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NeuroMolecular Medicine

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12.06.2018 | Original Paper

The Transcriptional Regulatory Properties of Amyloid Beta 1–42 may Include Regulation of Genes Related to Neurodegeneration

verfasst von: Duygu Gezen-Ak, İrem L. Atasoy, Esin Candaş, Merve Alaylıoğlu, Erdinç Dursun

Erschienen in: NeuroMolecular Medicine | Ausgabe 3/2018

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Abstract

Our previous study demonstrated the translocation of Aβ1–42 to the nucleus in response to antibiotic treatment, and interpreted it as a possible transcriptional response of Aβ1–42 to antibiotics. The present study aims to investigate how amyloid acts on the key elements of neurodegeneration and the molecules involved in the induction of Aβ1–42 production. For this purpose, we investigated the acute effect of Aβ1–42 on the transcriptional levels of genes that have roles in the mechanisms that produce Aβ itself: alpha secretase (ADAM10), beta secretase (BACE1), the gamma secretase complex (PS-1, PS-2, Nicastrin), the substrate APP, APOE (the significant risk factor for sporadic form of the AD), TREM2 (recently indicated as a contributor to AD risk), NMDAR subunits and PKCzeta (contributors of memory and learning), and key elements of tau pathology such as tau, GSK3α, GSK3β, and Cdk5. Additionally, we examined cholecalciferol metabolism-related enzyme 1α-hydroxylase (1αOHase) in primary cortical neurons with qRT-PCR. Our results indicate that Aβ1–42 has an effect on most of the target genes. This effect involves regulation of the amyloidogenic pathway in a complex manner, specifically, a general downregulation in NMDARs, ApoE, Trem2, and 1αOHase genes, and general up-regulation of tau pathway-related genes. We speculate that the presence of Aβ impacts the neurons not only with toxic events but also at the transcriptional level. The nuclear localization of Aβ1–42 and its regulatory effects on the target genes that we investigated in present study indicates Aβ1–42 as a transcriptional regulator of genes related to neurodegeneration.

Adzovic, L., & Domenici, L. (2014). Insulin induces phosphorylation of the AMPA receptor subunit GluR1, reversed by ZIP, and over-expression of Protein Kinase M zeta, reversed by amyloid beta. Journal of Neurochemistry, 131(5), 582–587. https://doi.org/10.1111/jnc.12947.PubMedCrossRef

Arbor, S. C., LaFontaine, M., & Cumbay, M. (2016). Amyloid-beta Alzheimer targets—protein processing, lipid rafts, and amyloid-beta pores. Yale Journal of Biology and Medicine, 89(1), 5–21.PubMed

Arioka, M., Tsukamoto, M., Ishiguro, K., Kato, R., Sato, K., Imahori, K., et al. (1993). Tau protein kinase II is involved in the regulation of the normal phosphorylation state of tau protein. Journal of Neurochemistry, 60(2), 461–468.PubMedCrossRef

Bailey, J. A., Maloney, B., Ge, Y. W., & Lahiri, D. K. (2011). Functional activity of the novel Alzheimer’s amyloid beta-peptide interacting domain (AbetaID) in the APP and BACE1 promoter sequences and implications in activating apoptotic genes and in amyloidogenesis. Gene, 488(1–2), 13–22. https://doi.org/10.1016/j.gene.2011.06.017.PubMedPubMedCentralCrossRef

Baitsch, D., Bock, H. H., Engel, T., Telgmann, R., Muller-Tidow, C., Varga, G., et al. (2011). Apolipoprotein E induces antiinflammatory phenotype in macrophages. Arteriosclerosis, Thrombosis, and Vascular Biology, 31(5), 1160–1168. https://doi.org/10.1161/ATVBAHA.111.222745.PubMedPubMedCentralCrossRef

Barucker, C., Harmeier, A., Weiske, J., Fauler, B., Albring, K. F., Prokop, S., et al. (2014). Nuclear translocation uncovers the amyloid peptide Abeta42 as a regulator of gene transcription. Journal of Biological Chemistry, 289(29), 20182–20191. https://doi.org/10.1074/jbc.M114.564690.PubMedCrossRef

Brijbassi, S., Amtul, Z., Newbigging, S., Westaway, D., St George-Hyslop, P., et al. (2007). Excess of nicastrin in brain results in heterozygosity having no effect on endogenous APP processing and amyloid peptide levels in vivo. Neurobiology of Disease, 25(2), 291–296. https://doi.org/10.1016/j.nbd.2006.09.013.PubMedCrossRef

Cicero, S., & Herrup, K. (2005). Cyclin-dependent kinase 5 is essential for neuronal cell cycle arrest and differentiation. Journal of Neurochemistry, 25(42), 9658–9668. https://doi.org/10.1523/JNEUROSCI.1773-05.2005.CrossRef

Dursun, E., Alaylioglu, M., Bilgic, B., Hanagasi, H., Lohmann, E., Atasoy, I. L., et al. (2016). Vitamin D deficiency might pose a greater risk for ApoEε4 non-carrier Alzheimer’s disease patients. Neurological Sciences, 37(10), 1633–1643. https://doi.org/10.1007/s10072-016-2647-1.PubMedCrossRef

Dursun, E., & Gezen-Ak, D. (2017). Vitamin D receptor is present on the neuronal plasma membrane and is co-localized with amyloid precursor protein, ADAM10 or Nicastrin. PLoS ONE, 12(11), e0188605. https://doi.org/10.1371/journal.pone.0188605.PubMedPubMedCentralCrossRef

Dursun, E., Gezen-Ak, D., & Yilmazer, S. (2011). A novel perspective for Alzheimer’s disease: Vitamin D receptor suppression by amyloid-beta and preventing the amyloid-beta induced alterations by vitamin D in cortical neurons. Journal of Alzheimer’s Disease, 23(2), 207–219. https://doi.org/10.3233/JAD-2010-101377.PubMedCrossRef

Dursun, E., Gezen-Ak, D., & Yilmazer, S. (2013a). Beta amyloid suppresses the expression of the vitamin D receptor gene and induces the expression of the vitamin D catabolic enzyme gene in hippocampal neurons. Dementia and Geriatric Cognitive Disorders, 36(1–2), 76–86. https://doi.org/10.1159/000350319.PubMedCrossRef

Dursun, E., Gezen-Ak, D., & Yilmazer, S. (2013b). A new mechanism for amyloid-beta induction of iNOS: Vitamin D-VDR pathway disruption. Journal of Alzheimer’s Disease, 36(3), 459–474. https://doi.org/10.3233/JAD-130416.PubMedCrossRef

Ferrari, A., Hoerndli, F., Baechi, T., Nitsch, R. M., & Götz, J. (2003). β-Amyloid induces PHF-like tau filaments in tissue culture. Journal of Biological Chemistry, 278(41), 40162–40168.PubMedCrossRef

Gatta, L. B., Albertini, A., Ravid, R., & Finazzi, D. (2002). Levels of beta-secretase BACE and alpha-secretase ADAM10 mRNAs in Alzheimer hippocampus. Neuroreport, 13(16), 2031–2033.PubMedCrossRef

Gezen-Ak, D., Atasoy, I. L., Candas, E., Alaylioglu, M., Yilmazer, S., & Dursun, E. (2017). Vitamin D receptor regulates amyloid beta 1–42 production with protein disulfide isomerase A3. ACS Chemical Neuroscience, 8(10), 2335–2346. https://doi.org/10.1021/acschemneuro.7b00245.PubMedCrossRef

Gezen-Ak, D., Dursun, E., & Yilmazer, S. (2011). The effects of vitamin D receptor silencing on the expression of LVSCC-A1C and LVSCC-A1D and the release of NGF in cortical neurons. PLoS ONE, 6(3), e17553. https://doi.org/10.1371/journal.pone.0017553.PubMedPubMedCentralCrossRef

Gezen-Ak, D., Dursun, E., & Yilmazer, S. (2013). Vitamin D inquiry in hippocampal neurons: Consequences of vitamin D-VDR pathway disruption on calcium channel and the vitamin D requirement. Neurological Sciences, 34(8), 1453–1458.PubMedCrossRef

Gezen-Ak, D., Yilmazer, S., & Dursun, E. (2014). Why vitamin D in Alzheimer’s disease? The hypothesis. Journal of Alzheimer’s Disease, 40(2), 257–269. https://doi.org/10.3233/JAD-131970.PubMedCrossRef

Guerreiro, R., Wojtas, A., Bras, J., Carrasquillo, M., Rogaeva, E., Majounie, E., et al. (2013). TREM2 variants in Alzheimer’s disease. The New England Journal of Medicine, 368(2), 117–127. https://doi.org/10.1056/NEJMoa1211851.PubMedCrossRef

Hardy, J. (1997). Amyloid, the presenilins and Alzheimer’s disease. Trends in Neurosciences, 20, 154–159.PubMedCrossRef

Hardy, J. (2006). A hundred years of Alzheimer’s disease research. Neuron, 52(1), 3–13. https://doi.org/10.1016/j.neuron.2006.09.016.PubMedCrossRef

Huang, Y., & Mahley, R. W. (2014). Apolipoprotein E: Structure and function in lipid metabolism, neurobiology, and Alzheimer’s diseases. Neurobiology of Disease. https://doi.org/10.1016/j.nbd.2014.08.025.CrossRefPubMedPubMedCentral

Huang, Y. A., Zhou, B., Wernig, M., & Sudhof, T. C. (2017). ApoE2, ApoE3, and ApoE4 differentially stimulate APP transcription and Abeta secretion. Cell, 168(3), 427–441. https://doi.org/10.1016/j.cell.2016.12.044.PubMedPubMedCentralCrossRef

Iqbal, K., & Iqbal, I. G. (1991). Alzheimer’s disease: From cytoskeletal protein pathology to neuronal degeneration. In K. Iqbal, DRC McLachlan, B. Winbald & H. M. Wisniewski (Eds.), Alzheimer’s disease: Basic mechanisms, diagnosis and therapeutic strategies (pp. 173–180). Chichester: Wiley.

Jang, B. G., In, S., Choi, B., & Kim, M. J. (2014). Beta-amyloid oligomers induce early loss of presynaptic proteins in primary neurons by caspase-dependent and proteasome-dependent mechanisms. Neuroreport, 25(16), 1281–1288. https://doi.org/10.1097/WNR.0000000000000260.PubMedCrossRef

Jendresen, C., Arskog, V., Daws, M. R., & Nilsson, L. N. (2017). The Alzheimer’s disease risk factors apolipoprotein E and TREM2 are linked in a receptor signaling pathway. Journal of Neuroinflammation. https://doi.org/10.1186/s12974-017-0835-4.PubMedPubMedCentralCrossRef

Kimura, T., Ishiguro, K., & Hisanaga, S. (2014). Physiological and pathological phosphorylation of tau by Cdk5. Frontiers in Molecular Neuroscience. https://doi.org/10.3389/fnmol.2014.00065.PubMedPubMedCentralCrossRef

Kirouac, L., Rajic, A. J., Cribbs, D. H., & Padmanabhan, J. (2017). Activation of Ras-ERK signaling and GSK-3 by amyloid precursor protein and amyloid beta facilitates neurodegeneration in Alzheimer’s disease. eNeuro. https://doi.org/10.1523/ENEURO.0149-16.2017.CrossRefPubMedPubMedCentral

Kober, D. L., Alexander-Brett, J. M., Karch, C. M., Cruchaga, C., Colonna, M., Holtzman, M. J., et al. (2016). Neurodegenerative disease mutations in TREM2 reveal a functional surface and distinct loss-of-function mechanisms. Elife. https://doi.org/10.7554/eLife.20391.PubMedPubMedCentralCrossRef

Kuhn, P. H., Wang, H., Dislich, B., Colombo, A., Zeitschel, U., Ellwart, J. W., et al. (2010). ADAM10 is the physiologically relevant, constitutive alpha-secretase of the amyloid precursor protein in primary neurons. EMBO Journal, 29(17), 3020–3032. https://doi.org/10.1038/emboj.2010.167.PubMedCrossRef

Lahiri, D. K., & Maloney, B. (2010). Beyond the signaling effect role of amyloid-ss42 on the processing of APP, and its clinical implications. Experimental Neurology, 225(1), 51–54. https://doi.org/10.1016/j.expneurol.2010.04.018.PubMedPubMedCentralCrossRef

Li, F., & Tsien, J. Z. (2009). Memory and the NMDA receptors. The New England Journal of Medicine, 361(3), 302–303. https://doi.org/10.1056/NEJMcibr0902052.PubMedPubMedCentralCrossRef

Li, T., Hawkes, C., Qureshi, H. Y., Kar, S., & Paudel, H. K. (2006). Cyclin-dependent protein kinase 5 primes microtubule-associated protein tau site-specifically for glycogen synthase kinase 3beta. Biochemistry, 45(10), 3134–3145. https://doi.org/10.1021/bi051635j.PubMedCrossRef

Liu, C. C., Liu, C. C., Kanekiyo, T., Xu, H., & Bu, G. (2013). Apolipoprotein E and Alzheimer disease: Risk, mechanisms and therapy. Nature Reviews Neurology, 9(2), 106–118. https://doi.org/10.1038/nrneurol.2012.263.PubMedPubMedCentralCrossRef

Liu, J., Chang, L., Roselli, F., Almeida, O. F., Gao, X., Wang, X., et al. (2010). Amyloid-beta induces caspase-dependent loss of PSD-95 and synaptophysin through NMDA receptors. Journal of Alzheimer’s Disease, 22(2), 541–556. https://doi.org/10.3233/JAD-2010-100948.PubMedCrossRef

Lopes, J. P., Oliveira, C. R., & Agostinho, P. (2009). Cdk5 acts as a mediator of neuronal cell cycle re-entry triggered by amyloid-beta and prion peptides. Cell Cycle, 8(1), 97–104. https://doi.org/10.4161/cc.8.1.7506.PubMedCrossRef

Lue, L. F., Schmitz, C. T., Serrano, G., Sue, L. I., Beach, T. G., & Walker, D. G. (2015). TREM2 protein expression changes correlate with Alzheimer’s disease neurodegenerative pathologies in post-mortem temporal cortices. Brain Pathology, 25(4), 469–480. https://doi.org/10.1111/bpa.12190.PubMedCrossRef

Maloney, B., Ge, Y. W., Petersen, R. C., Hardy, J., Rogers, J. T., Perez-Tur, J., et al. (2010). Functional characterization of three single-nucleotide polymorphisms present in the human APOE promoter sequence: Differential effects in neuronal cells and on DNA-protein interactions. American Journal of Medical Genetics Part B: Neuropsychiatric Genetics, 153B(1), 185–201. https://doi.org/10.1002/ajmg.b.30973.CrossRef

Maloney, B., & Lahiri, D. K. (2011). The Alzheimer’s amyloid beta-peptide (Abeta) binds a specific DNA Abeta-interacting domain (AbetaID) in the APP, BACE1, and APOE promoters in a sequence-specific manner: Characterizing a new regulatory motif. Gene, 488(1–2), 1–12. https://doi.org/10.1016/j.gene.2011.06.004.PubMedPubMedCentralCrossRef

Maloney, B., & Lahiri, D. K. (2016). Epigenetics of dementia: Understanding the disease as a transformation rather than a state. The Lancet Neurology, 15(7), 760–774. https://doi.org/10.1016/S1474-4422(16)00065-X.PubMedCrossRef

Mamada, N., Tanokashira, D., Hosaka, A., Kametani, F., Tamaoka, A., & Araki, W. (2015). Amyloid beta-protein oligomers upregulate the beta-secretase, BACE1, through a post-translational mechanism involving its altered subcellular distribution in neurons. Molecular Brain. https://doi.org/10.1186/s13041-015-0163-5.PubMedPubMedCentralCrossRef

Manassero, G., Guglielmotto, M., Zamfir, R., Borghi, R., Colombo, L., Salmona, M., et al. (2016). Beta-amyloid 1–42 monomers, but not oligomers, produce PHF-like conformation of Tau protein. Aging Cell, 15(5), 914–923. https://doi.org/10.1111/acel.12500.PubMedPubMedCentralCrossRef

Mandelkow, E. M., & Mandelkow, E. (1998). Tau in Alzheimer’s disease. Trends Cell Biol, 8, 425–427.PubMedCrossRef

Matsushima, H., Shimohama, S., Chachin, M., Taniguchi, T., & Kimura, J. (1996). Ca²⁺-dependent and Ca²⁺-independent protein kinase C changes in the brain of patients with Alzheimer’s disease. Journal of Neurochemistry, 67(1), 317–323.PubMedCrossRef

Moh, C., Kubiak, J. Z., Bajic, V. P., Zhu, X., Smith, M. A., & Lee, H. G. (2011). Cell cycle deregulation in the neurons of Alzheimer’s disease. Results and Problems in Cell Differentiation, 53, 565–576. https://doi.org/10.1007/978-3-642-19065-0_23.PubMedPubMedCentralCrossRef

Moreno, H., Morfini, G., Buitrago, L., Ujlaki, G., Choi, S., Yu, E., et al. (2016). Tau pathology-mediated presynaptic dysfunction. Neuroscience, 325, 30–38. https://doi.org/10.1016/j.neuroscience.2016.03.044.PubMedPubMedCentralCrossRef

Multhaup, G., Huber, O., Buee, L., & Galas, M. C. (2015). Amyloid precursor protein (APP) metabolites APP intracellular fragment (AICD), Abeta42, and Tau in nuclear roles. Journal of Biological Chemistry, 290(39), 23515–23522. https://doi.org/10.1074/jbc.R115.677211.PubMedCrossRef

Nolan, T., Hands, B. E., & Bustin, S. A. (2006). Quantification of mRNA using real-time RT-PCR. Natureprotocols, 1(3), 1556–1582.

Parsons, M. P., & Raymond, L. A. (2014). Extrasynaptic NMDA receptor involvement in central nervous system disorders. Neuron, 82(2), 279–293. https://doi.org/10.1016/j.neuron.2014.03.030.PubMedCrossRef

Pearson, H. A., & Peers, C. (2006). Physiological roles for amyloid beta peptides. The Journal of Physiology, 575(Pt 1), 5–10. https://doi.org/10.1113/jphysiol.2006.111203.PubMedPubMedCentralCrossRef

Price, P., & Brewer, G. J. (1998). Serum-free media for neural cell cultures. In S. Fedoroff & A. Richardson (Eds.), Protocols for neural cell culture (3 ed., pp. 255–264). New Jersey: Humana Press.

Refolo, L. M., Eckman, C., Prada, C. M., Yager, D., Sambamurti, K., Mehta, N., et al. (1999). Antisense-induced reduction of presenilin 1 expression selectively increases the production of amyloid beta42 in transfected cells. Journal of Neurochemistry, 73(6), 2383–2388.PubMedCrossRef

Sacktor, T. C., Osten, P., Valsamis, H., Jiang, X., Naik, M. U., & Sublette, E. (1993). Persistent activation of the zeta isoform of protein kinase C in the maintenance of long-term potentiation. Proceedings of the National Academy of Sciences of the United States of America, 90(18), 8342–8346.PubMedPubMedCentralCrossRef

Selkoe, D. J., & Hardy, J. (2016). The amyloid hypothesis of Alzheimer’s disease at 25 years. EMBO Molecular Medicine, 8(6), 595–608. https://doi.org/10.15252/emmm.201606210.PubMedPubMedCentralCrossRef

Seo, S. J., Hwang, D. Y., Cho, J. S., Chae, K. R., Kim, C. K., Shim, S. B., et al. (2007). PEN-2 overexpression induces gamma-secretase protein and its activity with amyloid beta-42 production. Neurochemical Research, 32(6), 1016–1023. https://doi.org/10.1007/s11064-006-9262-0.PubMedCrossRef

Sidera, C., Liu, C., & Austen, B. (2002). Pro-domain removal in ASP-2 and the cleavage of the amyloid precursor are influenced by pH. BMC Biochemistry, 3, 25.PubMedPubMedCentralCrossRef

Soscia, S. J., Kirby, J. E., Washicosky, K. J., Tucker, S. M., Ingelsson, M., Hyman, B., et al. (2010). The Alzheimer’s disease-associated amyloid beta-protein is an antimicrobial peptide. PLoS ONE, 5(3), e9505. https://doi.org/10.1371/journal.pone.0009505.PubMedPubMedCentralCrossRef

Sutherland, M. K., Somerville, M. J., Yoong, L. K., Bergeron, C., Haussler, M. R., & McLachlan, D. R. (1992). Reduction of vitamin D hormone receptor mRNA levels in Alzheimer as compared to Huntington hippocampus: Correlation with calbindin-28 k mRNA levels. Molecular Brain Research, 13(3), 239–250.PubMedCrossRef

Takahashi-Yanaga, F., & Sasaguri, T. (2008). GSK-3beta regulates cyclin D1 expression: A new target for chemotherapy. Cell Signal, 20(4), 581–589. https://doi.org/10.1016/j.cellsig.2007.10.018.PubMedCrossRef

Tsai, L. H., Takahashi, T., Caviness, V. S. Jr., & Harlow, E. (1993). Activity and expression pattern of cyclin-dependent kinase 5 in the embryonic mouse nervous system. Development, 119(4), 1029–1040.PubMed

Vadukul, D. M., Gbajumo, O., Marshall, K. E., & Serpell, L. C. (2017). Amyloidogenicity and toxicity of the reverse and scrambled variants of amyloid-beta 1–42. FEBS Letter, 591(5), 822–830. https://doi.org/10.1002/1873-3468.12590.CrossRef

Wang, Z. F., Li, H. L., Li, X. C., Zhang, Q., Tian, Q., Wang, Q., et al. (2006). Effects of endogenous beta-amyloid overproduction on tau phosphorylation in cell culture. Journal of Neurochemistry, 98(4), 1167–1175. https://doi.org/10.1111/j.1471-4159.2006.03956.x.PubMedCrossRef

Yu, H., Saura, C. A., Choi, S. Y., Sun, L. D., Yang, X., Handler, M., et al. (2001). APP processing and synaptic plasticity in presenilin-1 conditional knockout mice. Neuron, 31(5), 713–726.PubMedCrossRef

Zhang, Y., Zong, W., Zhang, L., Ma, Y., & Wang, J. (2016). Protein kinase M zeta and the maintenance of long-term memory. Neurochemistry International, 99, 215–220. https://doi.org/10.1016/j.neuint.2016.07.007.PubMedCrossRef

Zheng, L., Cedazo-Minguez, A., Hallbeck, M., Jerhammar, F., Marcusson, J., & Terman, A. (2012). Intracellular distribution of amyloid beta peptide and its relationship to the lysosomal system. Translational Neurodegeneration, 1(1), 19. https://doi.org/10.1186/2047-9158-1-19.PubMedPubMedCentralCrossRef

Titel: The Transcriptional Regulatory Properties of Amyloid Beta 1–42 may Include Regulation of Genes Related to Neurodegeneration
verfasst von: Duygu Gezen-Ak
İrem L. Atasoy
Esin Candaş
Merve Alaylıoğlu
Erdinç Dursun
Publikationsdatum: 12.06.2018
Verlag: Springer US
Erschienen in: NeuroMolecular Medicine / Ausgabe 3/2018
Print ISSN: 1535-1084
Elektronische ISSN: 1559-1174
DOI: https://doi.org/10.1007/s12017-018-8498-6

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