Faculty Opinions recommendation of SIRT3 regulates mitochondrial fatty-acid oxidation by reversible enzyme deacetylation.

By A. Means. 2010

697 citations recorded by the source corpus.

Subfields: Geriatrics and Gerontology, Physiology

View Paper: https://www.semanticscholar.org/paper/3dcec26d8ffe3eb54ac9c1586100eccd7f69bcc1

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In Geriatrics and Gerontology

In Physiology

Citations in the corpus

Sirt3 Mediates Reduction of Oxidative Damage and Prevention of Age-related Hearing Loss under Caloric Restriction (2010, positive): “We also note that other mitochondrial effects of Sirt3, such as regulation of fatty acid oxidation (Hirschey et al., 2010) and modulation of complex I activity (Ahn, et al., 2008), are likely to contribute to themetabolic adaptations in response to CR.”
Acetyl-CoA and the Regulation of Metabolism: Mechanisms and Consequences (2015, positive): “In this model, failure of sirtuins to remove aberrant acylation modifications would hinder the function of effected proteins and consequently lead to dysfunctions in metabolism and susceptibility to disease [47,55,57].”
SIRT1 and other sirtuins in Metabolism (2013, positive): “Upon fasting or calorie restriction, SIRT3 protein level and activity are upregulated in mitochondria [26] to promote fatty acid oxidation via deacetylating long-chainspecific acyl-coenzyme A dehydrogenase (LCAD) [71].”
Exercise metabolism and the molecular regulation of skeletal muscle adaptation. (2013, positive): “The subsequent deacetylation of lysine residues on transcriptional regulators (Nemoto et al., 2005) andmitochondrial enzymes (Hirschey et al., 2010) allows the coupling of alterations in the cellular redox state to the adaptive changes in gene expression and cellular metabolism (Lagouge et al.,…”
β-Hydroxybutyrate (2017, positive): “Acetylation---and deacetylation by SIRT3---is widespread in mitochondria (105) and regulates the function of several mitochondrial enzymes, including HMGCS2 (118) and the long-chain acyl-CoA dehydrogenase (51).”
Circadian Clock NAD+ Cycle Drives Mitochondrial Oxidative Metabolism in Mice (2013, positive): “Clock Regulates Acetylation and Activity of Mitochondrial Oxidative Enzymes NAD is an important cofactor in oxidative metabolism, and NAD-dependent deacetylase activity affects protein acetylation in mitochondria (17, 25, 26).”
The Biochemistry and Physiology of Mitochondrial Fatty Acid β-Oxidation and Its Genetic Disorders. (2016, positive): “Hyperacetylation of LCAD in Sirt3 knockout (KO) mice reduced enzymatic activity (59, 60).”
Sirtuin Regulation of Mitochondria - Energy Production, Apoptosis, and Signaling (2010, positive): “Consistent with the hypothesis that nutrient stress alters sirtuin activity, a recent report identified significant metabolic abnormalities in Sirt3-/- mice during fasting [38].”
SIRT3 opposes reprogramming of cancer cell metabolism through HIF1α destabilization (2011, positive): “SIRT3 induces fatty acid oxidation during fasting in hepatocytes via deacetylation of LCAD (Hirschey et al., 2010).”
SIRTUIN 1 AND SIRTUIN 3: PHYSIOLOGICAL MODULATORS OF METABOLISM (2012, positive): “In this line, another study demonstrated that SIRT3 induced fatty acid oxidation through the deacetylation of long-chain acyl coenzyme A dehydrogenase (LCAD) and mice lacking SIRT3 showed lower fatty acid oxidation (136).”
NAD(H) and NADP(H) Redox Couples and Cellular Energy Metabolism (2018, positive): “Moreover, SIRT3 stimulates mitochondrial fatty acid oxidation by deacetylation and activation of longchain acyl coenzyme A dehydrogenase in murine liver (64).”
CD38 dictates age-related NAD decline and mitochondrial dysfunction through a SIRT3-dependent mechanism (2016, positive): “SIRT3 is one of the sirtuins localized in mitochondria that regulate key mitochondrial proteins important for metabolism and oxidative homeostasis such as LCAD, IDH2, SDH, and MnSOD (Finley et al., 2011; Hirschey et al., 2010; Shimazu et al., 2010; Tao et al., 2010; Yu et al., 2012).”