Trichostatin A ameliorates Alzheimer’s disease-related pathology and cognitive deficits by increasing albumin expression and Aβ clearance in APP/PS1 mice

Su, Qiang; Li, Tian; He, Pei-Feng; Lu, Xue-Chun; Yu, Qi; Gao, Qi-Chao; Wang, Zhao-Jun; Wu, Mei-Na; Yang, Dan; Qi, Jin-Shun

doi:10.1186/s13195-020-00746-8

Cited by 77Alzheimer's disease research and treatmentsNeuroinflammation and Neurodegeneration MechanismsDementia and Cognitive Impairment Research

The DOI matches its Crossref record; 67 of the 67 references it cites were found in a registry or an index.

Trichostatin A ameliorates Alzheimer’s disease-related pathology and cognitive deficits by increasing albumin expression and Aβ clearance in APP/PS1 mice

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Su, Qiang, Li, Tian, He, Pei-Feng, Lu, Xue-Chun, Yu, Qi, Gao, Qi-Chao, Wang, Zhao-Jun, Wu, Mei-Na, Yang, Dan, Qi, Jin-Shun·2021·Alzheimer's Research & Therapy

DOI 10.1186/s13195-020-00746-8PMC PMC7784383

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Abstract

BACKGROUND: Alzheimer's disease (AD) is an intractable neurodegenerative disorder in the elderly population, currently lacking a cure. Trichostatin A (TSA), a histone deacetylase inhibitor, showed some neuroprotective roles, but its pathology-improvement effects in AD are still uncertain, and the underlying mechanisms remain to be elucidated. The present study aims to examine the anti-AD effects of TSA, particularly investigating its underlying cellular and molecular mechanisms. METHODS: Novel object recognition and Morris water maze tests were used to evaluate the memory-ameliorating effects of TSA in APP/PS1 transgenic mice. Immunofluorescence, Western blotting, Simoa assay, and transmission electron microscopy were utilized to examine the pathology-improvement effects of TSA. Microglial activity was assessed by Western blotting and transwell migration assay. Protein-protein interactions were analyzed by co-immunoprecipitation and LC-MS/MS. RESULTS: TSA treatment not only reduced amyloid β (Aβ) plaques and soluble Aβ oligomers in the brain, but also effectively improved learning and memory behaviors of APP/PS1 mice. In vitro study suggested that the improvement of Aβ pathology by TSA was attributed to the enhancement of Aβ clearance, mainly by the phagocytosis of microglia, and the endocytosis and transport of microvascular endothelial cells. Notably, a meaningful discovery in the study was that TSA dramatically upregulated the expression level of albumin in cell culture, by which TSA inhibited Aβ aggregation and promoted the phagocytosis of Aβ oligomers. CONCLUSIONS: These findings provide a new insight into the pathogenesis of AD and suggest TSA as a novel promising candidate for the AD treatment.

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ITSA-1 counteracts the activity of TSA, a potent inhibitor of class I and II HDACs, on histone acetylation and transcriptional activation.
“ITSA-1 is an activator of HDACs and counteracts the activity of TSA, a potent inhibitor of class I and II HDACs, on histone acetylation and transcriptional activation [48–50].”
From CI-994 is a dual modulator of class I HDACs and Wnt/β-catenin signaling for the treatment of Alzheimer's disease (2026) · cites this paper as [49]
The Results report that ITSA-1 suppressed TSA-induced histone H4 acetylation in BV2 cells and reversed TSA-induced albumin expression in endothelial cells. The Background identifies TSA as an HDAC inhibitor. Our copy does not establish that ITSA-1 activates HDACs, that TSA specifically inhibits class I and II HDACs, or that ITSA-1 counteracts transcriptional activation generally. (LLM, conf=0.85)
Experimental — accuracy not yet measured
ITSA-1 is an activator of HDACs.
“ITSA-1 is an activator of HDACs and counteracts the activity of TSA, a potent inhibitor of class I and II HDACs, on histone acetylation and transcriptional activation [48–50].”
From CI-994 is a dual modulator of class I HDACs and Wnt/β-catenin signaling for the treatment of Alzheimer's disease (2026) · cites this paper as [49]
The Results section describes ITSA-1 as a specific inhibitor of TSA and reports that it reversed TSA-induced albumin expression and suppressed other TSA-induced effects. It does not say that ITSA-1 activates HDACs; counteracting TSA is not, by itself, evidence of HDAC activation (no page number provided). (LLM, conf=0.72)
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Additional file 1 of Histone deacetylase inhibitors VPA and WT161 ameliorate the pathological features and cognitive impairments of the APP/PS1 Alzheimer’s disease mouse model by regulating the expression of APP secretases
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Additional file 1 of Trichostatin A ameliorates Alzheimer’s disease-related pathology and cognitive deficits by increasing albumin expression and Aβ clearance in APP/PS1 mice
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Authors: Su, Q., Li, T., He, P.-F., Lu, X.-C., Yu, Q., Gao, Q.-C., Wang, Z.-J., Wu, M.-N., Yang, D., & Qi, J.-S.
Affiliations: Shanxi Medical University (CN)
Corresponding author: He, Pei-Feng
Qi, Jin-Shun
ORCID: Su, Qiang
Li, Tian
He, Pei-Feng
Yu, Qi
Wang, Zhao-Jun
Qi, Jin-Shun
Venue: Alzheimer's Research & Therapy
Publisher: Springer Science and Business Media LLC
Published: 2021-01-04
Volume: 13
Issue: 1
Pages: 7-7
ISSN: 1758-9193 (ISSN-L)
DOI: 10.1186/s13195-020-00746-8
PMC: PMC7784383
OpenAlex: W3119600274
Cited by: 75
References: 67
Citations by year: 2026: 10 · 2025: 24 · 2024: 21 · 2023: 8 · 2022: 8 · 2021: 4
FWCI: 6.76
Type: journal article
Language: en
Open access: gold
doi.org
Licence: cc-by
creativecommons.org/licenses/by/4.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor)
Locations: Alzheimer s Research & Therapy (publishedVersion, cc-by)
PubMed Central (publishedVersion, cc-by)
PubMed (publishedVersion)
DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
Funders: National Natural Science Foundation of China (31471080)
Shanxi “1331 Project” Key Subjects Construction
Fund Program for “Sanjin Scholars” of Shanxi Province
Shanxi Province Science Foundation for Excellent Young Scholars (201801D211005)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › 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: trichostatin A, Alzheimer's disease, histone deacetylase inhibitors, amyloid-beta clearance, albumin, microglial phagocytosis, amyloid-beta oligomers, APP/PS1 mice, cognitive impairment, memory impairment, microvascular endothelial cells, amyloid-beta aggregation, neuroprotection
MeSH terms: Aged, Albumins, Alzheimer Disease, Animals, Chromatography, Liquid, Cognition, Disease Models, Animal, Humans, Hydroxamic Acids, Mice, Transgenic, Amyloid beta-Peptides, Amyloid beta-Protein Precursor, Endothelial Cells, Mice, Tandem Mass Spectrometry, Presenilin-1

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Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

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Trichostatin A ameliorates Alzheimer’s disease-related pathology and cognitive deficits by increasing albumin expression and Aβ clearance in APP/PS1 mice

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