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KMID : 0613820120220010016
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Journal of Life Science
2012 Volume.22 No. 1 p.16 ~ p.24
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Modulation of Adhesion Proteins Integrin β1 and FAK, and Cytoskeletal Protein Actin by Spermine in MCF-7 Cells
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Jee Hye-Jin
Kim Byeong-Gee
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Abstract
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Polyamines are essential for cell growth and differentiation; however their precise roles are unclear yet. In the present study, the cytotoxic effect of spermine (spm) on MCF-7 cells was investigated. In the MTT assay of MCF-7 cells treated with spm, cell viability was significantly decreased in a time-and dose-dependent manner. Cell viability measurement was confirmed by trypan blue staining. FACS analysis shows that sub-G1 was increased in a time-and dose-dependent manner too. When the cells were treated with spm, cells started to show morphological changes within 2 hrs. The expression of adhesion proteins (FAK and integrin β1), and cytoskeletal protein (actin) was checked by Western blotting analysis. Integrin β1 levels were slightly decreased, and FAK and actin levels were rapidly decreased with spm treatment. In confocal laser scanning microscopy, the distribution of actin did not change but the expression decreased in a dose-dependent manner with spm treatment. FAK was evenly distributed under the plasma membrane in the untreated control. However, at 10 μM spm FAK seemed to move toward the cell nucleus. Integrin β1, which was mainly found in the focal point of the plasma membrane in the untreated control, dispersed through the entire plasma membrane in spm treatment. The present results indicate that cytotoxic effects of spm are triggered by the disruption of adhesion proteins and cytoskeletal protein.
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KEYWORD
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Actin, ECM, FAK, Integrin, spermine
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