[P3-449]: THE CONTRIBUTION OF HYPERPHOSPHORYLATED-TAU PATHOLOGY TO NEUROPSYCHIATRIC SYMPTOMS IN ALZHEIMER's DISEASE

2017 ◽  
Vol 13 (7S_Part_23) ◽  
pp. P1142-P1144
Author(s):  
Alexander J. Ehrenberg ◽  
Claudia K. Suemoto ◽  
Cathrine Petersen ◽  
Joel H. Kramer ◽  
Rana April Eser ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Neuropsychiatric Symptoms ◽  
Hyperphosphorylated Tau ◽  
Tau Pathology

scholarly journals Alzheimer’s disease brain contains tau fractions with differential prion-like activities

2021 ◽  
Vol 9 (1) ◽  
Author(s):  
Longfei Li ◽  
Ruirui Shi ◽  
Jianlan Gu ◽  
Yunn Chyn Tung ◽  
Yan Zhou ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Cultured Cells ◽  
Regional Distribution ◽  
Proteinase K ◽  
Hyperphosphorylated Tau ◽  
Terminal Portion ◽  
Tau Pathology ◽  
Heat Stable ◽  
Tau Aggregation

AbstractNeurofibrillary tangles (NFTs) made of abnormally hyperphosphorylated tau are a hallmark of Alzheimer’s disease (AD) and related tauopathies. Regional distribution of NFTs is associated with the progression of the disease and has been proposed to be a result of prion-like propagation of misfolded tau. Tau in AD brain is heterogenous and presents in various forms. In the present study, we prepared different tau fractions by sedimentation combined with sarkosyl solubility from AD brains and analyzed their biochemical and pathological properties. We found that tau in oligomeric fraction (O-tau), sarkosyl-insoluble fractions 1 and 2 (SI1-tau and SI2-tau) and monomeric heat-stable fraction (HS-tau) showed differences in truncation, hyperphosphorylation, and resistance to proteinase K. O-tau, SI1-tau, and SI2-tau, but not HS-tau, were hyperphosphorylated at multiple sites and contained SDS- and β-mercaptoethanol–resistant high molecular weight aggregates, which lacked the N-terminal portion of tau. O-tau and SI2-tau displayed more truncation and less hyperphosphorylation than SI1-tau. Resistance to proteinase K was increased from O-tau to SI1-tau to SI2-tau. O-tau and SI1-tau, but not SI2-tau or HS-tau, captured tau from cell lysates and seeded tau aggregation in cultured cells. Heat treatment could not kill the prion-like activity of O-tau to capture normal tau. Hippocampal injection of O-tau into 18-month-old FVB mice induced significant tau aggregation in both ipsilateral and contralateral hippocampi, but SI1-tau only induced tau pathology in the ipsilateral hippocampus, and SI2-tau and HS-tau failed to induce any detectable tau aggregation. These findings suggest that O-tau and SI1-tau have prion-like activities and may serve as seeds to recruit tau and template tau to aggregate, resulting in the propagation of tau pathology. Heterogeneity of tau pathology within AD brain results in different fractions with different biological and prion-like properties, which may pose a major challenge in targeting tau for development of effective therapeutic treatments.

scholarly journals The impact of concomitant LATE‐NC on hyperphosphorylated tau pathology and cognitive decline in Alzheimer’s disease

2020 ◽  
Vol 16 (S2) ◽  
Author(s):  
Lauren Walker ◽  
Kirsty E. McAleese ◽  
Daniel Erskine ◽  
Johannes Attems
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Cognitive Decline ◽  
Hyperphosphorylated Tau ◽  
Tau Pathology ◽  
The Impact

scholarly journals Association between regional tau pathology and neuropsychiatric symptoms in aging and dementia due to Alzheimer's disease

2021 ◽  
Vol 7 (1) ◽  
Author(s):  
Cécile Tissot ◽  
Joseph Therriault ◽  
Tharick A. Pascoal ◽  
Mira Chamoun ◽  
Firoza Z. Lussier ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Neuropsychiatric Symptoms ◽  
Tau Pathology

P1-319: THE ROLE OF CORTICAL HYPERPHOSPHORYLATED TAU PATHOLOGY IN THE PATHOGENESIS OF WHITE MATTER LESIONS IN ALZHEIMER'S DISEASE

2014 ◽  
Vol 10 ◽  
pp. P428-P429
Author(s):  
Kirsty Elizabeth McAleese ◽  
Madhurima Dey ◽  
Michael Firbank ◽  
Shane McParland ◽  
John T. O'Brien ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
White Matter ◽  
White Matter Lesions ◽  
Hyperphosphorylated Tau ◽  
Tau Pathology

Amelioration of Tau Pathology by Anle138b Rescues Neuronal Function in a Mouse Model of Human Alzheimer's Disease Tau

2019 ◽  
Author(s):  
M Deussing ◽  
T Blume ◽  
L Kaiser ◽  
F Probst ◽  
F Overhoff ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Mouse Model ◽  
Neuronal Function ◽  
Tau Pathology
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