Actin is one of the major constituents of the cytoskeleton in eukaryotic cells. A large number of cellular processes, including cytokinesis, endocytosis and chemotaxis are mediated by polymerization of actin filaments. Actin as a cytoskeletal protein is believed to be connected with chromatin reorganization in the cell nucleus as well as with apoptosis. Previous studies showed actin association with RNA polymerases and suggest significance of actin in transcription. The main purpose of this study is the evaluation of fibrilar actin (F- actin) reorganization in nuclei isolated from the human leukemia cell line HL-60, after induction of apoptosis, using arsenic trioxide (As₂O₃). The cells were treated with three different doses of cytostatic drug during 24 hours. Nuclei were isolated and purified by centrifugation in gradient of glycerol. Purity and integrity of isolated nuclei were determined spectrophotometrically and with the use of transmission electron microscopy (TEM). Changes in F- actin organization were qualitative performed by fluorescence microscopy with the use of phallacidin - BODIPY and semi-quantitative measured by flow cytometry assay. Morphological features of apoptosis were observed in light and fluorescence microscope.

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