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Curcumin Protects SK-N-MC Cells from H2O2-Induced Cell Death by Modulation of Notch Signaling Pathway

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DOI: 10.4236/cellbio.2014.32008    3,480 Downloads   4,514 Views   Citations

ABSTRACT

Oxidative stress has been implicated to play a crucial role in the pathogenesis of Alzheimer’s disease (AD). Currently, it is known that numerous signaling pathways involved in neurodegenerative disorders are activated in response to oxidative stress. Recent directions on AD treatments have focused on the use of antioxidants including Curcumin, a hydrophobic polyphenol derived from the rhizome of the herb Curcuma longa, to augment the intracellular antioxidant defences. In the present study, hydrogen peroxide (H2O2) was used to evaluate the effects of oxidative stress on apoptotic SK-N-MC cells death with focus on changes in activity of Notch signaling pathway. The extent of lipid peroxidation, protein oxidation and intracellular ROS (Reactive Oxygen Species) levels was investigated as oxidative stress biomarkers. Here, we showed that H2O2 reduced GSH levels and activity of antioxidant enzymes and also influenced Notch signaling activation. The present data concluded that Curcumin protected cells against oxidative stress-induced apoptosis.

Conflicts of Interest

The authors declare no conflicts of interest.

Cite this paper

Kamarehei, M. , Yazdanparast, R. and Aghazadeh, S. (2014) Curcumin Protects SK-N-MC Cells from H2O2-Induced Cell Death by Modulation of Notch Signaling Pathway. CellBio, 3, 72-86. doi: 10.4236/cellbio.2014.32008.

References

[1] Cadenas, E. (2004) Mitochondrial Free Radical Production and Cell Signaling. Molecular Aspects of Medicine, 25, 17-26.
http://dx.doi.org/10.1016/j.mam.2004.02.005
[2] Cadenas, E. and Davies, K.J. (2000) Mitochondrial Free Radical Generation, Oxidative Stress, and Aging. Free Radical Biology and Medicine, 29, 222-230. http://dx.doi.org/10.1016/S0891-5849(00)00317-8
[3] Conde de la Rosa, L., Schoemaker, M., Vrenken, T., et al. (2006) Superoxide Anions and Hydrogen Peroxide Induce Hepatocyte Death by Different Mechanisms: Involvement of JNK and ERK MAP Kinases. Journal of Hepatology, 5, 918-929.
[4] Halliwell, B. and Aruoma, O.I. (1991) DNA Damage by Oxygen-Derived Species. Its Mechanism and Measurement in Mammalian Systems. FEBS Letters, 281, 9-19.
http://dx.doi.org/10.1016/0014-5793(91)80347-6
[5] Uttara, B., Singh, A., Zamboni, P., et al. (2009) Oxidative Stress and Neurodegenerative Diseases: A Review of Upstream and Downstream Antioxidant Therapeutic Options. Current Neuropharmacology, 7, 65-74.
http://dx.doi.org/10.2174/157015909787602823
[6] Rhee, S.G. (1991) Redox Signaling: Hydrogen Peroxide as Intracellular Messenger. Experimental and Molecular Medicine, 31, 53-59.
http://dx.doi.org/10.1038/emm.1999.9
[7] Bray, S. (1998) Notch Signaling in Drosophila: Three Ways to Use a Pathway. Cell and Developmental Biology, 9, 591-597.
http://dx.doi.org/10.1006/scdb.1998.0262
[8] Borggrefe, T. and Oswald, F. (2009) The Notch Signaling Pathway: Transcriptional Regulation at Notch Target Genes. Cell and Molecular Life Sciences, 10, 1631-1646.
http://dx.doi.org/10.1007/s00018-009-8668-7
[9] Yang, X., Klein, R., Tian, X., et al. (2004) Notch Activation Induces Apoptosis in Neural Progenitor Cells through a p53-Dependent Pathway. Developmental Biology, 269, 81-94.
http://dx.doi.org/10.1016/j.ydbio.2004.01.014
[10] Verdi, J.M., Schmandt, R., Bashirullah, A., et al. (1996) Mammalian Numb Is an Evolutionarily Conserved Signaling Adapter Protein That Specifies Cell Fate. Current Biology, 69, 1134-1145.
http://dx.doi.org/10.1016/S0960-9822(02)70680-5
[11] Prior, R.L. and Cao, G. (2000) Flavonoids: Diet and Health Relationships. Nutrition in Clinical Care, 2, 279-288.
http://dx.doi.org/10.1046/j.1523-5408.2000.00074.x
[12] Aggarwal, B.B., Kumar, A. and Bharti, A.C. (2003) Anticancer Potential of Curcumin: Preclinical and Clinical Studies. Anticancer Research, 23, 363-398.
[13] Sharma, O.P. (1976) Antioxidant Activity of Curcumin and Related Compounds. Biochemical Pharmacology, 25, 1811-1812.
http://dx.doi.org/10.1016/0006-2952(76)90421-4
[14] Srimal, R.C. and Dhawan, B.N. (1973) Pharmacology of Diferuloyl Methane (Curcumin), a Non-Steroidal Anti Inflammatory Agent. Journal of Pharmacy and Pharmacology, 25, 447-452.
http://dx.doi.org/10.1111/j.2042-7158.1973.tb09131.x
[15] Jordan, W.C. and Drew, C.R. (1996) Curcumin—A Natural Herb with Anti-HIV Activity. Journal of the National Medical Association, 88, 333.
[16] Kuttan, R., Bhanumathy, P., Nirmala, K. and George, M.C. (1985) Potential Anticancer Activity of Turmeric (Curcuma longa). Cancer Letters, 29, 197-202.
http://dx.doi.org/10.1016/0304-3835(85)90159-4
[17] Kiso, Y., Suzuki, Y., Watanabe, N., Oshima, Y. and Hikino, H. (1983) Antihepatotoxic Principles of Curcuma longa Rhizomes. Planta Medica, 49, 185-187.
http://dx.doi.org/10.1055/s-2007-969845
[18] Venkatesan, N., Punithavathi, D. and Arumugam, V. (2000) Curcumin Prevents Adriamycin Nephrotoxicity in Rats. British Journal of Pharmacology, 129, 231-234.
http://dx.doi.org/10.1038/sj.bjp.0703067
[19] Srivastava, R., Dikshit, M., Srimal, R.C., et al. (1985) Anti-Thrombotic Effect of Curcumin. Thrombosis Research, 40, 413-417.
http://dx.doi.org/10.1016/0049-3848(85)90276-2
[20] Dikshit, M., Rastogi, L., Shukla, R. and Srimal, R.C. (1995) Prevention of Ischaemia-Induced Biochemical Changes by Curcumin and Quinidine in the Cat Heart. Indian Journal of Medical Research, 101, 31-35.
[21] Chandra, V., Ganguli, M., Pandav, R., et al. (1998) Prevalence of Alzheimer’s Disease and Other Dementias in Rural India: The Indo-US Study. Neurology, 51, 1000-1008.
http://dx.doi.org/10.1212/WNL.51.4.1000
[22] Lim, G.P., Chu, T., Yang, F., Beech, W., Frautschy, S.A. and Cole, G.M. (2001) The Curry Spice Curcumin Reduces Oxidative Damage and Amyloid Pathology in an Alzheimer Transgenic Mouse. Journal of Neuroscience, 21, 8370- 8377.
[23] Litwinienko, G. and Ingold, K.U. (2004) Abnormal Solvent Effects on Hydrogen Atom Abstraction. 2. Resolution of the Curcumin Antioxidant Controversy. The Role of Sequential Proton Loss Electron Transfer. The Journal of Organic Chemistry, 69, 5888-5896.
http://dx.doi.org/10.1021/jo049254j
[24] Shen, L., Zhang, H.Y. and Ji, H.F. (2005) Successful Application of TD-DFT in Transient Absorption Spectra Assignment. Organic Letters, 7, 243-246.
http://dx.doi.org/10.1021/ol047766e
[25] Ono, K., Hasegawa, K., Naiki, H. and Yamada, M. (2004) Curcumin Has Potent Anti-Amyloidogenic Effects for Alzheimer’s Beta Fibrils in Vitro. Journal of Neuroscience Research, 75, 742-750.
http://dx.doi.org/10.1002/jnr.20025
[26] Yang, F., Lim, G.P., Begum, A.N., Ubeda, O.J., Simmons, M.R., Ambegaokar, S.S., et al. (2005) Curcumin Inhibits Formation of Amyloid Beta Oligomers and Fibrils, Binds Plaques, and Reduces Amyloid in Vivo. Journal of Biological Chemistry, 280, 5892-5901.
http://dx.doi.org/10.1074/jbc.M404751200
[27] Gomes, A., Fernandes, E. and Lima, J.L.F.C. (2005) Fluorescence Probes Used for Detection of Reactive Oxygen Species. Journal of Biochemical and Biophysical Methods, 65, 45-80.
http://dx.doi.org/10.1016/j.jbbm.2005.10.003
[28] LeBel, C.P., Ischiropoulos, H. and Bondy, S.C. (1992) Evaluation of the Probe 2’,7’-Dichlorofluorecein as an Indicator of Reactive Oxygen Species Formation and Oxidative Stress. Chemical Research in Toxicology, 5, 227-231.
http://dx.doi.org/10.1021/tx00026a012
[29] Aebi, H. (1984) Catalase in Vitro. Methods in Enzymology, 105, 121-126.
http://dx.doi.org/10.1016/S0076-6879(84)05016-3
[30] Lowry, O.H., Rosebrough, N.J., Farr, A.L. and Randall, R.J. (1951) Protein Measurement with the Folin Phenol Reagent. Journal of Biological Chemistry, 193, 265-275.
[31] Flohe, L. and Gunzler, W.A. (1984) Assays of Glutathione Peroxidase. Methods in Enzymology, 105, 114-121.
http://dx.doi.org/10.1016/S0076-6879(84)05015-1
[32] Drapper, H.H. and Hadley, M. (1990) Malondialdehyde Determination as Index of Lipid Peroxidation. Methods in Enzymology, 186, 421-431.
http://dx.doi.org/10.1016/0076-6879(90)86135-I
[33] Jollow, D., Mitchell, L., Zampaglione, N. and Gillete, J. (1974) Bromobenzene Induced Liver Necrosis. Protective Role of Glutathione and Evidence for 3, 4-Bromobenzenoxide as the Hepatotoxic Intermediate. Pharmacology, 11, 151-169.
http://dx.doi.org/10.1159/000136485
[34] Hermes-Lima, M. (2004) Oxygen in Biology and Biochemistry: Role of Free Radicals. In: Storey, K.B., Ed., Functional Metabolism: Regulation and Adaptation, John Wiley & Sons, Inc., Hoboken, 319-368.
[35] Kubbutat, M.H., Jones, S.N. and Vousden, K.H. (1997) Regulation of p53 Stability by Mdm2. Nature, 387, 299-303.
http://dx.doi.org/10.1038/387299a0
[36] El-Deiry, W.S., Tokino, T., Velculescu, V.E., Levy, D.B., Parsons, R., et al. (1993) WAF1, a Potential Mediator of p53 Tumor Suppression. Cell, 75, 817-825.
http://dx.doi.org/10.1016/0092-8674(93)90500-P
[37] Dumont, M. and Beal, M.F. (2011) Neuroprotective Strategies Involving ROS in Alzheimer Disease. Free Radical Biology and Medicine, 51, 1014-1026.
http://dx.doi.org/10.1016/j.freeradbiomed.2010.11.026
[38] Lynch, T., Cherny, R.A. and Bush, A.I. (2000) Oxidative Processes in Alzheimer’s Disease: The Role of Aβ-Metal Interactions. Experimental Gerontology, 35, 445-451.
http://dx.doi.org/10.1016/S0531-5565(00)00112-1
[39] Reddy, A.C. and Lokesh, B.R. (1994) Studies on the Inhibitory Effects of Curcumin and Eugenol on the Formation of Reactive Oxygen Species and the Oxidation of Ferrous Iron. Molecular and Cellular Biochemistry, 137, 1-8.
http://dx.doi.org/10.1007/BF00926033
[40] Ortiz-Ortiz, M.A., Morán, J.M., Bravosanpedro, J.M., González-Polo, R.A., Niso-Santano, M., Anantharam, V., Kanthasamy, A.G., Soler, G. and Fuentes, J.M. (2009) Curcumin Enhances Paraquat-Induced Apoptosis of N27 Mesencephalic Cells via the Generation of Reactive Oxygen Species. NeuroToxicolgy, 30, 1008-1018.
http://dx.doi.org/10.1016/j.neuro.2009.07.016
[41] Butterfield, D.A., Drake, J., Pocernich, C. and Castegna, A. (2001) Evidence of Oxidative Damage in Alzheimer’s Disease Brain: Central Role of Amyloid β-Peptide. Trends in Molecular Medicine, 7, 548-554.
http://dx.doi.org/10.1016/S1471-4914(01)02173-6
[42] Stadtman, E.R. and Berlett, B.S. (1997) Reactive Oxygen-Mediated Protein Oxidation in Aging and Disease. Chemical Research in Toxicology, 10, 485-494.
http://dx.doi.org/10.1021/tx960133r
[43] Lauderback, C.M., Hackett, J.M., Huang, F.F., Keller, J.N., Szweda, L.I., Markesbery, W.R. and Butterfield, D.A. (2001) The Glial Glutamate Transporter, GLT-1, Is Oxidatively Modified by 4-Hydroxy-2-Nonenal in the Alzheimer’s Disease Brain: The Role of Abeta1-42. Journal of Neurochemistry, 78, 413-416.
[44] Subramaniam, R., Roediger, F., Jordan, B., Mattson, M.P., Keller, J.N., Waeg, G. and Butterfield, D.A. (1997) The Lipid Peroxidation Product, 4-Hydroxy-2-Trans-Nonenal, Alters the Conformation of Cortical Synaptosomal Membrane Proteins. Journal of Neurochemistry, 69, 1161-1169.
http://dx.doi.org/10.1046/j.1471-4159.1997.69031161.x
[45] Chambers, C.B., Peng, Y., Nguyen, H., Gaiano, N., Fishell, G. and Nye, J.S. (2001) Spatiotemporal Selectivity of Response to Notch1 Signals in Mammalian Forebrain Precursors. Development, 128, 689-702.
[46] Furukawa, T., Mukherjee, S., Bao, Z., Morrow, E.M. and Cepko, C.L. (2000) Rax, Hes1, and Notch1 Promote the Formation of Muller Glia by Postnatal Retinal Progenitor Cells. Neuron, 26, 383-394.
http://dx.doi.org/10.1016/S0896-6273(00)81171-X
[47] Tanigaki, K., Nogaki, F., Takahashi, J., Tashiro, K., Kurooka, H. and Honjo, T. (2001) Notch1 and Notch3 Instructively Restrict bFGF-Responsive Multi-Potent Neural Progenitor Cells to an Astroglial Fate. Neuron, 29, 45-55.
http://dx.doi.org/10.1016/S0896-6273(01)00179-9
[48] Dorsky, R.I., Rapaport, D.H. and Harris, W.A. (1995) Xotch Inhibits Cell Differentiation in the Xenopus Retina. Neuron, 14, 487-496.
http://dx.doi.org/10.1016/0896-6273(95)90305-4
[49] Scheer, N., Groth, A., Hans, S. and Campos-Ortega, J.A. (2001) An Instructive Function for Notch in Promoting Gliogenes Is in the Zebra Fish Retina. Development, 128, 1099-1107.
[50] Chin, Y.E., Kitagawa, M., Su, W.C.S., You, Z.H., Iwamoto, Y. and Fu, X.Y. (1996) Cell Growth Arrest and Induction of Cyclin-Dependent Kinase Inhibitor p21WAF1/CIP1 Mediated by STAT1. Science, 272, 719-722.
http://dx.doi.org/10.1126/science.272.5262.719
[51] Huang, Q., Raya, A., DeJesus, P., Chao, S.H., Quon, K.C., Caldwell, J.S., et al. (2004) Identification of p53 Regulators by Genome-Wide Functional Analysis. Proceedings of the National Academy of Sciences of the United States of America, 101, 3456-3461.
[52] McGill, M.A. and McGlade, C.J. (2003) Mammalian Numb Proteins Promote Notch1 Receptor Ubiquitination and Degradation of the Notch1 Intracellular Domain. The Journal of Biological Chemistry, 278, 23196-23203.
http://dx.doi.org/10.1074/jbc.M302827200
[53] Wakamatsu, Y., Maynard, T.M., Jones, S.U. and Weston, J.A. (1999) NUMB Localizes in the Basal Cortex of Mitotic Avian Neuroepithelial Cells and Modulates Neuronal Differentiation by Binding to NOTCH-1. Neuron, 23, 71-81.
http://dx.doi.org/10.1016/S0896-6273(00)80754-0

  
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