Depletion of CRAT in cardiomyocyte results in DCM

Carnitine acetyltransferase (CRAT) is a mitochondrial enzyme and catalyzes the conversion of acetyl-CoA to acetyl-Carnitine, which enables its export from mitochondria. It was reported that CRAT played a central role in regulating metabolic flexibility and promoting substrate switching from fatty acid to glucose in skeletal myocytes5. Interestingly, CRAT is most abundantly expressed in the heart and its activity is dramatically decreased in the mouse model of HF5,9. However, the specific contribution of this enzyme in the pathogenesis of HF remains largely uncharacterized. Neonatal rat ventricular cardiomyocytes were infected with lentivirus expressing control shRNA (WT) or CRAT shRNA (KO). Cells were harvested after 5 days and RNAs was extracted for RNA-sequencing analysis. We have two WT samples and two KD samples.