AMP-activated protein kinase regulates nicotinamide phosphoribosyl transferase expression in skeletal muscle

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Josef Brandauer, Sara Gry Vienberg, Marianne Agerholm Andersen, Stine Ringholm Jørgensen, Steve Risis, Per Larsen, Jonas Møller Kristensen, Christian Frøsig, Lotte Leick, Joachim Fentz, Sebastian Beck Jørgensen, Bente Kiens, Jørgen Wojtaszewski, Erik Richter, Juleen R Zierath, Laurie J. Goodyear, Henriette Pilegaard, Jonas Thue Treebak

Deacetylases such as sirtuins convert nicotinamide adenine dinucleotide (NAD) to nicotinamide (NAM). Nicotinamide phosphoribosyl transferase (Nampt) is the rate-limiting enzyme in the NAD salvage pathway responsible for converting NAM to NAD to maintain cellular redox state. Activation of AMP-activated protein kinase (AMPK) increases sirtuin activity by elevating NAD levels. As NAM directly inhibits sirtuins, increased Nampt activation or expression could be a metabolic stress response. Evidence suggests that AMPK regulates Nampt mRNA content, but whether repeated AMPK activation is necessary for increasing Nampt protein levels is unknown. To this end, we assessed whether exercise training- or 5-amino-1-β-D-ribofuranosyl-imidazole-4-carboxamide (AICAR)-mediated increases in skeletal muscle Nampt abundance are AMPK dependant. One-legged knee-extensor exercise training in humans increased Nampt protein by 16% (p
OriginalsprogEngelsk
TidsskriftJournal of Physiology
Vol/bind591
Sider (fra-til)5207-5220
Antal sider14
ISSN0022-3751
DOI
StatusUdgivet - 2013

Bibliografisk note

CURIS 2013 NEXS 227

ID: 49373796