ArticleThe Journal of biological chemistry2011
Inhibition of beta2-microglobulin amyloid fibril formation by alpha2-macroglobulin.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
9 citing papers in PubMed, 22 citations in OpenAlex.
- Molecular mechanisms underlying uremic toxin-related systemic disorders in chronic kidney disease: focused on βClinical and experimental nephrology · 2019Review
- Unraveling the genes implicated in Alzheimer's disease.Biomedical reports · 2017Article
- Multifaceted anti-amyloidogenic and pro-amyloidogenic effects of C-reactive protein and serum amyloid P component in vitro.Scientific reports · 2016Article
- Systemic amyloidosis: lessons from β2-microglobulin.The Journal of biological chemistry · 2015Review
- Alpha-2-Macroglobulin Is Acutely Sensitive to Freezing and Lyophilization: Implications for Structural and Functional Studies.PloS one · 2015Article
- Hypochlorite-induced structural modifications enhance the chaperone activity of human α2-macroglobulin.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Association of cerebrospinal fluid Aβ42 with A2M gene in cognitively normal subjects.Neurobiology of aging · 2014Article
- The extracellular chaperone haptoglobin prevents serum fatty acid-promoted amyloid fibril formation of β2-microglobulin, resistance to lysosomal degradation, and cytotoxicity.The Journal of biological chemistry · 2013Article
- Structure, folding dynamics, and amyloidogenesis of D76N β2-microglobulin: roles of shear flow, hydrophobic surfaces, and α-crystallin.The Journal of biological chemistry · 2013Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The relationship between various amyloidoses and chaperones is gathering attention. In patients with dialysis-related amyloidosis, α(2)-macroglobulin (α2M), an extracellular chaperone, forms a complex with β(2)-microglobulin (β2-m), a major component of amyloid fibrils, but the molecular mechanisms and biological implications of the complex formation remain unclear. Here, we found that α2M substoichiometrically inhibited the β2-m fibril formation at a neutral pH in the presence of SDS, a model for anionic lipids. Binding analysis showed that the binding affinity between α2M and β2-m in the presence of SDS was higher than that in the absence of SDS. Importantly, SDS dissociated tetrameric α2M into dimers with increased surface hydrophobicity. Western blot analysis revealed that both tetrameric and dimeric α2M interacted with SDS-denatured β2-m. At a physiologically relevant acidic pH and in the presence of heparin, α2M was also dissociated into dimers, and both tetrameric and dimeric α2M interacted with β2-m, resulting in the inhibition of fibril growth reaction. These results suggest that under conditions where native β2-m is denatured, tetrameric α2M is also converted to dimeric form with exposed hydrophobic surfaces to favor the hydrophobic interaction with denatured β2-m, thus dimeric α2M as well as tetrameric α2M may play an important role in controlling β2-m amyloid fibril formation.
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Registered trials
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