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Study on the endocytosis and the internalization mechanism of aminosilane-coated Fe3O4 nanoparticles in vitro

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Abstract

In this study, the endocytosis and the internalization mechanism of aminosilane-coated Fe3O4 nanoparticles into human lung cancer cell line SPC-A1 was studied compared with human lung cell line WI-38 in vitro. The particle endocytosis behavior was studied by using Transmission Electron Microscope (TEM) and Coupled Plasma-Atomic Emission Spectrometry (ICP-AES). It was found that aminosilane-coated Fe3O4 nanoparticles could be greatly taken up by SPC-A1 human cancer cells (202 pg iron/cell) but not by WI-38 human lung cells (13 pg iron/cell). The particles could be retained in SPC-A1 cells over a number of generations in vitro. Different endocytosis was observed by TEM after SPC-A1 cells were treated with different temperature or with/without Cytochalasin B (Inhibitor of phagocytosis) at 37 °C. No nanoparticles were taken up by SPC-A1 after the endocytosis inhibited in low temperature. Restoring the endocytosis activity at 37 °C, the process of nanoparticles from coated pit to endosomes and lysosomes was observed by TEM. Endocytosis activity was effectively inhibited by the presence of Cytochalasin B at 37 °C, while a lot of nanoparticles were uptaken to the cytoplasm of SPC-A1 cells in the control group. Our results suggest that the process of endocytosis of aminosilane-coated Fe3O4 nanoparticles can efficiently takes place in lung cancer cells and nanoparticles can be kept in cancer cells for generations. Phagocytosis may be involved in the internalization process of aminosilane-coated Fe3O4 nanoparticles.

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Acknowledgements

This work was supported by 863 Hi-Tech Research and Development Program 2004AA302023 and 2005AA302H10.

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Correspondence to Hong-Chen Gu.

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Ma, YJ., Gu, HC. Study on the endocytosis and the internalization mechanism of aminosilane-coated Fe3O4 nanoparticles in vitro. J Mater Sci: Mater Med 18, 2145–2149 (2007). https://doi.org/10.1007/s10856-007-3015-8

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  • DOI: https://doi.org/10.1007/s10856-007-3015-8

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