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Academic literature on the topic 'Tau protein deposits'

Author: Grafiati
Published: 10 December 2022
Last updated: 28 January 2023

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Journal articles on the topic "Tau protein deposits"

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Andrés-Benito, Pol, Margarita Carmona, Mónica Jordán, Joaquín Fernández-Irigoyen, Enrique Santamaría, José Antoni del Rio, and Isidro Ferrer. "Host Tau Genotype Specifically Designs and Regulates Tau Seeding and Spreading and Host Tau Transformation Following Intrahippocampal Injection of Identical Tau AD Inoculum." International Journal of Molecular Sciences 23, no. 2 (January 10, 2022): 718. http://dx.doi.org/10.3390/ijms23020718.

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Several studies have demonstrated the different characteristics of tau seeding and spreading following intracerebral inoculation in murine models of tau-enriched fractions of brain homogenates from AD and other tauopathies. The present study is centered on the importance of host tau in tau seeding and the molecular changes associated with the transformation of host tau into abnormal tau. The brains of three adult murine genotypes expressing different forms of tau—WT (murine 4Rtau), hTau (homozygous transgenic mice knock-out for murine tau protein and heterozygous expressing human forms of 3Rtau and 4Rtau proteins), and mtWT (homozygous transgenic mice knock-out for murine tau protein)—were analyzed following unilateral hippocampal inoculation of sarkosyl-insoluble tau fractions from the same AD and control cases. The present study reveals that (a) host tau is mandatory for tau seeding and spreading following tau inoculation from sarkosyl-insoluble fractions obtained from AD brains; (b) tau seeding does not occur following intracerebral inoculation of sarkosyl-insoluble fractions from controls; (c) tau seeding and spreading are characterized by variable genotype-dependent tau phosphorylation and tau nitration, MAP2 phosphorylation, and variable activation of kinases that co-localize with abnormal tau deposits; (d) transformation of host tau into abnormal tau is an active process associated with the activation of specific kinases; (e) tau seeding is accompanied by modifications in tau splicing, resulting in the expression of new 3Rtau and 4Rtau isoforms, thus indicating that inoculated tau seeds have the capacity to model exon 10 splicing of the host mapt or MAPT with a genotype-dependent pattern; (e) selective regional and cellular vulnerabilities, and different molecular compositions of the deposits, are dependent on the host tau of mice injected with identical AD tau inocula.
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Ukmar-Godec, T., P. Fang, A. Ibáñez de Opakua, F. Henneberg, A. Godec, K. T. Pan, M. S. Cima-Omori, et al. "Proteasomal degradation of the intrinsically disordered protein tau at single-residue resolution." Science Advances 6, no. 30 (July 2020): eaba3916. http://dx.doi.org/10.1126/sciadv.aba3916.

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Intrinsically disordered proteins (IDPs) can be degraded in a ubiquitin-independent process by the 20S proteasome. Decline in 20S activity characterizes neurodegenerative diseases. Here, we examine 20S degradation of IDP tau, a protein that aggregates into insoluble deposits in Alzheimer’s disease. We show that cleavage of tau by the 20S proteasome is most efficient within the aggregation-prone repeat region of tau and generates both short, aggregation-deficient peptides and two long fragments containing residues 1 to 251 and 1 to 218. Phosphorylation of tau by the non-proline–directed Ca2+/calmodulin-dependent protein kinase II inhibits degradation by the 20S proteasome. Phosphorylation of tau by GSK3β, a major proline-directed tau kinase, modulates tau degradation kinetics in a residue-specific manner. The study provides detailed insights into the degradation products of tau generated by the 20S proteasome, the residue specificity of degradation, single-residue degradation kinetics, and their regulation by posttranslational modification.
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Oliveira, Francine Hehn de, Edson Rodrigues Neto, Mariana Kumaira Fonseca, André Silvestre Reitz da Costa, Marcio Aloisio Bezerra Cavalcanti Rockenbach, Renata dos Santos Padilha, Liana Lisboa Fernandez, and Arlete Hilbig. "Neurodegenerative changes in the brainstem and olfactory bulb in people older than 50 years old: a descriptive study." Arquivos de Neuro-Psiquiatria 73, no. 7 (July 2015): 569–77. http://dx.doi.org/10.1590/0004-282x20150066.

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With the increase in life expectancy in Brazil, concerns have grown about the most prevalent diseases in elderly people. Among these diseases are neurodegenerative diseases, such as Alzheimer’s and Parkinson’s diseases. Protein deposits related to the development of these diseases can pre-date the symptomatic phases by years. The tau protein is particularly interesting: it might be found in the brainstem and olfactory bulb long before it reaches the limbic cortex, at which point symptoms occur. Of the 14 brains collected in this study, the tau protein was found in the brainstems of 10 (71.42%) and in olfactory bulbs of 3 out 11. Of the 7 individuals who had a final diagnosis of Alzheimer’s disease (AD), 6 presented tau deposits in some region of the brainstem. Our data support the idea of the presence of tau protein in the brainstem and olfactory bulb in the earliest stages of AD.
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Kovacs, G. G., S. Klotz, P. Fischer, M. Hinterberger, G. Ricken, S. Hönigschnabl, and E. Gelpi. "Complex Protein Astrogliopathy in an Octogenarian." Canadian Journal of Neurological Sciences / Journal Canadien des Sciences Neurologiques 48, s2 (July 2021): S10. http://dx.doi.org/10.1017/cjn.2021.169.

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Combination of multiple neurodegenerative proteinopathies is frequent in the elderly. We report the case of an octogenarian who attempted suicide and deceased after hospital admission. Anatomical mapping was performed in several cortical and subcortical brain regions using antibodies against phospho-tau, 4R tau, 3R tau, phospho-TDP-43, ubiquitin, α-synuclein, Aβ and p62. Unexpectedly, histopathologic examination showed prominent subpial, subependymal, grey and white matter, and perivascular aging-related tau astrogliopathy (ARTAG) affecting cortical and subcortical brain regions. This pathology was associated with intermediate Alzheimer’s disease neuropathologic change, cerebral amyloid angiopathy, Lewy-body-type and astroglial synuclein proteinopathy and a multiple system TDP-43 proteinopathy involving also the astroglia. This unusual case of extensive and widespread ARTAG with a complex multiproteinopathy may represent an independent disease entity in the elderly with tau astrogliopathy as the leading force.Learning ObjectiveRecognize astroglial protein deposits in neurodegeneration
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5

Goedert, M., R. Jakes, R. A. Crowther, M. Hasegawa, M. J. Smith, and M. G. Spillantini. "Intraneuronal filamentous tau protein and α-synuclein deposits in neurodegenerative diseases." Biochemical Society Transactions 26, no. 3 (August 1, 1998): 463–71. http://dx.doi.org/10.1042/bst0260463.

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Piccardo, Pedro, Declan King, Deborah Brown, and Rona M. Barron. "Variable tau accumulation in murine models with abnormal prion protein deposits." Journal of the Neurological Sciences 383 (December 2017): 142–50. http://dx.doi.org/10.1016/j.jns.2017.10.040.

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Rodrigues Neto, Edson, Mariana K. Fonseca, Álvaro C. B. Guedes, Francine H. Oliveira, Arlete Hilbig, and Liana Lisboa Fernandez. "Neuropathological findings in entorhinal cortex of subjects aged 50 years or older and their correlation with dementia in a sample from Southern Brazil." Dementia & Neuropsychologia 11, no. 1 (March 2017): 24–31. http://dx.doi.org/10.1590/1980-57642016dn11-010005.

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ABSTRACT Introduction: The aims of this study were to survey neurodegenerative changes detected by abnormal protein deposits in the Entorhinal Cortex (EC) of subjects aged 50 years or older and to correlate these findings with suspected dementia, as detected by the IQCODE (Informant Questionnaire on Cognitive Decline in the Elderly) . Methods: Fourteen brains were submitted to the immunohistochemistry technique for different proteins (beta-amyloid, tau, -synuclein and phospho-TDP-43) and data obtained compared with IQCODE scores. Results: Fifty-seven percent of the individuals exhibited IQCODE results compatible with dementia, being classified into the demented group (DG): 87.5% of patients had neuropathological findings corresponding to Alzheimer's-like brain pathology (ALBP). Of the patients in the non-demented group (NDG), 16.7% met neuropathological criteria for ALBP. All individuals in the DG showed deposits of more than one kind of protein in the EC. The most common association was hyperphosphorylated tau and beta-amyloid protein (87.5%). Discussion: Most individuals with dementia had neuropathological findings of ALBP, as did one individual with no signs of dementia, characterizing a preclinical stage. The results of this study suggest that deposits of a single type of anomalous protein are normal findings in an aging brain, while more than one kind of protein or the combined presence of anomalous protein deposits indicate the presence of dementia.
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Kasho, Kazutoshi, Lukas Krasauskas, Vytautas Smirnovas, Gorazd Stojkovič, Ludmilla A. Morozova-Roche, and Sjoerd Wanrooij. "Human Polymerase δ-Interacting Protein 2 (PolDIP2) Inhibits the Formation of Human Tau Oligomers and Fibrils." International Journal of Molecular Sciences 22, no. 11 (May 28, 2021): 5768. http://dx.doi.org/10.3390/ijms22115768.

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A central characteristic of Alzheimer’s disease (AD) and other tauopathies is the accumulation of aggregated and misfolded Tau deposits in the brain. Tau-targeting therapies for AD have been unsuccessful in patients to date. Here we show that human polymerase δ-interacting protein 2 (PolDIP2) interacts with Tau. With a set of complementary methods, including thioflavin-T-based aggregation kinetic assays, Tau oligomer-specific dot-blot analysis, and single oligomer/fibril analysis by atomic force microscopy, we demonstrate that PolDIP2 inhibits Tau aggregation and amyloid fibril growth in vitro. The identification of PolDIP2 as a potential regulator of cellular Tau aggregation should be considered for future Tau-targeting therapeutics.
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Maj, Magdalena, Wolfgang Gartner, Aysegul Ilhan, Dashurie Neziri, Johannes Attems, and Ludwig Wagner. "Expression of TAU in insulin-secreting cells and its interaction with the calcium-binding protein secretagogin." Journal of Endocrinology 205, no. 1 (January 8, 2010): 25–36. http://dx.doi.org/10.1677/joe-09-0341.

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Tauopathies have been associated with Alzheimer's disease (AD), which frequently manifests together with diabetes mellitus type 2. Calcium-binding proteins such as the recently identified secretagogin (SCGN) might exert protective effects. As pancreatic β-cells and neurons share common electrophysiological properties, we investigated the appearance of TAU (listed as MAPT in the HUGO and MGI Databases) protein at the islets of Langerhans and β-cell-derived cell lines which highly express the neuroendocrine-specific protein SCGN. Six predominant TAU isoforms could be identified by immunoblotting, which formed TAU deposits detectable by immunofluorescence and sarkosyl-insoluble pellets. Using GST–SCGN pull-down assays, a calcium-dependent SCGN–TAU interaction was found. In this line, sucrose density gradient fractionation and differential ultracentrifugation studies of TAU and SCGN revealed co-appearance of both proteins. Co-localization of TAU and SCGN within insulinoma cells and islets of Langerhans mainly restricted to insulin-positive β-cells was demonstrated by confocal microscopy. Motivated by these findings, we looked if SCGN overexpression could exert protective function on Rin-5F cells, which showed differences in TAU levels. Testing the vulnerability of Rin-5F clones by MTT assay, we revealed that high TAU levels going along with highest TAU aggregates could not be antagonized by high levels of SCGN protein. Our findings demonstrated for the first time the association of TAU and the calcium-binding protein SCGN and support earlier results implicating that β-cells might represent an extra cerebral site of tauopathy.
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Kundra, Rishika, Prajwal Ciryam, Richard I. Morimoto, Christopher M. Dobson, and Michele Vendruscolo. "Protein homeostasis of a metastable subproteome associated with Alzheimer’s disease." Proceedings of the National Academy of Sciences 114, no. 28 (June 26, 2017): E5703—E5711. http://dx.doi.org/10.1073/pnas.1618417114.

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Alzheimer’s disease is the most common cause of dementia. A hallmark of this disease is the presence of aberrant deposits containing by the Aβ peptide (amyloid plaques) and the tau protein (neurofibrillary tangles) in the brains of affected individuals. Increasing evidence suggests that the formation of these deposits is closely associated with the age-related dysregulation of a large set of highly expressed and aggregation-prone proteins, which make up a metastable subproteome. To understand in more detail the origins of such dysregulation, we identify specific components of the protein homeostasis system associated with these metastable proteins by using a gene coexpression analysis. Our results reveal the particular importance of the protein trafficking and clearance mechanisms, including specific branches of the endosomal–lysosomal and ubiquitin–proteasome systems, in maintaining the homeostasis of the metastable subproteome associated with Alzheimer’s disease.
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Book chapters on the topic "Tau protein deposits"

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Amin, Mohamed M. "Neurodegenerative Disorders." In Advances in Medical Diagnosis, Treatment, and Care, 195–216. IGI Global, 2019. http://dx.doi.org/10.4018/978-1-5225-5282-6.ch009.

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Neurodegenerative diseases (NDs) are characterized by specific dysfunction and damage of neurons related to pathologically changed proteins that deposit in the patient brain but also in peripheral organs. These proteins can be used for therapy or used as biomarkers. Except for a plethora of alterations revealed for dissimilar neurodegeneration-related proteins, amyloid-β, prion protein, TAR DNA-binding protein 43 (TDP-43, transactive response DNA binding protein 43 kDa), tau and α-synuclein, or fused in sarcoma protein (FUS), molecular classification of NDs depend on the full morphological assessment of protein deposits, their spreading in the brain, and their correspondence to clinical signs with specific genetic modifications. The current chapter represents the etiology of neurodegeneration, classification of NDs, concentrating on the maximum applicable biochemical and anatomical characteristics and most imperative NDs.
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Duyckaerts, Charles, James Lowe, and Matthew Frosch. "Pathology of Degenerative Diseases of the Nervous System." In Escourolle and Poirier's Manual of Basic Neuropathology, 173–204. Oxford University Press, 2013. http://dx.doi.org/10.1093/med/9780199929054.003.0008.

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Degenerative diseases of the nervous system are characterized by lesions involving specific systems of functionally related neurons. The abnormality is manifest by neuronal loss with variable astrocytic and microglial reactive changes. Accumulation of specific protein aggregates (e.g., Aβ‎, tau, α‎-synuclein, TAR-DNA-binding protein 43, polyglutamine) is a common feature, giving rise to distinctive intracellular inclusions or extracellular deposits. For some diseases, there are well-characterized genetic abnormalities. This chapter describes and illustrates the morphologic changes and genetic data in the different diseases. These are classified, according to the dominant clinical features, into five categories: degenerations of the cerebral cortex (dementia), movement disorders, cerebellar ataxia, motor neuron disease, and conditions associated with autonomic failure.
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Duyckaerts, Charles. "Pathology of Degenerative Diseases of the Nervous System." In Escourolle and Poirier's Manual of Basic Neuropathology, 186–218. Oxford University Press, 2018. http://dx.doi.org/10.1093/med/9780190675011.003.0008.

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Degenerative diseases of the nervous system are characterized by lesions involving specific systems of functionally related neurons. The abnormality is manifest by neuronal loss with variable astrocytic and microglial reactive changes. Accumulation of specific protein aggregates (e.g., Aβ‎, tau, α‎-synuclein, TAR-DNA binding protein 43, polyglutamine) is a common feature giving rise to distinctive intracellular inclusions or extracellular deposits. For some diseases, there are well-characterized genetic abnormalities. This chapter describes and illustrates the morphological changes and genetic data in the different diseases. These are classified, per the dominant clinical features, into five categories: degenerations of the cerebral cortex (dementia), movement disorders, cerebellar ataxia, motor neuron disease, and conditions associated with autonomic failure.
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Sanjay V. and Swarnalatha P. "DL-EDAD Deep Learning Approach to Early Detection for Alzheimer's Disease Using E-GKFCM." In Deep Learning Research Applications for Natural Language Processing, 239–53. IGI Global, 2022. http://dx.doi.org/10.4018/978-1-6684-6001-6.ch016.

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In Alzheimer's disease (AD), memory and cognitive abilities deteriorate, affecting the capacity to do basic activities. In and around brain cells, aberrant amyloid and tau protein accumulation is believed to cause it. Amyloid deposits create plaques surrounding brain cells, whereas tau deposits form tangles inside brain cells. The plagues and tangles harm healthy brain cells, causing shrinkage. This damage seems to be occurring in the hippocampus, a brain region involved in memory formation. There are presently no methods that provide the most accurate outcomes. The current techniques do not identify AD early. The proposed DL-EDAD method achieves excellent clustering using CNN with E-GKFCM (enhanced gaussian kernel fuzzy c-means clustering). The E-GKFCM utilizes an elbow method to determine the number of clusters in a dataset. Unlike other medical pictures, brain scans are extremely sensitive.
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