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NADH inhibition of SIRT1 links energy state to transcription during time-restricted feeding.

Nature metabolism (2021-12-15)
Daniel C Levine, Hsin-Yu Kuo, Hee-Kyung Hong, Jonathan Cedernaes, Chelsea Hepler, Alexandra G Wright, Meredith A Sommars, Yumiko Kobayashi, Biliana Marcheva, Peng Gao, Olga R Ilkayeva, Chiaki Omura, Kathryn M Ramsey, Christopher B Newgard, Grant D Barish, Clara Bien Peek, Navdeep S Chandel, Milan Mrksich, Joseph Bass
RESUMEN

In mammals, circadian rhythms are entrained to the light cycle and drive daily oscillations in levels of NAD+, a cosubstrate of the class III histone deacetylase sirtuin 1 (SIRT1) that associates with clock transcription factors. Although NAD+ also participates in redox reactions, the extent to which NAD(H) couples nutrient state with circadian transcriptional cycles remains unknown. Here we show that nocturnal animals subjected to time-restricted feeding of a calorie-restricted diet (TRF-CR) only during night-time display reduced body temperature and elevated hepatic NADH during daytime. Genetic uncoupling of nutrient state from NADH redox state through transduction of the water-forming NADH oxidase from Lactobacillus brevis (LbNOX) increases daytime body temperature and blood and liver acyl-carnitines. LbNOX expression in TRF-CR mice induces oxidative gene networks controlled by brain and muscle Arnt-like protein 1 (BMAL1) and peroxisome proliferator-activated receptor alpha (PPARα) and suppresses amino acid catabolic pathways. Enzymatic analyses reveal that NADH inhibits SIRT1 in vitro, corresponding with reduced deacetylation of SIRT1 substrates during TRF-CR in vivo. Remarkably, Sirt1 liver nullizygous animals subjected to TRF-CR display persistent hypothermia even when NADH is oxidized by LbNOX. Our findings reveal that the hepatic NADH cycle links nutrient state to whole-body energetics through the rhythmic regulation of SIRT1.

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Millipore
Microesferas magnéticas anti-FLAG® M2, affinity isolated antibody
Sigma-Aldrich
Anticuerpo anti-Sirt1(Sir2), Upstate®, from rabbit
Sigma-Aldrich
Anticuerpo anti-acetil-histona H4 (Lys16), Upstate®, from rabbit
Sigma-Aldrich
Anti-BMAL1, from guinea pig