Cited by 137Alzheimer's disease research and treatmentsNeuroinflammation and Neurodegeneration MechanismsDementia and Cognitive Impairment Research

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Overexpression of Monocyte Chemotactic Protein-1/CCL2 in β-Amyloid Precursor Protein Transgenic Mice Show Accelerated Diffuse β-Amyloid Deposition

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Yamamoto, Masaru, Horiba, Masahide, Buescher, James L., Huang, DeReng, Gendelman, Howard E., Ransohoff, Richard M., Ikezu, Tsuneya·2005·The American Journal of Pathology

DOI 10.1016/s0002-9440(10)62364-4PMC PMC1606401

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Abstract

Microglia accumulation at the site of amyloid plaques is a strong indication that microglia play a major role in Alzheimer's disease pathogenesis. However, how microglia affect amyloid-beta peptide (Abeta) deposition remains poorly understood. To address this question, we developed a novel bigenic mouse that overexpresses both amyloid precursor protein (APP) and monocyte chemotactic protein-1 (MCP-1; CCL2 in systematic nomenclature). CCL2 expression, driven by the glial fibrillary acidic protein promoter, induced mononuclear phagocyte (MP; monocyte-derived macrophage and microglial) accumulation in the brain. When APP/CCL2 transgenic mice were compared to APP mice, a fivefold increase in Abeta deposition was present despite increased MP accumulation around hippocampal and cortical amyloid plaques. Levels of full-length APP, its C-terminal fragment, and Abeta-degrading enzymes (insulin-degrading enzyme and neprilysin) in APP/CCL2 and APP mice were indistinguishable. Sodium dodecyl sulfate-insoluble Abeta (an indicator of fibrillar Abeta) was increased in APP/CCL2 mice at 5 months of age. Apolipoprotein E, which enhances Abeta deposition, was also increased (2.2-fold) in aged APP/CCL2 as compared to APP mice. We propose that although CCL2 stimulates MP accumulation, it increases Abeta deposition by reducing Abeta clearance through increased apolipoprotein E expression. Understanding the mechanisms underlying these events could be used to modulate microglial function in Alzheimer's disease and positively affect disease outcomes.

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Authors: Yamamoto, M., Horiba, M., Buescher, J. L., Huang, D., Gendelman, H. E., Ransohoff, R. M., & Ikezu, T.
Affiliations: University of Nebraska Medical Center (US)
Cleveland Clinic (US)
Corresponding author: Ikezu, Tsuneya
ORCID: Gendelman, Howard E.
Ikezu, Tsuneya
Venue: The American Journal of Pathology
Publisher: Elsevier BV
Published: 2005-05
Volume: 166
Issue: 5
Pages: 1475-1485
ISSN: 0002-9440 (ISSN-L)
DOI: 10.1016/s0002-9440(10)62364-4
PMC: PMC1606401
OpenAlex: W2053953952
Cited by: 137
References: 62
Citations by year: 2026: 3 · 2025: 5 · 2024: 6 · 2023: 3 · 2022: 6 · 2021: 5 · 2020: 6 · 2019: 5 · 2018: 4 · 2017: 4 · 2016: 3 · 2015: 3 · 2014: 10 · 2013: 13 · 2012: 8
FWCI: 5.42
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
Locations: American Journal Of Pathology (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health (RO1 NS32151, 2 R37 NS36126, P01 NS043985)
University of Nebraska Medical Center
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: MCP-1, amyloid precursor protein, amyloid-beta deposition, Alzheimer's disease, microglia, mononuclear phagocytes, macrophages, apolipoprotein E, amyloid plaques, fibrillar amyloid-beta, insulin-degrading enzyme, neprilysin, glial fibrillary acidic protein promoter
MeSH terms: Animals, Brain, Cerebral Cortex, Female, Hippocampus, Male, Mice, Transgenic, Phagocytes, Tissue Distribution, Amyloid beta-Peptides, Amyloid beta-Protein Precursor, Chemokine CCL2, Mice

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Overexpression of Monocyte Chemotactic Protein-1/CCL2 in β-Amyloid Precursor Protein Transgenic Mice Show Accelerated Diffuse β-Amyloid Deposition

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