AMP-activated protein kinase regulates nicotinamide phosphoribosyl transferase expression in skeletal muscle
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AMP-activated protein kinase regulates nicotinamide phosphoribosyl transferase expression in skeletal muscle. / Brandauer, Josef; Vienberg, Sara Gry; Andersen, Marianne Agerholm; Jørgensen, Stine Ringholm; Risis, Steve; Larsen, Per; Kristensen, Jonas Møller; Frøsig, Christian; Leick, Lotte; Fentz, Joachim; Jørgensen, Sebastian Beck; Kiens, Bente; Wojtaszewski, Jørgen; Richter, Erik; Zierath, Juleen R; Goodyear, Laurie J.; Pilegaard, Henriette; Treebak, Jonas Thue.
I: Journal of Physiology, Bind 591, 2013, s. 5207-5220.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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T1 - AMP-activated protein kinase regulates nicotinamide phosphoribosyl transferase expression in skeletal muscle
AU - Brandauer, Josef
AU - Vienberg, Sara Gry
AU - Andersen, Marianne Agerholm
AU - Jørgensen, Stine Ringholm
AU - Risis, Steve
AU - Larsen, Per
AU - Kristensen, Jonas Møller
AU - Frøsig, Christian
AU - Leick, Lotte
AU - Fentz, Joachim
AU - Jørgensen, Sebastian Beck
AU - Kiens, Bente
AU - Wojtaszewski, Jørgen
AU - Richter, Erik
AU - Zierath, Juleen R
AU - Goodyear, Laurie J.
AU - Pilegaard, Henriette
AU - Treebak, Jonas Thue
N1 - CURIS 2013 NEXS 227
PY - 2013
Y1 - 2013
N2 - 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
AB - 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
U2 - 10.1113/jphysiol.2013.259515
DO - 10.1113/jphysiol.2013.259515
M3 - Journal article
C2 - 23918774
VL - 591
SP - 5207
EP - 5220
JO - The Journal of Physiology
JF - The Journal of Physiology
SN - 0022-3751
ER -
ID: 49373796