Supplementation of Annatto (Bixa orellana)-Derived δ-Tocotrienol Produced High Number of Morula through Increased Expression of 3-Phosphoinositide- Dependent Protein Kinase-1 (PDK1) in Mice
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Supplementation of Annatto (Bixa orellana)-Derived δ-Tocotrienol Produced High Number of Morula through Increased Expression of 3-Phosphoinositide- Dependent Protein Kinase-1 (PDK1) in Mice

Authors: S. M. M. Syairah, M. H. Rajikin, A-R. Sharaniza

Abstract:

Several embryonic cellular mechanism including cell cycle, growth and apoptosis are regulated by phosphatidylinositol-3- kinase (PI3K)/Akt signaling pathway. The goal of present study is to determine the effects of annatto (Bixa orellana)-derived δ-tocotrienol (δ-TCT) on the regulations of PI3K/Akt genes in murine morula. Twenty four 6-8 week old (23-25g) female balb/c mice were randomly divided into four groups (G1-G4; n=6). Those groups were subjected to the following treatments for 7 consecutive days: G1 (control) received tocopherol stripped corn oil, G2 was given 60 mg/kg/day of δ-TCT mixture (contains 90% delta & 10% gamma isomers), G3 was given 60 mg/kg/day of pure δ-TCT (>98% purity) and G4 received 60 mg/kg/day α-TOC. On Day 8, females were superovulated with 5 IU Pregnant Mare’s Serum Gonadotropin (PMSG) for 48 hours followed with 5 IU human Chorionic Gonadotropin (hCG) before mated with males at the ratio of 1:1. Females were sacrificed by cervical dislocation for embryo collection 48 hours post-coitum. About fifty morulas from each group were used in the gene expression analyses using Affymetrix QuantiGene Plex 2.0 Assay. Present data showed a significant increase (p<0.05) in the average number (mean + SEM) of morula produced in G2 (27.32 + 0.23), G3 (25.42 + 0.21) and G4 (27.21 + 0.34) compared to control group (G1 – 14.61 + 0.25). This is parallel with the high expression of PDK1 gene with increase of 2.75-fold (G2), 3.07-fold (G3) and 3.59-fold (G4) compared to G1. From the present data, it can be concluded that supplementation with δ-TCT(s) and α-TOC induced high expression of PDK1 in G2-G4 which enhanced the PI3K/Akt signaling activity, resulting in the increased number of morula.

Keywords: Embryonic development, morula, nicotine, vitamin E.

Digital Object Identifier (DOI): doi.org/10.5281/zenodo.1108018

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References:


[1] S. Sherman, Lawrence, et al. Human embryology. 3rd ed. Elsevier Publications, 2001.
[2] Marcader, Amparo et al. (2008) “Human embryo culture”. in Essential stem cell methods, Lanza, Robert & I. Klimanskaya, Ed. Academic Press, 2008, pp343.
[3] C. Lingyi, W. Dekun, W. Zhaoting, M. Liping, and Q. D. George, “Molecular basis of the first cell fate determination in mouse embryogenesis,” Cell Res., vol. 20, pp. 982-993, 2010.
[4] J. K. Riley, M. O. Carayannopoulos, A. H. Wyman, M. Chi, C. K. Ratajczak, and K. H. Moley, “The PI3K/Akt pathway is present and functional in the preimplantation mouse embryo,” Dev. Biol., vol. 284, pp.377-386, 2005.
[5] S. R. Datta, A. Brunet, and M. E. Greenberg, “Cellular survival: A play in three Akts,” Genes Dev., vol. 13, pp.2905-2927, 1999.
[6] F. J. A. Vara, E. Casado, J. de Castro, P. Cejas, C. Belda-Iniesta, and M. Gonzalez-Baron, “PI3K./Akt signaling pathway and cancer,” Cancer Treat.Rev. vol. 30, no.2, pp.193-204, 2004.
[7] M. A. Lawlor, and D. R. Alessi, “PKB/Akt: a key mediator of cell proliferation survival and insulin responses?” J. Cell Sci., vol. 114, pp.2903–10, 2001.
[8] D. A. Butterfield, A. Castegna, J. Drake, G. Scapagnini, and V. Calabrese “Vitamin E and neurodegenerative disorders associated with oxidative stress,” Nutr. Neurosci. vol. 5, pp.229-239, 2002.
[9] T. Koga, P. Kwan, L. Zubik, C. Ameho, D. Smith, and M. Meydani, “Vitamin E supplementation suppresses macrophage accumulation and endothelial cell expression of adhesion molecules in the aorta of hypercholesterolemic rabbits,” Atherosclerosis, vol. 176, no. 2, pp. 265- 272, 2004.
[10] W. N. Yap, P. N. Chang, H. Y. Han, D. T. W. Lee, M. T. Ling, Y. C. Wong, and Y. L. Yap, “γ-Tocotrienol suppresses prostate cancer cell proliferation and invasion through multiple-signalling pathways,” British Journal of Cancer, vol. 99, no. 11, pp.1832-1841, 2008.
[11] A. Nasibah, M. H. Rajikin, M .N. K. Nor-Ashikin, and A. S. Nuraliza, “Tocotrienol improves the quality of impaired mouse embryos induced by corticosterone,” in Conf. Rec. 2012 Symposium on Humanities, Science and Engineering Research (SHUSER2012), pp.135-138.
[12] A. Nasibah, M. H. Rajikin, M. N. K. Nor-Ashikin, and A. S. Nuraliza, “Effects of tocotrienol supplementation on pregnancy outcome in mice subjected to maternal corticosterone administration,” Journal of Oil Palm Research, vol. 24, pp. 1550-1558, 2012b.
[13] Y. S. Kamsani, M. H. Rajikin, M .N. K. Nor-Ashikin, A.S. Nuraliza, and A. Chatterjee, “Nicotine-induced cessation of embryonic development is reversed by γ-tocotrienol in mice,” Med. Sci. Monit. Basic Res, vol. 19, pp. 87-92, 2013.
[14] E. Lee, S. H. Min, B. S. Song, J. Y. Yeon, J. W. Kim, J. H. Bae, S. Y. Park, Y. H. Lee, S. U. Kim, D. S. Lee, K. T. Chang, and D.B. Koo, “Exogenous gamma-tocotrienol promotes preimplantation development and improves the quality of porcine embryos,” Reprod. Fertil. Dev., DOI 10.1071/RD13167, 2014.
[15] I. Miclea, M. Zhan, V. Miclea, A. Hettig, J. Roman, and F. Ghiuru, “Influence of alpha-tocopherol on swine embryo development,” Bulletin UASVM Animal Science and Biotechnologies, vol. 67, pp. 1-2, 2010.
[16] R. Natarajan, M. S. Bhawani, and M. Deecaraman, “Effect of α- tocopherol supplementation on in vitro maturation of sheep oocytes and in vitro development of preimplantation sheep embryos to the blastocyst stage,” J. Assist. Reprod. Genet.vol. 27, no. 8, pp. 483-490, 2010.
[17] D. A. Fruman, R. E. Meyers, and L. C. Cantley, “Phosphoinositide kinases,” Annual Review of Biochemistry, vol. 67, pp. 481-507, 1998.
[18] J. R. Bayascas, “Dissecting the role of the 3-phosphoinositide-dependent protein kinase-1 (PDK1) signaling pathways,” Cell Cycle, vol. 7, no. 19, pp. 2978-82, 2008.
[19] C. O’neill, “Phosphatidylinositol 3-kinase signaling in mammalian preimplantation embryo development,” Reprod. vol. 136, pp. 147-156, 2008.
[20] C. C. Milburn, M. Deak, S. M. Kelly, N. C. Price, D. R. Alessi, and A. D. M. Van, “Binding of phosphatidylinositol3,4,5-triphosphate to the pleckstrin homology domain of protein kinase B induces a conformational change,” Biochem J. vol. 1375, no. 3, pp. 531-538, 2003.
[21] K. George, and J. W. Michael, “Akt-dependent and –independent survival signaling pathways utilized by insulin-like growth factor,” Mol. Cell Biol. vol. 18, no. 11, pp. 6711-6718, 1998.
[22] A. M. Dieterle, P. Böhler, H. Keppeler, S. Alers, N. Berleth, S. DrieBen, N. Hieke, S. Pietkiewicz, A.S. Loffler, C. Peter, A. Gray, N.R. Leslie, H. Shinohara, T. Kurosaki, M. Engelke, J. Wienands, M. Bonin, S. Wesselborg and B. Stork, “PDK1 controls upstream PI3K expression and PIP3 generation,” Oncogene. vol. 33. no. 23. pp. 3043 – 3053, 2014.