scholarly journals Seed‐competent high‐molecular‐weight tau species accumulates in the cerebrospinal fluid of Alzheimer's disease mouse model and human patients

2016 ◽  
Vol 80 (3) ◽  
pp. 355-367 ◽  
Author(s):  
Shuko Takeda ◽  
Caitlin Commins ◽  
Sarah L. DeVos ◽  
Chloe K. Nobuhara ◽  
Susanne Wegmann ◽  
...  
2015 ◽  
Vol 11 (7S_Part_14) ◽  
pp. P644-P644
Author(s):  
Shuko Takeda ◽  
Caitlin Commins ◽  
Susanne Wegmann ◽  
Allyson D. Roe ◽  
Zhanyun Fan ◽  
...  

1986 ◽  
Vol 63 (2) ◽  
pp. 141-146 ◽  
Author(s):  
Adrian R. Pierotti ◽  
Anthony J. Harmar ◽  
James Simpson ◽  
Celia M. Yates

2021 ◽  
pp. 1-14
Author(s):  
Christiana Bjorkli ◽  
Claire Louet ◽  
Trude Helen Flo ◽  
Mary Hemler ◽  
Axel Sandvig ◽  
...  

Background: Preclinical models of Alzheimer’s disease (AD) can provide valuable insights into the onset and progression of the disease, such as changes in concentrations of amyloid-β (Aβ) and tau in cerebrospinal fluid (CSF). However, such models are currently underutilized due to limited advancement in techniques that allow for longitudinal CSF monitoring. Objective: An elegant way to understand the biochemical environment in the diseased brain is intracerebral microdialysis, a method that has until now been limited to short-term observations, or snapshots, of the brain microenvironment. Here we draw upon patient-based findings to characterize CSF biomarkers in a commonly used preclinical mouse model for AD. Methods: Our modified push-pull microdialysis method was first validated ex vivo with human CSF samples, and then in vivo in an AD mouse model, permitting assessment of dynamic changes of CSF Aβ and tau and allowing for better translational understanding of CSF biomarkers. Results: We demonstrate that CSF biomarker changes in preclinical models capture what is observed in the brain; with a decrease in CSF Aβ observed when plaques are deposited, and an increase in CSF tau once tau pathology is present in the brain parenchyma. We found that a high molecular weight cut-off membrane allowed for simultaneous sampling of Aβ and tau, comparable to CSF collection by lumbar puncture in patients. Conclusion: Our approach can further advance AD and other neurodegenerative research by following evolving neuropathology along the disease cascade via consecutive sampling from the same animal and can additionally be used to administer pharmaceutical compounds and assess their efficacy (Bjorkli, unpublished data).


1987 ◽  
Vol 145 (1) ◽  
pp. 241-248 ◽  
Author(s):  
William M. Pardridge ◽  
Harry V. Vinters ◽  
Bruce L. Miller ◽  
Wallace W. Tourtellotte ◽  
Jody B. Eisenberg ◽  
...  

PLoS ONE ◽  
2017 ◽  
Vol 12 (4) ◽  
pp. e0174630 ◽  
Author(s):  
Takashi Kasai ◽  
Masaki Kondo ◽  
Ryotaro Ishii ◽  
Akihiro Tanaka ◽  
Suzuka Ataka ◽  
...  

2019 ◽  
Vol 69 (2) ◽  
pp. 585-593 ◽  
Author(s):  
Sunkuk Kwon ◽  
Ines Moreno-Gonzalez ◽  
Kathleen Taylor-Presse ◽  
George Edwards III ◽  
Nazaret Gamez ◽  
...  

2011 ◽  
Vol 2011 ◽  
pp. 1-8 ◽  
Author(s):  
Susanne Aileen Funke

The diagnosis of probable Alzheimer's disease (AD) can be established premortem based on clinical criteria like neuropsychological tests. Post mortem, specific neuropathological changes like amyloid plaques define AD. However, the standard criteria based on medical history and mental status examinations do not take into account the long preclinical features of the disease, and a biomarker for improved diagnosis of AD is urgently needed. In a large number of studies, amyloid-β(Aβ) monomer concentrations in CSF of AD patients are consistently and significantly reduced when compared to healthy controls. Therefore, monomeric Aβin CSF was suggested to be a helpful biomarker for the diagnosis of preclinical AD. However, not the monomeric form, but Aβoligomers have been shown to be the toxic species in AD pathology, and their quantification and characterization could facilitate AD diagnosis and therapy monitoring. Here, we review the current status of assay development to reliably and routinely detect Aβoligomers and high-molecular-weight particles in CSF.


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