Study on Apoptosis of Human Promyelocytic Leukemia HL-60 Cells Induced by Fucosterol via Mitochondrial Pathway

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The purpose of this study is to investigate the effect of fucosterol on the induction of apoptosis and the molecular mechanism involved in Human promyelocytic leukemia HL-60 Cells. HL-60 Cells were treated with different concentrations of fucosterol at different time. MTT method was used to study fucosterol anti-tumor activity. Morphology observation was performed to determine the effects of fucosterol on apoptosis of HL-60 cells. Flow cytometry (FCM) was used to detect the cell cycle. Laser scanning confocal microscope (LSCM) was used to analyze mitochondrial membrane potential (MMP). Western blot was performed to analyze the expressions of Cyt-C, Caspase-9 and Caspase-3. The results showed fucosterol could inhibit the growth of HL-60 cells, and the apoptosis morphology for 48 h treatment was obvious, which showed cell protuberance, cytoplasm concentrated and apoptotic body. Fucosterol treatment for 24 h decreased MMP in dose-dependent manners. It also induced the release of Cyt-C and the activation of Caspase-9 and-3. In conclusion, Fucosterol could induce HL-60 cells apoptosis through a mitochondrial pathway.

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611-614

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September 2013

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© 2013 Trans Tech Publications Ltd. All Rights Reserved

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[1] Yoo MS, Shin JS, Choi HE, et al. Fucosterol isolated from Undaria pinnatifida inhibits lipo-polysaccharide-induced production of nitric oxide and pro-inflammatory cytokines via the inactivation of nuclear factor-κB and p.38 mitogen-activated protein kinase in RAW264. 7 macrophages. Food Chem. Vol. 135 (2012).

DOI: 10.1016/j.foodchem.2012.05.039

Google Scholar

[2] Khanavi M, Gheidarloo R, Sadati N, et al. Cytotoxicity of fucosterol containing fraction of marine algae against breast and colon carcinoma cell line. Pharmacogn Mag. Vol. 8 (2012), p.60.

DOI: 10.4103/0973-1296.93327

Google Scholar

[3] Lee JM. The mitochondrial permeability transition pore: A molecular target for amyotrophic lateral sclerosis therapy. BBA-Mol Basis Dis. Vol. 1802 (2010), p.186.

DOI: 10.1016/j.bbadis.2009.07.009

Google Scholar

[4] Lemeshko W. Potential-dependent membrane permeabilization and mitochondrial aggregation caused by anticancer polyarginine-KLA peptides. Arch Biochem Biophy. Vol. 493 (2010), p.213.

DOI: 10.1016/j.abb.2009.11.004

Google Scholar

[5] Luca S. Opening the doors to cytochrome c: Changes in mitochondrial shape and apoptosis. Int J Biochem Cell B. Vol. 41 (2010), p.1875.

Google Scholar

[6] Dos Santos A B, Dorta DJ, Pestana CR, et al. Dehydromonocrotaline induces cyclosporine A-insensitive mitochondrial permeability transition/cytochrome c release. Toxicon. Vol. 54 (2009), p.16.

DOI: 10.1016/j.toxicon.2009.03.004

Google Scholar

[7] Lee HJ, Lee HJ, Lee EO, et al. Mitochondria-cytochrome C-caspase-9 cascade mediates isorhamnetin-induced apoptosis. Cancer Lett. Vol. 270 (2008), p.342.

DOI: 10.1016/j.canlet.2008.05.040

Google Scholar