scholarly journals Effect of Quercetin Treatment on Mitochondrial Biogenesis and Exercise-Induced AMP-Activated Protein Kinase Activation in Rat Skeletal Muscle

Nutrients ◽  
2020 ◽  
Vol 12 (3) ◽  
pp. 729 ◽  
Author(s):  
Keiichi Koshinaka ◽  
Asuka Honda ◽  
Hiroyuki Masuda ◽  
Akiko Sato
Keyword(s):  
Skeletal Muscle ◽  
Protein Kinase ◽  
Endurance Exercise ◽  
Mitochondrial Biogenesis ◽  
Exercise Performance ◽  
Term Therapy ◽  
High Dose ◽  
Rat Skeletal Muscle ◽  
Amp Activated Protein Kinase ◽  
Quercetin Treatment

The purpose of this study was to evaluate the effect of chronic quercetin treatment on mitochondrial biogenesis, endurance exercise performance and activation levels of AMP-activated protein kinase (AMPK) in rat skeletal muscle. Rats were assigned to a control or quercetin group and were fed for 7 days. Rats treated with quercetin showed no changes in the protein levels of citrate synthase or cytochrome C oxidase IV or those of sirtuin 1, peroxisome proliferator-activated receptor gamma coactivator-1α or phosphorylated AMPK. After endurance swimming exercise, quercetin-treated rats demonstrated no differences in blood and muscle lactate levels or glycogen utilization speed compared to control rats. These results indicate that quercetin treatment does not stimulate mitochondrial biogenesis in skeletal muscle and does not influence metabolism in a way that might enhance endurance exercise capacity. On the other hand, the AMPK phosphorylation level immediately after exercise was significantly lower in quercetin-treated muscles, suggesting that quercetin treatment might provide a disadvantage to muscle adaptation when administered with exercise training. The molecular results of this study indicate that quercetin treatment may not be advantageous for improving endurance exercise performance, at least after high-dose and short-term therapy.

AMP-activated protein kinase activity and glucose uptake in rat skeletal muscle

2001 ◽  
Vol 280 (5) ◽  
pp. E677-E684 ◽  
Author(s):  
Nicolas Musi ◽  
Tatsuya Hayashi ◽  
Nobuharu Fujii ◽  
Michael F. Hirshman ◽  
Lee A. Witters ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Protein Kinase ◽  
Glucose Uptake ◽  
Muscle Contractions ◽  
Treadmill Running ◽  
Dependent Manner ◽  
Rat Skeletal Muscle ◽  
Amp Activated Protein Kinase ◽  
Dose Dependent

The AMP-activated protein kinase (AMPK) has been hypothesized to mediate contraction and 5-aminoimidazole-4-carboxamide 1-β-d-ribonucleoside (AICAR)-induced increases in glucose uptake in skeletal muscle. The purpose of the current study was to determine whether treadmill exercise and isolated muscle contractions in rat skeletal muscle increase the activity of the AMPKα1 and AMPKα2 catalytic subunits in a dose-dependent manner and to evaluate the effects of the putative AMPK inhibitors adenine 9-β-d-arabinofuranoside (ara-A), 8-bromo-AMP, and iodotubercidin on AMPK activity and 3- O-methyl-d-glucose (3-MG) uptake. There were dose-dependent increases in AMPKα2 activity and 3-MG uptake in rat epitrochlearis muscles with treadmill running exercise but no effect of exercise on AMPKα1 activity. Tetanic contractions of isolated epitrochlearis muscles in vitro significantly increased the activity of both AMPK isoforms in a dose-dependent manner and at a similar rate compared with increases in 3-MG uptake. In isolated muscles, the putative AMPK inhibitors ara-A, 8-bromo-AMP, and iodotubercidin fully inhibited AICAR-stimulated AMPKα2 activity and 3-MG uptake but had little effect on AMPKα1 activity. In contrast, these compounds had absent or minimal effects on contraction-stimulated AMPKα1 and -α2 activity and 3-MG uptake. Although the AMPKα1 and -α2 isoforms are activated during tetanic muscle contractions in vitro, in fast-glycolytic fibers, the activation of AMPKα2-containing complexes may be more important in regulating exercise-mediated skeletal muscle metabolism in vivo. Development of new compounds will be required to study contraction regulation of AMPK by pharmacological inhibition.

Inactivation of acetyl-CoA carboxylase and activation of AMP-activated protein kinase in muscle during exercise

1996 ◽  
Vol 270 (2) ◽  
pp. E299-E304 ◽  
Author(s):  
W. W. Winder ◽  
D. G. Hardie
Keyword(s):  
Skeletal Muscle ◽  
Fatty Acid ◽  
Protein Kinase ◽  
Ammonium Sulfate ◽  
Quadriceps Muscle ◽  
Acid Oxidation ◽  
Acetyl Coa Carboxylase ◽  
Rat Skeletal Muscle ◽  
Malonyl Coa ◽  
Amp Activated Protein Kinase

Malonyl-CoA, an inhibitor of fatty acid oxidation in skeletal muscle mitochondria, decreases in rat skeletal muscle during exercise or in response to electrical stimulation. Regulation of rat skeletal muscle acetyl-CoA carboxylase (ACC), the enzyme that synthesizes malonyl-CoA, was studied in vitro and in vivo. Avidin-Sepharose affinity-purified ACC from hindlimb skeletal muscle was phosphorylated by purified liver AMP-activated protein kinase with a concurrent decrease in ACC activity. AMP-activated protein kinase was quantitated in resuspended ammonium sulfate precipitates of the fast-twitch red (type IIa fibers) region of the quadriceps muscle. Rats running on a treadmill at 21 m/min up a 15% grade show a 2.4-fold activation of AMP-activated protein kinase concurrently with a marked decrease in ACC activity in the resuspended ammonium sulfate precipitates at all citrate concentrations ranging from 0 to 20 mM. Malonyl-CoA decreased from a resting value of 1.85 +/- 0.29 to 0.50 +/- 0.09 nmol/g in red quadriceps muscle after 30 min of treadmill running. The activation of the AMP-activated protein kinase with consequent phosphorylation and inactivation of ACC may be one of the primary events in the control of malonyl-CoA and hence fatty acid oxidation during exercise.

scholarly journals Caffeine activates preferentially α1-isoform of 5′AMP-activated protein kinase in rat skeletal muscle

2011 ◽  
Vol 201 (2) ◽  
pp. 227-238 ◽  
Author(s):  
T. Egawa ◽  
T. Hamada ◽  
X. Ma ◽  
K. Karaike ◽  
N. Kameda ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Protein Kinase ◽  
Rat Skeletal Muscle ◽  
Amp Activated Protein Kinase

scholarly journals Effect of Short-Term Endurance Exercise on COX IV and PGC-1a mRNA Expression Levels in Rat Skeletal Muscle

2019 ◽  
Vol 12 (3) ◽  
pp. 1309-1316 ◽  
Author(s):  
Nova Sylviana ◽  
Christina Natalia ◽  
Hanna Goenawan ◽  
Yuni Susanti Pratiwi ◽  
Iwan Setiawan ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Mrna Expression ◽  
Endurance Exercise ◽  
Mitochondrial Biogenesis ◽  
Control Group ◽  
Muscle Adaptation ◽  
Rat Skeletal Muscle ◽  
Short Term ◽  
Expression Levels ◽  
Mrna Expression Levels

Endurance exercise induces specific skeletal muscle adaptation by increasing mitochondrial oxidative phosphorylation eficiency and mitochondrial biogenesis. Many previous studies suggesting both PGC-1a and COX IV as a potential biomarker of skeletal muscle adaptation induced by exercise. But most of them only studied the effect of long-term endurance exercise, whereas the effect of short-term exercise remains unclear. To investigate short-term physiological adaptation induced by endurance exercise on expression of COX IV and PGC-1a mRNA in rat skeletal muscle. Twenty healthy male Wistar rats (Rattus norvegicus) aged 10-11 weeks old were used in this experiment. Rats were randomly assigned into 4 groups based on the time period of exercise: 1) control (C; n=5), 2) three days of exercise (E3; n=5), 3) six days of exercise (E6; n=5), 4) fifteen days of exercise (E15; n=5). The exercise groups were run at 20m/s for 30 minutes on the rat treadmill and the stationary control group was only placed inside treadmill with the machines turned off. On the last day of exercise, the rats were sacrificed then RNA from skeletal muscle was extracted. COX IV and PGC-1a mRNA expressions were measured by Reverse Transcriptase PCR. The results showed that there were statistically significant differences of PGC-1a mRNA expression levels in both soleus (F(3,16)=3.740, ps=0.033) and gastrocnemius (F(3,16)=3.969, pg=0.027) muscles. The COX IV mRNA expression levels in soleus (F(3,16)=3.801, ps=0.031) and gastrocnemius (F(3,16)=5.429, ps=0.009) muscles were also significantly increased. There were significant increases of PGC-1a and COX IV expressions in fifteen days of exercise group compared to control group in both muscles. Short-term endurance exercise induced mitochondrial biogenesis marker and mitochondrial activity marker by increasing the PGC-1a and COX IV mRNA expression levels in rat skeletal muscle significantly following the time periods of exercise.

scholarly journals Muscle contractions, AICAR, and insulin cause phosphorylation of an AMPK-related kinase

2005 ◽  
Vol 289 (6) ◽  
pp. E986-E992 ◽  
Author(s):  
Jonathan S. Fisher ◽  
Jeong-Sun Ju ◽  
Peter J. Oppelt ◽  
Jill L. Smith ◽  
Atsushi Suzuki ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Protein Kinase ◽  
Protein Kinase B ◽  
Cross Reactivity ◽  
Muscle Contractions ◽  
Rt Pcr ◽  
Rat Skeletal Muscle ◽  
Apparent Increase ◽  
A Site ◽  
Amp Activated Protein Kinase

We hypothesized that AMP-activated protein kinase-related kinase 5 (ARK5)/novel kinase family 1 (NUAK1), an AMP-activated protein kinase (AMPK)-related kinase that has been found to be stimulated by protein kinase B (Akt), would be expressed in rat skeletal muscle and activated by electrically elicited contractions, 5-aminoimidazole-4-carboxamide-1-β-d-ribofuranoside (AICAR), or insulin. We verified expression of ARK5 in muscle through RT-PCR and Western blot. Cross-reactivity of ARK5 immunoprecipitates with antibodies against phospho-AMPK was increased by ∼30% by muscle contractions and ∼60% by incubation of muscle with AICAR. AMPK was not detected in the ARK5 immunoprecipitates. Despite the apparent increase in phosphorylation of ARK5 at a site essential to its activation, neither contractions nor AICAR increased ARK5 activity. For muscles from animals injected with saline or insulin, we probed nonimmunoprecipitated samples in sequence for phosphotyrosine (P-Tyr), ARK5, and phosphorylated substrates of Akt (P-AS) and found that the ARK5 band could be precisely superimposed on phosphoprotein bands from the P-Tyr and P-AS blots. In the band corresponding to ARK5, insulin increased P-Tyr content by ∼45% and cross-reactivity with the antibody against P-AS by approximately threefold. We also detected ARK5 in phosphotyrosine immunoprecipitates. Our data suggest that increased phosphorylation of ARK5 by muscle contractions or exposure to AICAR is insufficient to activate ARK5 in skeletal muscle, suggesting that some other modification (e.g., phosphorylation on tyrosine or by Akt) may be necessary to its activity in muscle.

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