5'AMP-activated protein kinase (AMPK)之主要功能為細胞能量狀態的感測者,並調節細胞代謝途徑之運作。運動或肌肉收縮可提高細胞內AMP/ATP之比值,使AMPK產生異位調控作用並提升被LKB1 (AMPKK)活化的程度;AMPK活化後,會啓動eNOS-NO-cGMP-PKG、p38MAPK等訊息系統增加GLUT4的轉位與活化,增加葡萄糖吸收能力。此外,長期運動訓練可能亦透過重複活化AMPK訊息系統,提高CaMK-IV與PGC-1α基因與蛋白質表現並調節下游轉錄因子表現,同時亦活化eNOS-NO訊息,進而引起肌肉粒腺體增生、GLUT4蛋白合成、肝醣儲存量提高、微血管增生與肌纖維型態轉變等訓練適應效應。
5'-AMP-activated protein kinase (AMPK) plays a central role as the intracellular energy sensor, and regulates various cellular metabolic pathways. Both exercise and muscle contraction, which result in the elevation of the ratio of AMP and ATP, cause the conformation change and allosteric regulation of AMPK molecule; then AMPK can be activated obviously by the upstream regulator LKB1 (AMPKK). After AMPK activated, AMPK is able to phosphorylate eNOS-NO-cGMP-PKG and p38MAPK signaling systems to induce GLUT4 containing vesicles translocation and activation, which enhance skeletal muscle glucose uptake. Moreover, exercise training-induced physiological adaptations might be mediated by AMPK signaling. It has been shown that repeated AMPK activation elevates the gene and protein level of CaMK-IV and PGC-1α, then initiates several downstream gene transcription factors activation and expression; simultaneously, AMPK also causes eNOS-NO signaling activation. It thus appears that exercise training induces muscle glycogen storage, angiogenesis, fiber type transformation, GLUT4 content, and mitochondrial biogenesis though the above AMPK-activated intracellular pathways.