Role of tau protein in neurodegenerative dementias Elizabeta B Mukaetova-Ladinska

Dementia 3Ed ◽  
2005 ◽  
pp. 440-469
Keyword(s):  
Tau Protein ◽  
Neurodegenerative Dementias

The role of tau-protein in the diagnosis of cognitive impairment in diabetes

2020 ◽  
Author(s):  
Mariia Matveeva ◽  
Julia Samoilova ◽  
Natalie Zhukova
Keyword(s):  
Cognitive Impairment ◽  
Tau Protein

Structure, Function and Interactions of Tau: Particular Focus on Potential Drug Targets for the Treatment of Tauopathies

2018 ◽  
Vol 17 (5) ◽  
pp. 325-337 ◽  
Author(s):  
Hojjat Borna ◽  
Kasim Assadoulahei ◽  
Gholamhossein Riazi ◽  
Asghar Beigi Harchegani ◽  
Alireza Shahriary
Keyword(s):  
Tau Protein ◽  
Drug Targets ◽  
Brain Injuries ◽  
Potential Drug ◽  
Microtubule Network ◽  
Wide Range ◽  
Potential Risk Factors ◽  
Range Of Functions ◽  
Potential Drug Targets

Background & Objective: Neurodegenrative diseases are among the most widespread lifethreatening disorders around the world in elderly ages. The common feature of a group of neurodegenerative disorders, called tauopathies, is an accumulation of microtubule associated protein tau inside the neurons. The exact mechanism underlying tauopathies is not well-understood but several factors such as traumatic brain injuries and genetics are considered as potential risk factors. Although tau protein is well-known for its key role in stabilizing and organization of axonal microtubule network, it bears a broad range of functions including DNA protection and participation in signaling pathways. Moreover, the flexible unfolded structure of tau facilitates modification of tau by a wide range of intracellular enzymes which in turn broadens tau function and interaction spectrum. The distinctive properties of tau protein concomitant with the crucial role of tau interaction partners in the progression of neurodegeneration suggest tau and its binding partners as potential drug targets for the treatment of neurodegenerative diseases. Conclusion: This review aims to give a detailed description of structure, functions and interactions of tau protein in order to provide insight into potential therapeutic targets for treatment of tauopathies.

An in vitro study of the role of docosahexaenoic acid in human tau protein aggregation

2016 ◽  
Vol 35 (14) ◽  
pp. 3176-3181
Author(s):  
Elham Sadat Mostafavi ◽  
Mohammad Ali Nasiri Khalili ◽  
Sirus Khodadadi ◽  
Gholam Hossein Riazi
Keyword(s):  
Docosahexaenoic Acid ◽  
Protein Aggregation ◽  
Tau Protein ◽  
In Vitro Study ◽  
Vitro Study

scholarly journals Anti-Aβ antibodies bound to neuritic plaques enhance microglia activity and mitigate tau pathology

2020 ◽  
Vol 8 (1) ◽  
Author(s):  
Vanessa Laversenne ◽  
Sameer Nazeeruddin ◽  
Emma C. Källstig ◽  
Philippe Colin ◽  
Christel Voize ◽  
...  
Keyword(s):  
Mouse Model ◽  
Tau Protein ◽  
Hippocampal Formation ◽  
Dystrophic Neurites ◽  
Neuritic Plaques ◽  
Tau Pathology ◽  
Continuous Administration ◽  
Plaque Deposition ◽  
5Xfad Mice

AbstractThe brain pathology of Alzheimer’s disease (AD) is characterized by the misfolding and aggregation of both the amyloid beta (Aβ) peptide and hyperphosphorylated forms of the tau protein. Initial Aβ deposition is considered to trigger a sequence of deleterious events contributing to tau pathology, neuroinflammation and ultimately causing the loss of synapses and neurons. To assess the effect of anti-Aβ immunization in this context, we generated a mouse model by overexpressing the human tau protein in the hippocampus of 5xFAD mice. Aβ plaque deposition combined with human tau overexpression leads to an array of pathological manifestations including the formation of tau-positive dystrophic neurites and accumulation of hyperphosphorylated tau at the level of neuritic plaques. Remarkably, the presence of human tau reduces microglial clustering in proximity to the Aβ plaques, which may affect the barrier role of microglia. In this mouse model, continuous administration of anti-Aβ antibodies enhances the clustering of microglial cells even in the presence of tau. Anti-Aβ immunization increases plaque compaction, reduces the spread of tau in the hippocampal formation and prevents the formation of tau-positive dystrophic neurites. However, the treatment does not significantly reduce tau-induced neurodegeneration in the dentate gyrus. These results highlight that anti-Aβ immunization is able to enhance microglial activity around neuritic plaques, mitigating part of the tau-induced pathological manifestations.

scholarly journals Liquid–liquid phase separation of tau protein: The crucial role of electrostatic interactions

2019 ◽  
Vol 294 (29) ◽  
pp. 11054-11059 ◽  
Author(s):  
Solomiia Boyko ◽  
Xu Qi ◽  
Tien-Hao Chen ◽  
Krystyna Surewicz ◽  
Witold K. Surewicz
Keyword(s):  
Phase Separation ◽  
Liquid Phase ◽  
Tau Protein ◽  
Crucial Role ◽  
Electrostatic Interactions ◽  
Liquid Phase Separation ◽  
Liquid Liquid Phase Separation

scholarly journals Alzheimer´s Disease in the Perspective of Neuroimmunology

2018 ◽  
Vol 12 (1) ◽  
pp. 50-56 ◽  
Author(s):  
Ricardo B. Maccioni ◽  
Andrea González ◽  
Víctor Andrade ◽  
Nicole Cortés ◽  
José Pablo Tapia ◽  
...  
Keyword(s):  
Cognitive Impairment ◽  
Tau Protein ◽  
Microglial Activation ◽  
Neurodegenerative Disorder ◽  
Vicious Cycle ◽  
Considerable Research ◽  
Dopaminergic Pathway ◽  
The World ◽  
Main Culprit

Background:Alzheimer’s Disease (AD) is a severe neurodegenerative disorder that includes the occurrence of behavioral disorders as well as memory and cognitive impairment as major symptoms. AD affects around 12% of the aged population in the world. Considerable research efforts have pointed to the role of innate immunity as the main culprit in the pathogenesis of AD. In this context, and according to with our neuroimmunomodulation theory, microglial activation modifies the cross-talks between microglia and neurons. We postulated that glial activation triggered by “damage signals” activates a pathological molecular cascade that finally leads to hyperphosphorylation and oligomerization of the tau protein. Interestingly, these modifications correlate with the gradual cognitive impairment of patients with the AD. Microglial activation is determined by the nature and strength of the stimulus. In the AD, a continuous activation state of microglia appears to generate neuronal injury and neurodegeneration, producing the outflow of pathological tau from the inner of neurons to the extraneuronal space. Released tau, together with the contribution of ApoE4 protein, would then produce reactivation of microglia, thus inducing a positive feedback that stimulates the vicious cycle in neurodegeneration.Conclusion:Nevertheless, from the pathophysiological perspective AD is significantly more than a loss of memory. In the initial stages of AD pathogenesis, variations in the dopaminergic pathway along with serotonin diminution play an important role. This may explain why depression is associated with the onset of AD. All these pathophysiological events take place together with immunomodulatory changes that trigger tau oligomerization in the course of neurofibrillary tangles formation. Interestingly, mood disorders appear to be followed by neuroinflammatory processes and structural/functional alterations that lead to cognitive impairment in the context of AD.

Role of tau protein in Alzheimer's disease: The prime pathological player

2020 ◽  
Vol 163 ◽  
pp. 1599-1617 ◽  
Author(s):  
Shibi Muralidar ◽  
Senthil Visaga Ambi ◽  
Saravanan Sekaran ◽  
Diraviyam Thirumalai ◽  
Balamurugan Palaniappan
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Tau Protein

Possible Role of Each Repeat Structure of the Microtubule-Binding Domain of the Tau Protein in In Vitro Aggregation

2005 ◽  
Vol 138 (4) ◽  
pp. 413-423 ◽  
Author(s):  
Koji Tomoo ◽  
Tian-Ming Yao ◽  
Katsuhiko Minoura ◽  
Shuko Hiraoka ◽  
Miho Sumida ◽  
...  
Keyword(s):  
Tau Protein ◽  
Binding Domain ◽  
Microtubule Binding ◽  
Repeat Structure ◽  
Microtubule Binding Domain
Sign in / Sign up

Export Citation Format

Share Document