Abstract
Adenosine monophosphate – activated kinase (AMPK) plays a key role in the coordination of the heart’s anabolic and catabolic pathways. It induces a cellular cascade at the center of maintaining energy homeostasis in the cardiomyocytes.. The activated AMPK is a heterotrimeric protein, separated into a catalytic α - subunit (63kDa), a regulating β - subunit (38kDa) and a γ - subunit (38kDa), which is allosterically adjusted by adenosine triphosphate (ATP) and adenosine monophosphate (AMP). The actual binding of AMP to the γ – subunit is the step which activates AMPK. AMPK serves also as a protein kinase in several metabolic pathways of the heart, including cellular energy sensoring or cardiovascular protection. The AMPK cascade represents a sensitive system, activated by cellular stresses that deplete ATP and acts as an indicator of intracellular ATP/AMP. In the context of cellular stressors (i.e. hypoxia, pressure overload, hypertrophy or ATP deficiency) the increasing levels of AMP promote allosteric activation and phosphorylation of AMPK. As the concentration of AMP begins to increase, ATP competitively inhibits further phosphorylation of AMPK. The increase of AMP may also be induced either from an iatrogenic emboli, percutaneous coronary intervention, or from atherosclerotic plaque rupture leading to an ischemia in the microcirculation. To modulate energy metabolism by phosphorylation and dephosphorylation is vital in terms of ATP usage, maintaining transmembrane transporters and preserving membrane potential. In this article, we review AMPK and its role as an important regulatory enzyme during periods of myocardial stress, regulating energy metabolism, protein synthesis and cardiovascular protection.
Highlights
Adenosine monophosphate-activated kinase (AMPK) induces a cellular cascade at the center of maintaining energy homeostasis in the cell
We review AMPK and its role as an important regulatory enzyme during periods of myocardial stress, regulating energy metabolism, protein synthesis and cardiovascular protection
The activated AMPK is a heterotrimeric protein, separated into a catalytic - subunit (63kDa), a regulating subunit (38kDa) and a - subunit (38kDa), which is allosterically adjusted by adenosine triphosphate (ATP) and adenosine monophosphate (AMP) [2]
Summary
Adenosine monophosphate-activated kinase (AMPK) induces a cellular cascade at the center of maintaining energy homeostasis in the cell. Carlson described AMPK as an enzyme which works as a function of the intracellular ATP/AMP quotient, which regulates ACC in response to energetic stress [1, 2]. AMPK serves as a protein kinase in several metabolic pathways of the heart, including cellular energy sensoring or cardiovascular protection [3,4,5] - previously examined in animal models [6,7,8,9]. In the context of cellular stressors (i.e. hypoxia, pressure overload, hypertrophy or ATP deficiency) the increasing levels of AMP promote allosteric activation and phosphorylation of AMPK [3,4,5]. In general we could establish the hypothesis that AMPK works as a key stress signalling enzyme in heart or as a cellular energy sensor for cardiovascular protection [3, 4]
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