Immunohistochemical Studies on HDAC-4 in Experimentally Induced Parkinson's Diseases
The environmental toxin hypothesis was dominant for much of the 20th century, and posits that PD-related neurodegeneration results from exposure to a dopaminergic neurotoxin. Living in a rural environment appears to confer an increased risk of PD, perhaps due to increased exposureto pesticide use and wood preservatives. Cigarette smoking and coffee drinking are inversely associated with the risk for the development of PD. These modifications are likely to contribute to the onset and progression of complex human diseases including neurodegenerative ones. Oxidative stress also is thought to be a common underlying mechanism that leads to cellular dysfunction and demise in PD. This study was aimed to assess the effect of butyric acid in PD experimental model through HDAC activities. The study was carried out on five rat groups, control group, Parkinsonism group, and sodium butyrate group, two Parkinson’s disease groups co-administered and post treated with sodium butyrate. Parkinsonism was induced by ip injection of paraquat. Laboratory measurements included serum HDAC activity and HDAC-4 antibody stain. PD group, PD co-administered and post treated with sodium butyrate showed significant increase in HDAC activity. Histological and Immunohistochemical investigate. The increments in HDAC activities are one of the pathogenic mechanisms of the disease or it affords PD patients neuroprotection and benefits. Also, sodium butyrate is one of best antioxidant and neuroprotective agents. We recommended for further studies in HDAC and sodium butyrate as inhibitor in neurodegerative diseases, other diseases and normal state. Further investigation is required by determining activity of HDAC to clarify its role in Parkinsonism.
Parkinson’s Disease, Intra Peritoneal, Histone Deacetylase, Methy Phenyl Tetrahydro Pyridine, Histone Acetyl Transferase, Sodium Butyrate
[1]
Ajamian, F., Salminen, A. and Reeben, M. (2004): Selective regulation of class I and class II histone deacetylases expression by inhibitors of histone deacetylases in cultured mouse neural cells. Neurosci. Lett. 365 (1); 64-8.
[2]
Allfrey, V., Faulkner, R. and Mirsky, A. (1964): Acetylation and methylation of histones and their possible role in the regulation of RNA synthesis. Proc. Natl. Acad. Sci. USA. 51; 786–794.
[3]
Bancroft, J.D. and Stevens, G.A. (1990): Theory and Practice of Histological Techniques; 2nd Ed. Churchill Livingstone, London.
[4]
Bandyopadhyay, D., Mishra, A. and Medrano, E. E. (2004): Overexpression of histone deacetylase 1 confers resistance to sodium butyrate-mediated apoptosis in melanoma cells through a p53-mediated pathway. Cancer Res. 1; 64 (21); 7706-10.
[5]
Berger, S. L. (2007): The complex language of chromatin regulation during transcription. Nature. 447; 407–412.
[6]
Blottiere, H. M., Buecher, B. and Galmiche, J. P. (2003): Molecular analysis of the effect of short-chain fatty acids on intestinal cell proliferation J. Proc. Natr. Soc. 62 (1); 101-106.
[7]
Boffa, L. C., Gruss, R. J. and Allfrey, V. G. (1981): Manifold effects of sodium butyrate on nuclear function. J. Biol. Chem., 256; 9612-9621.
[8]
Camarero, N., Nadal, A. and Barrero, M. J. (2003): Histone deacetylase inhibitors stimulate mitochondrial HMG-CoA synthase gene expression via a promoter proximal Spl site [J]. Nucleic Acids Res, 31(6); 1693-1703.
[9]
Cannon, J. and Greenamyre, J. (2011): The Role of Environmental Exposures in Neurodegeneration and Neurodegenerative Diseases. Toxicol. Sci. 124 (2); 225-250.
[10]
Chen, J. S. and Faller, D. V. (2005): Histone deacetylase inhibition-mediated post-translational elevation of p27Kip1 protein levels is required for G1 arrest in fibroblasts. J. Biol. Chem. 202; 87-99.
[11]
Chen, J. S., Faller, D. V. and Spanjaard, R. A. (2003): Short-chain fatty acid inhibitors of histone deacetylases: promising anticancer therapeutics? Current Cancer Drug Targets 3; 219-236.
[12]
Cousens, L. S., Gallwitz, D., and Alberts, B. M. (1979): Different accessibilities in chromatin to histone acetylase. J. Biol. Chem., 254; 1716-1723.
[13]
Dinis-Oliveira, R., Duarte, J., Sanchez-Navarro, A., Remiao, F., Bastos, M. and Carvalho, F. (2008): Paraquat poisonings: mechanisms of lung toxicity, clinical features, and treatment. Crit. Rev. Toxicol. 38 (1); 13–71.
[14]
Fernagut, P., Diguet, E., Labattu, B. and Tison, F. (2002): A simple method to measure stride length as an index of nigrostriatal dysfunction in mice. Journal of Neuroscience Methods. 113; 123–130.
[15]
Foglietta, F., Serpe, L., Canaparo, R., Vivenza, N., Riccio, G., Imbalzano, E., Gasco, P. and Zara, G. P. (2014): Modulation of butyrate anticancer activity by solid lipid nanoparticle delivery: an in vitro investigation on human breast cancer and leukemia cell lines. J. Pharm. Pharm. Sci. 17 (2); 231-47.
[16]
Franco, R., Li, S., Rodriguez-Rocha, H., Burns, M. and Panayiotidisb, M. (2010): Molecular mechanisms of pesticide-induced neurotoxicity: Relevance to Parkinson’s disease. Chemico-Biological Interactions. 188 (2); 289–300.
[17]
Franco, R., Li, S., Rodriguez-Rocha, H., Burns, M. and Panayiotidisb, M. (2010): Molecular mechanisms of pesticide-induced neurotoxicity: Relevance to Parkinson’s disease. Chemico-Biological Interactions. 188 (2); 289–300.
[18]
Grayson, D. R., Kundakovic, M. and Sharma, R. P. (2010): Is there a future for histone deacetylase inhibitors in the pharmacotherapy of psychiatric disorders? Mol. Pharmacol. 77 (2); 126-35.
[19]
Gre´goire, S., Xiao, L., Nie, J., Xu, M., Wong, J., Seto, E. and Yang, X. (2007): Histone deacetylase 3 interacts and deacetylates MEF2 transcription factors. Mol. Cell Biol. 27 (4); 1280–1295.
[20]
Guardiola, A. R. and Yao, T. P. (2002): Molecular cloning and characterization of a novel histone deacetylase HDAC10. J. Biol. Chem. 277 (5); 3350-6.
[21]
Hisahara, S. and Shimohama, S. (2010): Toxin-induced and genetic animal models of Parkinson's disease. Parkinsons Dis. 1-14.
[22]
Hong, S., Hwang, J., Kim, J., Shin, K. and Kang, S. (2014): Heptachlor induced nigral dopaminergic neuronal loss and Parkinsonism-like movement deficits in mice. Exp. Mol. Med. 46; 1-10.
[23]
Hsieh, J., Nakashima, K., Kuwabara, T., Mejia, E. and Gage, F. H. (2004): Histone deacetylase inhibition-mediated neuronal differentiation of multipotent adult neural progenitor cells. Proc. Natl Acad. Sci. USA 101; 16659–16664.
[24]
Kanthasamy, A., Kitazawa, M., Yang, Y., Anantharam, V., and Kanthasamy, A. (2008): Environmental neurotoxin dieldrin induces apoptosis via caspase-3-dependent proteolytic activation of protein kinase C delta (PKCdelta): implications for neurodegeneration in Parkinson’s disease. Molecular Brain. 1(12); 1-15.
[25]
Levy-Wilson, B. (1981) Enhanced phosphorylation of high-mobility-group proteins in nuclease-sensitive mononucleosomes from butyrate-treated HeLa cells. Proc. Nati. Acad. Sci. USA, 78: 2189-2193.
[26]
Lewis, G., Byblon, W. and Walt, S. (2000): Stride length regulation in Parkinson’s disease: the use of extrinsic, visual cues. Brain. 123; 2077–2090.
[27]
Li, L., Dai, H., Ye, M., Wang, S., Xiao, X., Zheng, J., Chen, H., Luo, Y. and Liu, J. (2012): Lycorine induces cell-cycle arrest in the G0/G1 phase in K562 cells via HDAC inhibition. Cancer Cell International. 12 (1); 49-54.
[28]
Li-Jung Juan, Wei-Jong Shia, Mei-Hui Chen, Wen-Ming Yang, Edward Seto, Young-Sun Lin and Cheng-Wen Wu (2000): Histone Deacetylases Specifically Down-regulate p53-dependent Gene Activation. J. Biol. Chem. 275; 20436-20443.
[29]
Matsuura, K., Kabuto, H., Makino, H. and Ogawa, N. (1997): Pole test is a useful method for evaluating the mouse movement disorder caused by striatal dopamine depletion. J. Neurosci. Methods. 73; 45–48.
[30]
McCormack, A., Atienza, J., Johnston, L., Andersen, J., Vu, S. and Di Monte, D. (2005): Role of oxidative stress in paraquat-induced dopaminergic cell degeneration. J. Neurochem. 93 (4); 1030-1037.
[31]
Meredith, G. and Kang, U. (2006): Behavioral models of Parkinson’s disease in rodents: a new look at an old problem. Mov. Disord. 21; 1595–1606.
[32]
Miura, K., Taura, K., Kodama, Y., Schnabl, B. and Brenner, D. (2008): Hepatitis C Virus–Induced Oxidative Stress Suppresses Hepcidin Expression Through Increased Histone Deacetylase Activity. Hepatology. 48 (5); 1420-1429.
[33]
Moretto, A. and Colosio, C. (2011): Biochemical and toxicological evidence of neurological effects of pesticides: the example of Parkinson's disease. Neurotoxicology. 32 (4); 383-391.
[34]
Mork, C. A., Spanjaard, R. A. and Faller, D. V. (2005): A mechanistic approach to anticancer therapy: targeting the cell cycle with histone deacetylase inhibitors. Curr. Rev. Pharmacol. 11: 1091-1104.
[35]
Morrison, B., Majdzadeh, N. and D'Mello, S. (2007): Histone deacetylases: Focus on the nervous system. Cell. Mol. Life Sci. 64 (17); 2258-2269.
[36]
Muthukumaran, K., Leahy, S., Harrison, K., Sikorska, M., Sandhu, J., Cohen, J., Keshan, C., Lopatin, D., Miller, H., Borowy-Borowski, H., Lanthier, P., Weinstock, S. and Pandey, S. (2014): Orally delivered water soluble Coenzyme Q10 (Ubisol-Q10) blocks on-going neurodegeneration in rats exposed to paraquat: potential for therapeutic application in Parkinson's disease. BMC Neurosci. 15 (21); 1-11.
[37]
Nisticò, R., Mehdawy, B., Piccirilli, S. and Mercuri, N. (2011): Paraquat- and rotenone-induced models of Parkinson's disease. Int. J. Immunopathol. Pharmacol. 24 (2); 313-322.
[38]
Ouyang, W., Zhang, D., Li, J., Verma, U., Costa, M. and Huang, C. (2009): Soluble and insoluble nickel compounds exert a differential inhibitory effect on cell growth through IKKα-dependent cyclin D1 down-regulation, J. Cell Physiol. 218 (1); 205–214.
[39]
Pan-Montojo, F. and Reichmann, H. (2014): Considerations on the role of environmental toxins in idiopathic Parkinson’s disease pathophysiology. Transl. Neurodegener. 3 (10); 1-13.
[40]
Peng, J., Mao, X., Stevenson, F., Hsu, M. and Andersen, J. (2004): The herbicide paraquat induces dopaminergic nigral apoptosis through sustained activation of the JNK pathway. J. Biol. Chem. 279 (31); 32626-32632.
[41]
Peng, J., Peng, L., Stevenson, F., Doctrow, S. and Andersen, J. (2007): Iron and Paraquat as Synergistic Environmental Risk Factors in Sporadic Parkinson’s Disease Accelerate Age-Related Neurodegeneration. The Journal of Neuroscience. 27 (26); 6914–6922.
[42]
Ramprasad, M.P., Terpstra, V., Kondratenko, N., Quehenberger, O. and Steinberg, D. (1996): Cell surface expression of mouse macrosialin and human CD68 and their role as macrophage receptors for oxidized low density lipoprotein. Proc. Natl. Acad. Sci. USA, 93: 14833-14838.
[43]
Ropero, S. and Esteller, M. (2007): The role of histone deacetylases (HDACs) in human cancer. Mol. Oncol. 1(1); 19-25.
[44]
Sauer, J., Richter, K. K. and Pool-Zobel, B. L. (2007): Physiological concentrations of butyrate favorably modulate genes of oxidative and metabolic stress in primary human colon cells. J. Nutr. Biochem. 18: 736-745.
[45]
Schneider, F. H. (1976): Effects of sodium butyrate on mouse neuroblastoma cells in culture. Biochem. Pharmacol. 25: 2309-2317.
[46]
Schut, H. A. J., Hughes, E. H., and Thorgeirsson, S. S. (1981): Differential effects of dimethylsulfoxide and sodium butyrate on α-fetoprotein, albumin, and transferrin production by rat hepatomas in culture. In Vitro. 77; 275- 283.
[47]
Shimizu, K., Ohtaki, K., Matsubara, K., Aoyama, K., Uezono, T., Saito, O., Suno M., Ogawa, K., Hayase, N. and Kimura, K. (2001): Carrier-mediated processes in blood-brain barrier penetration and neural uptake of paraquat. Brain Res. 906 (1–2); 135-142.
[48]
Sibaji Sarkar, Ana L. Abujamra, Jenny E. Loew, Loraw Forman, Susan P. Perrine and Douglas V. Faller (2011): Histone Deacetylase Inhibitors Reverse CpG Methylation by Regulating DNMT1 through ERK Signaling. Anticanc. Res. 31; 2723-2732.
[49]
Singh, B., Zhang, G., Hwa, Y., Li, J., Dowdy, S. and Jiang, S. (2010): Nonhistone protein acetylation as cancer therapy targets. Expert Rev. Anticancer Ther. 10 (6); 935-954.
[50]
Taylor, T., Greene, J., and Miller, G. (2010): Behavioral phenotyping of mouse models of Parkinson's disease. Behav. Brain Res. 211 (1); 1–10.
[51]
Telles, E. and Seto, E. (2012): Modulation of Cell Cycle Regulators by HDACs. Front. Biosci. 4; 831–839.
[52]
Thiruchelvam, M., Richfield, E., Baggs, R., Tank, A. and Cory-Slechta, D. (2000): The nigrostriatal dopaminergic system as a preferential target of repeated exposures to combined paraquat and maneb: implications for Parkinson's disease. J. Neurosci. 20 (24); 9207-9214.
[53]
Tieu, K. (2011): A Guide to Neurotoxic Animal Models of Parkinson’s disease. Cold Spring Harb. Perspect. Med. 1(1); 1-20.
[54]
Tillerson, J., Caudle, W., Reveron, M. and Miller, G. (2002): Detection of behavioral impairments correlated to neurochemical deficits in mice treated with moderate doses of 1-methyl-4-phenyl-1,2,3,6- tetrahydropyridine. Exp. Neurol. 178; 80–90.
[55]
Vidali, G., Boffa, L. C., Bradbury, E. M. and Allfrey, F. G. (1978): Butyrate suppression of histone deacetylation leads to accumulation of multiacetylated forms of histories H3 and H4 and increased DNase I sensitivity of the associated DNA sequences. Proc. Nati. Acad. Sci. USA, 75; 2239-2243.
[56]
Xie, H., Bandhakavi, S., Roe, M. and Griffin, T. (2007): Preparative peptide isoelectric focusing as a tool for improving the identification of lysine-acetylated peptides from complex mixtures. J. Proteome Res. 6; 2019–2026.
[57]
Yamaguchi, T., Cubizolles, F., Zhang, Y., Reichert, N., Kohler, H., Seiser, C. and Matthias, P. (2010): Histone deacetylases 1 and 2 act in concert to promote the G1-to-S progression. Genes Dev. 24 (5): 455-469.
[58]
Yao, X., Nguyen, H. and Nyomba, B. (2013): Prenatal Ethanol Exposure Causes Glucose Intolerance with Increased Hepatic Gluconeogenesis and Histone Deacetylases in Adult Rat Offspring: Reversal by Tauroursodeoxycholic Acid. PLoS One. 8 (3); 1-10.
[59]
Zupkovitz, G., Grausenburger, R., Brunmeir, R., Senese, S. and Tischler, J. (2010): The cyclin-dependent kinase inhibitor p21 is a crucial target for histone deacetylase 1 as a regulator of cellular proliferation. Mol. Cell Biol. 30; 1171-1181.
