AMP-activated protein kinase regulates nicotinamide phosphoribosyl transferase expression in skeletal muscle
Research output: Contribution to journal › Journal article › Research › peer-review
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
Original language | English |
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Journal | Journal of Physiology |
Volume | 591 |
Pages (from-to) | 5207-5220 |
Number of pages | 14 |
ISSN | 0022-3751 |
DOIs | |
Publication status | Published - 2013 |
ID: 49373796