique in that no spindle microtubules were formed, and vesicles appeared inside the nucleus forming a transverse partition of the nuclear envelope. The presence of actin filaments in those nuclei was demonstrated by a binding study with skeletal muscle myosin subfragment-1, and their possible involvement in this mode of nuclear division is discussed. |
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