Preserved protein synthesis in the heart in response to acute fasting and chronic food restriction despite reductions in liver and skeletal muscle. Am J Physiol 295:E216-E222

Department of Nutrition, Case Western Reserve University School of Medicine, 10900 Euclid Ave., Cleveland, OH 44106, USA.
AJP Endocrinology and Metabolism (Impact Factor: 3.79). 08/2008; 295(1):E216-22. DOI: 10.1152/ajpendo.00545.2007
Source: PubMed


Whole body protein synthesis is reduced during the fed-to-fasted transition and in cases of chronic dietary restriction; however, less is known about tissue-specific alterations. We have assessed the extent to which protein synthesis in cardiac muscle responds to dietary perturbations compared with liver and skeletal muscle by applying a novel (2)H(2)O tracer method to quantify tissue-specific responses of protein synthesis in vivo. We hypothesized that protein synthesis in cardiac muscle would be unaffected by acute fasting or food restriction, whereas protein synthesis in the liver and gastrocnemius muscle would be reduced when there is a protein-energy deficit. We found that, although protein synthesis in liver and gastrocnemius muscle was significantly reduced by acute fasting, there were no changes in protein synthesis in the left ventricle of the heart for either the total protein pool or in isolated mitochondrial or cytosolic compartments. Likewise, a chronic reduction in calorie intake, induced by food restriction, did not affect protein synthesis in the heart, whereas protein synthesis in skeletal muscle and liver was decreased. The later observations are supported by changes in the phosphorylation state of two critical mediators of protein synthesis (4E-BP1 and eIF2alpha) in the respective tissues. We conclude that cardiac protein synthesis is maintained in cases of nutritional perturbations, in strong contrast to liver and gastrocnemius muscle, where protein synthesis is decreased by acute fasting or chronic food restriction.

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Available from: Yi Li, May 14, 2015
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    • "It has been long known that protein synthesis in the body as a whole is sensitive to nutritional status [57]–[59], with greater rates observed in the fed compared with the fasted state. More recently, it was reported that liver protein synthesis was more significantly reduced by fasting than other organs [60]. Furthermore, consumption of the daily food all in one meal distorted the circadian rhythm, particularly when it was taken in the morning, and a morning meal increased the total 24 hour synthesis of protein in liver, whereas an evening meal did not [61]. "
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    • "Protein turnover is cyclical in nature, with the synthesis of proteins being counterbalanced by their degradation rates such that tissue protein mass remains constant in a mature dry (non-lactating) well-nourished animal. It has long been recognized that fluctuations in tissue protein synthesis rates (also protein mass) can occur during a transition from dry to lactating-states in smaller sized ruminants [16], [17] and/or the nutritional-state of the animal [18], [19], [20]. Tissue protein fractional synthesis rates (FSR) are calculated by the change in tissue protein enrichment over time with respect to the precursor pool (usually plasma or tissue free) from which the labeled amino acid is incorporated into the protein [8]. "
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    • "Liver and myocardium tissues have different rate of protein synthesis, being higher in hepatocytes, which are able to produce elevated levels of secretory proteins, than in myocardium. However, while the liver can regulate protein synthesis and inhibition according to its own physiological needs and energy demands, the myocardium is resistant to suppression of protein synthesis [35]. The upregulation of the UPR markers along the PERK-eIF2α axis as CHOP, GADD34 and ATF4, although significant, is low when compared with in vitro studies where cell cultures were exposed to anoxia or severe hypoxia. "
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