Epigenetic modification is linked to Alzheimer’s disease: is it a maker or a marker?
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Alzheimer's disease (AD) is the most common age-dependent neurodegenerative disorder and shows progressive memory loss and cognitive decline. Intraneuronal filaments composed of aggregated hyperphosphorylated tau protein, called neurofibrillary tangles, along with extracellular accumulations of amyloid β protein (Aβ), called senile plaques, are known to be the neuropathological hallmarks of AD. In light of recent studies,epigenetic modification has emerged as one of the pathogenic mechanisms of AD. Epigenetic changes encompass an array of molecular modifications to both DNA and chromatin,including transcription factors and cofactors. In this review, we summarize how DNA methylation and changes to DNA chromatin packaging by post-translational histone modification are involved in AD. In addition, we describe the role of SIRTs, histone deacetylases, and the effect of SIRT-modulating drugs on AD. Lastly, we discuss how amyloid precursor protein (APP)intracellular domain (AICD) regulates neuronal transcription. Our understanding of the epigenomes and transcriptomes of AD may warrant future identification of novel biological markers and beneficial therapeutic targets for AD.
Abstract
Alzheimer's disease (AD) is the most common age-dependent neurodegenerative disorder and shows progressive memory loss and cognitive decline. Intraneuronal filaments composed of aggregated hyperphosphorylated tau protein, called neurofibrillary tangles, along with extracellular accumulations of amyloid β protein (Aβ), called senile plaques, are known to be the neuropathological hallmarks of AD. In light of recent studies,epigenetic modification has emerged as one of the pathogenic mechanisms of AD. Epigenetic changes encompass an array of molecular modifications to both DNA and chromatin,including transcription factors and cofactors. In this review, we summarize how DNA methylation and changes to DNA chromatin packaging by post-translational histone modification are involved in AD. In addition, we describe the role of SIRTs, histone deacetylases, and the effect of SIRT-modulating drugs on AD. Lastly, we discuss how amyloid precursor protein (APP)intracellular domain (AICD) regulates neuronal transcription. Our understanding of the epigenomes and transcriptomes of AD may warrant future identification of novel biological markers and beneficial therapeutic targets for AD.
참고문헌 (51)
- Marques, S. C., "Alzheimer's disease: the quest to understand complexity", J. Alzheimers. Dis., 21, pp.373~383 (2010)
- Chouliaras, L., "Epigenetic regulation in the pathophysiology of Alzheimer's disease", Prog. Neurobiol., 90, pp.498~510 (2010)
- Suzuki, M. M., "DNA methylation landscapes: provocative insights from epigenomics", Nat. Rev. Genet., 9, pp.465~476 (2008)
- Tohgi, H., "Reduction with age in methylcytosine in the promoter region -224 approximately-101 of the amyloid precursor protein gene in autopsy human cortex", Brain Res. Mol. Brain Res., 70, pp.288~292 (1999)
- West, R. L., "Hypomethylation of the amyloid precursor protein gene in the brain of an Alzheimer’s disease patient", J. Mol. Neurosci., 6, pp.141~146 (1995)
- Wang, S. C., "Agespecific epigenetic drift in late onset Alzheimer’s disease", PLoS ONE, 3, pp.e2698~ (2008)
- Poulsen, P., "The epigenetic basis of twin discordance in age-related diseases", Pediatr. Res., 61, pp.38R~42R (2007)
- Mastroeni, D., "Epigenetic differences in cortical neurons from a pair of monozygotic twins discordant for Alzheimer's disease", PLoS One, 4, pp.e6617~ (2009)
- Silva, P. N., "Promoter methylation analysis of SIRT3, SMARCA5, HTERT and CDH1 genes in aging and Alzheimer's disease", J. Alzheimers. Dis., 13, pp.173~176 (2008)
- Akiyama, H., "Inflammation and Alzheimer’s disease", Neurobiol. Aging, 21, pp.383~421 (2000)
- Bannister, A. J., "Histone methylation: dynamic or static?", Cell, 109, pp.801~806 (2002)
- Felsenfeld, G., "Controlling the double helix", Nature, 421, pp.448~453 (2003)
- Hake, S. B., "Linking the epigenetic ‘language’ of covalent histone modifications to cancer", Br. J. Cancer, 90, pp.761~769 (2004)
- Jenuwein, T., "Translating the histone code", Science, 293, pp.1074~1080 (2001)
- Sadri-Vakili, G., "Mechanisms of disease: histone modifications in Huntington’s disease", Nat. Clin. Pract. Neurol., 2, pp.330~338 (2006)
- Mattson, M. P., "Perturbed signal transduction in neurodegenerative disorders involving aberrant protein aggregation", Neuromolecular. Med., 4, pp.109~132 (2003)
- Robakis, N. K., "An Alzheimer's disease hypothesis based on transcriptional dysregulation", Amyloid., 10, pp.80~85 (2003)
- Kilgore, M., "Inhibitors of class 1 histone deacetylases reverse contextual memory deficits in a mouse model of Alzheimer's disease", Neuropsychopharmacology, 35, pp.870~880 (2010)
- Ogawa, O., "Ectopic localization of phosphorylated histone H3 in Alzheimer's disease: a mitotic catastrophe?", Acta. Neuropathol., 105, pp.524~528 (2003)
- Alarcon, J. M., "Chromatin acetylation, memory, and LTP are impaired in CBP＋", −mice: a model for the cognitive deficit in Rubinstein-Taybi syndrome and its amelioration, 2004, pp.42, 947~959
- Korzus, E., "CBP histone acetyltransferase activity is a critical component of memory consolidation", Neuron, 42, pp.961~972 (2004)
- Oliveira, A. M., "Transgenic mice expressing an inhibitory truncated form of p300 exhibit long-term memory deficits", Learn. Mem., 14, pp.564~572 (2007)
- Strahl, B. D., "The language of covalent histone modifications", Nature, 403, pp.41~45 (2000)
- Hake, S. B., "Histone H3 variants and their potential role in indexing mammalian genomes: the ‘H3 barcode hypothesis’", Proc. Natl. Acad. Sci. U.S.A., 통권 : 103, pp.6428~6435 (2006)
- Papp, B., "Histone trimethylation and the maintainence of transcriptional ON and OFF states by trxG and PcG proteins", Genes Dev., 20, pp.2041~2054 (2006)
- Ferrante, R. J., "Histone deacetylase inhibition by sodium butyrate chemotherapy ameliorates the neurodegenerative phenotype in Huntington’s disease mice", J. Neurosci., 23, pp.9418~9427 (2003)
- Gardian, G., "Neuroprotective effects of phenylbutyrate in the N171-82Q transgenic mouse model of Huntington’s disease", J. Biol. Chem., 280, pp.556~563 (2005)
- McCampbell, A., "Histone deacetylase inhibitors reduce polyglutamine toxicity", Proc. Natl Acad. Sci. U.S.A., 통권 : 98, pp.15179~15184 (2001)
- Ryu, H., "Sodium phenylbutyrate prolongs survival and regulates expression of anti-apoptotic genes in transgenic amyotrophic lateral sclerosis mice", J. Neurochem., 93, pp.1087~1098 (2005)
- Steffan, J. S., "Histone deacetylase inhibitors arrest polyglutamine-dependent neurodegeneration in Drosophila", Nature, 413, pp.739~743 (2001)
- Hockly, E., "Suberoylanilide hydroxamic acid, a histone deacetylase inhibitor, ameliorates motor deficits in a mouse model of Huntington’s disease", Proc. Natl. Acad. Sci. U.S.A., 통권 : 100, pp.2041~2046 (2003)
- Hahnen, E., "Histone deacetylase inhibitors: possible implications for neurodegenerative disorders", Expert. Opin. Investig. Drugs., 17, pp.169~184 (2008)
- Guan, J. S., "HDAC2 negatively regulates memory formation and synaptic plasticity", Nature, 7, pp.55~60 (2009)
- Julien, C., "Sirtuin 1 reduction parallels the accumulation of tau in Alzheimer disease", J. Neuropathol. Exp. Neurol., 68, pp.48~58 (2009)
- Donmez, G., "SIRT1 suppresses beta-amyloid production by activating the alpha-secretase gene ADAM10", Cell, 42, pp.320~332 (2010)
- Wolfe, M. S., "Giving Alzheimer's the old one-two", Cell, 142, pp.194~196 (2010)
- Albani, D., "Sirtuins as novel targets for Alzheimer's disease and other neurodegenerative disorders: experimental and genetic evidence", J. Alzheimers. Dis., 19, pp.11~26 (2010)
- De Oliveira, R. M., "Sirtuins: common targets in aging and in neurodegeneration", Curr. Drug. Targets., 11, pp.1270~1280 (2010)
- Green, K. N., "Nicotinamide restores cognition in Alzheimer's disease transgenic mice via a mechanism involving sirtuin inhibition and selective reduction of Thr231-phosphotau", J. Neurosci., 28, pp.11500~11510 (2008)
- Luo, J., "Negative control of p53 by Sir2 alphapromotes cell survival under stress", Cell, 107, pp.137~148 (2001)
- Karuppagounder, S. S., "Dietary supplementation with resveratrol reduces plaque pathology in a transgenic model of Alzheimer’s disease", Neurochem. Int., 54, pp.111~118 (2009)
- Markus, M. A., "Resveratrol in prevention and treatment of common clinical conditions of aging", Clin. Interv. Aging., 3, pp.331~339 (2008)
- Ryan, K. A., "Activation of GSK-3 and phosphorylation of CRMP2 in transgenic mice expressing APP intracellular domain", J. Cell Biol., 171, pp.327~335 (2005)
- Munoz, D. G., "Hirano bodies accumulate C-terminal sequences of beta-amyloid precursor protein (beta-APP) epitopes", J. Neuropathol. Exp. Neurol., 52, pp.14~21 (1993)
- Artavanis-Tsakonas, S., "Notch signaling: cell fate control and signal integration in development", Science, 284, pp.770~776 (1999)
- McLoughlin, D. M., "The intracellular cytoplasmic domain of the Alzheimer’s disease amyloid precursor protein interacts with phosphotyrosine-binding domain proteins in the yeast two-hybrid system", FEBS Lett., 397, pp.197~200 (1996)
- active complex of APP with Fe65 and histone acetyltransferase Tip60, "Science", 2001, 115~120
- Baek, S. H., "Exchange of N-CoR corepressor and Tip60 coactivator complexes links gene expression by NF-kappa B and beta-amyloid precursor protein", Cell, 110, pp.55~67 (2002)
- Siegmund, K. D., "DNA methylation in the human cerebral cortex is dynamically regulated throughout the life span and involves differentiated neurons", PLoS One, 2, pp.e895~ (2007)
- Abdolmaleky, H. M., "Methylomics in psychiatry: modulation of gene-environment interactions may be through DNA methylation", Am. J. Med. Genet. B. Neuropsychiatr. Genet., 127B, pp.51~59 (2004)
- Ryu, H., "ESET", SETDB1 gene expression and histone H3 (K9) trimethylation in Huntington's disease, 2006, pp.통권 : 103, 19176~19181