Correlation Engine 2.0
Clear Search sequence regions


  • acetyl- coa (3)
  • amp (13)
  • Ampd1 (4)
  • AMPK (7)
  • atp (4)
  • cells (1)
  • homeostasis (1)
  • imp (1)
  • male (1)
  • mice knockout (1)
  • nucleotides (3)
  • rats (1)
  • rats wistar (1)
  • skeletal muscle (4)
  • transport (1)
  • vitro (1)
  • Sizes of these terms reflect their relevance to your search.

    AMP-activated protein kinase (AMPK) plays a central role in regulating metabolism and energy homeostasis. It achieves its function by sensing fluctuations in the AMP:ATP ratio. AMP deaminase (AMPD) converts AMP into IMP, and the AMPD1 isoenzyme is expressed in skeletal muscles. Here, effects of pharmacological inhibition and genetic deletion of AMPD were examined in contracting skeletal muscles. Pharmacological AMPD inhibition potentiated rises in AMP, AMP:ATP ratio, AMPK Thr172, and acetyl-CoA carboxylase (ACC) Ser218 phosphorylation induced by electrical stimulation, without affecting glucose transport. In incubated extensor digitorum longus and soleus muscles from Ampd1 knockout mice, increases in AMP levels and AMP:ATP ratio by electrical stimulation were potentiated considerably compared with muscles from wild-type mice, whereas enhanced AMPK activation was moderate and only observed in soleus, suggesting control by factors other than changes in adenine nucleotides. AMPD inhibitors could be useful tools for enhancing AMPK activation in cells and tissues during ATP-depletion.

    Citation

    Catheline Plaideau, Yu-Chiang Lai, Samanta Kviklyte, Nadège Zanou, Lars Löfgren, Harriet Andersén, Didier Vertommen, Philippe Gailly, Louis Hue, Mohammad Bohlooly-Y, Stefan Hallén, Mark H Rider. Effects of pharmacological AMP deaminase inhibition and Ampd1 deletion on nucleotide levels and AMPK activation in contracting skeletal muscle. Chemistry & biology. 2014 Nov 20;21(11):1497-1510

    Expand section icon Mesh Tags

    Expand section icon Substances


    PMID: 25459662

    View Full Text