ER AND METABOLISM

Oxidative protein folding and pathogenesis of metabolic disorders

 Coordinatore THE CHANCELLOR, MASTERS AND SCHOLARS OF THE UNIVERSITY OF CAMBRIDGE 

 Organization address address: The Old Schools, Trinity Lane
city: CAMBRIDGE
postcode: CB2 1TN

contact info
Titolo: Ms.
Nome: Renata
Cognome: Schaeffer
Email: send email
Telefono: +44 1223 333543
Fax: +44 1223 332988

 Nazionalità Coordinatore United Kingdom [UK]
 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-2010-RG
 Funding Scheme MC-IRG
 Anno di inizio 2011
 Periodo (anno-mese-giorno) 2011-03-01   -   2015-02-28

 Partecipanti

# participant  country  role  EC contrib. [€] 
1    THE CHANCELLOR, MASTERS AND SCHOLARS OF THE UNIVERSITY OF CAMBRIDGE

 Organization address address: The Old Schools, Trinity Lane
city: CAMBRIDGE
postcode: CB2 1TN

contact info
Titolo: Ms.
Nome: Renata
Cognome: Schaeffer
Email: send email
Telefono: +44 1223 333543
Fax: +44 1223 332988

UK (CAMBRIDGE) coordinator 100˙000.00

Mappa


 Word cloud

Esplora la "nuvola delle parole (Word Cloud) per avere un'idea di massima del progetto.

insulin    et    ero    oxidative    disulfide    folding    zito    al    signaling    cells    bond    protein    er    prdx    responsive    nutrient   

 Obiettivo del progetto (Objective)

'Endoplasmic reticulum (ER) oxidation 1 (ERO1) trasfers disulfide bonds to protein disulfide isomerase (PDI) and is essential for oxidative protein folding in simple eukaryotes such as yeast and worms. Higher eucaryotes have alternative pathways for disulfide bond formation (Zito et al., 2010). Recently we have discovered that the ER localized peroxiredoxin 4 (PRDX4) is able to couple use of hydroperoxides for oxidative protein folding, independently of ERO1 (Zito et al., 2010b). Hydrogen peroxide production is coupled both to nutrient assimilation and to insulin signaling whereas disulfide bond formation is limiting to the production of important signaling molecules such as insulin itself (in nutrient and insulin-responsive beta cells) and adipokines (in insulin responsive adipose tissue). The aim of this proposal is to evaluate, in cultured cells and intact mice, the impact of PRDX4 and ERO1 activity on the biosynthesis and the functional state of insulin and adypokines and consequently on intermediary metabolism. Recent evidence indicates that disulfide bond formation can be manipulated with chemical probes (Blais et al., 2010). Therefore the proposed study may bring to light novel targets for pharmacological intervention in diabetes and insulin resistance states.'

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