The stimulation of heart glycolysis by increased workload does not require AMP‐activated protein kinase but a wortmannin‐sensitive mechanism

FEBS Letters

Hue, Louis²  Rider, Mark H²  Bertrand, Luc²  Marsin, Anne-Sophie²  Vanoverschelde, Jean-Louis¹  Beauloye, Christophe² 

[1]Division of Cardiology, University of Louvain Medical School, Brussels, Belgium

[2]Hormone and Metabolic Research Unit, Christian de Duve Institute of Cellular Pathology, ICP-UCL 7529, 75, avenue Hippocrate, B-1200 Brussels, Belgium

关键词: Adenosine monophosphate-activated protein kinase;    Heart work;    Fructose-2;    6-bisphosphate;    Protein kinase B;    Wortmannin;    ACC;    acetyl coenzyme A carboxylase;    AMPK;    adenosine monophosphate (AMP)-activated protein kinase;    Cr;    creatine;    p70S6K;    p70 ribosomal S6 kinase;    PI3K;    phosphatidylinositol-3-kinase;    PCr;    phosphocreatine;    PFK-1;    6-phosphofructo-1-kinase;    PFK-2;    6-phosphofructo-2-kinase;    PKB;    protein kinase B;   

DOI  :  10.1016/S0014-5793(02)03552-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Increasing heart workload stimulates glycolysis by enhancing glucose transport and fructose-2,6-bisphosphate (Fru-2,6-P₂), the latter resulting from 6-phosphofructo-2-kinase (PFK-2) activation. Here, we investigated whether adenosine monophosphate (AMP)-activated protein kinase (AMPK) mediates PFK-2 activation in hearts submitted to increased workload. When heart work was increased, PFK-2 activity, Fru-2,6-P₂ content and glycolysis increased, whereas the AMP:adenosine triphosphate (ATP) and phosphocreatine/creatine (PCr:Cr) ratios, and AMPK activity remained unchanged. Wortmannin, the well-known phosphatidylinositol-3-kinase inhibitor, blocked the activation of protein kinase B and the increase in glycolysis and Fru-2,6-P₂ content induced by increased work. Therefore, the control of heart glycolysis by contraction differs from that in skeletal muscle where AMPK is involved.

【 授权许可】

Unknown