Prion diseases are a group of fatal neurodegenerative disorders of humans and animals which may be sporadic or inherited in origin and can be transmitted. The emergence of a new variant of CJD in the UK, which is proposed to be causally linked to BSE, has increased the urgency to identify and develop therapeutic compounds due to fear of a possible future epidemic. In this study we showed that tetracyline prevents aggregation and acquisition of protease resistance of PrP peptides, disrupts PrP peptide aggregates, and abolishes the neurotoxicity and astroglial proliferation induced by PrP peptides in vitro.
Therapeutic Approaches to Prion Diseases : In Vitro Studies with Tetracycline Compounds / T. Awan, E.M. Ragg, G. Forloni, S. Iussich, G. Rossi, L. Colombo, L. Girola, T. Massignan, O. Bugiani, M. Salmona, F. Tagliavini - In: Alzheimer's Disease / [a cura di] K. Iqbal, S. S. Sisodia, B. Winblad. - New York : John Wiley & Sons, 2002 Apr 18. - ISBN 9780471521761. - pp. 809-820 [10.1002/0470846453.ch75]
Therapeutic Approaches to Prion Diseases : In Vitro Studies with Tetracycline Compounds
E.M. Ragg;
2002
Abstract
Prion diseases are a group of fatal neurodegenerative disorders of humans and animals which may be sporadic or inherited in origin and can be transmitted. The emergence of a new variant of CJD in the UK, which is proposed to be causally linked to BSE, has increased the urgency to identify and develop therapeutic compounds due to fear of a possible future epidemic. In this study we showed that tetracyline prevents aggregation and acquisition of protease resistance of PrP peptides, disrupts PrP peptide aggregates, and abolishes the neurotoxicity and astroglial proliferation induced by PrP peptides in vitro.
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