Synergistic effects of amyloid peptides and lead on human neuroblastoma cells

• Autorzy: Suresh Ch. , Johnson J. , Mohan R. , Chetty C. S.
• Języki publikacji: EN

Abstrakty

EN

Aggregated amyloid peptides (AP), major components of senile plaques, have been considered to play a very important and crucial role in the development and neuro-pathogenesis of Alzheimer’s disease (AD). In the present in vitro, study the synergistic effects of Pb2+, a heavy metal, and AP on the human neuroblastoma SH-SY5Y cells were investigated. The cells treated with Pb2+ (0.01–10 μM) alone exhibited a significant decrease in viability and IC50 was 5 μM. A similar decrease in viability was also observed when the cells were exposed to AP, Aβ1–40 (20–120 μM) and Aβ25-35 (2.5–15 μM) for 48 hrs. The IC50 values were 60 μM and 7.5 μM for Aβ1–40 and Aβ25–35 respectively. To assess the synergistic effects the cells were exposed to IC50 of both AP and Pb2+, which resulted in further reduction of the viability. The study was extended to determine the lactate dehydrogenase (LDH) release to assess the cytotoxic effects, 8-isoprostane for extent of oxidative damage, COX 1 and 2 for inflammation related changes, p53 protein for DNA damage and protein kinases A and C for signal transduction. The data suggest that the toxic effects of AP were most potent in the presence of Pb2+, resulting in an aggravated clinical pathological condition. This could be attributed to the oxidative stress, inflammation neuronal apoptosis and an alteration in the activities of the signaling enzymes.

Słowa kluczowe

EN

synergistic effect; amyloid peptide; lead; man; neuroblastoma cell; lactate dehydrogenase; human disease; Alzheimer's disease; inflammation; oxidative stress; neuronal apoptosis; signalling; signal transduction

• Wydawca: -
• Czasopismo: Cellular and Molecular Biology Letters
• Rocznik: 2012
• Tom: 17
• Numer: 3
• Opis fizyczny: p.408-421,fig.,ref.

Twórcy

autor

Suresh Ch.

• Department of Natural Sciences, Savannah State University, Savannah, GA 31404, USA

autor

Johnson J.

autor

Mohan R.

autor

Chetty C. S.

Bibliografia

• 1. Lesné S, Koh, M.T., Kotilinek, L., Kayed, R., Glabe, C.G., Yang, A., Gallagher, M. and Ashe K.H. A specific amyloid-beta protein assembly in the brain impairs memory. Nature 440 (2006) 352-357.
• 2. Lee, V.M., Goedert M. and Trojanowski J.Q. Neurodegenerative tauopathies. Annu. Rev. Neurosci. 24 (2001) 1121-1159.
• 3. Selkoe, D.J. Alzheimer's disease results from the cerebral accumulation and cytotoxicity of amyloid beta-protein. J. Alzheimers Dis. 3 (2001) 75-80.
• 4. Hardy, J. and Selkoe, D.J. The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 297 (2002) 353-356.
• 5. Abramov, A.Y., Canevari, L. and Duchen, M.R. Changes in intracellular calcium and glutathione in astrocytes as the primary mechanism of amyloid neurotoxicity. J. Neurosci. 15 (2003) 5088-5095.
• 6. Crack, P.J., Cimdins, K., Ali, U., Hertzog, P.J. and Iannello, R.C. Lack of glutathione peroxidase-1 exacerbates abeta-mediated neurotoxicity in cortical neurons. J. Neural Transm. 113 (2006) 645-657.
• 7. Fukui, K., Takatsu, H., Shinkai, T., Suzuki, S., Abe, K. and Urano, S. Appearance of amyloid beta-like substances and delayed-type apoptosis in rat hippocampus CA1 region through aging and oxidative stress. J. Alzheimers Dis. 8 (2005) 299-309.
• 8. Kadowaki, H., Nishitoh, H., Urano, F., Sadamitsu, C., Matsuzawa, A., Takeda, K., Masutani, H., Yodoi, J., Urano, Y., Nagano, T. and Ichijo, H. Amyloid beta induces neuronal cell death through ROS-mediated ASK1 activation. Cell Death Differ. 12 (2005) 19-24.
• 9. Selkoe, D.J. Alzheimer's disease: genotypes, phenotypes and treatments. Science 275 (1997) 630-631.
• 10. Cummings, J.L., Vinters, H.V., Cole, G.M. and Khachaturian, Z.S. Alzheimer's disease: etiologies, pathophysiology, cognitive reserve, and treatment opportunities. Neurology 51 (1998) S2-S17.
• 11. Klein, W.L., Kraft, G.A. and Finch, C.E. Targeting small abeta oligomers: the solution to an Alzheimer's disease conundrum? Trends Neurosci. 24 (2001) 219-224.
• 12. Kelly, B.L. and Ferreira, A. Beta-amyloid-induced dynamin 1 degradation is mediated by N-methyl-D-aspartate receptors in hippocampal neurons. J. Biol. Chem. 281 (2006) 28079-28089.
• 13. Shih T.M. and Hamin N. Chronic lead exposure in mature animals: neurochemical correlates. Life Sci. 21 (1978) 877-888.
• 14. Silbergeld, E.K. and Goldberg, A. Hyperacidity: lead induced behavior disorder. Environ. Health Perspect. 7 (1974) 227-232.
• 15. Nihei, M.K. and Guilarte, T.R. Molecular mechanisms of low-level Pb2+ neurotoxicity. In: Handbook of Neurotoxicology 1 (2002) 107-133.
• 16. Platt, B. Experimental approaches to assess metallotoxicity and aging in models of Alzheimer's disease. J. Alzheimers Dis. 10 (2006) 203-213.
• 17. Chellu, S.C., Mohan, C.V., Khamisi, C. and Challa, S. Lead induced cell death of human neuroblastoma cells involves GSH deprivation. Cell. Mol. Biol. Lett. 10 (2005) 413-423.
• 18. Tang, J., Xu, H., Fan, X., Li, D., Rancourt, D., Zhou, G., Li, Z. and Yang, L. Embryonic stem cell-derived neural precursor cells improve memory dysfunction in A-beta (1-40) injured rats. Neurosci. Res. 62 (2008) 86-96.
• 19. Zhang, L., Xing, D., Zhu, D. and Chen, Q. Low-Power Laser irradiation inhibiting A-beta 25-35 induced PC12 cell apoptosis via PKC activation. Cell Physiol. Biochem. 22 (2008) 215-222.
• 20. Shimohama, S. Apoptosis in Alzheimer’s disease: an update. Apoptosis 5 (2000) 9-16.
• 21. Roth, K.A. Caspases, apoptosis, and Alzheimer’s disease: causation, correlation, and confusion. J. Neuropathol. Exp. 60 (2001) 829-838.
• 22. Khalil, N., Wilson, J. W., Talbott, E.O., Morrow, L.A., Hochberg, M.C., Hillier, T.A., Muldoon, S.B., Cummings, S.R. and Cauley, J.A. Association of blood lead concentrations with mortality in older women: a pospective cohort study. Environ. Health 8 (2009) 1-10.
• 23. Yatin, S.M., Varadarajan, S., Link, C.D. and Butterfield, D.A. In vitro and in vivo oxidative stress associated with Alzheimer’s amyloid beta-peptide (1-42). Neurobiol. Aging 20 (1999) 325-330.
• 24. Cardoso, S.M., Santos, S., Swerdlow, R.H. and Oliveira, C.R. Functional mitochondria are required for amyloid beta-mediated neurotoxicity. FASEB 15 (2001) 1439-1441.
• 25. Lesne, S., Koh, M.T., Kotilinek, L., Kayed, R., Glabe, C.G., Yang, A., Gallagher, M. and Ashe, K.H. A specific amyloid-beta protein assembly in the brain impairs memory. Nature 440 (2006) 352-357.
• 26. Sonnen, J.A., Breitner, J.C., Lovell, M.A., Markesbery, W.R., Quinn, J.F. and Montine, T.J. Free radical-mediated damage to brain in Alzheimer's disease and its transgenic mouse models. Free Radical Biol. Med. 45 (2008) 219-230.
• 27. Gilgun-Sherki, Y., Melamed, E. and Offen, D. Antioxidant treatment in Alzheimer's disease: current state. J. Mol. Neurosci. 21 (2003) 1-11.
• 28. Morrow, J.D., Hill, K.E., Burk, R.F., Nammour, T.M., Badr, K.F. and Roberts, L.J. A series of prostaglandin F2-like compounds are produced in vivo in humans by a noncyclooxygenase, free radical-catalyzed mechanism. Proc. Natl. Acad. Sci. U.S.A. 87 (1990) 9383-9387.
• 29. Roberts, L.J. and Morrow, J.D. Measurement of F2-isoprostanes as an index of oxidative stress in vivo. Free Radic. Biol. Med. 28 (2000) 505-513.
• 30. Basu S. F2-isoprostane induced prostaglandin formation in the rabbit. Free Radic. Res. 40 (2006) 273-277.
• 31. Basu, S. Isoprostanes: novel bioactive products of lipid peroxidation. Free Radic. Res. 38 (2004) 105-122.
• 32. Montuschi, P., Barnes, P.J. and Roberts, L.J. Isoprostanes: markers and mediators of oxidative stress. FASEB J. 18 (2004) 1791-1800.
• 33. Qin, W., Ho, L., Pompl, P.N., Peng, Y., Zhao, Z., Xiang, Z., Robakis, N.K., Shioi, J., Suh, J. and Pasinetti, G.M. Cyclooxygenase COX-2 and COX-1 potentiate betaamyloid peptide generation through mechanisms that involve gamma-secretase activity. J. Biol. Chem. 278 (2003) 50970-50977.
• 34. Xiang, Z., Ho, L., Yemul, S., Zhao, Z., Qing, W., Pompl, P., Kelley, K., Dang, A., Teplow, D. and Pasinetti, G.M. Cyclooxygenase-2 promotes amyloid plaque deposition in a mouse model of Alzheimer’s disease neuropathology. Gene Expr. 10 (2002) 271-278.
• 35. Alvarez, S., Serramia, M.J., Fresno, M. and Munoz Fernandez, M. Human immunodeficiency virus type 1 envelope glycoprotein 120 induces cyclooxygenase-2 expression in neuroblastoma cells through a nuclear factor kappa B and activating protein1 mediated mechanism. J. Neurochem. 94 (2005) 850-861.
• 36. Alvarez, S., Blanco, A., Kern, F., Fresno, M., Munoz Fernandez, M.A. HIV-2 induces NF-kappa B activation and cyclooxygenase-2 expression in human astroglial cells. Virology 380 (2008) 144-151.
• 37. Tatton, W.G. and Olanow, C.W. Apoptosis in neurodegenerative diseases: the role of mitochondria. Biochem. Biophys. Acta 1410 (1999) 195-213.
• 38. Zhang, Y., McLaughlin, R., Goodyear, C., LeBlanc, A. Selective cytotoxicity of intracellular amyloid beta peptide 1–42 through p53 and Bax in cultured primary human neurons. J. Cell Biol. 156 (2002) 519-529.
• 39. Hecquet, C., Lefevre, G., Valtink, M., Engelmann, K. and Mascarelli, F. Cyclic AMP inhibits the proliferation of retinal pigmented epithelial cells through the inhibition of ERK1/2 in a PKA-independent manner. Oncogene 21 (2002) 6101-6112.
• 40. Nishihara, H., Kizaka-Kondoh, S., Insel P.A. and Eckmann, L. Inhibition of apoptosis in normal and transformed intestinal epithelial cells by cyclic AMP through induction of inhibitor of apoptosis protein (IAP)-2. Proc. Natl. Acad. Sci. U.S.A. 100 (2003) 8921-8926.
• 41. Cardell, M. and Wieloch, T. Time course of the translocation and inhibition of protein kinase C during complete cerebral ischemia in the rat. J. Neurochem. 61 (1993) 1308-1314.
• 42. Busto, R., Globus, M.Y., Neary, J.T. and Ginsberg, M.D. Regional alterations of protein kinase C activity following transient cerebral ischemia: effects of intra-ischemic brain temperature modulation. J. Neurochem. 63 (1994) 1095-1103.
• 43. Liang, Z., Liu, F., Grundke-Iqbal, I., Iqbal, K. and Gong, C.X. Downregulation of cAMP-dependent protein Kinase by over-activated calpain in Alzheimer diseased brain. J. Neurochem. 103 (2007) 2462-2470.
• 44. Gong, B., Cao, Z., Zheng, P., Vitolo, O.V. and Liu, S. Ubiquitin hydrolase uch-L1 rescues beta-amyloid-induced decreases in synaptic function and contextual memory. Cell 126 (2006) 775-788.
• 45. Wang, P., Chen, L.L., Yan, H. and Li, J.C. Trichosanthin suppresses HeLa cell proliferation through inhibition of the PKC/MAPK signaling pathway. Cell Biol. Toxicol. 25 (2009) 479-488.
• 46. Iijima-Ando, K., Hearn, S.A., Shenton, C., Gatt, A., Zhao, L. and Iijima, K. Mitochondrial mis-localization underlies A-42 induced neuronal dysfunction in a drosophila model of Alzheimer's disease. PLoS One 4 (2009) 1-13.