scholarly journals Luminex-based quantification of Alzheimer’s disease neuropathologic change in formalin-fixed post-mortem human brain tissue

2018 ◽  
Vol 99 (7) ◽  
pp. 1056-1067
Author(s):  
C. Dirk Keene ◽  
Angela M. Wilson ◽  
Mitchell D. Kilgore ◽  
Lauren T. Bruner ◽  
Nadia O. Postupna ◽  
...  
The Analyst ◽  
2020 ◽  
Vol 145 (5) ◽  
pp. 1724-1736 ◽  
Author(s):  
Benjamin Lochocki ◽  
Tjado H. J. Morrema ◽  
Freek Ariese ◽  
Jeroen J. M. Hoozemans ◽  
Johannes F. de Boer

Raman spectroscopy was used to examine unstained, formalin fixed Alzheimer's disease human brain tissue to potentially identify a unique spectral signature of amyloid-beta plaques.


1993 ◽  
Vol 13 (6) ◽  
pp. 2540-2550 ◽  
Author(s):  
KA Crutcher ◽  
SA Scott ◽  
S Liang ◽  
WV Everson ◽  
J Weingartner

NeuroImage ◽  
2020 ◽  
Vol 210 ◽  
pp. 116523 ◽  
Author(s):  
Mareike Töpperwien ◽  
Franziska van der Meer ◽  
Christine Stadelmann ◽  
Tim Salditt

1997 ◽  
Vol 16 (9) ◽  
pp. 512-515 ◽  
Author(s):  
F. Martin ◽  
FM Corrigan ◽  
Ofx Donard ◽  
J. Kelly ◽  
Jao Besson ◽  
...  

As blood tin concentrations are elevated in Alzheimer's disease and as some low molecular weight organotin compounds are neurotoxic, we have attempted to detect organotins in brain in Alzheimer's Disease. First we measured the concentration of trimethyltin (TMT) in the brains of rats which had been exposed to memory- impairing concentrations of TMT and, as the method of linking hydride generation, cryogenic trapping, gas chromatographic separation and atomic absorption spec trophotometric detection permitted the measurements of organotin compounds when the total tin was greater than 0.2 nanograms, we applied these techniques to human brain tissue, some of which showed neuropathological evidence of Alzheimer's Disease. No low molecular weight organotin compounds were detected in the human brain tissue, but it is possible that tin may be complexed with large organic molecules, the hydrides of which would not be volatile, but which could be identified by liquid chromatography.


Methods ◽  
2010 ◽  
Vol 52 (4) ◽  
pp. 359-366 ◽  
Author(s):  
Chun-Qing Liu ◽  
Ling Shan ◽  
Rawien Balesar ◽  
Sabina Luchetti ◽  
Joop J. Van Heerikhuize ◽  
...  

2021 ◽  
Vol 4 (1) ◽  
Author(s):  
Benjamin Lochocki ◽  
Baayla D. C. Boon ◽  
Sander R. Verheul ◽  
Liron Zada ◽  
Jeroen J. M. Hoozemans ◽  
...  

AbstractAlzheimer’s disease (AD) neuropathology is characterized by hyperphosphorylated tau containing neurofibrillary tangles and amyloid-beta (Aβ) plaques. Normally these hallmarks are studied by (immuno-) histological techniques requiring chemical pretreatment and indirect labelling. Label-free imaging enables one to visualize normal tissue and pathology in its native form. Therefore, these techniques could contribute to a better understanding of the disease. Here, we present a comprehensive study of high-resolution fluorescence imaging (before and after staining) and spectroscopic modalities (Raman mapping under pre-resonance conditions and stimulated Raman scattering (SRS)) of amyloid deposits in snap-frozen AD human brain tissue. We performed fluorescence and spectroscopic imaging and subsequent thioflavin-S staining of the same tissue slices to provide direct confirmation of plaque location and correlation of spectroscopic biomarkers with plaque morphology; differences were observed between cored and fibrillar plaques. The SRS results showed a protein peak shift towards the β-sheet structure in cored amyloid deposits. In the Raman maps recorded with 532 nm excitation we identified the presence of carotenoids as a unique marker to differentiate between a cored amyloid plaque area versus a non-plaque area without prior knowledge of their location. The observed presence of carotenoids suggests a distinct neuroinflammatory response to misfolded protein accumulations.


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