Blockade of EphA4 signaling ameliorates hippocampal synaptic dysfunctions in mouse models of Alzheimer’s disease
Open accessAbstract
Significance: Synaptic loss and dysfunction is associated with cognitive impairment in Alzheimer’s disease (AD). However, the pathophysiological mechanisms underlying synaptic impairment are largely unknown. Here, we reveal a previously unidentified signaling pathway whereby activation of a receptor tyrosine kinase EphA4 is critical for synaptic dysfunctions in AD. Proof-of-concept studies undertaken in both in vitro and in vivo systems demonstrate its importance in mediating the deficit of synaptic transmission and hippocampal long-term potentiation in AD models. Specifically, blocking the EphA4-dependent pathway through knockdown studies or the use of small-molecule inhibitors effectively rescues the impaired synaptic transmission induced by Aβ and reverses impaired synaptic plasticity in AD mouse models. Thus, this study reveals a new disease-modifying therapeutic intervention for AD.
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Rhynchophylline blocks EphA4 signaling, thereby preventing LTP impairment in an AD mice model.
“In addition, a plant alkaloid rhynchophylline was shown to block EphA4 signaling, thereby preventing LTP impairment in an AD mice model [81].”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [81]
oAβ can bind to EphA4 and induce its activation, and inhibition or absence of EphA4 in hippocampal neurons prevents synaptic loss.
“oAβ can bind to EphA4 and induce its activation, and inhibition or absence of EphA4 in hippocampal neurons prevents synaptic loss [81].”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [81]
LTP is significantly impaired in 6- to 7-mo-old APP/PS1 mice.
“Whereas high-frequency stimulation significantly increased the magnitude of long-term potentiation (LTP) at Schaffer collateral (SC)-CA1 synapses in the hippocampus of wild type (WT) mice, LTP was significantly impaired in 6-to 7-mo-old APP/PS1 mice (17,18).”
From IL-33 ameliorates Alzheimer's disease-like pathology and cognitive decline (2016) · cites this paper as [18]
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Cites
Alzheimer's Disease Is a Synaptic Failure
Selkoe, D. J. (2002) · Science · doi:10.1126/science.1074069 · Cited by 4,420 · see citing works
Walsh, D. M., Klyubin, I., Fadeeva, J. V., Cullen, W. K., Anwyl, R., Wolfe, M. S., Rowan, M. J., & Selkoe, D. J. (2002) · Nature · doi:10.1038/416535a · Cited by 4,291 · see citing works
Shankar, G. M., Li, S., Mehta, T. H., Garcia-Munoz, A., Shepardson, N. E., Smith, I., Brett, F. M., Farrell, M. A., Rowan, M. J., Lemere, C. A., et al. (2008) · Nature Medicine · doi:10.1038/nm1782 · Cited by 3,685 · see citing works
Lambert, M. P., Barlow, A. K., Chromy, B. A., Edwards, C., Freed, R., Liosatos, M., Morgan, T. E., Rozovsky, I., Trommer, B., Viola, K. L., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.6448 · Cited by 3,506 · see citing works
A semiempirical free energy force field with charge‐based desolvation
Huey, R., Morris, G. M., Olson, A. J., & Goodsell, D. S. (2007) · Journal of Computational Chemistry · doi:10.1002/jcc.20634 · Cited by 2,246 · see citing works
Alzheimer Mechanisms and Therapeutic Strategies
Huang, Y., & Mucke, L. (2012) · Cell · doi:10.1016/j.cell.2012.02.040 · Cited by 1,758 · see citing works
Shankar, G. M., Bloodgood, B. L., Townsend, M., Walsh, D. M., Selkoe, D. J., & Sabatini, B. L. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.4970-06.2007 · Cited by 1,592 · see citing works
Regulation of NMDA receptor trafficking by amyloid-β
Snyder, E. M., Nong, Y., Almeida, C. G., Paul, S., Moran, T., Choi, E. Y., Nairn, A. C., Salter, M. W., Lombroso, P. J., Gouras, G. K., et al. (2005) · Nature Neuroscience · doi:10.1038/nn1503 · Cited by 1,561 · cited 1× · see citing works
“Synaptic defects triggered by Aβ are mediated by the internalization and downregulation of both NMDA- and AMPA-type glutamate receptors (8, 9) together with a reduction of dendritic spines (6), where excitatory synapses are located.”
Eph-Ephrin Bidirectional Signaling in Physiology and Disease
Pasquale, E. B. (2008) · Cell · doi:10.1016/j.cell.2008.03.011 · Cited by 1,251 · see citing works
Lacor, P. N., Buniel, M. C., Furlow, P. W., Sanz Clemente, A., Velasco, P. T., Wood, M., Viola, K. L., & Klein, W. L. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.3501-06.2007 · Cited by 1,188 · see citing works
AMPAR Removal Underlies Aβ-Induced Synaptic Depression and Dendritic Spine Loss
Hsieh, H., Boehm, J., Sato, C., Iwatsubo, T., Tomita, T., Sisodia, S., & Malinow, R. (2006) · Neuron · doi:10.1016/j.neuron.2006.10.035 · Cited by 1,042 · see citing works
Neurotoxicity of Amyloid -Protein: Synaptic and Network Dysfunction
Mucke, L., & Selkoe, D. J. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006338 · Cited by 1,000 · see citing works
Li, S., Hong, S., Shepardson, N. E., Walsh, D. M., Shankar, G. M., & Selkoe, D. (2009) · Neuron · doi:10.1016/j.neuron.2009.05.012 · Cited by 972 · see citing works
Synaptic Targeting by Alzheimer's-Related Amyloid β Oligomers
Lacor, P. N., Buniel, M. C., Chang, L., Fernandez, S. J., Gong, Y., Viola, K. L., Lambert, M. P., Velasco, P. T., Bigio, E. H., Finch, C. E., et al. (2004) · The Journal of Neuroscience · doi:10.1523/jneurosci.3432-04.2004 · Cited by 954 · see citing works
Koffie, R. M., Meyer-Luehmann, M., Hashimoto, T., Adams, K. W., Mielke, M. L., Garcia-Alloza, M., Micheva, K. D., Smith, S. J., Kim, M. L., Lee, V. M., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0811698106 · Cited by 850 · see citing works
EphB Receptors Interact with NMDA Receptors and Regulate Excitatory Synapse Formation
Dalva, M. B., Takasu, M. A., Lin, M. Z., Shamah, S. M., Hu, L. S., Gale, N. W., & Greenberg, M. E. (2000) · Cell · doi:10.1016/s0092-8674(00)00197-5 · Cited by 716 · see citing works
Early-onset behavioral and synaptic deficits in a mouse model of Alzheimer's disease
Jacobsen, J. S., Wu, C.-C., Redwine, J. M., Comery, T. A., Arias, R., Bowlby, M., Martone, R., Morrison, J. H., Pangalos, M. N., Reinhart, P. H., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0600948103 · Cited by 701 · see citing works
Control of hippocampal dendritic spine morphology through ephrin-A3/EphA4 signaling
Murai, K. K., Nguyen, L. N., Irie, F., Yamaguchi, Y., & Pasquale, E. B. (2003) · Nature Neuroscience · doi:10.1038/nn994 · Cited by 516 · see citing works
Synapses and Alzheimer's Disease
Sheng, M., Sabatini, B. L., & Sudhof, T. C. (2012) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a005777 · Cited by 436 · see citing works
Reversing EphB2 depletion rescues cognitive functions in Alzheimer model
Cissé, M., Halabisky, B., Harris, J., Devidze, N., Dubal, D. B., Sun, B., Orr, A., Lotz, G., Kim, D. H., Hamto, P., et al. (2011) · Nature · doi:10.1038/nature09635 · Cited by 433 · see citing works
Bidirectional modulation of synaptic functions by Eph/ephrin signaling
Klein, R. (2008) · Nature Neuroscience · doi:10.1038/nn.2231 · Cited by 419 · see citing works
Shen, L., Kim, S., Risacher, S. L., Nho, K. T., Swaminathan, S., West, J. D., Foroud, T., Pankratz, N., Moore, J. H., Sloan, C., et al. (2010) · NeuroImage · doi:10.1016/j.neuroimage.2010.01.042 · Cited by 379 · see citing works
Vaccination with soluble Aβ oligomers generates toxicity‐neutralizing antibodies
Lambert, M. P., Viola, K. L., Chromy, B. A., Chang, L., Morgan, T. E., Yu, J., Venton, D. L., Krafft, G. A., Finch, C. E., & Klein, W. L. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00592.x · Cited by 349 · see citing works
Cdk5 regulates EphA4-mediated dendritic spine retraction through an ephexin1-dependent mechanism
Fu, W., Chen, Y., Şahin, M., Zhao, X.-S., Shi, L., Bikoff, J. B., Lai, K., Yung, W., Fu, A. K. Y., Greenberg, M. E., et al. (2006) · Nature Neuroscience · doi:10.1038/nn1811 · Cited by 311 · see citing works
Self-citationAβ1-42 inhibition of LTP is mediated by a signaling pathway involving caspase-3, Akt1 and GSK-3β
Jo, J., Whitcomb, D. J., Olsen, K. M., Kerrigan, T. L., Lo, S.-C., Bru-Mercier, G., Dickinson, B., Scullion, S., Sheng, M., Collingridge, G., et al. (2011) · Nature Neuroscience · doi:10.1038/nn.2785 · Cited by 305 · see citing works
Sala, C., Futai, K., Yamamoto, K., Worley, P. F., Hayashi, Y., & Sheng, M. (2003) · The Journal of Neuroscience · doi:10.1523/jneurosci.23-15-06327.2003 · Cited by 288 · see citing works
Neuron-glia communication via EphA4/ephrin-A3 modulates LTP through glial glutamate transport
Filosa, A., Paixão, S., Honsek, S. D., Carmona, M. A., Becker, L., Feddersen, B., Gaitanos, L., Rudhard, Y., Schoepfer, R., Klopstock, T., et al. (2009) · Nature Neuroscience · doi:10.1038/nn.2394 · Cited by 283 · see citing works
A Comprehensive Genetic Association Study of Alzheimer Disease in African Americans
Logue, M. W. (2011) · Archives of Neurology · doi:10.1001/archneurol.2011.646 · Cited by 250 · see citing works
APCCdh1 mediates EphA4-dependent downregulation of AMPA receptors in homeostatic plasticity
Fu, A. K. Y., Hung, K.-W., Fu, W., Shen, C., Chen, Y., Xia, J., Lai, K., & Ip, N. Y. (2010) · Nature Neuroscience · doi:10.1038/nn.2715 · Cited by 180 · see citing works
Self-citationRhynchophylline and isorhynchophylline inhibit NMDA receptors expressed in Xenopus oocytes
Kang, T.-H., Murakami, Y., Matsumoto, K., Takayama, H., Kitajima, M., Aimi, N., & Watanabe, H. (2002) · European Journal of Pharmacology · doi:10.1016/s0014-2999(02)02581-5 · Cited by 152 · see citing works
Zhou, J., & Zhou, S. (2010) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2010.08.041 · Cited by 151 · see citing works
The EphA4 receptor regulates dendritic spine remodeling by affecting β1-integrin signaling pathways
Bourgin, C., Murai, K. K., Richter, M., & Pasquale, E. B. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200610139 · Cited by 147 · see citing works
Abnormal Glutamate Transport Function in Mutant Amyloid Precursor Protein Transgenic Mice
Masliah, E., Alford, M. F., Mallory, M. E., Rockenstein, E. M., Moechars, D., & LEUVEN, F. V. (2000) · Experimental Neurology · doi:10.1006/exnr.2000.7386 · Cited by 145 · see citing works
Small Molecules Can Selectively Inhibit Ephrin Binding to the EphA4 and EphA2 Receptors
Noberini, R., Koolpe, M., Peddibhotla, S., Dahl, R. S., Su, Y., Cosford, N. D. P., Roth, G. P., & Pasquale, E. B. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m804103200 · Cited by 135 · see citing works
Kang, T.-H., Murakami, Y., Takayama, H., et al. (2004) · Life Sciences · doi:10.1016/j.lfs.2004.08.012 · Cited by 122 · see citing works
Simón, A. M., de Maturana, R. L., Ricobaraza, A., Escribano, L., Schiapparelli, L., Cuadrado‐Tejedor, M., Pérez‐Mediavilla, A., Ávila, J., Rı́o, J. D., & Frechilla, D. (2009) · Journal of Alzheimer s Disease · doi:10.3233/jad-2009-1096 · Cited by 110 · see citing works
Eph receptors and ephrins in neuron–astrocyte communication at synapses
Murai, K. K., & Pasquale, E. B. (2011) · Glia · doi:10.1002/glia.21226 · Cited by 109 · see citing works
α2-Chimaerin interacts with EphA4 and regulates EphA4-dependent growth cone collapse
Shi, L., Fu, W., Hung, K.-W., Porchetta, C., Hall, C., Fu, A. K. Y., & Ip, N. Y. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0706626104 · Cited by 109 · see citing works
Self-citationTargeting the EphA4 receptor in the nervous system with biologically active peptides
Murai, K. K., Nguyen, L. N., Koolpe, M., McLennan, R., Krull, C. E., & Pasquale, E. B. (2003) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2003.08.006 · Cited by 106 · see citing works
Qin, H., Noberini, R., Huan, X., Shi, J., Pasquale, E. B., & Song, J. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.064824 · Cited by 101 · see citing works
Shen, Y., Fu, W., Cheng, E. Y. L., Fu, A. K. Y., & Ip, N. Y. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.3282-12.2013 · Cited by 96 · see citing works
Self-citationStructural Plasticity of Eph Receptor A4 Facilitates Cross-Class Ephrin Signaling
Bowden, T. A., Aricescu, A. R., Nettleship, J. E., Siebold, C., Rahman-Huq, N., Owens, R. J., Stuart, D. I., & Jones, E. Y. (2009) · Structure · doi:10.1016/j.str.2009.07.018 · Cited by 95 · see citing works
The EphA4 Receptor Regulates Neuronal Morphology through SPAR-Mediated Inactivation of Rap GTPases
Richter, M., Murai, K. K., Bourgin, C., Pak, D. T. S., & Pasquale, E. B. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.2746-07.2007 · Cited by 89 · see citing works
Qin, H., Shi, J., Noberini, R., Pasquale, E. B., & Song, J. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m804114200 · Cited by 80 · see citing works
Cameron, B., Tse, W., Lamb, R., Li, X., Lamb, B. T., & Landreth, G. E. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.1729-12.2012 · Cited by 75 · see citing works
Eph receptors at synapses: Implications in neurodegenerative diseases
Chen, Y., Fu, A. K. Y., & Ip, N. Y. (2011) · Cellular Signalling · doi:10.1016/j.cellsig.2011.11.016 · Cited by 75 · see citing works
Self-citationIsoliquiritigenin is a Novel NMDA Receptor Antagonist in Kampo Medicine Yokukansan
Kawakami, Z., Ikarashi, Y., & Kase, Y. (2011) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-011-9722-1 · Cited by 73 · see citing works
A novel method for monitoring surface membrane trafficking on hippocampal acute slice preparation
Thomas-Crusells, J., Vieira, A. V., Saarma, M., & Rivera, C. (2003) · Journal of Neuroscience Methods · doi:10.1016/s0165-0270(03)00050-5 · Cited by 58 · see citing works
Lamberto, I., Qin, H., Noberini, R., Premkumar, L., Bourgin, C., Riedl, S. J., Song, J., & Pasquale, E. B. (2012) · Biochemical Journal · doi:10.1042/bj20120408 · Cited by 48 · see citing works
A Disalicylic Acid‐Furanyl Derivative Inhibits Ephrin Binding to a Subset of Eph Receptors
Noberini, R., De, S. K., Zhang, Z., Wu, B., Dhanya, R.-P., Chen, V., Vázquez, J., Qin, H., Song, J., Cosford, N. D. P., et al. (2011) · Chemical Biology & Drug Design · doi:10.1111/j.1747-0285.2011.01199.x · Cited by 41 · see citing works
Singla, N., Goldgur, Y., Xu, K. Y., Paavilainen, S., Nikolov, D. B., & Himanen, J. P. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.07.109 · Cited by 30 · see citing works
Bidirectional signaling of ErbB and Eph receptors at synapses
Chen, Y., Fu, A. K. Y., & Ip, N. Y. (2008) · Neuron Glia Biology · doi:10.1017/s1740925x09990287 · Cited by 27 · see citing works
Self-citationEphA4 is localized in clathrin‐coated and synaptic vesicles in adult mouse brain
Bouvier, D. S., Tremblay, M., Riad, M., Corera, A. T., Gingras, D., Horn, K. E., Fotouhi, M., Girard, M., Murai, K. K., Kennedy, T. E., et al. (2010) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2010.06582.x · Cited by 19 · see citing works
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Self-citation
- Authors
- Fu, A. K. Y., Hung, K.-W., Huang, H., Gu, S., Shen, Y., Cheng, E. Y. L., Ip, F. C. F., Huang, X., Fu, W.-Y., & Ip, N. Y.
- Affiliations
- Division of Life Science,
- Hong Kong University of Science and Technology (HK)
- ORCID
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2014-06-23
- Volume
- 111
- Issue
- 27
- Pages
- 9959-9964
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC4103318
- OpenAlex
- W1970200165
- Cited by
- 201
- References
- 54
- Citations by year
- 2026: 14 · 2025: 14 · 2024: 13 · 2023: 22 · 2022: 14 · 2021: 17 · 2020: 21 · 2019: 15 · 2018: 15 · 2017: 19 · 2016: 16 · 2015: 13 · 2014: 8
- FWCI
- 12.63
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Rare & Special e-Zone (The Hong Kong University of Science and Technology) (submittedVersion)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Health Sciences › Medicine › Pharmacology › Cholinesterase and Neurodegenerative Diseases
- Keywords
- EphA4, Alzheimer's disease, synaptic dysfunction, hippocampus, long-term potentiation, rhynchophylline, amyloid-beta oligomers, APP/PS1 mice, synaptic plasticity, postsynaptic signaling, therapeutic target
- MeSH terms
- Alzheimer Disease, Animals, Disease Models, Animal, Hippocampus, Mice, Transgenic, Synapses, Receptor, EphA4, Mice
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