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Axonal Transport Defects in Neurodegenerative Diseases
Open accessAbstract
Adult-onset neurodegenerative diseases (AONDs) comprise a heterogeneous group of neurological disorders characterized by a progressive, age-dependent decline in neuronal function and loss of selected neuronal populations. Alterations in synaptic function and axonal connectivity represent early and critical pathogenic events in AONDs, but molecular mechanisms underlying these defects remain elusive. The large size and complex subcellular architecture of neurons render them uniquely vulnerable to alterations in axonal transport (AT). Accordingly, deficits in AT have been documented in most AONDs, suggesting a common defect acquired through different pathogenic pathways. These observations suggest that many AONDs can be categorized as dysferopathies, diseases in which alterations in AT represent a critical component in pathogenesis. Topics here address various molecular mechanisms underlying alterations in AT in several AONDs. Illumination of such mechanisms provides a framework for the development of novel therapeutic strategies aimed to prevent axonal and synaptic dysfunction in several major AONDs.
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Cites
The Amyloid Hypothesis of Alzheimer’s Disease: Progress and Problems on the Road to Therapeutics
Hardy, J., & Selkoe, D. J. (2002) · Science · doi:10.1126/science.1072994 · Cited by 13,864
Amyloid oligomers exacerbate tau pathology in a mouse model of tauopathy
Selenica, M.-L. B., Brownlow, M., Jimenez, J. P., Lee, D. C., Pena, G., Dickey, C. A., Gordon, M. N., & Morgan, D. (2013) · Neurodegenerative Diseases · doi:10.1159/000337230 · Cited by 10,359
Pathways towards and Away from Alzheimer’s Disease
Mattson, M. P. (2004) · Nature · doi:10.1038/nature02621 · Cited by 3,052
Molecular biology of amyotrophic lateral sclerosis: insights from genetics
Pasinelli, P., & Brown, R. H. (2006) · Nature Reviews Neuroscience · doi:10.1038/nrn1971 · Cited by 1,107
Self-citationDisruption of Cnp1 uncouples oligodendroglial functions in axonal support and myelination
Lappe-Siefke, C., Goebbels, S., Gravel, M., Nicksch, E., Lee, J., Braun, P. E., Griffiths, I. R., & Nave, K.-A. (2003) · Nature Genetics · doi:10.1038/ng1095 · Cited by 1,036
Self-citationAxon degeneration mechanisms: Commonality amid diversity
Coleman, M. (2005) · Nature reviews. Neuroscience · doi:10.1038/nrn1788 · Cited by 819
Molecular pathways to neurodegeneration
Bossy-Wetzel, E., Schwarzenbacher, R., & Lipton, S. A. (2004) · Nature Medicine · doi:10.1038/nm1067 · Cited by 740
Phosphorylation determines two distinct species of tau in the central nervous system
Papasozomenos, S. C., & Binder, L. I. (1987) · Cell Motility · doi:10.1002/cm.970080303 · Cited by 420
Self-citationALZHEIMER'S DISEASE: Genetic Studies and Transgenic Models
Price, D. L., Tanzi, R. E., Borchelt, D. R., & Sisodia, S. S. (1998) · Annual Review of Genetics · doi:10.1146/annurev.genet.32.1.461 · Cited by 406
Neurons May Live for Decades with Neurofibrillary Tangles
Morsch, R., Simon, W., & Coleman, P. D. (1999) · Journal of Neuropathology and Experimental Neurology · doi:10.1097/00005072-199902000-00008 · Cited by 370
Cited by
Hallmarks of neurodegenerative diseases
Wilson, D. M., Cookson, M. R., Van Den Bosch, L., Zetterberg, H., Holtzman, D. M., & Dewachter, I. (2023) · Cell · doi:10.1016/j.cell.2022.12.032 · Cited by 1,789
The Intersection of Amyloid Beta and Tau at Synapses in Alzheimer’s Disease
Spires-Jones, T. L., & Hyman, B. T. (2014) · Neuron · doi:10.1016/j.neuron.2014.05.004 · Cited by 1,201
Trafficking and Proteolytic Processing of APP
Haass, C., Kaether, C., Thinakaran, G., & Sisodia, S. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006270 · Cited by 1,075
Mitochondrial optic neuropathies—Disease mechanisms and therapeutic strategies
Yu-Wai-Man, P., Griffiths, P. G., & Chinnery, P. F. (2011) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2010.11.002 · Cited by 633
Tau Oligomers: Cytotoxicity, Propagation, and Mitochondrial Damage
Shafiei, S. S., Guerrero-Muñoz, M. J., & Castillo-Carranza, D. L. (2017) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2017.00083 · Cited by 314
The Axon-Myelin Unit in Development and Degenerative Disease
Stassart, R. M., Möbius, W., Nave, K.-A., & Edgar, J. M. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00467 · Cited by 246
Self-citationKandalepas, P. C., Sadleir, K. R., Eimer, W. A., Zhao, J., Nicholson, D. A., & Vassar, R. (2013) · Acta Neuropathologica · doi:10.1007/s00401-013-1152-3 · Cited by 240
Soluble forms of tau are toxic in Alzheimer's disease
Kopeikina, K., Hyman, B., & Spires-Jones, T. (2012) · Translational Neuroscience · doi:10.2478/s13380-012-0032-y · Cited by 232
Masson, P., & Lockridge, O. (2010) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2009.12.005 · Cited by 233
Vinsant, S., Mansfield, C., Jimenez‐Moreno, R., Moore, V. D. G., Yoshikawa, M., Hampton, T. G., Prevette, D., Caress, J., Oppenheim, R. W., & Milligan, C. (2013) · Brain and Behavior · doi:10.1002/brb3.142 · Cited by 172
Cortical tau load is associated with white matter hyperintensities
McAleese, K. E., Firbank, M., Dey, M., Colloby, S. J., Walker, L., Johnson, M., Beverley, J. R., Taylor, J. P., Thomas, A. J., O’Brien, J. T., et al. (2015) · Acta Neuropathologica Communications · doi:10.1186/s40478-015-0240-0 · Cited by 161
Moraes, C. A., Santos, G., Spohr, T. C. L. D. S. E., D’Avila, J. C., Lima, F. R. S., Benjamim, C. F., Bozza, F. A., & Gomes, F. C. A. (2015) · Molecular Neurobiology · doi:10.1007/s12035-014-8868-5 · Cited by 145
Mechanisms of protein toxicity in neurodegenerative diseases
Chung, C. G., Lee, H., & Lee, S. B. (2018) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-018-2854-4 · Cited by 142
Phosphorylation in the amino terminus of tau prevents inhibition of anterograde axonal transport
Kanaan, N. M., Morfini, G., Pigino, G., LaPointe, N. E., Andreadis, A., Song, Y., Leitman, E., Binder, L. I., & Brady, S. T. (2012) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.06.006 · Cited by 134
Self-citationAxonal degeneration as a therapeutic target in the CNS
Lingor, P., Koch, J. C., Tönges, L., & Bähr, M. (2012) · Cell and Tissue Research · doi:10.1007/s00441-012-1362-3 · Cited by 119
Tau directs intracellular trafficking by regulating the forces exerted by kinesin and dynein teams
Chaudhary, A. R., Berger, F., Berger, C. L., & Hendricks, A. G. (2018) · Traffic · doi:10.1111/tra.12537 · Cited by 118
Calsyntenin-1 mediates axonal transport of the amyloid precursor protein and regulates A production
Vagnoni, A., Perkinton, M. S., Gray, E. H., Francis, P. T., Noble, W., & Miller, C. C. J. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds109 · Cited by 114
Kamagata, K., Zalesky, A., Hatano, T., Ueda, R., Di Biase, M. A., Okuzumi, A., Shimoji, K., Hori, M., Caeyenberghs, K., Pantelis, C., et al. (2017) · Human Brain Mapping · doi:10.1002/hbm.23628 · Cited by 106
Axonal degeneration in tauopathies: disease relevance and underlying mechanisms
Kneynsberg, A., Combs, B., Christensen, K., Morfini, G., & Kanaan, N. M. (2017) · Frontiers in Neuroscience · doi:10.3389/fnins.2017.00572 · Cited by 102
Self-citationSequential formation of different layers of dystrophic neurites in Alzheimer’s brains
Sharoar, M. G., Hu, X., Ma, X.-M., Zhu, X., & Yan, R. (2019) · Molecular Psychiatry · doi:10.1038/s41380-019-0396-2 · Cited by 87
Axonal transport of APP and the spatial regulation of APP cleavage and function in neuronal cells
Brunholz, S., Sisodia, S., Lorenzo, A., Deyts, C., Kins, S., & Morfini, G. (2012) · Experimental Brain Research · doi:10.1007/s00221-011-2870-1 · Cited by 92
Self-citationAge-Related Phasic Patterns of Mitochondrial Maintenance in Adult Caenorhabditis elegans Neurons
Morsci, N. S., Hall, D. H., Driscoll, M., & Sheng, Z.-H. (2016) · The Journal of Neuroscience · doi:10.1523/jneurosci.2799-15.2016 · Cited by 92
BORC Regulates the Axonal Transport of Synaptic Vesicle Precursors by Activating ARL-8
Niwa, S., Tao, L., Lu, S. Y., Liew, G. M., Feng, W., Nachury, M. V., & Shen, K. (2017) · Current Biology · doi:10.1016/j.cub.2017.07.013 · Cited by 92
Morel, M., Authelet, M., Dedecker, R., & Brion, J. P. (2010) · Neuroscience · doi:10.1016/j.neuroscience.2010.02.077 · Cited by 46
The Pathophysiology of Axonal Transport in Alzheimer's Disease
Vicario-Orri, E., Opazo, C. M., & Muñoz, F. J. (2014) · Journal of Alzheimer’s Disease · doi:10.3233/jad-141080 · Cited by 41
Hannan, S. B., Dräger, N. M., Rasse, T. M., Voigt, A., & Jahn, T. R. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13532 · Cited by 38
Davtyan, H., Chen, W. W., Zagorski, K., Davis, J., Petrushina, I., Kazarian, K., Cribbs, D. H., Agadjanyan, M. G., Blurton-Jones, M., & Ghochikyan, A. (2017) · Vaccine · doi:10.1016/j.vaccine.2017.03.020 · Cited by 30
Metadata
- Authors
- Morfini, G. A., Burns, M., Binder, L. I., Kanaan, N. M., LaPointe, N., Bosco, D. A., Brown, R. H., Brown, H., Tiwari, A., Hayward, L., Edgar, J., Nave, K.-A., Garberrn, J., Atagi, Y., Song, Y., Pigino, G., & Brady, S. T.
- Venue
- The Journal of Neuroscience
- Publisher
- Society for Neuroscience
- Published
- 2009-10-14
- Volume
- 29
- Issue
- 41
- Pages
- 12776-12786
- ISSN
- 0270-6474 (ISSN-L)
- 1529-2401
- OpenAlex
- W2021258666
- Cited by
- 464
- References
- 13
- FWCI
- 17.44
- Type
- journal article
- Language
- en
- Open access
- hybrid
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