title: AMP-activated protein kinase and chemotransduction in the carotid body.
abstract: AMP-activated protein kinase (AMPK) is a key component of a kinase cascade that regulates energy balance at the cellular level. Our recent research has raised the possibility that AMPK may also function to couple hypoxic inhibition of mitochondrial oxidative phosphorylation to O(2)-sensitive K(+) channel inhibition and hence underpin carotid body type I cell excitation. Thus, in addition to maintaining the cellular energy state AMPK may act as the primary metabolic sensor and effector of hypoxic chemotransduction in type I cells. These findings provide a unifying link between two previously separate theories pertaining to O(2)-sensing in the carotid body, namely the 'membrane hypothesis' and the 'mitochondrial hypothesis'. Furthermore, our data suggest that in addition to its effects at the cellular level the AMPK signalling cascade can mediate vital physiological mechanisms essential for meeting the metabolic needs of the whole organism.
authors.affiliation: Department of Neuroscience, Wright State University, Dayton, OH 45435, USA.
authors.forename: Christopher N
authors.initials: CN
authors.lastname: Wyatt
authors.forename: A Mark
authors.initials: AM
authors.lastname: Evans
mesh_terms: D055372:AMP-Activated Protein Kinases; D000818:Animals; D002344:Carotid Body / Q000502:physiology*; D002462:Cell Membrane / Q000378:metabolism; D006801:Humans; D000860:Hypoxia / Q000378:metabolism / Q000503:physiopathology; D040542:Mechanotransduction, Cellular / Q000502:physiology*; D008928:Mitochondria / Q000378:metabolism; D008954:Models, Biological; D009097:Multienzyme Complexes / Q000378:metabolism*; D015221:Potassium Channels / Q000378:metabolism; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism*; D015398:Signal Transduction / Q000502:physiology*
chemical_list: D009097:Multienzyme Complexes; D015221:Potassium Channels; D017346:Protein Serine-Threonine Kinases; D055372:AMP-Activated Protein Kinases