Phenformin and 5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside (AICAR) activation of AMP-activated protein kinase inhibits transepithelial Na+ transport across H441 lung cells

J Physiol. 2005 Aug 1;566(Pt 3):781-92. doi: 10.1113/jphysiol.2005.088674. Epub 2005 May 26.

Abstract

Active re-absorption of Na+ across the alveolar epithelium is essential to maintain lung fluid balance. Na+ entry at the luminal membrane is predominantly via the amiloride-sensitive Na+ channel (ENaC) down its electrochemical gradient. This gradient is generated and maintained by basolateral Na+ extrusion via Na+,K+-ATPase an energy-dependent process. Several kinases and factors that activate them are known to regulate these processes; however, the role of AMP-activated protein kinase (AMPK) in the lung is unknown. AMPK is an ultra-sensitive cellular energy sensor that monitors energy consumption and down-regulates ATP-consuming processes when activated. The biguanide phenformin has been shown to independently decrease ion transport processes, influence cellular metabolism and activate AMPK. The AMP mimetic drug 5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside (AICAR) also activates AMPK in intact cells. Western blotting revealed that both the alpha1 and alpha2 catalytic subunits of AMPK are present in Na+ transporting H441 human lung epithelial cells. Phenformin and AICAR increased AMPK activity in H441 cells in a dose-dependent fashion, stimulating the kinase maximally at 5-10 mm (P = 0.001, n = 3) and 2 mm (P < 0.005, n = 3), respectively. Both agents significantly decreased basal ion transport (measured as short circuit current) across H441 monolayers by approximately 50% compared with that of controls (P < 0.05, n = 4). Neither treatment altered the resistance of the monolayers. Phenformin and AICAR significantly reduced amiloride-sensitive transepithelial Na+ transport compared with controls (P < 0.05, n = 4). This was a result of both decreased Na+,K+-ATPase activity and amiloride-sensitive apical Na+ conductance. Transepithelial Na+ transport decreased with increasing concentrations of phenformin (0.1-10 mm) and showed a significant correlation with AMPK activity. Taken together, these results show that phenformin and AICAR suppress amiloride-sensitive Na+ transport across H441 cells via a pathway that includes activation of AMPK and inhibition of both apical Na+ entry through ENaC and basolateral Na+ extrusion via the Na+,K+-ATPase. These are the first studies to provide a cellular signalling mechanism for the action of phenformin on ion transport processes, and also the first studies showing AMPK as a regulator of Na+ absorption in the lung.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • AMP-Activated Protein Kinases
  • Aminoimidazole Carboxamide / administration & dosage
  • Aminoimidazole Carboxamide / analogs & derivatives*
  • Biological Transport, Active / drug effects
  • Biological Transport, Active / physiology
  • Cell Line
  • Dose-Response Relationship, Drug
  • Enzyme Activation
  • Humans
  • Lung / drug effects
  • Lung / metabolism*
  • Multienzyme Complexes / drug effects*
  • Multienzyme Complexes / metabolism*
  • Phenformin / administration & dosage*
  • Protein Serine-Threonine Kinases / drug effects*
  • Protein Serine-Threonine Kinases / metabolism*
  • Respiratory Mucosa / metabolism
  • Ribonucleotides / administration & dosage*
  • Sodium / metabolism*

Substances

  • Multienzyme Complexes
  • Ribonucleotides
  • Aminoimidazole Carboxamide
  • Sodium
  • Phenformin
  • PRKAA2 protein, human
  • Protein Serine-Threonine Kinases
  • AMP-Activated Protein Kinases
  • PRKAA1 protein, human
  • AICA ribonucleotide