Formic acid is essential for immunohistochemical detection of aggregated intraneuronal Aβ peptides in mouse models of Alzheimer's disease
Open accessAbstract
The staining protocols so far applied to study intracellular Abeta accumulation in human tissue have been inconsistent with varying use of heat and formic acid (FA) for antigen retrieval. Microwave heat treatment has been reported to enhance the staining of intraneuronal Abeta as compared to no or enzymatic pretreatment. FA is widely used to increase the staining of plaque pathology in AD, yet the effect of FA on intraneuronal Abeta staining has been reported to be low and similar to the effect of heat or even to counteract the enhancing effect of heat pretreatment on intraneuronal Abeta immunohistochemical detection. To overcome these inconsistencies, there is a need for optimization of the staining protocol for intraneuronal Abeta detection and more knowledge is required concerning the effects of the different antigen retrieval methods. In the present work, we optimized the staining protocol for intraneuronal Abeta in paraffin-embedded sections in relation to heat and FA using four different mouse models known to accumulate intraneuronal Abeta peptides. It was found that FA is essential for the staining of highly aggregated intraneuronal Abeta peptides in AD transgenic mouse tissue.
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Postmortem interval, pre-treatments, counter-stains, fixation and post-fixation, detergent, and blocking solutions can influence interpretation of immuno-histochemistry, and also that of intraneuronal Aβ.
“Postmortem interval, pre-treatments, counter-stains, fixation and post-fixation, detergent, and blocking solutions, all can influence interpretation of immuno-histochemistry, and also that of intraneuronal Aβ [34, 39].”
From Intraneuronal β-amyloid accumulation and synapse pathology in Alzheimer’s disease (2010) · cites this paper as [34]
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Additional file 6 of LILRB2-mediated TREM2 signaling inhibition suppresses microglia functions
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Additional file 5 of LILRB2-mediated TREM2 signaling inhibition suppresses microglia functions
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Additional file 3 of LILRB2-mediated TREM2 signaling inhibition suppresses microglia functions
Zhao, P., Xu, Y., Jiang, L.-L., Fan, X., Ku, Z., Li, L., Liu, X., Deng, M., Arase, H., Zhu, J.-J., et al. (2022) · Figshare · doi:10.6084/m9.figshare.20098691
Additional file 2 of LILRB2-mediated TREM2 signaling inhibition suppresses microglia functions
Zhao, P., Xu, Y., Jiang, L.-L., Fan, X., Ku, Z., Li, L., Liu, X., Deng, M., Arase, H., Zhu, J.-J., et al. (2022) · Figshare · doi:10.6084/m9.figshare.20098688
Additional file 4 of LILRB2-mediated TREM2 signaling inhibition suppresses microglia functions
Zhao, P., Xu, Y., Jiang, L.-L., Fan, X., Ku, Z., Li, L., Liu, X., Deng, M., Arase, H., Zhu, J.-J., et al. (2022) · Figshare · doi:10.6084/m9.figshare.20098694
Additional file 10 of LILRB2-mediated TREM2 signaling inhibition suppresses microglia functions
Zhao, P., Xu, Y., Jiang, L.-L., Fan, X., Ku, Z., Li, L., Liu, X., Deng, M., Arase, H., Zhu, J.-J., et al. (2022) · Figshare · doi:10.6084/m9.figshare.20098679
Additional file 1 of LILRB2-mediated TREM2 signaling inhibition suppresses microglia functions
Zhao, P., Xu, Y., Jiang, L.-L., Fan, X., Ku, Z., Li, L., Liu, X., Deng, M., Arase, H., Zhu, J.-J., et al. (2022) · Figshare · doi:10.6084/m9.figshare.20098685
Additional file 8 of LILRB2-mediated TREM2 signaling inhibition suppresses microglia functions
Zhao, P., Xu, Y., Jiang, L.-L., Fan, X., Ku, Z., Li, L., Liu, X., Deng, M., Arase, H., Zhu, J.-J., et al. (2022) · Figshare · doi:10.6084/m9.figshare.20098706
Additional file 7 of LILRB2-mediated TREM2 signaling inhibition suppresses microglia functions
Zhao, P., Xu, Y., Jiang, L.-L., Fan, X., Ku, Z., Li, L., Liu, X., Deng, M., Arase, H., Zhu, J.-J., et al. (2022) · Figshare · doi:10.6084/m9.figshare.20098703
Additional file 9 of LILRB2-mediated TREM2 signaling inhibition suppresses microglia functions
Zhao, P., Xu, Y., Jiang, L.-L., Fan, X., Ku, Z., Li, L., Liu, X., Deng, M., Arase, H., Zhu, J.-J., et al. (2022) · Figshare · doi:10.6084/m9.figshare.20098712
Additional file 11 of LILRB2-mediated TREM2 signaling inhibition suppresses microglia functions
Zhao, P., Xu, Y., Jiang, L.-L., Fan, X., Ku, Z., Li, L., Liu, X., Deng, M., Arase, H., Zhu, J.-J., et al. (2022) · Figshare · doi:10.6084/m9.figshare.20098682
- Authors
- Christensen, D. Z., Bayer, T. A., & Wirths, O.
- Affiliations
- University of Göttingen (DE)
- Corresponding author
- Wirths, Oliver
- Venue
- Brain Research
- Publisher
- Elsevier BV
- Published
- 2009-11
- Volume
- 1301
- Pages
- 116-125
- ISSN
- 0006-8993 (ISSN-L)
- OpenAlex
- W2001167489
- Cited by
- 47
- References
- 51
- Citations by year
- 2025: 4 · 2024: 1 · 2023: 1 · 2022: 13 · 2021: 2 · 2020: 2 · 2019: 3 · 2017: 5 · 2016: 2 · 2015: 3 · 2014: 1 · 2013: 3 · 2012: 2
- FWCI
- 1.55
- Type
- journal article
- Language
- en
- Open access
- Licence
- Locations
- Brain Research (publishedVersion)
- PubMed (publishedVersion)
- GoeScholar The Publication Server of the Georg-August-Universität Göttingen (Georg-August-Universität Göttingen) (submittedVersion, other-oa)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- formic acid, intraneuronal amyloid-beta, Alzheimer's disease, antigen retrieval, thermal pretreatment, paraffin sections, transgenic mouse model, amyloid-beta aggregation
- MeSH terms
- Alzheimer Disease, Analysis of Variance, Animals, Cell Count, Cerebral Cortex, Formates, Image Processing, Computer-Assisted, Immunohistochemistry, Mice, Transgenic, Microscopy, Fluorescence, Neurons, Staining and Labeling, Thalamus, Amyloid beta-Peptides, Amyloid beta-Protein Precursor, Paraffin Embedding, Tissue Fixation, Mice, CA1 Region, Hippocampal
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