Apoptosis Activity of Persea declinata (Bl.) Kosterm Bark Methanolic Crude Extract
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Apoptosis Activity of Persea declinata (Bl.) Kosterm Bark Methanolic Crude Extract

Authors: P. Narrima, C. Y. Looi, M. A. Mohd, H. M. Ali

Abstract:

Persea declinata (Bl.) Kosterm is a member of the Lauraceae family, widely distributed in Southeast Asia. It is from the same genus with avocado (Persea americana Mill), which is widely consumed as food and for medicinal purposes. In the present study, we examined the anticancer properties of Persea declinata (Bl.) Kosterm bark methanolic crude extract (PDM). PDM exhibited a potent antiproliferative effect in MCF-7 human breast cancer cells, with an IC50 value of 16.68 .g/mL after 48h of treatment. We observed that PDM caused cell cycle arrest and subsequent apoptosis in MCF-7 cells, as exhibited by increased population at G0/G1 phase, higher lactate dehydrogenase (LDH) release, and DNA fragmentation. Mechanistic studies showed that PDM caused significant elevation in ROS production, leading to perturbation of mitochondrial membrane potential, cell permeability, and activation of caspases-3/7. On the other hand, real-time PCR and Western blot analysis showed that PDM treatment increased the expression of the proapoptotic molecule, Bax, but decreased the expression of prosurvival proteins, Bcl-2 and Bcl-xL, in a dose-dependent manner. These findings imply that PDM could inhibit proliferation in MCF-7 cells via cell cycle arrest and apoptosis induction, indicating its potential as a therapeutic agent worthy of further development.

Keywords: Antiproliferative, apoptosis, MCF-7 human breast cancer, Persea declinata.

Digital Object Identifier (DOI): doi.org/10.5281/zenodo.1096791

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References:


[1] K. H. Lee, “Antineoplastic agents and their analogues from Chinese traditional medicine,” in HumanMedicinal Agents from Plants, A. D. Kinghorn andM. Balandrin, Eds., vol. 534 of ACS Symposium Series, pp. 170–190, American Chemical Society, Washington, DC, USA, 1993.
[2] K.-H. Lee, “Anticancer drug design based on plant-derived natural products,” Journal of Biomedical Science, vol. 6, no. 4, pp. 236–250, 1999.
[3] H. Ding, Y.-W. Chin, A. D. Kinghorn, and S. M. D’Ambrosio, “Chemopreventive characteristics of avocado fruit,” Seminars in Cancer Biology, vol. 17, no. 5, pp. 386–394, 2007.
[4] V. R.Gummadi, S. Rajagopalan, C.Y. Looi et al., “Discovery of 7- azaindole based anaplastic lymphoma kinase (ALK) inhibitors: wild type and mutant (L1196M) active compounds with unique binding mode,” Bioorganic & Medicinal Chemistry Letters, vol. 23, no. 17, pp. 4911–4918, 2013.
[5] C. Y. Looi, M. Imanishi, S. Takaki et al., “Octa-Arginine mediated delivery of wild-type Lnk protein inhibits TPO-induced M-MOK megakaryoblastic leukemic cell growth by promoting apoptosis,” PLoS ONE, vol. 6, no. 8, article e23640, 2011.
[6] C. Y. Looi, B. Moharram, M. Paydar et al., “Induction of apoptosis in melanoma A375 cells by a chloroform fraction of Centratherum anthelminticum (L.) seeds involves NF-kappaB, p53 and Bcl-2- controlled mitochondrial signaling pathways,” BMC Complementary and Alternative Medicine, vol. 13, article 166, 2013.
[7] R. S. Ahmed, S. G. Suke, V. Seth, A. Chakraborti, A. K. Tripathi, and B.D. Banerjee, “Protective effects of dietaryginger (Zingiber officinales Rose) on lindane-induced oxidative stress in rats,” Phytotherapy Research, vol. 22, no. 7, pp. 902–906, 2008.
[8] R. S. Ahmed, S. G. Suke, V. Seth, A. Chakraborti, A. K. Tripathi, and B.D. Banerjee, “Protective effects of dietaryginger (Zingiber officinales Rose) on lindane-induced oxidative stress in rats,” Phytotherapy Research, vol. 22, no. 7, pp. 902–906, 2008.
[9] A. S. Naura and R. Sharma, “Toxic effects of hexaammine cobalt (III) chloride on liver and kidney in mice: implication of oxidative stress,” Drug and Chemical Toxicology, vol. 32, no. 3, pp. 293–299, 2009.
[10] J M. Germain, E. B. Affar, D. D’Amours, V. M. Dixit, G. S. Salvesen, and G. G. Poirier, “Cleavage of automodified poly(ADP-ribose) polymerase during apoptosis. Evidence for involvement of caspase-7,” The Journal of Biological Chemistry, vol. 274, no. 40, pp. 28379–28384, 1999.
[11] S. Shimizu, Y. Eguchi, W. Kamiike et al., “Bcl-2 blocks loss of mitochondrial membrane potential while ICE inhibitors act at a different step during inhibition of death induced by respiratory chain inhibitors,” Oncogene, vol. 13, no. 1, pp. 21–29, 1996.
[12] J. Yang, X. Liu, K. Bhalla et al., “Prevention of apoptosis by Bcl2: release of cytochrome c frommitochondria blocked,” Science, vol. 275, no. 5303, pp. 1129–1132, 1997.
[13] Y. Hu, M. A. Benedict, D. Wu, N. Inohara, and G. Nunez, “Bcl-XL interacts with Apaf-1 and inhibits Apaf-1-dependent caspase-9 activation,” Proceedings of the National Academy of Sciences of the United States of America, vol. 95, no. 8, pp. 4386–4391, 1998.