Open Access
Review
AMPK: a cellular metabolic and redox sensor. A minireview
Najeeb A Shirwany1,Ming-Hui Zou1,*
1
Section of Molecular Medicine, Department of Medicine, and Department of Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center, Oklahoma City, OK 73104, USA
DOI: 10.2741/4218 Volume 19 Issue 3, pp.447-474
Published: 01 January 2014
*Corresponding Author(s):  
Ming-Hui Zou
E-mail:  
ming-hui-zou@ouhsc.edu
Abstract

AMPK is a serine/threonine kinase that is found in all eukaryotes and is ubiquitously expressed in all organ systems. Once activated, AMPK stimulates hepatic fatty acid oxidation and ketogenesis, inhibits cholesterol synthesis, lipogenesis, and triglyceride synthesis, inhibits adipocyte lipolysis and lipogenesis, stimulates skeletal muscle fatty acid oxidation and muscle glucose uptake, and modulates insulin secretion by the pancreas. Thus its importance in many critical cellular processes is well established. For cells it is critical that energy supply and demand are closely matched. AMPK is recognized as a critical integrator of this balance. It is known to be allosterically activated by an increased AMP:ATP ratio. Activation of the kinase switches on catabolic pathways while switching off anabolic ones. It also acts as a redox sensor in endothelial cells where oxidative stress can disturb NO signaling. Abnormal NO signaling leads to disturbed vasodilatory responses. By inhibiting the formation of reactive oxygen species in the endothelium, AMPK can optimize the redox balance in the vasculature. Here, we review the role of AMPK in the cell.

Key words

AMPK, Cell cycle, ATP, AMP, Catabolism, Redox sensor, Review

Share and Cite
Najeeb A Shirwany, Ming-Hui Zou. AMPK: a cellular metabolic and redox sensor. A minireview. Frontiers in Bioscience-Landmark. 2014. 19(3); 447-474.