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1 School of Medicine, Universite catholique de Louvain, Division of cardiology, Brussels, Belgium
2 Universite Paris-Sud, U-446 INSERM, Cardiologie Cellulaire et Moleculaire, Chatenay Malabry, France
3 Universite catholique de Louvain and Christian de Duve Institute of Cellular Pathology, Hormone and Metabolic Research Unit, Brussels, Belgium
4 Rene Descartes University, Institut Cochin, Department of Genetic, Development and Molecular Pathology, U-567 INSERM, UMR 8104 CNRS, Paris, France
* To whom correspondence should be addressed. E-mail: bertrand{at}card.ucl.ac.be.
AMP-activated protein kinase (AMPK) is a major sensor and regulator of the energetic state of the cell. Little is known about the specific role of the AMPK
2 isoform, the major isoform present in heart, in response to global ischemia. We used knockout mice for this isoform (AMPK2-/- mice) to evaluate the consequences of its deletion in normoxic and ischemic conditions with glucose as sole substrate. The function of AMPK2-/- mice hearts studied under normoxia by echocardiographic and hemodynamic measurements did not reveal any significant modification in comparison with wild-type animals. By contrast, the response of the AMPK2-/- mice heart to no-flow ischemia was characterized by a more rapid onset of ischemic contracture. This ischemic contracture was associated to a decrease in ATP content, in lactate production, in glycogen content and in AMPK
2 isoform content. AMPK2-/- mice hearts were also characterized by a decreased phosphorylation state of acetyl-CoA carboxylase under both normoxic and ischemic conditions. Despite an apparent worse metabolic adaptation during the ischemic episode, the absence of AMPK2 isoform does not exacerbate the impairment of postischemic contractile function recovery. In conclusion, the 2 isoform of AMPK is required for the metabolic response of the heart to no-flow ischemia. The remaining AMPK1 isoform cannot compensate for the absence of the second catalytic isoform.
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