Advanced glycation end products (AGE) and their receptor (RAGE) in the brain of patients with Creutzfeldt-Jakob disease with prion plaques.

Sasaki, Nobuyuki; Takeuchi, Masayoshi; Chowei, Hiroshi; Kikuchi, Seiji; Hayashi, Yorihide; Nakano, Norihito; Ikeda, Hiroshi; Yamagishi, Sho Ichi; Kitamoto, Tetsuyuki; Saito, Toshikazu; Makita, Zenji

doi:10.1016/s0304-3940(02)00310-5

Cited by 98 publications

(50 citation statements)

References 14 publications

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“…While multiple overlapping mechanisms probably play a role in IAPP toxicity (17,39), this work demonstrates that RAGE-mediated processes clearly contribute to and may be one of the pivotal initiating events for many of the downstream cellular pathways associated with h-IAPP toxicity. Our findings are consistent with the hypothesis that many amyloidogenic proteins invoke common mechanisms of cytotoxicity (56) and provide a foundation and blueprint for defining distinct, toxic RAGE-binding entities in other amyloidosis diseases for which RAGE has been postulated to impart pathogenic consequences (57)(58)(59)(60)(61).…”

Section: Discussionsupporting

confidence: 86%

RAGE binds preamyloid IAPP intermediates and mediates pancreatic β cell proteotoxicity

Abedini

Cao

Plesner

et al. 2018

Journal of Clinical Investigation

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Section: Discussionsupporting

confidence: 86%

RAGE binds preamyloid IAPP intermediates and mediates pancreatic β cell proteotoxicity

Abedini

Cao

Plesner

et al. 2018

Journal of Clinical Investigation

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“…The accumulation of AGEs has been reported to be more apparent in the elderly and those with diabetic complications, arteriosclerotic diseases and Alzheimer's disease (1,2). Numerous studies have revealed the association of AGEs with neurodegenerative diseases (3)(4)(5), the growth and metastasis of malignant tumors (6) and inflammatory reactions. In the process of generating AGEs, Amadori rearrangement-induced compounds generate 3-deoxyglucosone (3-DG) (7).…”

Section: Introductionmentioning

confidence: 99%

Effect of natural flavonoids, stilbenes and caffeic acid oligomers on protein glycation

2014

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Abstract. The aim of the present study was to identify the inhibitory activity of natural flavonoids, stilbenes and caffeic acid oligomers on protein glycation. Antioxidant activity was evaluated using 1,1-diphenyl-2-picrylhydrazyl radical-scavenging activity. The production of 3-deoxyglucosone (3-DG) and advanced glycation end products (AGEs) by glycation reactions were determined by high-performance liquid chromatography and fluorescence, respectively. Certain flavonoids, stilbenes and caffeic acid oligomers prevented AGE production and the IC 50 values of the compounds were compared. These examined compounds are assumed to suppress AGE generation by inhibiting the increase in 3-DG production through a specific unknown mechanism in the early phase of the Maillard reaction, by inhibiting the generation of active oxygen in the later phase and by suppressing the progression of the reaction. Regular, daily consumption of these compounds in the form of a food or extract is expected to aid in the prevention or inhibition of non-enzymatic amino acid glycation in the living body, which is possibly associated with aging, diabetic complications, arteriosclerotic diseases and Alzheimer's disease, and they may also be effective agents in cosmetics promoting anti-aging.

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“…Amyloid plaques modified by AGE have been identified in brain tissue of Alzheimer's disease patients (22) and transmissible spongiform encephalopathy patients (23) and in the islets of Langerhans of diabetic patients (24). Furthermore, amyloid protein deposits as well as AGE are identified in plaques associated with dialysis-related amyloidosis, atherosclerosis, and vascular occlusions in patients suffering from diabetes (12,(25)(26)(27).…”

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confidence: 99%

Glycation Induces Formation of Amyloid Cross-β Structure in Albumin

Bouma¹,

Kroon-Batenburg²,

Wu³

et al. 2003

Journal of Biological Chemistry

264

177

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Amyloid fibrils are components of proteinaceous plaques that are associated with conformational diseases such as Alzheimer's disease, transmissible spongiform encephalopathies, and familial amyloidosis. Amyloid polypeptides share a specific quarternary structure element known as cross-␤ structure. Commonly, fibrillar aggregates are modified by advanced glycation end products (AGE). In addition, AGE formation itself induces protein aggregation. Both amyloid proteins and protein-AGE adducts bind multiligand receptors, such as receptor for AGE, CD36, and scavenger receptors A and B type I, and the serine protease tissue-type plasminogen activator (tPA). Based on these observations, we hypothesized that glycation induces refolding of globular proteins, accompanied by formation of cross-␤ structure. Using transmission electron microscopy, we demonstrate here that glycated albumin condensates into fibrous or amorphous aggregates. These aggregates bind to amyloid-specific dyes Congo red and thioflavin T and to tPA. In contrast to globular albumin, glycated albumin contains amino acid residues in ␤-sheet conformation, as measured with circular dichroism spectropolarimetry. Moreover, it displays cross-␤ structure, as determined with x-ray fiber diffraction. We conclude that glycation induces refolding of initially globular albumin into amyloid fibrils comprising cross-␤ structure. This would explain how glycated ligands and amyloid ligands can bind to the same multiligand "cross-␤ structure" receptors and to tPA.

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Advanced glycation end products (AGE) and their receptor (RAGE) in the brain of patients with Creutzfeldt-Jakob disease with prion plaques.

Cited by 98 publications

References 14 publications

RAGE binds preamyloid IAPP intermediates and mediates pancreatic β cell proteotoxicity

RAGE binds preamyloid IAPP intermediates and mediates pancreatic β cell proteotoxicity

Effect of natural flavonoids, stilbenes and caffeic acid oligomers on protein glycation

Glycation Induces Formation of Amyloid Cross-β Structure in Albumin

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