Title : Huntington's disease induced cardiac amyloidosis is reversed by modulating protein folding and oxidative stress pathways in the Drosophila heart.

Pub. Date : 2013

PMID : 24367279






5 Functional Relationships(s)
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1 Amyloid-like inclusions have been associated with Huntington"s disease (HD), which is caused by expanded polyglutamine repeats in the Huntingtin protein. polyglutamine huntingtin Drosophila melanogaster
2 We have generated a Drosophila model of cardiac amyloidosis that exhibits accumulation of PolyQ aggregates and oxidative stress in myocardial cells, upon heart-specific expression of Huntingtin protein fragments (Htt-PolyQ) with disease-causing poly-glutamine repeats (PolyQ-46, PolyQ-72, and PolyQ-102). polyglutamine huntingtin Drosophila melanogaster
3 We have generated a Drosophila model of cardiac amyloidosis that exhibits accumulation of PolyQ aggregates and oxidative stress in myocardial cells, upon heart-specific expression of Huntingtin protein fragments (Htt-PolyQ) with disease-causing poly-glutamine repeats (PolyQ-46, PolyQ-72, and PolyQ-102). polyglutamine huntingtin Drosophila melanogaster
4 Cardiac expression of GFP-tagged Htt-PolyQs resulted in PolyQ length-dependent functional defects that included increased incidence of arrhythmias and extreme cardiac dilation, accompanied by a significant decrease in contractility. polyglutamine huntingtin Drosophila melanogaster
5 Cardiac expression of GFP-tagged Htt-PolyQs resulted in PolyQ length-dependent functional defects that included increased incidence of arrhythmias and extreme cardiac dilation, accompanied by a significant decrease in contractility. polyglutamine huntingtin Drosophila melanogaster