PRISTINE-PD

Prion-like transmission of α-synuclein in Parkinson's disease

Coordinatore	LUNDS UNIVERSITET    more Spiacenti, non ci sono informazioni su questo coordinatore. Contattare Fabio per maggiori infomrazioni, grazie.
Nazionalità Coordinatore	Sweden [SE]
Totale costo	2˙499˙998 €
EC contributo	2˙499˙998 €
Programma	FP7-IDEAS-ERC Specific programme: "Ideas" implementing the Seventh Framework Programme of the European Community for research, technological development and demonstration activities (2007 to 2013)
Code Call	ERC-2010-AdG_20100317
Funding Scheme	ERC-AG
Anno di inizio	2011
Periodo (anno-mese-giorno)	2011-06-01   -   2016-05-31

 Partecipanti

#	participant	country	role	EC contrib. [€]
1	LUNDS UNIVERSITET  Organization address address: Paradisgatan 5c city: LUND postcode: 22100 contact info Titolo: Ms. Nome: Diana Cognome: Jerman Email: send email Telefono: +46 46 222 0529 Fax: +46 46 2220558	SE (LUND)	hostInstitution	2˙499˙998.00
2	LUNDS UNIVERSITET  Organization address address: Paradisgatan 5c city: LUND postcode: 22100 contact info Titolo: Prof. Nome: Patrik Cognome: Brundin Email: send email Telefono: +46 46 2220529 Fax: +46 46 2220531	SE (LUND)	hostInstitution	2˙499˙998.00

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 Obiettivo del progetto (Objective)

'Protein misfolding is implicated as a pathogenetic mechanism in several neurodegenerative disorders, including Parkinson¿s disease (PD). In prion disease, the misfolded protein spreads between cells and acts as a ¿permissive template¿, causing protein in the recipient cell to misfold. In 2008 we reported that classical neuropathological changes gradually propagate from a PD patient¿s brain to a graft of healthy neurons, over one decade after surgery. These groundbreaking findings suggest that the protein ¿-synuclei may transfer between cells and propagate protein aggregation in a ¿prion-like¿ fashion in PD. This molecular disease mechanism might explain how protein aggregates gradually spread throughout the nervous system and promote progression of disease symptoms. This highly novel concept represents a hitherto poorly explored route of intercellular communication and might have far-reaching implications well beyond PD. Little is known about how various forms of ¿-synuclein are taken up; if they seed aggregation in the recipient cell; how they affect proteostasis in the recipient cells; if they are transported axonally; and, finally, whether they can cause spreading of PD-like pathology in the nervous system. In a multidisciplinary project will now examine the molecular mechanisms underlying translocation of ¿-synuclein across a lipid membrane, from the outside to the inside of a cell; what the molecular and functional consequences are of importing ¿-synuclein; what the dynamics of ¿-synuclein transfer are in vivo; whether aggregates of misfolded ¿-synuclein can spread from one region of the nervous system to another; what genes influence the likelihood for ¿-synuclein transfer to take place; and, finally if small molecules that inhibit ¿-synuclein can be identified. Our studies will shed light on what appears to be a new principle for pathogenesis of neurodegenerative disorders and can open up avenues for new therapeutic strategies.'