Abstract
Heavy, chronic alcohol consumption is associated with a syndrome known as alcoholic heart muscle disease (AHMD), clinically characterized by ventricular dilation, thinning of the ventricular wall, and myocardial dysfunction. These changes occur as a result of a decreased rate of protein synthesis. The clinical manifestations of AHMD are consistent with alterations in structural and myofibrillar proteins. The current study used a proteomic approach with isotope coded affinity tag (ICAT) labeling and mass spectrometry to delineate changes in protein expression in a chronic (16 wk) alcohol rat model. Chronic alcohol ingestion was associated with falls in mitochondrial proteins associated with TCA cycle (citrate synthase, isocitrate dehydrogenase, succinyl‐CoA synthetase, malate dehydrogenase) as well as enzymes involved in electron transport (ubiquinone, adenine nucleotide translocator, F1‐ATPase, H+ transporting two‐sector ATPase) and energy transfer (nucleoside‐diphosphate kinase, creatine kinase). No changes were seen in pyruvate dehydrogenase complex, NADH coenzyme Q reductase, or ubiquinol cytochrome c reductase. The results indicate myocardial mitochondrial proteins are adversely affected in chronic alcoholism. (PHS; RO1 AA012814).
Sign-in/Register to access full text options 
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
