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Article type: Research Article
Authors: Cicconi, Simonaa; b; 1 | Gentile, Antoniettaa; b; 1 | Ciotti, Maria Teresaa; b | Parasassi, Tizianaa; b; 2 | Serafino, Annaluciaa; b; 2 | Calissano, Pietroa; b; *
Affiliations: [a] Institute of Neurobiology and Molecular Medicine, CNR, Roma, Italy | [b] European Brain Research Institute (EBRI), Roma, Italy
Correspondence: [*] Corresponding author: Pietro Calissano, Via del Fosso di Fiorano, 64 – 00143 Roma, Italy. Tel.: 06 501703004; Fax: 06 501703311; E-mail: [email protected].
Note: [1] These authors equally contributed to this work.
Note: [2] Present address: Via del Fosso del Cavaliere, 100 – 00133 Roma, Italy.
Note: [] Communicated by Antonino Cattaneo
Abstract: In this study we report that apoptotic death of primary cultures of cerebellar granule neurons is accompanied by release of thioflavin-binding proteins – indicative of the presence of β-sheet structures – and fibril formation in the culture medium. When the same neurons are subjected to an excytotoxic death caused by 100 µM glutamate exposure, the amount of thioflavin binding is markedly reduced. Western blot analysis shows that fibrils contain monomers, dimers and trimers of amyloid-β (Aβ) which, when observed at the electron microscope, have morphologies reminiscent of fibrils of senile plaques. These findings demonstrate that triggering an apoptotic pathway leads to β-sheet transition and fibril formation of a protein primarily involved in Alzheimer's disease and may be of direct relevance to the possible link between apoptosis and this neuropathology.
Keywords: Apoptosis, necrosis, β-sheet structures, Aβ, CGNs
DOI: 10.3233/JAD-2007-12301
Journal: Journal of Alzheimer's Disease, vol. 12, no. 3, pp. 211-220, 2007
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