Axonal degeneration in tauopathies: disease relevance and underlying mechanisms

Kneynsberg, Andrew; Combs, Benjamin; Christensen, Kyle; Morfini, Gerardo; Kanaan, Nicholas M.

doi:10.3389/fnins.2017.00572

Cited by 102Alzheimer's disease research and treatmentsAmyotrophic Lateral Sclerosis ResearchNeuroinflammation and Neurodegeneration Mechanisms

Axonal degeneration in tauopathies: disease relevance and underlying mechanisms

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Kneynsberg, Andrew, Combs, Benjamin, Christensen, Kyle, Morfini, Gerardo, Kanaan, Nicholas M.·2017·Frontiers in Neuroscience

DOI 10.3389/fnins.2017.00572PMC PMC5651019

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Abstract

Tauopathies are a diverse group of diseases featuring progressive dying back neurodegeneration of specific neuronal populations in association with accumulation of abnormal forms of the microtubule-associated protein tau. It is well established that the clinical symptoms characteristic of tauopathies correlate with deficits in synaptic function and neuritic connectivity early in the course of disease, but mechanisms underlying these critical pathogenic events remain largely unknown. Biochemical in vitro evidence fueled the widespread notion that microtubule stabilization represents tau’s primary biological role and that the marked atrophy of neurites observed in tauopathies results from loss of microtubule stability. However, this notion contrasts with the mild phenotype associated with tau deletion. Instead, an analysis of cellular hallmarks common to different tauopathies, including aberrant patterns of protein phosphorylation and early degeneration of axons, suggests that alterations in kinase-based signaling pathways and deficits in axonal transport associated with such alterations contribute to the loss of neuronal connectivity triggered by pathogenic forms of tau. Here, we review a body of literature providing evidence that axonal pathology represents an early and common pathogenic event among human tauopathies. Observations of axonal degeneration in animal models of specific tauopathies are discussed and similarities to human disease highlighted. Finally, we discuss potential mechanistic pathways other than microtubule destabilization by which disease-related forms of tau may promote axonopathy.

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EpoD at 1 mg/kg was sufficient to reduce measures of tauopathy, neurodegeneration and axonal dystrophy in PS19 tau mice in previous work.
“The dose for this experiment was chosen based upon previous work by Brunden et. al. and Zhang et. al. in which EpoD at 1mg/kg was sufficient to reduce measures of tauopathy, neurodegeneration and axonal dystrophy in PS19 tau mice 30, 31.”
From Amyloid-beta induced retrograde axonal degeneration in a mouse tauopathy model (2019) · cites this paper as [31]
The Animal models of tauopathies section discusses axonal pathology in transgenic mice, but not EpoD treatment. Searches of the full-text copy for EpoD, epothilone, PS19, Brunden, and the 1 mg/kg dose found no passage reporting the attributed treatment result; the paper’s References section does not establish it either. (LLM, conf=0.76)
Experimental — accuracy not yet measured
Previous studies have shown that EpoD and NAP can reduce p-tau pathology in AD model mice over several months of treatment.
“Additionally, previous studies utilizing EpoD as well as microtubule-stabilizing peptide NAP have both shown ability to reduce p-tau pathology in AD model mice over several months of treatment 31,66,67”
From Amyloid-beta induced retrograde axonal degeneration in a mouse tauopathy model (2019) · cites this paper as [31]
The Animal models of tauopathies section discusses tau pathology in mice, but not EpoD or NAP treatment. Searches of our copy for EpoD, NAP, and microtubule-stabilizing treatment found no passage reporting reduced phosphorylated-tau pathology after several months of treatment. (LLM, conf=0.74)
Experimental — accuracy not yet measured
EpoD can promote axonal health by reducing axonal dystrophy, increasing ON microtubule density and normalizing fast axonal transport.
“Data from previous studies have found evidence that EpoD can promote axonal health by reducing axonal dystrophy, increasing ON microtubule density and normalizing fast axonal transport 30, 31.”
From Amyloid-beta induced retrograde axonal degeneration in a mouse tauopathy model (2019) · cites this paper as [31]
The Introduction and ‘Pathogenic mechanisms linking abnormal tau to axonopathy’ discuss microtubules and axonal transport, but do not report EpoD treatment effects. Searches for EpoD, epothilone D, and ON microtubule density found no passage addressing reduced axonal dystrophy, increased density, or normalized fast axonal transport after EpoD. (LLM, conf=0.76)
Experimental — accuracy not yet measured

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Calcium dysregulation contributes to neurodegeneration in FTLD patient iPSC-derived neurons
Imamura, K., Sahara, N., Kanaan, N. M., Tsukita, K., Kondo, T., Kutoku, Y., Ohsawa, Y., Sunada, Y., Kawakami, K., Hotta, A., et al. (2016) · Scientific Reports · doi:10.1038/srep34904 · Cited by 84 · see citing works
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Acute Inactivation of Tau Has No Effect on Dynamics of Microtubules in Growing Axons of Cultured Sympathetic Neurons
Tint, I. S., Slaughter, T., Fischer, I., & Black, M. M. (1998) · Journal of Neuroscience · doi:10.1523/jneurosci.18-21-08660.1998 · Cited by 83 · see citing works
Novel mutation in MAPT exon 13 (p.N410H) causes corticobasal degeneration
Kouri, N., Carlomagno, Y., Baker, M., Liesinger, A. M., Caselli, R. J., Wszołek, Z. K., Petrucelli, L., Boeve, B. F., Parisi, J. E., Josephs, K. A., et al. (2013) · Acta Neuropathologica · doi:10.1007/s00401-013-1193-7 · Cited by 82 · see citing works
Tau binding to microtubules does not directly affect microtubule‐based vesicle motility
Morfini, G. A., Pigino, G. F., Mizuno, N., Kikkawa, M., & Brady, S. T. (2007) · Journal of Neuroscience Research · doi:10.1002/jnr.21154 · Cited by 81 · see citing works
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Strategies for diminishing katanin-based loss of microtubules in tauopathic neurodegenerative diseases
Sudo, H., & Baas, P. W. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq521 · Cited by 78 · see citing works
Pro-aggregant Tau impairs mossy fiber plasticity due to structural changes and Ca++ dysregulation
Decker, J., Krüger, L., Sydow, A., Zhao, S., Frotscher, M., Mandelkow, E., & Mandelkow, E. (2015) · Acta Neuropathologica Communications · doi:10.1186/s40478-015-0193-3 · Cited by 77 · see citing works
In vivo demonstration of microstructural brain pathology in progressive supranuclear palsy: A DTI study using TBSS
Knake, S., Belke, M., Menzler, K., Pilatus, U., Eggert, K. M., Oertel, W. H., Stamelou, M., & Höglinger, G. U. (2010) · Movement Disorders · doi:10.1002/mds.23054 · Cited by 76 · see citing works
Reduced number of axonal mitochondria and tau hypophosphorylation in mouse P301L tau knockin neurons
Rodríguez-Martín, T., Pooler, A. M., Lau, D. H. W., Mórotz, G. M., Vos, K. J. D., Gilley, J., Coleman, M. P., & Hanger, D. P. (2015) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.10.007 · Cited by 75 · see citing works
Glial levels determine severity of white matter disease in Alzheimer's disease: a neuropathological study of glial changes
Sjöbeck, M., & Englund, E. M. (2003) · Neuropathology and Applied Neurobiology · doi:10.1046/j.1365-2990.2003.00456.x · Cited by 73 · see citing works
Extracellular Tau Oligomers Induce Invasion of Endogenous Tau into the Somatodendritic Compartment and Axonal Transport Dysfunction
Swanson, E., Breckenridge, L., McMahon, L. P., Som, S., McConnell, I., & Bloom, G. S. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-170168 · Cited by 73 · see citing works
Reduction of Detyrosinated Microtubules and Golgi Fragmentation Are Linked to Tau-Induced Degeneration in Astrocytes
Yoshiyama, Y., Zhang, B., Bruce, J., Trojanowski, J. Q., & Lee, V. M.-Y. (2003) · The Journal of Neuroscience · doi:10.1523/jneurosci.23-33-10662.2003 · Cited by 72 · see citing works
Phosphoregulation of Tau modulates inhibition of kinesin-1 motility
Stern, J. L., Lessard, D. V., Hoeprich, G. J., Morfini, G. A., & Berger, C. L. (2017) · Molecular Biology of the Cell · doi:10.1091/mbc.e16-10-0728 · Cited by 69 · see citing works
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Interaction of Actin Filaments with Microtubules Is Mediated by Microtubule‐Associated Proteins and Regulated by Phosphorylationa
Selden, S. C., & Pollard, T. D. (1986) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1986.tb38464.x · Cited by 65 · see citing works
Tau pathology-mediated presynaptic dysfunction
Moreno, H., Morfini, G. A., Buitrago, L., Ujlaki, G., Choi, S., Yu, E., Moreira, J. E., Ávila, J., Brady, S. T., Pant, H., et al. (2016) · Neuroscience · doi:10.1016/j.neuroscience.2016.03.044 · Cited by 65 · see citing works
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Cytoskeletal pathology in non-Alzheimer degenerative dementia: new lesions in Diffuse Lewy body disease, Pick’s disease, and Corticobasal Degeneration
Dickson, D. W., Feany, M. Β., Yen, S. H., Mattiace, L. A., & Davies, P. (1996) · Journal of neural transmission. Supplementum · doi:10.1007/978-3-7091-6892-9_2 · Cited by 65 · see citing works
Conventional kinesin: Biochemical heterogeneity and functional implications in health and disease
Morfini, G. A., Schmidt, N., Weissmann, C., Pigino, G. F., & Kins, S. (2016) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2016.06.009 · Cited by 63 · see citing works
Self-citation
Tau antagonizes end-binding protein tracking at microtubule ends through a phosphorylation-dependent mechanism
Ramírez‐Ríos, S., Denarier, É., Prezel, E., Vinit, A., Stoppin‐Mellet, V., Devred, F., Barbier, P., Peyrot, V., Sayas, C. L., Ávila, J., et al. (2016) · Molecular Biology of the Cell · doi:10.1091/mbc.e16-01-0029 · Cited by 62 · see citing works
Presence of a carboxy-terminal pseudorepeat and disease-like pseudohyperphosphorylation critically influence tau’s interaction with microtubules in axon-like processes
Niewidok, B., Igaev, M., Sündermann, F., Janning, D., Bakota, L., & Brandt, R. (2016) · Molecular Biology of the Cell · doi:10.1091/mbc.e16-06-0402 · Cited by 60 · see citing works
Regulation of Kinesin: Implications for Neuronal Development
Morfini, G. A., Szebenyi, G., Richards, B. W., & Brady, S. T. (2001) · Developmental Neuroscience · doi:10.1159/000048720 · Cited by 59 · see citing works
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Tau Reduction Does Not Prevent Motor Deficits in Two Mouse Models of Parkinson's Disease
Morris, M., Koyama, A., Masliah, E., & Mucke, L. (2011) · PLoS ONE · doi:10.1371/journal.pone.0029257 · Cited by 56 · see citing works
Analysis of Isoform-specific Tau Aggregates Suggests a Common Toxic Mechanism Involving Similar Pathological Conformations and Axonal Transport Inhibition
Cox, K. K., Combs, B., Abdelmesih, B., Morfini, G., Brady, S., & Kanaan, N. (2016) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2016.07.015 · Cited by 54 · see citing works
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Progression of Microstructural Degeneration in Progressive Supranuclear Palsy and Corticobasal Syndrome: A Longitudinal Diffusion Tensor Imaging Study
Zhang, Y., Walter, R., Ng, P., Luong, P. N., Dutt, S., Heuer, H. W., Rojas-Rodriguez, J. C., Tsai, R. M., Litvan, I., Dickerson, B. C., et al. (2016) · PLoS ONE · doi:10.1371/journal.pone.0157218 · Cited by 53 · see citing works
Analysis of YFP(J16)-R6/2 reporter mice and postmortem brains reveals early pathology and increased vulnerability of callosal axons in Huntington's disease
Gatto, R. G., Chu, Y., Ye, A. Q., Price, S. D., Tavassoli, E., Buenaventura, A., Brady, S. T., Magin, R. L., Kordower, J. H., & Morfini, G. A. (2015) · Human Molecular Genetics · doi:10.1093/hmg/ddv248 · Cited by 52 · see citing works
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A Qualitative and Quantitative Study of Grumose Degeneration in Progressive Supranuclear Palsy
Ishizawa, K., Lin, W.-L., Tiseo, P. J., Honer, W. G., Davies, P. J., & Dickson, D. W. (2000) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/59.6.513 · Cited by 52 · see citing works
Pseudophosphorylation of tau at S422 enhances SDS-stable dimer formation and impairs both anterograde and retrograde fast axonal transport
Tiernan, C. T., Combs, B., Cox, K. K., Morfini, G. A., Brady, S. T., Counts, S., & Kanaan, N. M. (2016) · Experimental Neurology · doi:10.1016/j.expneurol.2016.06.030 · Cited by 46 · see citing works
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Lentiviral Delivery of the Human Wild-type Tau Protein Mediates a Slow and Progressive Neurodegenerative Tau Pathology in the Rat Brain
Caillierez, R., Bégard, S., Lécolle, K., Deramecourt, V., Zommer, N., Dujardin, S., Loyens, A., Dufour, N., Aurégan, G., Winderickx, J., et al. (2013) · Molecular Therapy · doi:10.1038/mt.2013.66 · Cited by 43 · see citing works
Axonal transport
Black, M. M. (2015) · Methods in cell biology · doi:10.1016/bs.mcb.2015.06.001 · Cited by 42 · see citing works
White matter magnetic resonance imaging hyperintensity in Alzheimer's disease: correlations with corpus callosum atrophy
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Progressive white matter pathology in the spinal cord of transgenic mice expressing mutant (P301L) human tau
Lin, W.-L., Zehr, C., Lewis, J. M., Hutton, M. L., Yen, S.-H. C., & Dickson, D. W. (2005) · Journal of Neurocytology · doi:10.1007/s11068-006-8726-0 · Cited by 41 · see citing works
No Overt Deficits in Aged Tau-Deficient C57Bl/6.Mapttm1(EGFP)Kit GFP Knockin Mice
van Hummel, A., Bi, M., Ippati, S., van der Hoven, J., Volkerling, A. M., Lee, W. S., Tan, D. C. S., Bongers, A., Ittner, A., Ke, Y. D., et al. (2016) · PLoS ONE · doi:10.1371/journal.pone.0163236 · Cited by 40 · see citing works
Chronic Traumatic Encephalopathy: A Neurodegenerative Consequence of Repetitive Traumatic Brain Injury
Kiernan, P. T., Montenigro, P. H., Solomon, T. M., & McKee, A. C. (2015) · Seminars in Neurology · doi:10.1055/s-0035-1545080 · Cited by 39 · see citing works
Accumulation of SNAP-25 immunoreactive material in axons of Alzheimerʼs disease
Dessi, F., Colle, M.-A., Hauw, J., & Duyckaerts, C. J. (1997) · Neuroreport · doi:10.1097/00001756-199712010-00006 · Cited by 39 · see citing works
Anisotropic fractional diffusion tensor imaging
Meerschaert, M. M., Magin, R. L., & Ye, A. Q. (2015) · Journal of Vibration and Control · doi:10.1177/1077546314568696 · Cited by 36 · see citing works
Systemic and network functions of the microtubule-associated protein tau: Implications for tau-based therapies
Bakota, L., Ussif, A. M., Jeserich, G., & Brandt, R. (2017) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2017.03.003 · Cited by 32 · see citing works
Gene Therapy Models of Alzheimer’s Disease and Other Dementias
Combs, B., Kneynsberg, A., & Kanaan, N. M. (2015) · Methods in molecular biology · doi:10.1007/978-1-4939-3271-9_25 · Cited by 31 · see citing works
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Quantitative and semi-quantitative measurements of axonal degeneration in tissue and primary neuron cultures
Kneynsberg, A., Collier, T. J., Manfredsson, F. P., & Kanaan, N. M. (2016) · Journal of Neuroscience Methods · doi:10.1016/j.jneumeth.2016.03.004 · Cited by 31 · see citing works
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Accumulation of human full-length tau induces degradation of nicotinic acetylcholine receptor α4 via activating calpain-2
Yin, Y., Wang, Y., Gao, D., Ye, J., Wang, X., Fang, L., Wu, D., Pi, G., Lu, C., Zhou, X., et al. (2016) · Scientific Reports · doi:10.1038/srep27283 · Cited by 30 · see citing works
Progression of tau pathology within cholinergic nucleus basalis neurons in chronic traumatic encephalopathy: A chronic effects of neurotrauma consortium study
Mufson, E. J., Perez, S. E., Nadeem, M., Mahady, L. J., Kanaan, N. M., Abrahamson, E. E., Ikonomović, M. D., Crawford, F., Alvarez, V. E., Stein, T. D., et al. (2016) · Brain Injury · doi:10.1080/02699052.2016.1219058 · Cited by 30 · see citing works
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Structural abnormalities in the cortex of the rTg4510 mouse model of tauopathy: a light and electron microscopy study
Ludvigson, A. E., Luebke, J. I., Lewis, J. M., & Peters, A. (2010) · Brain Structure and Function · doi:10.1007/s00429-010-0295-4 · Cited by 27 · see citing works
A Rapid Gene Delivery-Based Mouse Model for Early-Stage Alzheimer Disease-Type Tauopathy
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Synaptophysin immunoreactivity in Pick's disease: Comparison with Alzheimer's disease and dementia with Lewy bodies
Lippa, C. F. (2004) · American Journal of Alzheimer s Disease & Other Dementias® · doi:10.1177/153331750401900606 · Cited by 27 · see citing works
Severe panencephalic Pick's disease with Alzheimer's disease-like neuropil threads and synaptophysin immunoreactivity
Cochran, E. J., Fox, J. H., & Mutson, E. J. (1994) · Acta Neuropathologica · doi:10.1007/bf00389503 · Cited by 25 · see citing works
Tau phosphorylation in the mouse brain during aversive conditioning
Fujio, J., Hosono, H., Ishiguro, K., Ikegami, S., & Fujita, S. C. (2007) · Neurochemistry International · doi:10.1016/j.neuint.2007.04.024 · Cited by 24 · see citing works
Phospholipids and calmodulin modulate the inhibition of PMCA activity by tau
Berrocal, M., Corbacho‐Cuello, I., Sepúlveda, M. R., Gutiérrez‐Merino, C., & Mata, A. M. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2016.10.023 · Cited by 23 · see citing works
White matter hyperintensities on MRI in a patient with corticobasal degeneration
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Kinetically distinct phases of tau on microtubules regulate kinesin motors and severing enzymes
Siahaan, V., Krattenmacher, J., Hyman, A. A., Diez, S., Hernández-Vega, A., Lansky, Z., & Braun, M. (2019) · Nature Cell Biology · doi:10.1038/s41556-019-0374-6 · Cited by 169 · see citing works
GSK3β and tau protein in Alzheimer's disease and epilepsy
Toral-Rios, D., Pichardo-Rojas, P. S., Alonso-Vanegas, M., & Campos-Peña, V. (2020) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2020.00019 · Cited by 158 · see citing works
New Insights Into Drug Discovery Targeting Tau Protein
Soeda, Y., & Takashima, A. (2020) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.590896 · Cited by 133 · see citing works
Diffusion MRI Indices and Their Relation to Cognitive Impairment in Brain Aging: The Updated Multi-protocol Approach in ADNI3
Zavaliangos-Petropulu, A., Nir, T. M., Thomopoulos, S. I., Reid, R. I., Bernstein, M. A., Borowski, B., Jack Jr., C. R., Weiner, M. W., Jahanshad, N., & Thompson, P. M. (2019) · Frontiers in Neuroinformatics · doi:10.3389/fninf.2019.00002 · Cited by 101 · see citing works
“…of amyloid plaques and neurofibrillary tangles (NFTs) in the brain (Braak and Braak, 1991, 1996; Frank et al., 2003; Shaw et al., 2007) can directly impact WM (Lee et al., 2004; Roth et al., 2005), promoting myelin degeneration and axonal loss (Braak and Braak, 1996; Kneynsberg et al., 2017).”
Neuroprotective potential of berberine in modulating Alzheimer’s disease via multiple signaling pathways
Akbar, M., Shabbir, A., Rehman, K., Akash, M. S. H., & Shah, M. A. (2021) · Journal of Food Biochemistry · doi:10.1111/jfbc.13936 · Cited by 91 · see citing works
Tau and Axonal Transport Misregulation in Tauopathies
Combs, B., Mueller, R. L., Morfini, G. A., Brady, S. T., & Kanaan, N. M. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-32-9358-8_7 · Cited by 88 · see citing works
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Palmitoylation enables MAPK-dependent proteostasis of axon survival factors
Summers, D. W., Milbrandt, J., & DiAntonio, A. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1806933115 · Cited by 84 · see citing works
Pathophysiology of neurodegenerative diseases: An interplay among axonal transport failure, oxidative stress, and inflammation?
Tesco, G., & Lomoio, S. (2022) · Seminars in Immunology · doi:10.1016/j.smim.2022.101628 · Cited by 91 · see citing works
Berberine: A Plant-derived Alkaloid with Therapeutic Potential to Combat Alzheimer’s disease
Singh, A. K., Singh, S. K., Nandi, M. K., Mishra, G., Maurya, A., Rai, A., Rai, G. K., Awasthi, R., Sharma, B., & Kulkarni, G. T. (2019) · Central Nervous System Agents in Medicinal Chemistry · doi:10.2174/1871524919666190820160053 · Cited by 79 · see citing works
Tau: A Signaling Hub Protein
Mueller, R. L., Combs, B., Alhadidy, M. M., Brady, S. T., Morfini, G. A., & Kanaan, N. M. (2021) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2021.647054 · Cited by 78 · see citing works
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Altered ribosomal function and protein synthesis caused by tau
Evans, H. T., Taylor, D. W., Kneynsberg, A., Bodea, L., & Götz, J. (2021) · Acta Neuropathologica Communications · doi:10.1186/s40478-021-01208-4 · Cited by 70 · see citing works
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Mitochondrial transport serves as a mitochondrial quality control strategy in axons: Implications for central nervous system disorders
Zheng, Y., Zhang, X., & Chen, Z. (2019) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.13122 · Cited by 69 · see citing works
Obesity and Diabetes Mediated Chronic Inflammation: A Potential Biomarker in Alzheimer’s Disease
Khan, M. S. H., & Hegde, V. K. (2020) · Journal of Personalized Medicine · doi:10.3390/jpm10020042 · Cited by 64 · see citing works
Oligodendrogliopathy in neurodegenerative diseases with abnormal protein aggregates: The forgotten partner
Ferrer, I. (2018) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2018.07.004 · Cited by 62 · see citing works
Arginine π-stacking drives binding to fibrils of the Alzheimer protein Tau
Ferrari, L., Stucchi, R., Konstantoulea, K., van de Kamp, G., Kos, R., Geerts, W. J. C., van Bezouwen, L. S., Förster, F. G., Altelaar, M. A. F., Hoogenraad, C. C., et al. (2020) · Nature Communications · doi:10.1038/s41467-019-13745-7 · Cited by 62 · see citing works
Super-resolution microscopy: a closer look at synaptic dysfunction in Alzheimer disease
Padmanabhan, P., Kneynsberg, A., & Götz, J. (2021) · Nature reviews. Neuroscience · doi:10.1038/s41583-021-00531-y · Cited by 55 · see citing works
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A novel histone deacetylase 6 inhibitor improves myelination of Schwann cells in a model of Charcot–Marie–Tooth disease type 1A
Ha, N., Choi, Y. I., Jung, N., Song, J. Y., Bae, D. K., Kim, M. C., Lee, Y. J., Song, H., Kwak, G., Jeong, S., et al. (2020) · British Journal of Pharmacology · doi:10.1111/bph.15231 · Cited by 55 · see citing works
Recent advancement in therapeutic strategies for Alzheimer’s disease: Insights from clinical trials
Khan, T., Waseem, R., Shahid, M., Ansari, J., Ahanger, I. A., Hassan, M. I., & Islam, A. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.102113 · Cited by 57 · see citing works
Advances in the development paradigm of biosample‐based biosensors for early ultrasensitive detection of alzheimer’s disease
Karki, H. P., Jang, Y., Jung, J., & Oh, J. (2021) · Journal of Nanobiotechnology · doi:10.1186/s12951-021-00814-7 · Cited by 51 · see citing works
Tau and Alpha Synuclein Synergistic Effect in Neurodegenerative Diseases: When the Periphery Is the Core
Vacchi, E., Kaelin‐Lang, A., & Melli, G. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21145030 · Cited by 50 · see citing works
How do protein aggregates escape quality control in neurodegeneration?
Koopman, M., Ferrari, L., & Rüdiger, S. (2022) · Trends in Neurosciences · doi:10.1016/j.tins.2022.01.006 · Cited by 38 · see citing works
Neuronal and Glial Distribution of Tau Protein in the Adult Rat and Monkey
Kanaan, N. M., & Grabinski, T. (2021) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2021.607303 · Cited by 46 · see citing works
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Injury-Induced Inhibition of Bystander Neurons Requires dSarm and Signaling from Glia
Hsu, J.-M., Kang, Y., Corty, M. M., Mathieson, D., Peters, O. M., & Freeman, M. R. (2020) · Neuron · doi:10.1016/j.neuron.2020.11.012 · Cited by 44 · see citing works
Ribosome-Directed Therapies in Cancer
Temaj, G., Chichiarelli, S., Eufemi, M., Fabio Altieri, F., Hadžiselimović, R., Farooqı, A. A., Yaylım, İ., & Saso, L. (2022) · Biomedicines · doi:10.3390/biomedicines10092088 · Cited by 43 · see citing works
Exogenous brain-derived neurotrophic factor attenuates cognitive impairment induced by okadaic acid in a rat model of Alzheimer's disease
Xu, A., Yang, Y., Sun, Y., & Zhang, C. (2018) · Neural Regeneration Research · doi:10.4103/1673-5374.241471 · Cited by 39 · see citing works
Molecular pathology and synaptic loss in primary tauopathies: an 18F-AV-1451 and 11C-UCB-J PET study
Holland, N., Malpetti, M., Rittman, T., Mak, E. E., Passamonti, L., Kaalund, S. S., Hezemans, F. H., Jones, P. S., Savulich, G., Hong, Y. T., et al. (2022) · Brain · doi:10.1093/brain/awab282 · Cited by 39 · see citing works
Manganese-Enhanced Magnetic Resonance Imaging: Overview and Central Nervous System Applications With a Focus on Neurodegeneration
Cloyd, R., Koren, S. A., & Abisambra, J. F. (2018) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2018.00403 · Cited by 34 · see citing works
Systemic delivery of a specific antibody targeting the pathological N-terminal truncated tau peptide reduces retinal degeneration in a mouse model of Alzheimer’s Disease
Latina, V., Giacovazzo, G., Cordella, F., Balzamino, B. O., Micera, A., Varano, M., Marchetti, C., Malerba, F., Florio, R., Ercole, B. B., et al. (2021) · Acta Neuropathologica Communications · doi:10.1186/s40478-021-01138-1 · Cited by 33 · see citing works
Reduction of kinesin I heavy chain decreases tau hyperphosphorylation, aggregation, and memory impairment in Alzheimer’s disease and tauopathy models
Selvarasu, K., Singh, A. K., Iyaswamy, A., Sreenivasmurthy, S. G., Krishnamoorthi, S., Bera, A. K., Huang, J., & Durairajan, S. S. K. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.1050768 · Cited by 33 · see citing works
Reelin reverts biochemical, physiological and cognitive alterations in mouse models of Tauopathy
Rossi, D., Gruart, A., Contreras-Murillo, G., Muhaisen, A., Ávila, J., Delgado-García, J. M., Pujadas, L., & Soriano, E. (2020) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2019.101743 · Cited by 30 · see citing works
Resveratrol Protects Optic Nerve Head Astrocytes from Oxidative Stress-Induced Cell Death by Preventing Caspase-3 Activation, Tau Dephosphorylation at Ser422 and Formation of Misfolded Protein Aggregates
Means, J. C., Lopez, A. A., & Koulen, P. (2020) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-019-00781-6 · Cited by 32 · see citing works
Amyloid-beta induced retrograde axonal degeneration in a mouse tauopathy model
Nishioka, C., Liang, H.-F., Barsamian, B., & Sun, S.-W. (2019) · NeuroImage · doi:10.1016/j.neuroimage.2019.01.007 · Cited by 30 · see citing works
Shared pathophysiology: Understanding stroke and Alzheimer’s disease
Sriram, S., Mehkri, Y., Quintin, S. S., & Lucke-Wold, B. P. (2022) · Clinical Neurology and Neurosurgery · doi:10.1016/j.clineuro.2022.107306 · Cited by 29 · see citing works
Protein-protein interactions underlying the behavioral and psychological symptoms of dementia (BPSD) and Alzheimer’s disease
Mao, Y., Fisher, D. W., Yang, S., Keszycki, R. M., & Dong, H. (2020) · PLOS ONE · doi:10.1371/journal.pone.0226021 · Cited by 28 · see citing works
Phosphomimetics at Ser199/Ser202/Thr205 in Tau Impairs Axonal Transport in Rat Hippocampal Neurons
Christensen, K. R., Combs, B., Richards, C. J., Grabinski, T. M., Alhadidy, M. M., & Kanaan, N. M. (2023) · Molecular Neurobiology · doi:10.1007/s12035-023-03281-3 · Cited by 28 · see citing works
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The diagnosis of progressive supranuclear palsy: current opinions and challenges
Ali, F., & Josephs, K. A. (2018) · Expert Review of Neurotherapeutics · doi:10.1080/14737175.2018.1489241 · Cited by 27 · see citing works
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Tau and Axonopathy in Neurodegenerative Disorders
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Kinesin-1 transport reductions enhance human tau hyperphosphorylation, aggregation and neurodegeneration in animal models of tauopathies
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Authors: Kneynsberg, A., Combs, B., Christensen, K., Morfini, G., & Kanaan, N. M.
Affiliations: Michigan State University (US)
University of Illinois Chicago (US)
Trinity Health Grand Rapids (US)
Corresponding author: Morfini, Gerardo
Kanaan, Nicholas M.
ORCID: Kneynsberg, Andrew
Combs, Benjamin
Christensen, Kyle
Morfini, Gerardo
Kanaan, Nicholas M.
Venue: Frontiers in Neuroscience
Publisher: Frontiers Media SA
Published: 2017-10-17
Volume: 11
Pages: 572-572
ISSN: 1662-453X (ISSN-L)
DOI: 10.3389/fnins.2017.00572
PMC: PMC5651019
OpenAlex: W2763441547
Cited by: 102
References: 206
Citations by year: 2026: 6 · 2025: 7 · 2024: 8 · 2023: 6 · 2022: 15 · 2021: 18 · 2020: 18 · 2019: 16 · 2018: 8
FWCI: 1.41
Type: journal article
Language: en
Open access: gold
doi.org
Licence: cc-by
Locations: Frontiers in Neuroscience (publishedVersion, cc-by)
PubMed Central (publishedVersion, cc-by)
PubMed (publishedVersion)
DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders: National Institute on Aging (R01 AG044372)
National Institute of Neurological Disorders and Stroke (R01 NS082730, R21 NS096642, R01 NS066942)
BrightFocus Foundation (A2013364S)
Topics: Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
Health Sciences › Medicine › Neurology › Amyotrophic Lateral Sclerosis Research
Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
Keywords: tauopathy, axonal degeneration, axonopathy, tau protein, microtubule stabilization, microtubule destabilization, tau phosphorylation, kinase signaling pathways, axonal transport, neuronal connectivity, dying-back degeneration

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Axonal degeneration in tauopathies: disease relevance and underlying mechanisms

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