The Metabolic Consequences of Hepatic AMP-Kinase Phosphorylation in Rainbow TroutReport as inadecuate

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AMP-activated protein kinase AMPK, a phylogenetically conserved serine-threonine protein kinase, is proposed to function as a -fuel gauge- to monitor cellular energy status in response to nutritional environmental variations. However, in fish, few studies have addressed the metabolic consequences related to the activation of this kinase. This study demonstrates that the rainbow trout Oncorhynchus mykiss possesses paralogs of the three known AMPK subunits that co-diversified, that the AMPK protein is present in the liver and in isolated hepatocytes, and it does change in response to physiological fasting-re-feeding cycle and pharmacological AICAR and metformin administration and incubations manipulations. Moreover, the phosphorylation of AMPK results in the phosphorylation of acetyl-CoA carboxylase, a main downstream target of AMPK in mammals. Other findings include changes in hepatic glycogen levels and several molecular actors involved in hepatic glucose and lipid metabolism, including mRNA transcript levels for glucokinase, glucose-6-phosphatase and fatty acid synthase both in vivo and in vitro. The fact that most results presented in this study are consistent with the recognized role of AMPK as a master regulator of energy homeostasis in living organisms supports the idea that these functions are conserved in this piscine model.

Author: Sergio Polakof , Stéphane Panserat, Paul M. Craig, David J. Martyres, Elisabeth Plagnes-Juan, Sharareh Savari, Stéphane Aris-Br



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