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  • Title: Clusterin in Alzheimer's disease: An amyloidogenic inhibitor of amyloid formation?
    Author: Spatharas PM, Nasi GI, Tsiolaki PL, Theodoropoulou MK, Papandreou NC, Hoenger A, Trougakos IP, Iconomidou VA.
    Journal: Biochim Biophys Acta Mol Basis Dis; 2022 Jul 01; 1868(7):166384. PubMed ID: 35292360.
    Abstract:
    Clusterin is a heterodimeric glycoprotein (α- and β-chain), which has been described as an extracellular molecular chaperone. In humans, clusterin is an amyloid-associated protein, co-localizing with fibrillar deposits in several amyloidoses, including Alzheimer's disease. To clarify its potential implication in amyloid formation, we located aggregation-prone regions within the sequence of clusterin α-chain, via computational methods. We had peptide-analogues, which correspond to each of these regions, chemically synthesized and experimentally demonstrated that all of them can form amyloid-like fibrils. We also provide evidence that the same peptide-analogues can inhibit amyloid-β fibril formation, potentially making them appropriate drug candidates for Alzheimer's disease. At the same time, our findings hint that the respective aggregation-prone clusterin regions may be implicated in the molecular mechanism in which clusterin inhibits amyloid formation. Furthermore, we suggest that molecular chaperones with amyloidogenic properties might have a role in the regulation of amyloid formation, essentially acting as functional amyloids.
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