Cited by 233Alzheimer's disease research and treatmentsCell death mechanisms and regulationMicrotubule and mitosis dynamics

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Tau Cleavage and Dephosphorylation in Cerebellar Granule Neurons Undergoing Apoptosis

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Canu, Nadia, Dus, Laura, Barbato, Christian, Ciotti, Maria T., Brancolini, Claudio, Rinaldi, Anna M., Novak, Michal, Cattaneo, Antonino, Bradbury, Andrew, Calissano, Pietro·1998·The Journal of Neuroscience

DOI 10.1523/jneurosci.18-18-07061.1998PMC PMC6793249

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Abstract

Cerebellar granule cells undergo apoptosis in culture after deprivation of potassium and serum. During this process we found that tau, a neuronal microtubule-associated protein that plays a key role in the maintenance of neuronal architecture, and the pathology of which correlates with intellectual decline in Alzheimer’s disease, is cleaved. The final product of this cleavage is a soluble dephosphorylated tau fragment of 17 kDa that is unable to associate with microtubules and accumulates in the perikarya of dying cells. The appearance of this 17 kDa fragment is inhibited by both caspase and calpain inhibitors, suggesting that tau is an in vivo substrate for both of these proteases during apoptosis. Tau cleavage is correlated with disruption of the microtubule network, and experiments with colchicine and taxol show that this is likely to be a cause and not a consequence of tau cleavage. These data indicate that tau cleavage and change in phosphorylation are important early factors in the failure of the microtubule network that occurs during neuronal apoptosis. Furthermore, this study introduces new insights into the mechanism(s) that generate the truncated forms of tau present in Alzheimer’s disease.

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PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENT
Lowry, O. H., Rosebrough, N., Farr, A. L., & Randall, R. (1951) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)52451-6 · Cited by 316,394
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
LAEMMLI, U. K. (1970) · Nature · doi:10.1038/227680a0 · Cited by 249,961
Short-Term Effects of Nose-Only Cigarette Smoke Exposure on Glutathione Redox Homeostasis, Cytochrome P450 1A1/2 and Respiratory Enzyme Activities in Mice Tissues
Raza, H., John, A., & Nemmar, A. (2013) · Cellular Physiology and Biochemistry · doi:10.1159/000350087 · Cited by 47,311
Apoptosis: A Basic Biological Phenomenon with Wideranging Implications in Tissue Kinetics
Kerr, J. F. R., Wyllie, A. H., & Currie, A. R. (1972) · British Journal of Cancer · doi:10.1038/bjc.1972.33 · Cited by 15,673
Apoptosis in the Pathogenesis and Treatment of Disease
Thompson, C. B. (1995) · Science · doi:10.1126/science.7878464 · Cited by 6,524
Caspases: the executioners of apoptosis
Cohen, G. M. (1997) · Biochemical Journal · doi:10.1042/bj3260001 · Cited by 4,737
Abnormal phosphorylation of the microtubule-associated protein tau (tau) in Alzheimer cytoskeletal pathology.
Grundke-Iqbal, I., Iqbal, K., Tung, Y. C., Quinlan, M., Wisniewski, H. M., & Binder, L. I. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.13.4913 · Cited by 3,676
Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease
Goedert, M., Spillantini, M. G., Jakes, R., Rutherford, D., & Crowther, R. A. (1989) · Neuron · doi:10.1016/0896-6273(89)90210-9 · Cited by 2,492
Mechanisms and Genes of Cellular Suicide
Steller, H. (1995) · Science · doi:10.1126/science.7878463 · Cited by 2,469
Microtubule-associated protein tau. A component of Alzheimer paired helical filaments.
Grundke, I., Iqbal, K., Quinlan, M., Tung, Y. C., Zaidi, M. S., & Wisniewski, H. M. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)38495-8 · Cited by 1,780

Show all 71 references

Research works printed but not linked: 2

Fasulo, 1998, Tau truncation in Alzheimer’s disease: expression of a fragment encompassing PHF core tau induces apoptosis in COS cells., Alzheimer’s Rep, 1, 1
10.1128/MCB.9.4.1381 · DOI

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Ohm, T. G., & Meske, V. (2006) · Acta Neurologica Scandinavica · doi:10.1111/j.1600-0404.2006.00692.x · Cited by 20
Stable‐Tau Overexpression in Human Neuroblastoma Cells
Delobel, P., Vanbesien-Mailliot, C., Hamdane, M., Sambo, A., Bégard, S., Violleau, A., Delacourte, A., & Buée, L. (2003) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1299.115 · Cited by 21
Involvement of TLCK‐sensitive serine protease in colchicine‐induced cell death of sympathetic neurons in culture
Mitsui, C., Sakai, K., Ninomiya, T., & Koike, T. (2001) · Journal of Neuroscience Research · doi:10.1002/jnr.10008 · Cited by 20
AD-Related N-Terminal Truncated Tau Is Sufficient to Recapitulate In Vivo the Early Perturbations of Human Neuropathology: Implications for Immunotherapy
Borreca, A., Latina, V., Corsetti, V., Middei, S., Piccinin, S., Valle, F. D., Bussani, R., Ammassari‐Teule, M., Nisticò, R., Calissano, P., et al. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-0974-3 · Cited by 18
Self-citation
Amyloid-β Injection in Rat Amygdala Alters Tau Protein but Not mRNA Expression
Chambers, C. B., Sigurdsson, E. M., Hejna, M. J., Lorens, S. A., Lee, J. M., & Muma, N. A. (2000) · Experimental Neurology · doi:10.1006/exnr.2000.7325 · Cited by 19
Markers of apoptosis and models of programmed cell death in Alzheimer’s disease
Hugon, J., Terro, F., Esclaire, F., & Yardin, C. (2000) · Springer eBooks · doi:10.1007/978-3-7091-6781-6_15 · Cited by 19
Dual Mechanism of Toxicity for Extracellular Injection of Tau Oligomers versus Monomers in Human Tau Mice
Manassero, G., Guglielmotto, M., Monteleone, D., Vasciaveo, V., Butenko, O., Tamagno, E., Arancio, O., & Tabaton, M. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-170298 · Cited by 17
Memantine Differentially Regulates Tau Phosphorylation Induced by Chronic Restraint Stress of Varying Duration in Mice
Liu, Y., Cao, L., Zhang, X., Liang, Y., Xu, Y., & Zhu, C. (2019) · Neural Plasticity · doi:10.1155/2019/4168472 · Cited by 18
Proteasomal degradation of caspase‐6 in 17β‐estradiol‐treated neurons
Tounekti, O., Zhang, Y., Klaiman, G., Goodyer, C. G., & LeBlanc, A. C. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02349.x · Cited by 18
Evaluation of the neuronal apoptotic pathways involved in cytoskeletal disruption-induced apoptosis
Jordà, E. G., Verdaguer, E., Jiménez, A., de Arriba, S. G., Allgaier, C., Pallàs, M., & Camins, A. (2005) · Biochemical Pharmacology · doi:10.1016/j.bcp.2005.04.036 · Cited by 17
Apoptosis and cytochrome c release in cerebellar granule cells.
Bobba, A., Atlante, A., Lidia de, B. A. R. I., Passarella, S., & Marra, E. (2004) · PubMed · Cited by 17
Activated Caspase-3 and Neurodegeneration and Synaptic Plasticity in Alzheimer’s Disease
Płóciennik, A., Prendecki, M., Zuba, E. B., Siudzinski, M., & Dorszewska, J. (2015) · Advances in Alzheimer s Disease · doi:10.4236/aad.2015.43007 · Cited by 17
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Wang, Y.-P., Wang, X., Tian, Q., Yang, Y., Zhang, Q., Zhang, J.-Y., Zhang, Y.-C., Wang, Z.-F., Wang, Q., Li, H., et al. (2006) · Journal of Neural Transmission · doi:10.1007/s00702-006-0507-5 · Cited by 17
Effect of Staurosporine in the Morphology and Viability of Cerebellar Astrocytes: Role of Reactive Oxygen Species and NADPH Oxidase
Olguín‐Albuerne, M., Domínguez-Gómez, G., & Morán, J. (2014) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2014/678371 · Cited by 17
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Barbato, C. (2022) · Cells · doi:10.3390/cells11152375 · Cited by 17
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Wang, K., Moghieb, A. M., Yang, Z., & Zhang, Z. (2013) · Proceedings of SPIE, the International Society for Optical Engineering/Proceedings of SPIE · doi:10.1117/12.2020030 · Cited by 16
Atypical role of proximal caspase-8 in truncated Tau-induced neurite regression and neuronal cell death.
Chung, C., Hong, Y.-M., Song, S.-M., Woo, H.-N., Choi, Y.-H., Rohn, T., & Jung, Y.-K. (2003) · Neurobiology of Disease · doi:10.1016/j.nbd.2003.08.017 · Cited by 18
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Esposito, G., Viglino, P., Novák, M., & Cattaneo, A. (2000) · Journal of Peptide Science · doi:10.1002/1099-1387(200011)6:11 · Cited by 16
Self-citation
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Guan, P.-P., & Wang, P. (2023) · Molecular Neurobiology · doi:10.1007/s12035-023-03277-z · Cited by 15
DNA ligase I is dephosphorylated during the execution step of etoposide-induced apoptosis
Rossi, R., Montecucco, A., Donzelli, M., Denegri, M., Biamonti, G., & Scovassi, A. I. (2002) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4400961 · Cited by 15
CNS Injury: Posttranslational Modification of the Tau Protein as a Biomarker
Caprelli, M. T., Mothe, A. J., & Tator, C. H. (2017) · The Neuroscientist · doi:10.1177/1073858417742125 · Cited by 14
GT1b-induced neurotoxicity is mediated by the Akt/GSK-3/tau signaling pathway but not caspase-3 in mesencephalic dopaminergic neurons
Chung, E. S., Bok, E., Sohn, S., Lee, Y. D., Baik, H. H., & Jin, B. K. (2010) · BMC Neuroscience · doi:10.1186/1471-2202-11-74 · Cited by 14
Role of caspases in neuronal apoptosis
Ventimiglia, R., Lau, L., Kinloch, R. A., Hopkins, A. L., Karran, E. H., Petalidis, L. P., & Ward, R. V. (2001) · Drug Development Research · doi:10.1002/ddr.1155 · Cited by 14
Pathological-Like Assembly of tau Induced by a Paired Helical Filament Core Expressed at the Plasma Membrane
Campos‐Peña, V., Tapia-Ramı́rez, J., Sánchez‐Torres, C., & Meraz‐Ríos, M. A. (2009) · Journal of Alzheimer s Disease · doi:10.3233/jad-2009-1198 · Cited by 14
Early Events of Alzheimer-Like Neurodegeneration in Anti-Nerve Growth Factor Transgenic Mice
Capsoni, S., Giannotta, S., & Cattaneo, A. (2002) · Cited by 14
Self-citation
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Snigdha, S., Berchtold, N. C., Astarita, G., Saing, T., Piomelli, D., & Cotman, C. W. (2011) · PLoS ONE · doi:10.1371/journal.pone.0024652 · Cited by 13
Pseudo-phosphorylation at AT8 epitopes regulates the tau truncation at aspartate 421
Cao, L., Liang, Y., Liu, Y., Xu, Y., Wan, W., & Zhu, C. (2018) · Experimental Cell Research · doi:10.1016/j.yexcr.2018.06.010 · Cited by 13
Thioredoxin/thioredoxin reductase system involvement in cerebellar granule cell apoptosis
Bobba, A., Casalino, E., Petragallo, V. A., & Atlante, A. (2014) · APOPTOSIS · doi:10.1007/s10495-014-1023-y · Cited by 13
Chapter 11 Proteinase families and their inhibitors
Mykles, D. L. (2001) · Methods in cell biology · doi:10.1016/s0091-679x(01)66012-6 · Cited by 13

Authors: Canu, N., Dus, L., Barbato, C., Ciotti, M. T., Brancolini, C., Rinaldi, A. M., Novak, M., Cattaneo, A., Bradbury, A., & Calissano, P.
Affiliations: University of Rome Tor Vergata (IT)
Institute of Neurobiology and Molecular Medicine (IT)
AREA Science Park (IT)
Scuola Internazionale Superiore di Studi Avanzati (IT)
ORCID: Barbato, Christian
Brancolini, Claudio
Rinaldi, Anna M.
Cattaneo, Antonino
Bradbury, Andrew
Venue: The Journal of Neuroscience
Publisher: Society for Neuroscience
Published: 1998-09-15
Volume: 18
Issue: 18
Pages: 7061-7074
ISSN: 0270-6474 (ISSN-L)
1529-2401
DOI: 10.1523/jneurosci.18-18-07061.1998
PMC: PMC6793249
OpenAlex: W2122437043
Cited by: 232
References: 71
Citations by year: 2026: 1 · 2024: 1 · 2023: 1 · 2022: 4 · 2021: 3 · 2020: 6 · 2019: 6 · 2018: 13 · 2017: 7 · 2016: 3 · 2015: 7 · 2014: 13 · 2013: 9 · 2012: 6
FWCI: 8.40
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by-nc-sa
creativecommons.org/licenses/by-nc-sa/4.0/ (vor, 181 d)
Locations: Journal of Neuroscience (publishedVersion, cc-by-nc-sa)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Cineca Institutional Research Information System (Tor Vergata University) (submittedVersion, other-oa)
Institutional Research Information System (University of Udine) (submittedVersion)
Scuola Normale Superiore di Pisa (submittedVersion)
Funders: Consiglio Nazionale delle Ricerche
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
Keywords: tau protein, tau cleavage, tau dephosphorylation, cerebellar granule cells, neuronal apoptosis, caspases, calpain, microtubule-associated proteins, Alzheimer's disease
MeSH terms: Alzheimer Disease, Animals, Antineoplastic Agents, Phytogenic, Calpain, Cerebellum, Colchicine, Cysteine Endopeptidases, Cytoskeleton, Enzyme Precursors, Microtubules, Neurons, Oligopeptides, Peptide Fragments, Phosphorylation, Solubility, Cysteine Proteinase Inhibitors, tau Proteins, Rats, Wistar, Apoptosis, Paclitaxel, Caspases, Rats, Caspase 3

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Tau Cleavage and Dephosphorylation in Cerebellar Granule Neurons Undergoing Apoptosis

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