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  • Title: Only amyloidogenic intermediates of transthyretin induce apoptosis.
    Author: Andersson K, Olofsson A, Nielsen EH, Svehag SE, Lundgren E.
    Journal: Biochem Biophys Res Commun; 2002 Jun 07; 294(2):309-14. PubMed ID: 12051711.
    Abstract:
    In diseases like Alzheimer's disease and familial amyloidotic polyneuropathy (FAP) amyloid deposits co-localize with areas of neurodegeneration. FAP is associated with mutations of the plasma protein transthyretin (TTR). We can here show an apoptotic effect of amyloidogenic mutants of TTR on a human neuroblastoma cell line. Toxicity could be blocked by catalase indicating a free oxygen radical dependent mechanism. The toxic effect was dependent on the state of aggregation and unexpectedly mature fibrils from FAP-patients who failed to exert an apoptotic response. Morphological studies revealed a correlation between toxicity and the presence of immature amyloid. Thus, we can show that toxicity is associated with early stages of fibril formation and propose that mature full-length fibrils represent an inert end stage, which might serve as a rescue mechanism.
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