scholarly journals The effect of weight reduction on skeletal muscle UCP2 and UCP3 mRNA expression and UCP3 protein content in Type II diabetic subjects

Diabetologia ◽  
2000 ◽  
Vol 43 (11) ◽  
pp. 1408-1416 ◽  
Author(s):  
P. Schrauwen ◽  
G. Schaart ◽  
W. H. M. Saris ◽  
L. J. Slieker ◽  
J. F. C. Glatz ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Mrna Expression ◽  
Protein Content ◽  
Weight Reduction ◽  
Type Ii

Global and targeted gene expression and protein content in skeletal muscle of young men following short-term creatine monohydrate supplementation

2008 ◽  
Vol 32 (2) ◽  
pp. 219-228 ◽  
Author(s):  
Adeel Safdar ◽  
Nicholas J. Yardley ◽  
Rodney Snow ◽  
Simon Melov ◽  
Mark A. Tarnopolsky
Keyword(s):  
Gene Expression ◽  
Skeletal Muscle ◽  
Mrna Expression ◽  
Protein Content ◽  
Cellular Response ◽  
Glycogen Synthesis ◽  
Creatine Monohydrate ◽  
Fat Free Mass ◽  
Cell Swelling ◽  
Short Term

Creatine monohydrate (CrM) supplementation has been shown to increase fat-free mass and muscle power output possibly via cell swelling. Little is known about the cellular response to CrM. We investigated the effect of short-term CrM supplementation on global and targeted mRNA expression and protein content in human skeletal muscle. In a randomized, placebo-controlled, crossover, double-blind design, 12 young, healthy, nonobese men were supplemented with either a placebo (PL) or CrM (loading phase, 20 g/day × 3 days; maintenance phase, 5 g/day × 7 days) for 10 days. Following a 28-day washout period, subjects were put on the alternate supplementation for 10 days. Muscle biopsies of the vastus lateralis were obtained and were assessed for mRNA expression (cDNA microarrays + real-time PCR) and protein content (Kinetworks KPKS 1.0 Protein Kinase screen). CrM supplementation significantly increased fat-free mass, total body water, and body weight of the participants ( P < 0.05). Also, CrM supplementation significantly upregulated (1.3- to 5.0-fold) the mRNA content of genes and protein content of kinases involved in osmosensing and signal transduction, cytoskeleton remodeling, protein and glycogen synthesis regulation, satellite cell proliferation and differentiation, DNA replication and repair, RNA transcription control, and cell survival. We are the first to report this large-scale gene expression in the skeletal muscle with short-term CrM supplementation, a response that suggests changes in cellular osmolarity.

Interactions between the consumption of a high-fat diet and fasting in the regulation of fatty acid oxidation enzyme gene expression: an evaluation of potential mechanisms

2011 ◽  
Vol 300 (2) ◽  
pp. R212-R221 ◽  
Author(s):  
Bruce C. Frier ◽  
René L. Jacobs ◽  
David C. Wright
Keyword(s):  
Skeletal Muscle ◽  
Fatty Acid ◽  
Mrna Expression ◽  
Protein Content ◽  
Fatty Acid Oxidation ◽  
P38 Mapk ◽  
Acid Oxidation ◽  
Plasma Fatty Acid ◽  
High Fat ◽  
Fed State

The consumption of high-fat diets (HFDs) and fasting are known to increase the expression of enzymes involved in fatty acid oxidation (FAO). However, it has been reported that the ability of physiological stressors to induce enzymes of FAO in skeletal muscle is blunted with obesity. In this regard, we sought to explore the effects and potential mechanisms of an HFD on the expression of FAO enzymes in the fed and fasted state. The consumption of an HFD increased the mRNA expression or protein content of medium-chain acyl-CoA dehydrogenase (MCAD), uncoupling protein-3 (UCP3), and pyruvate dehydrogenase kinase 4 (PDK4) in the fed state. Fasting increased the mRNA expression of PDK4, MCAD, and UCP-3, and the protein content of UCP-3 in chow but not HFD rats. HFDs did not increase carnitine palmitoyl transfer-1 (CPT-1) mRNA levels in the fed state and the effects of fasting were markedly reduced compared with chow-fed rats. The expression of peroxisome-proliferator-activated receptor-γ coactivator-1β (PGC-1β) was increased in muscle from HFD rats in the fed state, while PGC-1-related coactivator (PRC) was increased with fasting in chow-fed but not HFD rats. Plasma fatty acid levels were elevated in the fed state from HFD rats but not increased further with fasting, whereas fasting increased plasma fatty acids in chow-fed animals. Fasting-mediated increases in plasma epinephrine, and the activation of PKA and AMPK in skeletal muscle were similar between chow and HFD rats. p38 MAPK phosphorylation was increased with fasting in chow-fed but not HFD rats. Our findings suggest that a blunted effect of fasting on the induction of PDK4, MCAD, and UCP3 in skeletal muscle from HFD rats is likely a result of already elevated levels of these enzymes, the induction of which is associated with increases in plasma fatty acid and PGC-1β. On the other hand, a blunted induction of PRC and CPT-1 mRNA may be explained by decreases in p38 MAPK signaling.

scholarly journals Short-term intense exercise training reduces stress markers and alters the transcriptional response to exercise in skeletal muscle

2017 ◽  
Vol 312 (3) ◽  
pp. R426-R433 ◽  
Author(s):  
J. Matthew Hinkley ◽  
Adam R. Konopka ◽  
Miranda K. Suer ◽  
Matthew P. Harber
Keyword(s):  
Skeletal Muscle ◽  
Exercise Training ◽  
Protein Stability ◽  
Mrna Expression ◽  
Protein Content ◽  
Cellular Stress ◽  
Transcriptional Response ◽  
Cycling Performance ◽  
Short Term ◽  
Exercise Induced

The purpose of this investigation was to examine the influence of short-term intense endurance training on cycling performance, along with the acute and chronic signaling responses of skeletal muscle stress and stability markers. Ten recreationally active subjects (25 ± 2 yr, 79 ± 3 kg, 47 ± 2 ml·kg−1·min−1) were studied before and after a 12-day cycling protocol to examine the effects of short-term intense (70–100% V̇o2max) exercise training on resting and exercise-induced regulation of molecular factors related to skeletal muscle cellular stress and protein stability. Skeletal muscle biopsies were taken at rest and 3 h following a 20-km cycle time trial on days 1 and 12 to measure mRNA expression and protein content. Training improved ( P < 0.05) cycling performance by 5 ± 1%. Protein oxidation was unaltered on day 12, while resting SAPK/JNK phosphorylation was reduced ( P < 0.05), suggesting a reduction in cellular stress. The maintenance in the myocellular environment may be due to synthesis of cytoprotective markers, along with enhanced degradation of damage proteins, as training tended ( P < 0.10) to increase resting protein content of manganese superoxide dismutase and heat shock protein 70 (HSP70), while mRNA expression of MuRF-1 was elevated ( P < 0.05). Following training ( day 12), the acute exercise-induced transcriptional response of TNF-α, NF-κB, MuRF-1, and PGC1α was attenuated ( P < 0.05) compared with day 1. Collectively, these data suggest that short-term intense training enhances protein stability, creating a cellular environment capable of resistance to exercise-induced stress, which may be favorable for adaptation.

Alterations in mRNA and protein levels of metalloproteinases-2, -9, and -14 and tissue inhibitor of metalloproteinase-2 responses to traumatic skeletal muscle injury

2009 ◽  
Vol 297 (6) ◽  
pp. C1501-C1508 ◽  
Author(s):  
Brian R. Barnes ◽  
Eric R. Szelenyi ◽  
Gordon L. Warren ◽  
Maria L. Urso
Keyword(s):  
Skeletal Muscle ◽  
Mrna Expression ◽  
Protein Content ◽  
Muscle Injury ◽  
Tissue Inhibitor Of Metalloproteinase ◽  
Mrna Levels ◽  
Tissue Inhibitor ◽  
Skeletal Muscle Injury ◽  
Protein Levels ◽  
Sequence Of Events

This study characterizes the temporal relationship of membrane type-1 matrix metalloproteinase (MT1-MMP) and tissue inhibitor of metalloproteinase-2 (TIMP-2) expression in skeletal muscle following injury. Tibialis anterior (TA) muscles from 60 mice were exposed and injured by applying a cold steel probe (−79°C) to the muscle for 10 s. Thereafter, TA muscles from uninjured and injured legs were collected at 3, 10, 24, 48, and 72 h postinjury for analysis of local MT1-MMP, TIMP-2, and matrix metalloproteinases-2 and -9 (MMP-2 and MMP-9) mRNA and protein content via quantitative RT-PCR, immunoblotting, zymography, and immunofluorescence. All data are expressed as fold change of injured leg vs. uninjured leg. MT1-MMP mRNA levels were decreased significantly at 48 and 72 h postinjury by ∼9- and 21-fold, respectively ( P < 0.01). Both TIMP-2 and MMP-2 mRNA expression significantly decreased in the injured leg by ∼4- to 10-fold at 10–72 h postinjury ( P < 0.01). MMP-9 mRNA expression was significantly increased at 10, 24, and 48 h postinjury by 6- ( P < 0.05), 25-, and 12-fold ( P < 0.01), respectively. Protein content of latent (63 kDa) MT1-MMP was decreased at 48 and 72 h postinjury by ∼2-fold ( P < 0.01). Content of the soluble (50 kDa) fragment of MT1-MMP was significantly increased by ∼17-, 25-, and 67-fold at 24 ( P < 0.05), 48, and 72 h ( P < 0.01) postinjury, respectively. TIMP-2 protein levels diminished from 3 to 48 h postinjury by 1.5-fold to 1.8-fold ( P < 0.01), before returning to baseline levels at 72 h postinjury. Zymography revealed visual increases in gelatinase activity in molecular weight regions corresponding to MMP-9 and MMP-2. In conclusion, skeletal muscle injury initiates a sequence of events in the MT1-MMP proteolytic cascade resulting in elevated levels of the soluble (50 kDa) fragment of MT1-MMP, which could enhance pericellular extracellular matrix remodeling.

The effects of apelin treatment on skeletal muscle mitochondrial content

2009 ◽  
Vol 297 (6) ◽  
pp. R1761-R1768 ◽  
Author(s):  
Bruce C. Frier ◽  
Deon B. Williams ◽  
David C. Wright
Keyword(s):  
Skeletal Muscle ◽  
Mrna Expression ◽  
Protein Content ◽  
Citrate Synthase ◽  
Uncoupling Protein ◽  
Whole Body ◽  
Mitochondrial Content ◽  
Ampk Signaling ◽  
Male Wistar Rats ◽  
Whole Body Metabolism

Adipose tissue is recognized as a key player in the regulation of whole body metabolism. Apelin, is a recently identified adipokine that when given to mice results in increases in skeletal muscle uncoupling protein 3 (UCP3) content. Similarly, acute apelin treatment has been shown to increase the activity of 5′-AMP-activated protein kinase (AMPK), a reputed mediator of skeletal muscle mitochondrial biogenesis. Given these findings, we sought to determine the effects of apelin on skeletal muscle mitochondrial content. Male Wistar rats were given daily intraperitoneal injections of apelin-13 (100 nmol/kg) for 2 wk. We made the novel observation that the activities of citrate synthase, cytochrome c oxidase, and β-hydroxyacyl coA dehydrogenase (βHAD) were increased in triceps but not heart and soleus muscles from apelin-treated rats. When confirming these results we found that both nuclear and mitochondrial-encoded subunits of the respiratory chain were increased in triceps from apelin-treated rats. Similarly, apelin treatment increased the protein content of components of the mitochondrial import and assembly pathway. The increases in mitochondrial marker proteins were associated with increases in proliferator-activated receptor-γ coactivator-1 (PGC-1β) but not PGC-1α or Pgc-1-related co-activator (PRC) mRNA expression. Chronic and acute apelin treatment did not increase the protein content and/or phosphorylation status of AMPK and its downstream substrate acetyl-CoA carboxylase. These findings are the first to demonstrate that apelin treatment can induce skeletal muscle mitochondrial content. Given the lack of an effect of apelin on AMPK signaling and PGC-1α mRNA expression, these results suggest that apelin increases skeletal muscle mitochondrial content through a mechanism that is distinct from that of more robust physiological stressors.

scholarly journals 17beta-estradiol upregulates the expression of peroxisome proliferator-activated receptor alpha and lipid oxidative genes in skeletal muscle

2003 ◽  
Vol 31 (1) ◽  
pp. 37-45 ◽  
Author(s):  
SE Campbell ◽  
KA Mehan ◽  
RJ Tunstall ◽  
MA Febbraio ◽  
D Cameron-Smith
Keyword(s):  
Skeletal Muscle ◽  
Mrna Expression ◽  
Protein Content ◽  
Pyruvate Dehydrogenase Kinase ◽  
Peroxisome Proliferator ◽  
Sprague Dawley ◽  
Peroxisome Proliferator Activated Receptor ◽  
Skeletal Muscle Lipid ◽  
Peroxisome Proliferator Activated Receptors ◽  
Cpt I

This study examined the actions of 17beta-estradiol (E(2)) and progesterone on the regulation of the peroxisome proliferator-activated receptors (PPARalpha and PPARgamma) family of nuclear transcription factors and the mRNA abundance of key enzymes involved in fat oxidation, in skeletal muscle. Specifically, carnitine palmitoyltransferase I (CPT I), beta-3-hydroxyacyl CoA dehydrogenase (beta-HAD), and pyruvate dehydrogenase kinase 4 (PDK4) were examined. Sprague-Dawley rats were ovariectomized and treated with placebo (Ovx), E(2), progesterone, or both hormones in combination (E+P). Additionally, sham-operated rats were treated with placebo (Sham) to serve as controls. Hormone (or vehicle only) delivery was via time release pellets inserted at the time of surgery, 15 days prior to analysis. E(2) treatment increased PPARalpha mRNA expression and protein content (P<0.05), compared with Ovx treatment. E(2) also resulted in upregulated mRNA of CPT I and PDK4 (P<0.05). PPARgamma mRNA expression was also increased (P<0.05) by E(2) treatment, although protein content remained unaltered. These data demonstrate the novel regulation of E(2) on PPARalpha and genes encoding key proteins that are pivotal in regulating skeletal muscle lipid oxidative flux.

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