Astrocytes expressing hyperphosphorylated tau protein without glial fibrillary tangles in argyrophilic grain disease

1999 ◽  
Vol 98 (3) ◽  
pp. 251-256 ◽  
Author(s):  
G. Botez ◽  
A. Probst ◽  
S. Ipsen ◽  
M. Tolnay
Keyword(s):  
Tau Protein ◽  
Hyperphosphorylated Tau ◽  
Argyrophilic Grain Disease ◽  
Hyperphosphorylated Tau Protein ◽  
Glial Fibrillary Tangles ◽  
Argyrophilic Grain

Argyrophilic grain disease: widespread hyperphosphorylation of tau protein in limbic neurons

1997 ◽  
Vol 93 (5) ◽  
pp. 477-484 ◽  
Author(s):  
M. Tolnay ◽  
M. G. Spillantini ◽  
M. Goedert ◽  
J. Ulrich ◽  
D. Langui ◽  
...  
Keyword(s):  
Tau Protein ◽  
Argyrophilic Grain Disease ◽  
Argyrophilic Grain

scholarly journals Neuronal Deposition of Amyloid-β Oligomers and Hyperphosphorylated Tau Is Closely Connected with Cognitive Dysfunction in Aged Dogs

2021 ◽  
pp. 1-12
Author(s):  
Umma Habiba ◽  
Makiko Ozawa ◽  
James K. Chambers ◽  
Kazuyuki Uchida ◽  
Joseph Descallar ◽  
...  
Keyword(s):  
Cognitive Dysfunction ◽  
Tau Protein ◽  
Senile Plaques ◽  
Amyloid Β ◽  
Hyperphosphorylated Tau ◽  
Diffuse Type ◽  
Hippocampal Region ◽  
Immunofluorescence Analysis ◽  
Relevant Model ◽  
Hyperphosphorylated Tau Protein

Background: Canine cognitive dysfunction (CCD) is a progressive syndrome recognized in mature to aged dogs with a variety of neuropathological changes similar to human Alzheimer’s disease (AD), for which it is thought to be a good natural model. However, the presence of hyperphosphorylated tau protein (p-Tau) in dogs with CCD has only been demonstrated infrequently. Objective: The aim of the present study was to investigate the presence of p-Tau and amyloid-β oligomer (Aβo) in cerebral cortex and hippocampus of dogs with CCD, with focus on an epitope retrieval protocol to unmask p-Tau. Methods: Immunohistochemical and immunofluorescence analysis of the cortical and hippocampal regions of five CCD-affected and two nondemented aged dogs using 4G8 anti-Aβp, anti-Aβ 1 - 42 nanobody (PrioAD13) and AT8 anti-p-Tau (Ser202, Thr205) antibody were used to demonstrate the presence of Aβ plaques (Aβp) and Aβ 1 - 42 oligomers and p-Tau deposits, respectively. Results: The extracellular Aβ senile plaques were of the diffuse type which lack the dense core normally seen in human AD. While p-Tau deposits displayed a widespread pattern and closely resembled the typical human neuropathology, they did not co-localize with the Aβp. Of considerable interest, however, widespread intraneuronal deposition of Aβ 1 - 42 oligomers were exhibited in the frontal cortex and hippocampal region that co-localized with p-Tau. Conclusion: Taken together, these findings reveal further shared neuropathologic features of AD and CCD, supporting the case that aged dogs afflicted with CCD offer a relevant model for investigating human AD.

Pick's disease: hyperphosphorylated tau protein segregates to the somatoaxonal compartment

1996 ◽  
Vol 92 (6) ◽  
pp. 588-596 ◽  
Author(s):  
A. Probst ◽  
M. Tolnay ◽  
D. Langui ◽  
M. Goedert ◽  
M. G. Spillantini
Keyword(s):  
Tau Protein ◽  
Pick's Disease ◽  
Hyperphosphorylated Tau ◽  
Pick’S Disease ◽  
Hyperphosphorylated Tau Protein
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