The metabolic consequences of hepatic AMP-kinase phosphorylation in rainbow trout

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 con...

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Bibliographic Details
Published in:PloS one 2011-05, Vol.6 (5), p.e20228-e20228
Main Authors: Polakof, Sergio, Panserat, Stéphane, Craig, Paul M, Martyres, David J, Plagnes-Juan, Elisabeth, Savari, Sharareh, Aris-Brosou, Stéphane, Moon, Thomas W
Format: Article
Language:English
Subjects:
Acetyl-CoA carboxylase
Adenylate Kinase - metabolism
Agriculture
AMP
AMP-activated protein kinase
Animals
Biology
Carassius auratus
Carassius carassius
Cellular Biology
Energy balance
Fatty acid synthesis
Fatty acids
Fatty-acid synthase
Fish
Fuel gages
Genomics
Glucokinase
Glucose
Glucose metabolism
Glucose-6-phosphatase
Glycogen
Hepatocytes
Homeostasis
Isoenzymes
Kinases
Life Sciences
Lipid metabolism
Liver
Liver - enzymology
Metabolism
Metformin
Oncorhynchus mykiss
Oncorhynchus mykiss - metabolism
Pharmacology
Phosphatases
Phosphorylation
Phylogeny
Protein kinases
Protein-serine/threonine kinase
Rodents
Salmon
Threonine
Transcription
Trout
Type 2 diabetes
Zebrafish
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Summary: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.
ISSN:1932-6203
1932-6203
DOI:10.1371/journal.pone.0020228