Cited by 254Advanced Glycation End Products researchAlzheimer's disease research and treatmentsDementia and Cognitive Impairment Research

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Immunohistochemical distribution of the receptor for advanced glycation end products in neurons and astrocytes in Alzheimer’s disease

Sasaki, Nobuyuki, Toki, Sadamu, Chowei, Hiroshi, Saito, Toshikazu, Nakano, Norihito, Hayashi, Yorihide, Takeuchi, Masayoshi, Makita, Zenji·2001·Brain Research

DOI 10.1016/s0006-8993(00)03075-4

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Abstract

Advanced glycation end products (AGE) and the receptor for AGE (RAGE) have been implicated in the chronic complications of diabetes mellitus (DM), and have been reported to play an important role in the pathogenesis of Alzheimer's disease (AD). In this study, we established a polyclonal anti-RAGE antibody, and examined the immunohistochemical localization of amyloid beta protein (Abeta), AGE, and RAGE in neurons and astrocytes from patients with AD and DM. Our anti-RAGE antibody recognized full-length RAGE (50 kd) and N-terminal RAGE (35 kd) in human brain tissue. Abeta-, AGE-, and RAGE-positive granules were identified in the perikaryon of hippocampal neurons (especially from CA3 and CA4) in all subjects. The distribution and staining pattern of these immunopositive granules showed good concordance with each antibody. In AD, most astrocytes contained both AGE-and RAGE-positive granules and their distribution was almost the same. Abeta-positive granules were less common, but Abeta-, AGE-, and RAGE-positive granules were colocalized in one part of a single astrocyte. In DM patients and control cases, AGE-and RAGE-positive astrocytes were very rare. These finding support the hypothesis that glycated Abeta is taken up via RAGE and is degraded through the lysosomal pathway in astrocytes. In addition to the presence of AGE, the process of AGE degradation and receptor-mediated reactions may contribute to neuronal dysfunction and promote the progression of AD.

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Authors: Sasaki, N., Toki, S., Chowei, H., Saito, T., Nakano, N., Hayashi, Y., Takeuchi, M., & Makita, Z.
Affiliations: Sapporo Medical University (JP)
Hokuriku University (JP)
Kurume University (JP)
Corresponding author: Sasaki, Nobuyuki
Venue: Brain Research
Publisher: Elsevier BV
Published: 2001-01
Volume: 888
Issue: 2
Pages: 256-262
ISSN: 0006-8993 (ISSN-L)
DOI: 10.1016/s0006-8993(00)03075-4
OpenAlex: W2091657472
Cited by: 253
References: 29
Citations by year: 2026: 2 · 2025: 8 · 2024: 6 · 2023: 5 · 2022: 12 · 2021: 15 · 2020: 13 · 2019: 10 · 2018: 8 · 2017: 7 · 2016: 11 · 2015: 10 · 2014: 13 · 2013: 20 · 2012: 8
FWCI: 6.28
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
Locations: Brain Research (publishedVersion)
PubMed (publishedVersion)
Funders: Ministry of Education, Culture, Sports, Science and Technology
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Advanced Glycation End Products research
Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
Keywords: receptor for advanced glycation end products, advanced glycation end products, Alzheimer's disease, amyloid-beta, astrocytes, hippocampal neurons, diabetes mellitus, lysosomal degradation, colocalization, neuronal dysfunction
MeSH terms: Receptor for Advanced Glycation End Products, Aged, Alzheimer Disease, Animals, Antibody Specificity, Astrocytes, Cattle, Diabetes Mellitus, Female, Humans, Immunohistochemistry, Male, Middle Aged, Neurons, Receptors, Immunologic, Blotting, Western, Amyloid beta-Peptides, Glycation End Products, Advanced

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Immunohistochemical distribution of the receptor for advanced glycation end products in neurons and astrocytes in Alzheimer’s disease

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