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Role of the ₂-isoform of AMP-activated protein kinase in the metabolic response of the heart to no-flow ischemia

¹Division of Cardiology, School of Medicine, ³Hormone and Metabolic Research Unit, Université catholique de Louvain and Christian de Duve Institute of Cellular Pathology, Brussels, Belgium; and ²Institut National de la Santé et de la Recherche Médicale, Unité 769, Université Paris-Sud, and IFR-141, Châtenay-Malabry; and ⁴Unité 567 Institut National de la Santé et de la Recherche Médicale, Unité Mixte de Recherche 8104 Centre National de la Recherche Scientifique, René Descartes University, Institut Cochin, Department of Endocrinology, Metabolism. and Cancer, Paris, France

Submitted 29 September 2005 ; accepted in final form 13 July 2006

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 AMPK₂, the major AMPK isoform in the heart, in response to global ischemia. We used AMPK₂-knockout (AMPK₂^–/–) mice to evaluate the consequences of AMPK₂ deletion during normoxia and ischemia, with glucose as the sole substrate. Hemodynamic measurements from echocardiography of hearts from AMPK₂^–/– mice during normoxia showed no significant modification compared with wild-type animals. In contrast, the response of hearts from AMPK₂^–/– mice to no-flow ischemia was characterized by a more rapid onset of ischemia-induced contracture. This ischemic contracture was associated with a decrease in ATP content, lactate production, glycogen content, and AMPK₂ content. Hearts from AMPK₂^–/– mice were also characterized by a decreased phosphorylation state of acetyl-CoA carboxylase during normoxia and ischemia. Despite an apparent worse metabolic adaptation during ischemia, the absence of AMPK₂ does not exacerbate impairment of the recovery of postischemic contractile function. In conclusion, AMPK₂ is required for the metabolic response of the heart to no-flow ischemia. The remaining AMPK₁ cannot compensate for the absence of AMPK₂.

glycogen; glycolysis; acetyl-CoA carboxylase

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