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Updated: May 16, 2026
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Full- versus Sub-Regional Quantification of Amyloid-Beta Load on Mouse Brain Sections
Published on: May 19, 2022
Amyloid β levels in human red blood cells
Takehiro Kiko1, Kiyotaka Nakagawa, Akira Satoh
1Food and Biodynamic Chemistry Laboratory, Graduate School of Agricultural Science, Tohoku University, Sendai, Japan.
Plos One
|November 21, 2012
Summary
Amyloid beta-peptide (Aβ) found in red blood cells (RBCs) increases with age and may contribute to Alzheimer's disease (AD). The antioxidant astaxanthin reduced RBC Aβ levels, suggesting a potential preventive strategy for dementia.
Area of Science:
- Neuroscience
- Biochemistry
- Gerontology
Background:
- Alzheimer's disease (AD) pathogenesis is linked to amyloid beta-peptide (Aβ) and impaired oxygen delivery by red blood cells (RBCs).
- The presence and distribution of Aβ within human RBCs remain largely uncharacterized.
- This study investigates Aβ in RBCs and its modulation by antioxidants.
Purpose of the Study:
- To quantify Aβ40 and Aβ42 levels in human RBCs.
- To determine the relationship between RBC Aβ levels, aging, and oxidative stress.
- To evaluate the effect of astaxanthin supplementation on RBC Aβ and oxidative stress markers.
Main Methods:
- Quantification of Aβ40 and Aβ42 in human RBCs using ELISA assays.
- Analysis of RBC Aβ levels in relation to participant age.
- Assessment of oxidative stress markers and RBC Aβ levels after astaxanthin supplementation.
Main Results:
- Significant levels of Aβ40 and Aβ42 were detected in human RBCs.
- RBC Aβ levels showed a positive correlation with aging.
- Astaxanthin supplementation decreased RBC Aβ and oxidative stress markers.
Conclusions:
- Plasma Aβ40 and Aβ42 likely bind to RBCs, potentially contributing to AD pathogenesis, especially with aging.
- RBC Aβ40 and Aβ42 may serve as novel biomarkers for Alzheimer's disease.
- Astaxanthin demonstrates potential as an anti-dementia agent by reducing RBC Aβ and oxidative stress.
Related Concept Videos
03:03Amyloid Fibrils
Amyloid fibrils are aggregates of misfolded proteins. Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils.
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
03:03Amyloid Fibrils
Amyloid fibrils are aggregates of misfolded proteins. Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils.
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...