Acknowledgement
This research was supported by intramural grants (2E31881) from the Korea Institute of Science and Technology (KIST) and the Basic Science Research Program (2018R1D1A1B07050182) from the Ministry of Education in Korea.
References
- Antonsson, B., Conti, F., Ciavatta, A., Montessuit, S., Lewis, S., Martinou, I., Bernasconi, L., Bernard, A., Mermod, J.J., Mazzei, G., et al. (1997). Inhibition of Bax channel-forming activity by Bcl-2. Science 277, 370-372. https://doi.org/10.1126/science.277.5324.370
- Asadi, M., Taghizadeh, S., Kaviani, E., Vakili, O., Taheri-Anganeh, M., Tahamtan, M., and Savardashtaki, A. (2022). Caspase-3: structure, function, and biotechnological aspects. Biotechnol. Appl. Biochem. 69, 1633-1645. https://doi.org/10.1002/bab.2233
- Baker, K.D., Edwards, T.M., and Rickard, N.S. (2013). The role of intracellular calcium stores in synaptic plasticity and memory consolidation. Neurosci. Biobehav. Rev. 37, 1211-1239. https://doi.org/10.1016/j.neubiorev.2013.04.011
- Berridge, M.J. (2011). Calcium signalling and Alzheimer's disease. Neurochem. Res. 36, 1149-1156. https://doi.org/10.1007/s11064-010-0371-4
- Bloom, G.S. (2014). Amyloid-beta and tau: the trigger and bullet in Alzheimer disease pathogenesis. JAMA Neurol. 71, 505-508. https://doi.org/10.1001/jamaneurol.2013.5847
- Bojarski, L., Herms, J., and Kuznicki, J. (2008). Calcium dysregulation in Alzheimer's disease. Neurochem. Int. 52, 621-633. https://doi.org/10.1016/j.neuint.2007.10.002
- Calissano, P., Matrone, C., and Amadoro, G. (2009). Apoptosis and in vitro Alzheimer's disease neuronal models. Commun. Integr. Biol. 2, 163-169. https://doi.org/10.4161/cib.7704
- Calvo-Rodriguez, M., Hou, S.S., Snyder, A.C., Kharitonova, E.K., Russ, A.N., Das, S., Fan, Z., Muzikansky, A., Garcia-Alloza, M., Serrano-Pozo, A., et al. (2020). Increased mitochondrial calcium levels associated with neuronal death in a mouse model of Alzheimer's disease. Nat. Commun. 11, 2146.
- Cascella, R. and Cecchi, C. (2021). Calcium dyshomeostasis in Alzheimer's disease pathogenesis. Int. J. Mol. Sci. 22, 4914.
- Corona, C., Masciopinto, F., Silvestri, E., Viscovo, A.D., Lattanzio, R., Sorda, R.L., Ciavardelli, D., Goglia, F., Piantelli, M., Canzoniero, L.M., et al. (2010). Dietary zinc supplementation of 3xTg-AD mice increases BDNF levels and prevents cognitive deficits as well as mitochondrial dysfunction. Cell Death Dis. 1, e91.
- Cregan, S.P., MacLaurin, J.G., Craig, C.G., Robertson, G.S., Nicholson, D.W., Park, D.S., and Slack, R.S. (1999). Bax-dependent caspase-3 activation is a key determinant in p53-induced apoptosis in neurons. J. Neurosci. 19, 7860-7869. https://doi.org/10.1523/JNEUROSCI.19-18-07860.1999
- D'Amelio, M., Sheng, M., and Cecconi, F. (2012). Caspase-3 in the central nervous system: beyond apoptosis. Trends Neurosci. 35, 700-709. https://doi.org/10.1016/j.tins.2012.06.004
- DeTure, M.A. and Dickson, D.W. (2019). The neuropathological diagnosis of Alzheimer's disease. Mol. Neurodegener. 14, 32.
- Du, Y., Fu, M., Huang, Z., Tian, X., Li, J., Pang, Y., Song, W., Tian Wang, Y., and Dong, Z. (2020). TRPV1 activation alleviates cognitive and synaptic plasticity impairments through inhibiting AMPAR endocytosis in APP23/PS45 mouse model of Alzheimer's disease. Aging Cell 19, e13113.
- Eimer, W.A. and Vassar, R. (2013). Neuron loss in the 5XFAD mouse model of Alzheimer's disease correlates with intraneuronal Aβ42 accumulation and Caspase-3 activation. Mol. Neurodegener. 8, 2.
- Elena-Real, C.A., Diaz-Quintana, A., Gonzalez-Arzola, K., Velazquez-Campoy, A., Orzaez, M., Lopez-Rivas, A., Gil-Caballero, S., De la Rosa, M.A., and Diaz-Moreno, I. (2018). Cytochrome c speeds up caspase cascade activation by blocking 14-3-3ε-dependent Apaf-1 inhibition. Cell Death Dis. 9, 365.
- Ferrer, I., Marin, C., Rey, M.J., Ribalta, T., Goutan, E., Blanco, R., Tolosa, E., and Marti, E. (1999). BDNF and full-length and truncated TrkB expression in Alzheimer disease. Implications in therapeutic strategies. J. Neuropathol. Exp. Neurol. 58, 729-739. https://doi.org/10.1097/00005072-199907000-00007
- Finkbeiner, S., Tavazoie, S.F., Maloratsky, A., Jacobs, K.M., Harris, K.M., and Greenberg, M.E. (1997). CREB: a major mediator of neuronal neurotrophin responses. Neuron 19, 1031-1047. https://doi.org/10.1016/S0896-6273(00)80395-5
- Fletcher, J.I., Meusburger, S., Hawkins, C.J., Riglar, D.T., Lee, E.F., Fairlie, W.D., Huang, D.C., and Adams, J.M. (2008). Apoptosis is triggered when prosurvival Bcl-2 proteins cannot restrain Bax. Proc. Natl. Acad. Sci. U. S. A. 105, 18081-18087. https://doi.org/10.1073/pnas.0808691105
- Folch, J., Busquets, O., Ettcheto, M., Sanchez-Lopez, E., Castro-Torres, R.D., Verdaguer, E., Garcia, M.L., Olloquequi, J., Casadesus, G., Beas-Zarate, C., et al. (2018). Memantine for the treatment of dementia: a review on its current and future applications. J. Alzheimers Dis. 62, 1223-1240. https://doi.org/10.3233/JAD-170672
- Fumagalli, F., Racagni, G., and Riva, M. (2006). The expanding role of BDNF: a therapeutic target for Alzheimer's disease? Pharmacogenomics J. 6, 8-15. https://doi.org/10.1038/sj.tpj.6500337
- Gorman, A.M., Ceccatelli, S., and Orrenius, S. (2000). Role of mitochondria in neuronal apoptosis. Dev. Neurosci. 22, 348-358. https://doi.org/10.1159/000017460
- Green, K.N. and LaFerla, F.M. (2008). Linking calcium to Abeta and Alzheimer's disease. Neuron 59, 190-194. https://doi.org/10.1016/j.neuron.2008.07.013
- Hippius, H. and Neundorfer, G. (2003). The discovery of Alzheimer's disease. Dialogues Clin. Neurosci. 5, 101-108. https://doi.org/10.31887/DCNS.2003.5.1/hhippius
- Ichimiya, Y., Emson, P.C., Mountjoy, C.Q., Lawson, D.E.M., and Heizmann, C.W. (1988). Loss of calbindin-28K immunoreactive neurones from the cortex in Alzheimer-type dementia. Brain Res. 475, 156-159. https://doi.org/10.1016/0006-8993(88)90210-7
- Impey, S., Obrietan, K., and Storm, D.R. (1999). Making new connections: role of ERK/MAP kinase signaling in neuronal plasticity. Neuron 23, 11-14. https://doi.org/10.1016/S0896-6273(00)80747-3
- Jadiya, P., Kolmetzky, D.W., Tomar, D., Di Meco, A., Lombardi, A.A., Lambert, J.P., Luongo, T.S., Ludtmann, M.H., Pratico, D., and Elrod, J.W. (2019). Impaired mitochondrial calcium efflux contributes to disease progression in models of Alzheimer's disease. Nat. Commun. 10, 3885.
- Jantas, D., Szymanska, M., Budziszewska, B., and Lason, W. (2009). An involvement of BDNF and PI3-K/Akt in the anti-apoptotic effect of memantine on staurosporine-evoked cell death in primary cortical neurons. Apoptosis 14, 900-912. https://doi.org/10.1007/s10495-009-0370-6
- Kim, J., Lee, S., Kim, J., Ham, S., Park, J.H.Y., Han, S., Jung, Y.K., Shim, I., Han, J.S., Lee, K.W., et al. (2020). Ca2+-permeable TRPV1 pain receptor knockout rescues memory deficits and reduces amyloid-β and tau in a mouse model of Alzheimer's disease. Hum. Mol. Genet. 29, 228-237. https://doi.org/10.1093/hmg/ddz276
- Ku, B., Liang, C., Jung, J.U., and Oh, B.H. (2011). Evidence that inhibition of BAX activation by BCL-2 involves its tight and preferential interaction with the BH3 domain of BAX. Cell Res. 21, 627-641. https://doi.org/10.1038/cr.2010.149
- LeBlanc, A.C. (2005). The role of apoptotic pathways in Alzheimer's disease neurodegeneration and cell death. Curr. Alzheimer Res. 2, 389-402. https://doi.org/10.2174/156720505774330573
- Lee, J., Saloman, J.L., Weiland, G., Auh, Q.S., Chung, M.K., and Ro, J.Y. (2012). Functional interactions between NMDA receptors and TRPV1 in trigeminal sensory neurons mediate mechanical hyperalgesia in the rat masseter muscle. Pain 153, 1514-1524. https://doi.org/10.1016/j.pain.2012.04.015
- Lu, J., Zhou, W., Dou, F., Wang, C., and Yu, Z. (2021). TRPV1 sustains microglial metabolic reprogramming in Alzheimer's disease. EMBO Rep. 22, e52013.
- Meller, R., Minami, M., Cameron, J.A., Impey, S., Chen, D., Lan, J.Q., Henshall, D.C., and Simon, R.P. (2005). CREB-mediated Bcl-2 protein expression after ischemic preconditioning. J. Cereb. Blood Flow Metab. 25, 234-246. https://doi.org/10.1038/sj.jcbfm.9600024
- Minichiello, L., Calella, A.M., Medina, D.L., Bonhoeffer, T., Klein, R., and Korte, M. (2002). Mechanism of TrkB-mediated hippocampal long-term potentiation. Neuron 36, 121-137. https://doi.org/10.1016/S0896-6273(02)00942-X
- Miranda, M., Morici, J.F., Zanoni, M.B., and Bekinschtein, P. (2019). Brain-derived neurotrophic factor: a key molecule for memory in the healthy and the pathological brain. Front. Cell. Neurosci. 13, 363.
- Park, E.M. and Cho, S. (2006). Enhanced ERK dependent CREB activation reduces apoptosis in staurosporine-treated human neuroblastoma SK-N-BE (2) C cells. Neurosci. Lett. 402, 190-194. https://doi.org/10.1016/j.neulet.2006.04.004
- Porter, A.G. and Janicke, R.U. (1999). Emerging roles of caspase-3 in apoptosis. Cell Death Differ. 6, 99-104. https://doi.org/10.1038/sj.cdd.4400476
- Rai, S.N., Dilnashin, H., Birla, H., Singh, S.S., Zahra, W., Rathore, A.S., Singh, B.K., and Singh, S.P. (2019). The role of PI3K/Akt and ERK in neurodegenerative disorders. Neurotox. Res. 35, 775-795. https://doi.org/10.1007/s12640-019-0003-y
- Robinson, D.M. and Keating, G.M. (2006). Memantine: a review of its use in Alzheimer's disease. Drugs 66, 1515-1534. https://doi.org/10.2165/00003495-200666110-00015
- Sairanen, T., Szepesi, R., Karjalainen-Lindsberg, M.L., Saksi, J., Paetau, A., and Lindsberg, P.J. (2009). Neuronal caspase-3 and PARP-1 correlate differentially with apoptosis and necrosis in ischemic human stroke. Acta Neuropathol. 118, 541-552. https://doi.org/10.1007/s00401-009-0559-3
- Santos, A.R., Comprido, D., and Duarte, C.B. (2010). Regulation of local translation at the synapse by BDNF. Prog. Neurobiol. 92, 505-516. https://doi.org/10.1016/j.pneurobio.2010.08.004
- Saura, C.A. and Valero, J. (2011). The role of CREB signaling in Alzheimer's disease and other cognitive disorders. Rev. Neurosci. 22, 153-169. https://doi.org/10.1515/rns.2011.018
- Scheff, S.W. and Price, D.A. (2006). Alzheimer's disease-related alterations in synaptic density: neocortex and hippocampus. J. Alzheimers Dis. 9(3 Suppl), 101-115. https://doi.org/10.3233/JAD-2006-9S312
- Shacka, J.J. and Roth, K.A. (2005). Regulation of neuronal cell death and neurodegeneration by members of the Bcl-2 family: therapeutic implications. Curr. Drug Targets CNS Neurol. Disord. 4, 25-39. https://doi.org/10.2174/1568007053005127
- Takahashi, K., Nakagawasai, O., Nemoto, W., Kadota, S., Isono, J., Odaira, T., Sakuma, W., Arai, Y., Tadano, T., and Tan-No, K. (2018). Memantine ameliorates depressive-like behaviors by regulating hippocampal cell proliferation and neuroprotection in olfactory bulbectomized mice. Neuropharmacology 137, 141-155. https://doi.org/10.1016/j.neuropharm.2018.04.013
- Tanqueiro, S.R., Ramalho, R.M., Rodrigues, T.M., Lopes, L.V., Sebastiao, A.M., and Diogenes, M.J. (2018). Inhibition of NMDA receptors prevents the loss of BDNF function induced by amyloid β. Front. Pharmacol. 9, 237.
- Vanhoutte, P. and Bading, H. (2003). Opposing roles of synaptic and extrasynaptic NMDA receptors in neuronal calcium signalling and BDNF gene regulation. Curr. Opin. Neurobiol. 13, 366-371. https://doi.org/10.1016/S0959-4388(03)00073-4
- Wang, X. (2001). The expanding role of mitochondria in apoptosis. Genes Dev. 15, 2922-2933.
- Wang, X., Chen, J., Wang, H., Yu, H., Wang, C., You, J., Wang, P., Feng, C., Xu, G., Wu, X., et al. (2017a). Memantine can reduce ethanol-induced caspase-3 activity and apoptosis in H4 cells by decreasing intracellular calcium. J. Mol. Neurosci. 62, 402-411. https://doi.org/10.1007/s12031-017-0948-3
- Wang, X., Yu, H., You, J., Wang, C., Feng, C., Liu, Z., Li, Y., Wei, R., Xu, S., Zhao, R., et al. (2018). Memantine can improve chronic ethanol exposure-induced spatial memory impairment in male C57BL/6 mice by reducing hippocampal apoptosis. Toxicology 406-407, 21-32. https://doi.org/10.1016/j.tox.2018.05.013
- Wang, Y., Shi, Y., and Wei, H. (2017b). Calcium dysregulation in Alzheimer's disease: a target for new drug development. J. Alzheimers Dis. Parkinsonism 7, 374.
- Yin, X.M., Oltvai, Z.N., and Korsmeyer, S.J. (1994). BH1 and BH2 domains of Bcl-2 are required for inhibition of apoptosis and heterodimerization with Bax. Nature 369, 321-323. https://doi.org/10.1038/369321a0
- Yuan, J., Murrell, G.A., Trickett, A., and Wang, M.X. (2003). Involvement of cytochrome c release and caspase-3 activation in the oxidative stress-induced apoptosis in human tendon fibroblasts. Biochim. Biophys. Acta 1641, 35-41. https://doi.org/10.1016/S0167-4889(03)00047-8
- Zarneshan, S.N., Fakhri, S., and Khan, H. (2022). Targeting Akt/CREB/BDNF signaling pathway by ginsenosides in neurodegenerative diseases: a mechanistic approach. Pharmacol. Res. 177, 106099.
- Zhai, K., Liskova, A., Kubatka, P., and Busselberg, D. (2020). Calcium entry through TRPV1: a potential target for the regulation of proliferation and apoptosis in cancerous and healthy cells. Int. J. Mol. Sci. 21, 4177.
- Zheng, Z., Sabirzhanov, B., and Keifer, J. (2010). Oligomeric amyloid-β inhibits the proteolytic conversion of brain-derived neurotrophic factor (BDNF), AMPA receptor trafficking, and classical conditioning. J. Biol. Chem. 285, 34708-34717. https://doi.org/10.1074/jbc.M110.150821
- Zhu, G., Li, J., He, L., Wang, X., and Hong, X. (2015). MPTP-induced changes in hippocampal synaptic plasticity and memory are prevented by memantine through the BDNF-TrkB pathway. Br. J. Pharmacol. 172, 2354-2368. https://doi.org/10.1111/bph.13061