Mapping the locations of hypertrophic cardiomyopathy gene variants onto the three-dimensional structures of contractile proteins revealed that these disrupt protein interactions are critical for normal cardiac relaxation and efficient energy usage.
Cardiac-specific overexpression of a recently discovered micropeptide, DWORF, enhances calcium cycling and contractility in the heart and rescues the heart failure phenotype of a genetic mouse model of dilated cardiomyopathy.
Integrative analysis of a Drosophila model of hypertrophic cardiomyopathy demonstrates that prolonged binding of the myosin cross-bridge to actin is a root cause of the disorder.
The melanocortin-4 receptor knockout mouse exhibits a cardiomyopathy syndrome, which raises concerns about cardiovascular function in patients with the similar loss of function mutations, and perhaps even in the 1 in 1500 patients with heterozygous loss of the gene.
The newly discovered Titin internal promoter may explain why the severity of dilated cardiomyopathy in patients with truncating mutations in Titin varies dramatically depending on position of the mutation.
A mutation that causes heart disease in humans increases the number of active myosin heads during contraction in the muscles of fruit flies, leading to the progressive dysfunction of the flight muscles and heart tube.
EphB4 maintains critical functional properties of the adult cardiac vasculature, namely mechanical resistance and fatty acid transport capability, and thereby prevents dilated cardiomyopathy-like defects.
TBX5-loss associated cardiomyocyte ectopy and atrial fibrillation is prevented by augmentation of SERCA2 activity, establishing a mechanism underlying the genetic basis for a Ca2+-dependent pathway for AF risk.
