Studies On 3/7 Caspase Activity And Apoptosis Induction By Diarylheptaniods Isolated From Garuga Pinnata Roxb
Main Article Content
Abstract
This study aims to evaluate the stimulation of caspase 3/7, 8 and 9 activity and induction of apoptosis by the diarylheptanoids isolated from Garuga pinnata (G. pinnata) RoxB. Garuganin 1, 3, 4 and 5 which were previously reported for their isolation have tested for their anticancer potencies by different caspase activation and apoptosis induction in MCF-7 and HCT-15 cell lines. However, based on the MTT assay results (Previously reported) Garuganin 3 and 5 were selected for this study. from the stem bark of G. pinnata. The activation of caspases 3/7, 8, and 9 is a conformational process of cancer cell death. Such activation of caspases by different concentrations (05, 10, 15, 20
Downloads
Article Details
This work is licensed under a Creative Commons Attribution 4.0 International License.
References
Ellis, H.M., Horvitz, H.R. (1986). Genetic control of programmed cell death in the nematode C. elegans. Cell, 44 ( 6 ), 817–829.
Yuan, J., Shaham, S., Ledoux, S., Ellis, H.M., Horvitz, H.R. (1993). The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1 beta-converting enzyme. Cell, 75 (4 ), 641–652.
Kumar, S., Tomooka, Y., Noda, M. (1992). Identification of a set of genes with developmentally down-regulated expression in the mouse brain. Biochem Biophys Res Commun, 185 ( 3 ), 1155–1161.
Eckhart, L., Ballaun, C., Hermann, M., VandeBerg, J.L., Sipos, W., Uthman, A. (2008). Identification of novel mammalian caspases reveals an important role of gene loss in shaping the human caspase repertoire. Mol Biol Evol, 25 (5 ), 831–841.
Fischer, H., Koenig, U., Eckhart L., Tschachler, E. (2002). Human caspase 12 has acquired deleterious mutations. Biochem Biophys Res Commun, 293 (2), 722–726.
Hoste, E., Kemperman, P., Devos, M., Denecker, G., Kezic, S., Yau, N. (2011). Caspase-14 is required for filaggrin degradation to natural moisturizing factors in the skin. J Invest Dermatol, 131 (11), 2233–2241.
Schulze-Osthoff, K., Ferrari, D, Los, M., Wesselborg, S., Peter, M.E. (1998). Apoptosis signaling by death receptors. Eur J Biochem, 254 (3), 439–459.
Hengartner, M.O. ( 2000). The biochemistry of apoptosis. Nature, 407 (1), 770–777.
Srilekha, K., Rajender V., Kireety S.A., Narashimulu, Devendar, B., Thupurani, M.K. (2003). Antiproliferative, molecular docking, and bioavailability studies of diarylheptanoids isolated from stem bark of Garuga pinnata Rox B. 3 Biotech, 13 (1), 208
Debatin, K. M (1997). Anticancer drugs, programmed cell death and the immune system: defining new roles in an old play. J Natl Cancer Inst, 89 (11), 750–753.
Herr, I., Debatin, K.M. (2001). Cellular stress response and apoptosis in cancer therapy. Blood, 98 (9), 2603–2614.
Leppa, S., Bohmann, D. (1999). Diverse functions of JNK signaling and c-Jun in stress response and apoptosis. Oncogene, 18 (3), 6158–6162.
Davis, R,J. (2000). Signal transduction by the JNK group of MAP kinases. Cell, 103 (2 ), 239–252.
Kaufmann, SH. (1989). Induction of endonucleolytic DNA cleavage in human acute myelogenous leukemia cells by etoposide, camptothecin, and other cytotoxic anticancer drugs: A cautionary note. Cancer Res, 49 (21), 5870–5878.
Earnshaw, W.C., Martins, L.M., Kaufmann, S. H (1999). Mammalian caspases: Structure, activation, substrates, and functions during apoptosis. Annu Rev Biochem, 68 (1), 383–424.