AD PATHOGENESIS

Role of CRMP2 and Pin1 in the pathogenesis of Alzheimer’s disease

 Coordinatore USTAV MOLEKULARNI GENETIKY AKADEMIE VED CESKE REPUBLIKY VEREJNA VYZKUMNA INSTITUCE 

 Organization address address: VIDENSKA 1083
city: PRAHA 4
postcode: 142 20

contact info
Titolo: Dr.
Nome: Radislav
Cognome: Sedlacek
Email: send email
Telefono: +420 2 41063198

 Nazionalità Coordinatore Czech Republic [CZ]
 Totale costo 100˙000 €
 EC contributo 100˙000 €
 Programma FP7-PEOPLE
Specific programme "People" implementing the Seventh Framework Programme of the European Community for research, technological development and demonstration activities (2007 to 2013)
 Code Call FP7-PEOPLE-2012-CIG
 Funding Scheme MC-CIG
 Anno di inizio 2013
 Periodo (anno-mese-giorno) 2013-03-01   -   2017-02-28

 Partecipanti

# participant  country  role  EC contrib. [€] 
1    USTAV MOLEKULARNI GENETIKY AKADEMIE VED CESKE REPUBLIKY VEREJNA VYZKUMNA INSTITUCE

 Organization address address: VIDENSKA 1083
city: PRAHA 4
postcode: 142 20

contact info
Titolo: Dr.
Nome: Radislav
Cognome: Sedlacek
Email: send email
Telefono: +420 2 41063198

CZ (PRAHA 4) coordinator 100˙000.00

Mappa


 Word cloud

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pin    deregulation    axon    crmp    cdk    aggregates    phosphorylation    ad    pathology    isoforms    related   

 Obiettivo del progetto (Objective)

'Collapsin response mediator protein 2 (CRMP2) is essential for neural development and function. It promotes axon growth but upon its phosphorylation it mediates axon retraction. Deregulation of CRMP2 has been implicated in Alzheimer’s disease (AD) where CRMP2 was detected to form hyperphosphorylated aggregates within neurofibrillary tangles. The mechanisms that regulate formation of CRMP2 aggregates are so far largely unknown. We have recently found that one CDK5-phosphorylated CRMP2 isoform is specifically stabilized by Pin1 - a unique phospho-specific isomerase linked to AD, suggesting that deregulation of Pin1 could contribute to AD related CRMP2 pathology. In the present proposal we will study how various CRMP2 isoforms are involved in CRMP2 aggregate formation and how high levels of Amyloid-b peptide, CDK5, and Pin1 affect phosphorylation, stability or localization of CRMP2 isoforms in AD using mouse models. Funding of the proposal will bring a new insight into the role of Pin1 in AD-related CRMP2 pathology.'

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