scholarly journals Sirtuin 3 overexpression preserves maximal sarco(endo)plasmic reticulum calcium ATPase activity in the skeletal muscle of mice subjected to high fat-high sucrose-feeding

2021 ◽  
Author(s):  
Christopher Oldfield ◽  
Teri L Moffatt ◽  
Vernon W Dolinsky ◽  
Todd A. Duhamel
Keyword(s):  
Skeletal Muscle ◽  
Gastrocnemius Muscle ◽  
Muscle Metabolism ◽  
Diabetic Mouse ◽  
High Fat ◽  
Protein Levels ◽  
Plasmic Reticulum ◽  
High Sucrose Feeding ◽  
And Function ◽  
High Sucrose

Sarco(endo)plasmic reticulum calcium (Ca<sup>2+</sup>) ATPase (SERCA) transports Ca<sup>2+</sup> in muscle. Impaired SERCA activity contributes to diabetic myopathy. Sirtuin (SIRT) 3 regulates muscle metabolism and function. However, it is unknown if SIRT3 regulates muscle SERCA activity. We determined if SIRT3 overexpression enhances SERCA activity in mouse gastrocnemius muscle and if SIRT3 overexpression preserves gastrocnemius SERCA activity in a model of type 2 diabetes, induced by high fat-high sucrose (HFHS)-feeding. We also determined if the acetylation status of SERCA proteins in mouse gastrocnemius is altered by SIRT3 overexpression or HFHS-feeding. Wild-type (WT) mice and SIRT3 transgenic (SIRT3<sub>TG</sub>) mice, overexpressing SIRT3 in skeletal muscle, were fed a standard- or HFHS-diet for 4-months. SIRT3<sub>TG</sub> and WT mice developed obesity and glucose intolerance after 4-months of HFHS-feeding. SERCA <i>V</i><sub>max</sub> was higher in gastrocnemius of SIRT3TG mice, compared to WT mice. HFHS-fed mice had lower SERCA1a protein levels and lower SERCA <i>V</i><sub>max</sub> in their gastrocnemius than control-fed mice. The decrease in SERCA <i>V</i><sub>max</sub> in gastrocnemius muscle due to HFHS-feeding was attenuated by SIRT3 overexpression in HFHS-fed SIRT3<sub>TG</sub> mice. SERCA1a and SERCA2a acetylation in mouse gastrocnemius was not altered by genotype or diet. These findings suggest SIRT3 overexpression improves SERCA function in diabetic mouse skeletal muscle.

P1-152 - High sucrose feeding-induced abnormalities of neuronal NO synthase in rat pancreatic bêta-cells and skeletal muscle

2006 ◽  
Vol 67 (5) ◽  
pp. 460-461
Author(s):  
K. Mezghenna ◽  
S. Péraldi-Roux ◽  
G. Dubois ◽  
M. Manteghetti ◽  
M. Tournier ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Beta Cells ◽  
Pancreatic Beta Cells ◽  
No Synthase ◽  
Neuronal No Synthase ◽  
Sucrose Feeding ◽  
High Sucrose Feeding ◽  
High Sucrose

scholarly journals An AMPK/Axin1-Rac1 signaling pathway mediates contraction-regulated glucose uptake in skeletal muscle cells

2020 ◽  
Vol 318 (3) ◽  
pp. E330-E342 ◽  
Author(s):  
Yingying Yue ◽  
Chang Zhang ◽  
Xuejiao Zhang ◽  
Shitian Zhang ◽  
Qian Liu ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Glucose Uptake ◽  
Signaling Pathway ◽  
Gastrocnemius Muscle ◽  
C2c12 Myotubes ◽  
Dependent Manner ◽  
Mouse Muscle ◽  
Protein Levels ◽  
Compound C ◽  
Skeletal Muscle Glucose Uptake

Contraction stimulates skeletal muscle glucose uptake predominantly through activation of AMP-activated protein kinase (AMPK) and Rac1. However, the molecular details of how contraction activates these signaling proteins are not clear. Recently, Axin1 has been shown to form a complex with AMPK and liver kinase B1 during glucose starvation-dependent activation of AMPK. Here, we demonstrate that electrical pulse-stimulated (EPS) contraction of C2C12 myotubes or treadmill exercise of C57BL/6 mice enhanced reciprocal coimmunoprecipitation of Axin1 and AMPK from myotube lysates or gastrocnemius muscle tissue. Interestingly, EPS or exercise upregulated total cellular Axin1 levels in an AMPK-dependent manner in C2C12 myotubes and gastrocnemius mouse muscle, respectively. Also, direct activation of AMPK with 5-aminoimidazole-4-carboxamide ribonucleotide treatment of C2C12 myotubes or gastrocnemius muscle elevated Axin1 protein levels. On the other hand, siRNA-mediated Axin1 knockdown lessened activation of AMPK in contracted myotubes. Further, AMPK inhibition with compound C or siRNA-mediated knockdown of AMPK or Axin1 blocked contraction-induced GTP loading of Rac1, p21-activated kinase phosphorylation, and contraction-stimulated glucose uptake. In summary, our results suggest that an AMPK/Axin1-Rac1 signaling pathway mediates contraction-stimulated skeletal muscle glucose uptake.

Incorporation and utilization of [3-13C]lactate and [1,2-13C]acetate by rat skeletal muscle

1999 ◽  
Vol 86 (6) ◽  
pp. 2077-2089 ◽  
Author(s):  
Loren A. Bertocci ◽  
Barbara F. Lujan
Keyword(s):  
Skeletal Muscle ◽  
Contractile Activity ◽  
Muscle Metabolism ◽  
Resonance Spectroscopy ◽  
Entry And Exit ◽  
Normal Muscle ◽  
Internal Organs ◽  
Indirect Discrimination ◽  
Simple Carbohydrates ◽  
And Function

Skeletal muscle can utilize many different substrates, and traditional methodologies allow only indirect discrimination between oxidative and nonoxidative uptake of substrate, possibly with contamination by metabolism of other internal organs. Our goal was to apply 1H- and13C-nuclear magnetic resonance spectroscopy to monitor the patterns of [3-13C]lactate and [1,2-13C]acetate (model of simple carbohydrates and fats, respectively) utilization in resting vs. contracting muscle extracts of the isolated perfused rat hindquarter. Total metabolite concentrations were measured by using NADH-linked fluorometric assays. Fractional oxidation of [3-13C]lactate was unchanged by contraction despite vascular endogenous lactate accumulation. Although label accumulated in several citric acid cycle (CAC) intermediates, contraction did not increase the concentration of CAC intermediates in any muscle extracts. We conclude that 1) the isolated rat hindquarter is a viable, well-controlled model for measuring skeletal muscle13C-labeled substrate utilization; 2) lactate is readily oxidized even during contractile activity; 3) entry and exit from the CAC, via oxidative and nonoxidative pathways, is a component of normal muscle metabolism and function; and 4) there are possible differences between gastrocnemius and soleus muscles in utilization of nonoxidative pathways.

Effect of respiratory alkalosis on skeletal muscle metabolism in the dog

1985 ◽  
Vol 58 (2) ◽  
pp. 658-664 ◽  
Author(s):  
A. G. Brice ◽  
H. G. Welch
Keyword(s):  
Skeletal Muscle ◽  
Hind Limb ◽  
Gastrocnemius Muscle ◽  
Minute Ventilation ◽  
Lactate Concentration ◽  
Muscle Metabolism ◽  
Respiratory Alkalosis ◽  
Whole Body ◽  
Venous Blood Flow ◽  
Skeletal Muscle Metabolism

These experiments were conducted to determine whether changes in skeletal muscle metabolism contribute to the previously reported increase in whole-body O2 uptake (VO2) during respiratory alkalosis. The hind-limb and gastrocnemius-plantaris preparations in anesthetized and paralyzed dogs were used. VO2 of the hindlimb and gastrocnemius muscle was calculated from measurements of venous blood flow and arterial and venous O2 concentrations (Van Slyke analysis). Whole-body VO2 was measured by the open-circuit method. Minute ventilation (hence blood gases and pH) was controlled by a mechanical respirator. Whole-body, hind-limb, and gastrocnemius muscle VO2 increased 14, 19, and 20%, respectively, during alkalosis (P less than 0.05). In all experiments, arterial lactate concentration increased significantly (P less than 0.05) during alkalosis. A positive venoarterial lactate difference across muscle during alkalosis indicated that skeletal muscle is a source of the elevated blood lactate. We concluded that VO2 of resting skeletal muscle is increased during states of respiratory alkalosis and that this increase can account for much of the increase in whole-body VO2.

scholarly journals Muscle RANK is a key regulator of Ca2+ storage, SERCA activity, and function of fast-twitch skeletal muscles

2016 ◽  
Vol 310 (8) ◽  
pp. C663-C672 ◽  
Author(s):  
Sébastien S. Dufresne ◽  
Nicolas A. Dumont ◽  
Antoine Boulanger-Piette ◽  
Val A. Fajardo ◽  
Daniel Gamu ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Osteoclast Differentiation ◽  
Nuclear Factor Κb ◽  
Skeletal Muscle Function ◽  
Inotropic Effects ◽  
Plasmic Reticulum ◽  
Receptor Activator ◽  
Slow Twitch ◽  
And Function ◽  
Fast Twitch

Receptor-activator of nuclear factor-κB (RANK), its ligand RANKL, and the soluble decoy receptor osteoprotegerin are the key regulators of osteoclast differentiation and bone remodeling. Here we show that RANK is also expressed in fully differentiated myotubes and skeletal muscle. Muscle RANK deletion has inotropic effects in denervated, but not in sham, extensor digitorum longus (EDL) muscles preventing the loss of maximum specific force while promoting muscle atrophy, fatigability, and increased proportion of fast-twitch fibers. In denervated EDL muscles, RANK deletion markedly increased stromal interaction molecule 1 content, a Ca2+ sensor, and altered activity of the sarco(endo)plasmic reticulum Ca2+-ATPase (SERCA) modulating Ca2+ storage. Muscle RANK deletion had no significant effects on the sham or denervated slow-twitch soleus muscles. These data identify a novel role for RANK as a key regulator of Ca2+ storage and SERCA activity, ultimately affecting denervated skeletal muscle function.

scholarly journals Female PAPP-A knockout mice are resistant to metabolic dysfunction induced by high-fat/high-sucrose feeding at middle age

AGE ◽  
2015 ◽  
Vol 37 (3) ◽  
Author(s):  
Cristal M. Hill ◽  
Oge Arum ◽  
Ravneet K. Boparai ◽  
Feiya Wang ◽  
Yimin Fang ◽  
...  
Keyword(s):  
Knockout Mice ◽  
Middle Age ◽  
Metabolic Dysfunction ◽  
High Fat ◽  
Sucrose Feeding ◽  
High Sucrose Feeding ◽  
High Sucrose

Protein catabolism and impairment of skeletal muscle insulin signalling in heart failure

2010 ◽  
Vol 119 (11) ◽  
pp. 465-466 ◽  
Author(s):  
P. Christian Schulze
Keyword(s):  
Heart Failure ◽  
Skeletal Muscle ◽  
Muscle Protein ◽  
Insulin Signalling ◽  
Muscle Metabolism ◽  
Exercise Intolerance ◽  
Skeletal Muscle Protein ◽  
Glucose And Lipid Metabolism ◽  
Muscle Protein Metabolism ◽  
And Function

Derangements in systemic and local metabolism develop in patients with CHF [chronic HF (heart failure)] and contribute to the progression of the disease. Impaired skeletal muscle metabolism, morphology and function leading to exercise intolerance are hallmarks of the syndrome of CHF. These changes result in abnormal glucose and lipid metabolism, and the associated insulin resistance, which contribute to progression of skeletal muscle catabolism and development of muscle atrophy in patients with advanced HF. In the present issue of Clinical Science, Toth and co-workers demonstrate the impairment of skeletal muscle protein metabolism in patients with HF, and specifically show an impaired anabolic response in the skeletal muscle of these patients following a period of nutritional deficiency.

Short-chain fatty acids as potential regulators of skeletal muscle metabolism and function

2020 ◽  
Vol 2 (9) ◽  
pp. 840-848 ◽  
Author(s):  
James Frampton ◽  
Kevin G. Murphy ◽  
Gary Frost ◽  
Edward S. Chambers
Keyword(s):  
Skeletal Muscle ◽  
Fatty Acids ◽  
Muscle Metabolism ◽  
Short Chain Fatty Acids ◽  
Short Chain ◽  
Skeletal Muscle Metabolism ◽  
And Function ◽  
Chain Fatty Acids

scholarly journals A comparative study on the effects of high-fat diet and endurance training on the PGC-1α-FNDC5/irisin pathway in obese and nonobese male C57BL/6 mice

2018 ◽  
Vol 43 (7) ◽  
pp. 651-662 ◽  
Author(s):  
Fatemeh Kazeminasab ◽  
Sayed Mohammad Marandi ◽  
Kamran Ghaedi ◽  
Zahra Safaeinejad ◽  
Fahimeh Esfarjani ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Endurance Training ◽  
Messenger Rna ◽  
Muscle Protein ◽  
Exercise Session ◽  
Mrna Levels ◽  
Skeletal Muscle Protein ◽  
High Fat ◽  
Low Fat ◽  
Protein Levels

The present study was performed to clarify how a combined exercise/diet treatment could affect the expression level of the muscle fibronectin type III domain containing 5 (Fndc5) with respect to body fat mass. Male C57BL/6 mice were divided into 2 groups including low-fat (LF) and high-fat (HF) diets for 12 weeks. Then, LF fed (nonobese) and HF fed mice (obese) were divided into the following 4 groups: HF-Exercise, HF-Sedentary, LF-Exercise, and LF-Sedentary. The exercise group exercised on a motor-driven treadmill for 45 min/day, 5 days/week for 8 weeks. Mice were sacrificed 24 h after the final exercise session. Gastrocnemius muscle and the visceral adipose tissue were excised and frozen for the assessment of proliferator-activated receptor gamma coactivator 1 alpha (Pgc-1α) and Fndc5 messenger RNA (mRNA) and protein levels. Data indicated that protein level of muscle PGC-1α was decreased in HF versus LF groups and in obese versus nonobese mice. Moreover, Fndc5 mRNA levels were increased in the muscle tissue of HF versus LF groups and in obese versus nonobese mice. Also, in the gastrocnemius skeletal muscle, protein levels of FNDC5 were significantly higher in the HF fed mice, as compared with their low-fat fed counterparts, similar to what was observed for exercised versus sedentary mice. Overall, we found that the HF diet increased Fndc5 transcript levels in the skeletal muscle, but exercise had a minimal effect on the transcript level of Fndc5, whereas endurance training increased the protein content of FNDC5 in the skeletal muscle.

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