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Tau oligomers

Jesus Avila, Juan S Jiménez, Carmen L Sayas, Marta Bolós, Juan C Zabala, Germán Rivas, Felix Hernández
Tau is a microtubule-associated protein that plays an important role in axonal stabilization, neuronal development, and neuronal polarity. In this review, we focus on the primary, secondary, tertiary, and quaternary tau structures. We describe the structure of tau from its specific residues until its conformation in dimers, oligomers, and larger polymers in physiological and pathological situations.
2016: Frontiers in Aging Neuroscience
Niyaz Mohammadzadeh Honarvar, Ahmad Saedisomeolia, Mina Abdolahi, Amir Shayeganrad, Gholamreza Taheri Sangsari, Babak Hassanzadeh Rad, Gerald Muench
Alzheimer's disease (AD) is considered as one of the most prevalent neurodegenerative disorders characterized by progressive loss of mental function and ability to learn. AD is a multifactorial disorder. Various hypotheses are suggested for the pathophysiology of AD including "Aβ hypothesis," "tau hypothesis," and "cholinergic hypothesis." Recently, it has been demonstrated that neuroinflammation is involved in the pathogenesis of AD. Neuroinflammation causes synaptic dysfunction and neuronal death within the brain...
November 18, 2016: Journal of Molecular Neuroscience: MN
Seung-Hoon Yang, Dongkeun Kenneth Lee, Jisu Shin, Sejin Lee, Seungyeop Baek, Jiyoon Kim, Hoyong Jung, Jung-Mi Hah, YoungSoo Kim
Alzheimer's disease (AD) is a neurodegenerative disorder characterized by cognitive symptoms of learning and memory deficits. Such cognitive impairments are attributed to brain atrophy resulting from progressive neuronal and synaptic loss; therefore, alleviation of neural cell death is as an important target of treatment as other classical hallmarks of AD, such as aggregation of amyloid-β (Aβ) and hyperphosphorylation of tau. Here, we found that an anti-necroptotic molecule necrostatin-1 (Nec-1) directly targets Aβ and tau proteins, alleviates brain cell death and ameliorates cognitive impairment in AD models...
November 17, 2016: EMBO Molecular Medicine
Nicola Voyle, Hamel Patel, Amos Folarin, Stephen Newhouse, Caroline Johnston, Pieter Jelle Visser, Richard J B Dobson, Steven J Kiddle
BACKGROUND: The search for a biomarker of Alzheimer's disease (AD) pathology (amyloid-β (Aβ) and tau) is ongoing, with the best markers currently being measurements of Aβ and tau in cerebrospinal fluid (CSF) and via positron emission tomography (PET) scanning. These methods are relatively invasive, costly, and often have high screening failure rates. Consequently, research is aiming to elucidate blood biomarkers of Aβ and tau. OBJECTIVE: This study aims to investigate a case/control polygenic risk score (PGRS) as a marker of tau and investigate blood markers of a combined Aβ and tau outcome for the first time...
November 6, 2016: Journal of Alzheimer's Disease: JAD
S Bhattacharyya, K Kim, H Nakazawa, M Umetsu, W Teizer
Obstacles in microtubule mediated neuronal transport can trigger dementia. We use bio-motility assays, that simulate the neuron chemistry in axonopathy, to screen chemicals, that retain the microtubule dynamics in healthy neuronal activity. Tau protein inhibits microtubule activity and leads to oligomerization. Iron(iii) untangles, whereas mono-sodium-glutamate destabilizes the microtubule oligomer.
October 27, 2016: Integrative Biology: Quantitative Biosciences From Nano to Macro
David J Koss, Glynn Jones, Anna Cranston, Heidi Gardner, Nicholas M Kanaan, Bettina Platt
Post-mortem investigations of human Alzheimer's disease (AD) have largely failed to provide unequivocal evidence in support of the original amyloid cascade hypothesis, which postulated deposition of β-amyloid (Aβ) aggregates to be the cause of a demented state as well as inductive to tau neurofibrillary tangles (NFTs). Conflicting evidence suggests, however, that Aβ plaques and NFTs, albeit to a lesser extent, are present in a substantial subset of non-demented individuals. Hence, a range of soluble tau and Aβ species has more recently been implicated as the disease-relevant toxic entities...
December 2016: Acta Neuropathologica
Moran Frenkel-Pinter, Sharon Tal, Roni Scherzer-Attali, Malak Abu-Hussien, Idan Alyagor, Tal Eisenbaum, Ehud Gazit, Daniel Segal
Alzheimer's disease (AD) is the most abundant tauopathy and is characterized by Aβ-derived plaques and tau-derived tangles, resulting from the unfolding of the corresponding monomeric subunits into ordered β-sheet oligomers and fibrils. Intervening in the toxic aggregation process is a promising therapeutic approach, but, to date, a disease-modifying therapy is neither available for AD nor for other tauopathies. Along these lines, we have previously demonstrated that a small naphthoquinone-tryptophan hybrid, termed NQTrp, is an effective modulator of tauopathy in vitro and in vivo...
October 20, 2016: Neuro-degenerative Diseases
Susanne Wegmann, Samantha Nicholls, Shuko Takeda, Zhanyun Fan, Bradley T Hyman
Tau is a neuronal microtubule binding protein that, in Alzheimer's disease and other neurodegenerative diseases, can form oligomeric and large fibrillar aggregates, which deposit in neurofibrillary tangles. Tau's physiological state of multimerization appears to vary across conditions, and a stable dimeric form of soluble tau has been suggested from experiments using recombinant tau in vitro. We tested if tau dimerization, or oligomerization, also occurs in cells, and if soluble tau oligomers are relevant for the release and internalization of tau...
October 12, 2016: Journal of Neurochemistry
Darrell Sawmiller, Ahsan Habib, Song Li, Donna Darlington, Huayan Hou, Jun Tian, R Douglas Shytle, Adam Smith, Brian Giunta, Takashi Mori, Jun Tan
Naturally-occurring bioactive flavonoids such as diosmin significantly reduces amyloid beta (Aβ) associated pathology in Alzheimer's disease (AD) mouse models. In the present study, oral administration of diosmin reduced cerebral Aβ oligomer levels, tau-hyperphosphorylation and cognitive impairment in the 3xTg-AD mouse model through glycogen synthase kinase-3 (GSK-3) and transient receptor potential canonical 6-related mechanisms. Diosmetin, one major bioactive metabolite of diosmin, increased inhibitory GSK-3β phosphorylation, while selectively reducing γ-secretase activity, Aβ generation, tau hyperphosphorylation and pro-inflammatory activation of microglia in vitro, without altering Notch processing...
October 15, 2016: Journal of Neuroimmunology
Ashley N Nilson, Kelsey C English, Julia E Gerson, T Barton Whittle, C Nicolas Crain, Judy Xue, Urmi Sengupta, Diana L Castillo-Carranza, Wenbo Zhang, Praveena Gupta, Rakez Kayed
It is well-established that inflammation plays an important role in Alzheimer's disease (AD) and frontotemporal lobar dementia (FTLD). Inflammation and synapse loss occur in disease prior to the formation of larger aggregates, but the contribution of tau to inflammation has not yet been thoroughly investigated. Tau pathologically aggregates to form large fibrillar structures known as tangles. However, evidence suggests that smaller soluble aggregates, called oligomers, are the most toxic species and form prior to tangles...
October 1, 2016: Journal of Alzheimer's Disease: JAD
Andrés Norambuena, Horst Wallrabe, Lloyd McMahon, Antonia Silva, Eric Swanson, Shahzad S Khan, Daniel Baerthlein, Erin Kodis, Salvatore Oddo, James W Mandell, George S Bloom
A major obstacle to presymptomatic diagnosis and disease-modifying therapy for Alzheimer's disease (AD) is inadequate understanding of molecular mechanisms of AD pathogenesis. For example, impaired brain insulin signaling is an AD hallmark, but whether and how it might contribute to the synaptic dysfunction and neuron death that underlie memory and cognitive impairment has been mysterious. Neuron death in AD is often caused by cell cycle reentry (CCR) mediated by amyloid-β oligomers (AβOs) and tau, the precursors of plaques and tangles...
September 29, 2016: Alzheimer's & Dementia: the Journal of the Alzheimer's Association
Julia E Gerson, Amrit Mudher, Rakez Kayed
The culmination of many years of increasing research into the toxicity of tau aggregation in neurodegenerative disease has led to the consensus that soluble, oligomeric forms of tau are likely the most toxic entities in disease. While tauopathies overlap in the presence of tau pathology, each disease has a unique combination of symptoms and pathological features; however, most study into tau has grouped tau oligomers and studied them as a homogenous population. Established evidence from the prion field combined with the most recent tau and amyloidogenic protein research suggests that tau is a prion-like protein, capable of seeding the spread of pathology throughout the brain...
September 21, 2016: Critical Reviews in Biochemistry and Molecular Biology
Abolfazl Jangholi, Mohammad Reza Ashrafi-Kooshk, Seyed Shahriar Arab, Gholamhossein Riazi, Farzad Mokhtari, Mansour Poorebrahim, Hamid Mahdiuni, Boris I Kurganov, Ali Akbar Moosavi-Movahedi, Reza Khodarahmi
In many neurodegenerative diseases, formation of protein fibrillar aggregates has been observed as a major pathological change. Neurofibrillary tangles, mainly composed of fibrils formed by the microtubule-associated protein; Tau, are a hallmark of a group of neurodegenerative diseases such as Alzheimer's disease. Tau belongs to the class of natively unfolded proteins and partially folds into an ordered β-structure during aggregation. Polyanionic cofactors such as heparin are commonly used as inducer of Tau aggregation in vitro...
November 1, 2016: Archives of Biochemistry and Biophysics
Mathew A Sherman, Michael LaCroix, Fatou Amar, Megan E Larson, Colleen Forster, Adriano Aguzzi, David A Bennett, Martin Ramsden, Sylvain E Lesné
UNLABELLED: Despite the demonstration that amyloid-β (Aβ) can trigger increased tau phosphorylation and neurofibrillary tangle (NFT) formation in vivo, the molecular link associating Aβ and tau pathologies remains ill defined. Here, we observed that exposure of cultured primary neurons to Aβ trimers isolated from brain tissue of subjects with Alzheimer's disease led to a specific conformational change of tau detected by the antibody Alz50. A similar association was supported by postmortem human brain analyses...
September 14, 2016: Journal of Neuroscience: the Official Journal of the Society for Neuroscience
Jun Yoshitake, Yoshiyuki Soeda, Tomoaki Ida, Akio Sumioka, Misato Yoshikawa, Kenji Matsushita, Takaaki Akaike, Akihiko Takashima
Neurofibrillar tangles caused by intracellular hyperphosphorylated tau inclusion and extracellular amyloid β peptide deposition are hallmarks of Alzheimer's disease. Tau contains one or two cysteine residues in three or four repeats of the microtubule binding region following alternative splicing of exon 10, and formation of intermolecular cysteine disulfide bonds accelerates tau aggregation. 8-Nitroguanosine 3',5'-cyclic monophosphate (8-nitro-cGMP) acts as a novel second messenger of nitric oxide (NO) by covalently binding cGMP to cysteine residues by electrophilic properties, a process termed protein S-guanylation...
October 21, 2016: Journal of Biological Chemistry
Siân Baker, Juan Carlos Polanco, Jϋrgen Götz
In Alzheimer's disease, the distribution of neurofibrillary tangles, a histological hallmark comprised of phosphorylated forms of the protein tau, follows a distinct pattern through anatomically connected brain regions. The well-documented correlation between the severity of tau pathology and disease progression implies a prion-like seeding and spreading mechanism for tau. Experimentally, this has been addressed in transgenic mice by the injection of protein lysates isolated from brains of transgenic mice or patients with tauopathies, including AD, that were shown to behave like seeds, accelerating tau pathology and tangle formation in predisposed mice...
October 4, 2016: Journal of Alzheimer's Disease: JAD
Qingwei Ruan, Grazia D'Onofrio, Daniele Sancarlo, Antonio Greco, Zhuowei Yu
Cognitive frailty (CF) overlaps with early neuropathological alterations associated with aging‑related major neurocognitive disorders, including Alzheimer's disease (AD). Fluid biomarkers for these pathological brain alterations allow for early diagnosis in the preclinical stages of AD, and for objective prognostic assessments in clinical intervention trials. These biomarkers may also be helpful in the screening of CF. The present study reviewed the literature and identified systematic reviews of cohort studies and other authoritative reports...
October 2016: Molecular Medicine Reports
Brian Spencer, Paula A Desplats, Cassia R Overk, Elvira Valera-Martin, Robert A Rissman, Chengbiao Wu, Michael Mante, Anthony Adame, Jazmin Florio, Edward Rockenstein, Eliezer Masliah
UNLABELLED: Alzheimer's disease (AD) is characterized by the progressive accumulation of amyloid β (Aβ) and microtubule associate protein tau, leading to the selective degeneration of neurons in the neocortex, limbic system, and nucleus basalis, among others. Recent studies have shown that α-synuclein (α-syn) also accumulates in the brains of patients with AD and interacts with Aβ and tau, forming toxic hetero-oligomers. Although the involvement of α-syn has been investigated extensively in Lewy body disease, less is known about the role of this synaptic protein in AD...
July 27, 2016: Journal of Neuroscience: the Official Journal of the Society for Neuroscience
Farzad Mokhtari, Gholamhossein Riazi, Saeed Balalaie, Reza Khodarahmi, Saeed Karima, Azam Hemati, Bahram Bolouri, Fatemeh Hedayati Katouli, Esmat Fathi
No abstract text is available yet for this article.
October 2016: Neuropeptides
Miquel Martorell, Katherine Forman, Natalia Castro, Xavier Capó, Silvia Tejada, Antoni Sureda
Alzheimer's disease (AD) is an age-associated neurodegenerative amyloid disease and is considered a social and clinical problem the last decades, particularly in the Western countries. Amyloid diseases are characterized by the deposition of typically aggregated protein/peptides in tissues that are associated with brain degeneration and progressive cognitive impairment. The amyloid plaques and neurofibrillary tangles arise as a result of self-assembly into fibrillar material of amyloid-β protein and hyperphosphorylated tau, respectively...
2016: Current Pharmaceutical Biotechnology
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