http://www.cnr.it/ontology/cnr/individuo/prodotto/ID178915
Conformation dependent pro-apoptotic activity of the recombinant human prion protein fragment 90-231. (Articolo in rivista)
- Type
- Label
- Conformation dependent pro-apoptotic activity of the recombinant human prion protein fragment 90-231. (Articolo in rivista) (literal)
- Anno
- 2006-01-01T00:00:00+01:00 (literal)
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- Corsaro A.; Paludi D.; Villa V.; D'Arrigo C.; Chiovitti K.; Thellung S.; Russo C.; Di Cola D; Ballerini P.; Patrone E.; Schettini G.; Aceto A. ; Florio T. (literal)
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- ISI Web of Science (WOS) (literal)
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- Paludi D. Univ Teramo, Dept Sci Alimenti, Sch Vet.
Chiovitti K.; Di Cola D ; Aceto A. ; Univ G DAnnunzio Chieti, Dept Biomed Sci, Biochem Sect.
Ballerini P. Univ G DAnnunzio Chieti, Dept Biomed Sci, Pharmacol Sect,
Corsaro A; Villa V; Thellung S.; Russo C.; Schettini G.; Florio T. Univ. Genova, Farmacol Sezione, Dept. Oncol Biol. e Genetica
D'Arrigo C.; Patrone E. ISMAC-GE (literal)
- Titolo
- Conformation dependent pro-apoptotic activity of the recombinant human prion protein fragment 90-231. (literal)
- Abstract
- The transition of prion protein from a mainly alpha-structured isoform (PrPC) to a beta sheet-containing protein (PrPSc) represents a major pathogenetic mechanism in prion diseases. To study the role of PrP structural conformation in prion-dependent neurodegeneration, we analysed the neurotoxicity of PrP in alpha and beta conformations, using a recombinant protein encompassing amino acids 90-231 of the human PrP (hPrP90-231). Using controlled thermal denaturation (53 degrees C, 1h) we converted hPrP90-231 in a structural isoform displaying PrPSc-related characteristics: high beta sheet content, increased aggregability and a slight increase in the resistance to protease K. In virtue of these structural changes, hPrP90-231 powerfully affected the survival of SH-SY5Y cells, inducing a caspase-3 and p38-dependent apoptosis. Conversely, in the native alpha-helix-rich conformation, hPrP90-231 did not show significant cell toxicity. The relationship between the structural state of hPrP90-231 and its neurotoxicity was demonstrated, inducing the thermal denaturation of the peptide in the presence of Congo red that prevented both the transition of hPrP90-231 into a beta-rich isoform and the acquisition of toxic properties. In conclusion, we report that the toxicity of hPrP90-231 is dependent on its three-dimensional structure, as is supposed to occur for the pathogen PrP during TSE. (literal)
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