ArticleCell stress & chaperones2010
αB-Crystallin inhibits the cell toxicity associated with amyloid fibril formation by κ-casein and the amyloid-β peptide.
Article in Cell stress & chaperones, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 72 citations in OpenAlex.
- Label-Free Proteomic Profiling of the dvls2 (CL2006) Caenorhabditis elegans Alzheimer's Disease (AD) Model Reveals Conserved Molecular Signatures Shared With the Human AD Brain.Journal of neurochemistry · 2025Article
- Small Heat Shock Proteins: Protein Aggregation Amelioration and Neuro- and Age-Protective Roles.International journal of molecular sciences · 2025Review
- Small HSPs at the crossroad between protein aggregation, autophagy and unconventional secretion: clinical implications and potential therapeutic opportunities in the context of neurodegenerative diseases.Frontiers in cell and developmental biology · 2025Review
- Modulation of Alzheimer's Disease Aβ40 Fibril Polymorphism by the Small Heat Shock Protein αB-Crystallin.Journal of the American Chemical Society · 2024Article
- NQO1 regulates expression and alternative splicing of apoptotic genes associated with Alzheimer's disease in PC12 cells.Brain and behavior · 2023Article
- Alzheimer's disease amyloid-β pathology in the lens of the eye.Experimental eye research · 2022Article
- αB-Crystallin Chaperone Inhibits Aβ Aggregation by Capping the β-Sheet-Rich Oligomers and Fibrils.The journal of physical chemistry. B · 2020Article
- The multifaceted nature of αB-crystallin.Cell stress & chaperones · 2020Review
- Small heat shock proteins in neurodegenerative diseases.Cell stress & chaperones · 2020Review
- Development of a brain-permeable peptide nanofiber that prevents aggregation of Alzheimer pathogenic proteins.PloS one · 2020Article
- A Novel PEGylated Block Copolymer in New Age Therapeutics for Alzheimer's Disease.Molecular neurobiology · 2019Article
- Small Heat Shock Proteins, Big Impact on Protein Aggregation in Neurodegenerative Disease.Frontiers in pharmacology · 2019Review
- Crystallins and neuroinflammation: The glial side of the story.Biochimica et biophysica acta · 2016Article
- Small heat-shock proteins: important players in regulating cellular proteostasis.Cellular and molecular life sciences : CMLS · 2015Review
- Article
- The mitochondria-targeted antioxidant SkQ1 restores αB-crystallin expression and protects against AMD-like retinopathy in OXYS rats.Cell cycle (Georgetown, Tex.) · 2014Article
- Interaction of amyloid inhibitor proteins with amyloid beta peptides: insight from molecular dynamics simulations.PloS one · 2014Article
- Abnormally upregulated αB-crystallin was highly coincidental with the astrogliosis in the brains of scrapie-infected hamsters and human patients with prion diseases.Journal of molecular neuroscience : MN · 2013Article
- Monitoring the interaction between β2-microglobulin and the molecular chaperone αB-crystallin by NMR and mass spectrometry: αB-crystallin dissociates β2-microglobulin oligomers.The Journal of biological chemistry · 2013Article
- Novel roles for α-crystallins in retinal function and disease.Progress in retinal and eye research · 2012Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Amyloid fibril formation is associated with diseases such as Alzheimer's, Parkinson's, and prion diseases. Inhibition of amyloid fibril formation by molecular chaperone proteins, such as the small heat-shock protein αB-crystallin, may play a protective role in preventing the toxicity associated with this form of protein misfolding. Reduced and carboxymethylated κ-casein (RCMκ-CN), a protein derived from milk, readily and reproducibly forms fibrils at physiological temperature and pH. We investigated the toxicity of fibril formation by RCMκ-CN using neuronal model PC12 cells and determined whether the inhibition of fibril formation altered its cell toxicity. To resolve ambiguities in the literature, we also investigated whether fibril formation by amyloid-β1-40 (Aβ(1-40)), the peptide associated with Alzheimer's disease, was inhibited by αB-crystallin and if this affected the toxicity of Aβ. To this end, either RCMκ-CN or Aβ(1-40) was incubated at neutral pH to induce fibril formation before treating PC12 cells and assessing cell viability. Incubated (fibrillar) RCMκ-CN was more toxic to PC12 cells than native RCMκ-CN with the highest level of toxicity being associated with mature fibrils and protofibrils. Furthermore, the toxicity of RCMκ-CN was attenuated when its fibril formation was inhibited, either through the chaperone action of αB-crystallin or when it interacted with its natural binding partners in milk, α(S)- and β-casein. Likewise, incubating Aβ(1-40) with αB-crystallin inhibited both Aβ(1-40) fibril formation and the associated cell toxicity. Importantly, by inhibiting fibril formation, αB-crystallin prevents the cell toxicity associated with protein misfolding.
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