scholarly journals The roles of IL-6 in the regulation of glucose homeostasis

2009 ◽  
Vol 34 (1) ◽  
pp. 83-84
Author(s):  
Jenny E. Gusba
Keyword(s):  
Skeletal Muscle ◽  
Protein Kinase ◽  
Muscle Contraction ◽  
Glucose Transport ◽  
Glucose Homeostasis ◽  
Muscle Glycogen ◽  
Glycogen Content ◽  
Glycogen Resynthesis ◽  
Muscle Glycogen Content ◽  
Tnf Α

This thesis examined the roles of interleukin (IL)-6 in the regulation of glucose homeostasis, with a specific focus on skeletal muscle. Study 1 sought to determine whether muscle glycogen content is a stimulus for the production of IL-6, examining the periods during and after exercise. The relationship between IL-6 and muscle glycogen content was measured during similar bouts of exhaustive exercise on 2 occasions that resulted in large increases in muscle messenger (m)RNA for IL-6 and circulating levels of IL-6. On 1 occasion, subjects received carbohydrate during recovery to facilitate rates of glycogen resynthesis. During exercise, subjects performed similar bouts of exercise, such that differences in an individual’s glycogen levels between trials could be compared with differences in IL-6. No correlation was detected between the net change in glycogen content and the net change in plasma IL-6 or IL-6 mRNA from rest to exhaustion. Moreover, when the difference within subjects at exhaustion in IL-6 and glycogen was compared, there was no correlation between the 2 variables. During recovery, although carbohydrate intake significantly increased glycogen resynthesis, there was no change in postexercise IL-6 mRNA level or plasma IL-6 concentration. Therefore, glycogen was not the sole regulator of IL-6 production in skeletal muscle. Study 2 examined the direct effect of IL-6 and tumor necrosis factor (TNF)-α on glucose transport and the phosphorylation of key signalling proteins with or without insulin and during rodent muscle contraction. Under basal conditions, IL-6 increased glucose transport in association with an increase in 5′AMP-activated protein kinase (AMPK) and AS160 phosphorylation, but IL-6 decreased insulin-stimulated glucose transport via a reduction in phosphorylation of calcium–calmodulin-dependent protein kinase (CaMK)II and AS160. A novel finding generated from these experiments was the direct involvement of IL-6 in contraction-mediated glucose transport. In the case of muscle contraction, IL-6 was found to increase the phosphorylation of CaMKII and AS160. This research suggests that the activation of CaMKII is involved in the actions of IL-6 under insulin-stimulated and contraction-mediated conditions. Furthermore, AS160 was identified as a common signalling intermediate, influenced by IL-6. It also suggests that AS160 may be a point of convergence for multiple signalling pathways. Finally, the actions of TNF-α mimicked those of IL-6, except during contraction, where TNF-α had no significant effect on glucose transport and attenuated the effects of IL-6.

Muscle glycogen content affects insulin-stimulated glucose transport and protein kinase B activity

2000 ◽  
Vol 279 (5) ◽  
pp. E947-E955 ◽  
Author(s):  
W. Derave ◽  
B. F. Hansen ◽  
S. Lund ◽  
S. Kristiansen ◽  
E. A. Richter
Keyword(s):  
Protein Kinase ◽  
Cell Surface ◽  
Glucose Transport ◽  
Muscle Glycogen ◽  
Glycogen Content ◽  
Protein Kinase B ◽  
Muscle Glycogen Content ◽  
Glut 4 ◽  
Fast Twitch ◽  
White Gastrocnemius

We investigated the possible regulatory role of glycogen in insulin-stimulated glucose transport and insulin signaling in skeletal muscle. Rats were preconditioned to obtain low (LG), normal, or high (HG) muscle glycogen content, and perfused isolated hindlimbs were exposed to 0, 100, or 10,000 μU/ml insulin. In the fast-twitch white gastrocnemius, insulin-stimulated glucose transport was significantly higher in LG compared with HG. This difference was less pronounced in the mixed-fiber red gastrocnemius and was absent in the slow-twitch soleus. In the white gastrocnemius, insulin activation of insulin receptor tyrosine kinase and phosphoinositide 3-kinase was unaffected by glycogen levels, whereas protein kinase B activity was significantly higher in LG compared with HG. In additional incubation experiments on fast-twitch epitrochlearis muscles, insulin-stimulated cell surface GLUT-4 content was significantly higher in LG compared with HG. The data indicate that, in fast-twitch muscle, the effect of insulin on glucose transport and cell surface GLUT-4 content is modulated by glycogen content, which does not involve initial but possibly more downstream signaling events.

5′‐AMP‐activated protein kinase regulates skeletal muscle glycogen content and ergogenics

2005 ◽  
Vol 19 (7) ◽  
pp. 771-779 ◽  
Author(s):  
Brian R. Barnes ◽  
Stephan Glund ◽  
Yun Chau Long ◽  
Göran Hjälm ◽  
Leif Andersson ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Protein Kinase ◽  
Muscle Glycogen ◽  
Glycogen Content ◽  
Muscle Glycogen Content ◽  
Skeletal Muscle Glycogen ◽  
Amp Activated Protein Kinase

Progressive increase in human skeletal muscle AMPKα2 activity and ACC phosphorylation during exercise

2002 ◽  
Vol 282 (3) ◽  
pp. E688-E694 ◽  
Author(s):  
T. J. Stephens ◽  
Z.-P. Chen ◽  
B. J. Canny ◽  
B. J. Michell ◽  
B. E. Kemp ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Muscle Glycogen ◽  
Human Skeletal Muscle ◽  
Glycogen Content ◽  
Vastus Lateralis ◽  
Moderate Intensity ◽  
Moderate Intensity Exercise ◽  
Western Blots ◽  
Muscle Glycogen Content ◽  
Muscle Creatine

The effect of prolonged moderate-intensity exercise on human skeletal muscle AMP-activated protein kinase (AMPK)α1 and -α2 activity and acetyl-CoA carboxylase (ACCβ) and neuronal nitric oxide synthase (nNOSμ) phosphorylation was investigated. Seven active healthy individuals cycled for 30 min at a workload requiring 62.8 ± 1.3% of peak O2consumption (V˙o 2 peak) with muscle biopsies obtained from the vastus lateralis at rest and at 5 and 30 min of exercise. AMPKα1 activity was not altered by exercise; however, AMPKα2 activity was significantly ( P < 0.05) elevated after 5 min (∼2-fold), and further elevated ( P < 0.05) after 30 min (∼3-fold) of exercise. ACCβ phosphorylation was increased ( P < 0.05) after 5 min (∼18-fold compared with rest) and increased ( P< 0.05) further after 30 min of exercise (∼36-fold compared with rest). Increases in AMPKα2 activity were significantly correlated with both increases in ACCβ phosphorylation and reductions in muscle glycogen content. Fat oxidation tended ( P = 0.058) to increase progressively during exercise. Muscle creatine phosphate was lower ( P < 0.05), and muscle creatine, calculated free AMP, and free AMP-to-ATP ratio were higher ( P < 0.05) at both 5 and 30 min of exercise compared with those at rest. At 30 min of exercise, the values of these metabolites were not significantly different from those at 5 min of exercise. Phosphorylation of nNOSμ was variable, and despite the mean doubling with exercise, statistically significance was not achieved ( P = 0.304). Western blots indicated that AMPKα2 was associated with both nNOSμ and ACCβ consistent with them both being substrates of AMPKα2 in vivo. In conclusion, AMPKα2 activity and ACCβ phosphorylation increase progressively during moderate exercise at ∼60% of V˙o 2 peak in humans, with these responses more closely coupled to muscle glycogen content than muscle AMP/ATP ratio.

scholarly journals Skeletal muscle glycogen content in patients with cirrhosis

Hepatology ◽  
1994 ◽  
Vol 20 (1) ◽  
pp. 135-141 ◽  
Author(s):  
Oliver Selberg ◽  
Eva Radoch ◽  
Gerhard Franz Walter ◽  
Manfred James Müller
Keyword(s):  
Skeletal Muscle ◽  
Muscle Glycogen ◽  
Glycogen Content ◽  
Muscle Glycogen Content ◽  
Skeletal Muscle Glycogen

Carbohydrate ingestion influences skeletal muscle cytokine mRNA and plasma cytokine levels after a 3-h run

2003 ◽  
Vol 94 (5) ◽  
pp. 1917-1925 ◽  
Author(s):  
D. C. Nieman ◽  
J. M. Davis ◽  
D. A. Henson ◽  
J. Walberg-Rankin ◽  
M. Shute ◽  
...  
Keyword(s):  
Gene Expression ◽  
Muscle Glycogen ◽  
Glycogen Content ◽  
Vastus Lateralis ◽  
Maximal Oxygen Consumption ◽  
Vastus Lateralis Muscle ◽  
Cytokine Mrna ◽  
Carbohydrate Ingestion ◽  
Muscle Glycogen Content ◽  
Tnf Α

Sixteen experienced marathoners ran on treadmills for 3 h at ∼70% maximal oxygen consumption (V˙o 2 max) on two occasions while receiving 1 l/h carbohydrate (CHO) or placebo (Pla) beverages. Blood and vastus lateralis muscle biopsy samples were collected before and after exercise. Plasma was analyzed for IL-6, IL-10, IL-1 receptor agonist (IL-1ra), IL-8, cortisol, glucose, and insulin. Muscle was analyzed for glycogen content and relative gene expression of 13 cytokines by using real-time quantitative RT-PCR. Plasma glucose and insulin were higher, and cortisol, IL-6, IL-10, and IL-1ra, but not IL-8, were significantly lower postexercise in CHO vs. Pla. Change in muscle glycogen content did not differ between CHO and Pla ( P = 0.246). Muscle cytokine mRNA content was detected preexercise for seven cytokines in this order (highest to lowest): IL-15, TNF-α, IL-8, IL-1β, IL-12p35, IL-6, and IFN-γ. After subjects ran for 3 h, gene expression above prerun levels was measured for five of these cytokines: IL-1β, IL-6, and IL-8 (large increases), and IL-10 and TNF-α (small increases). The increase in mRNA (fold difference from preexercise) was attenuated in CHO (15.9-fold) compared with Pla (35.2-fold) for IL-6 ( P = 0.071) and IL-8 (CHO, 7.8-fold; Pla, 23.3-fold; P = 0.063). CHO compared with Pla beverage ingestion attenuates the increase in plasma IL-6, IL-10, and IL-1ra and gene expression for IL-6 and IL-8 in athletes running 3 h at 70%V˙o 2 max despite no differences in muscle glycogen content.

Influence of muscle glycogen availability on ERK1/2 and Akt signaling after resistance exercise in human skeletal muscle

2005 ◽  
Vol 99 (3) ◽  
pp. 950-956 ◽  
Author(s):  
Andrew Creer ◽  
Philip Gallagher ◽  
Dustin Slivka ◽  
Bozena Jemiolo ◽  
William Fink ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Resistance Exercise ◽  
Muscle Glycogen ◽  
Human Skeletal Muscle ◽  
Glycogen Content ◽  
Vastus Lateralis ◽  
Akt Signaling ◽  
Cellular Growth ◽  
Muscle Glycogen Content ◽  
Ribosomal S6 Kinase

Two pathways that have been implicated for cellular growth and development in response to muscle contraction are the extracellular signal-regulated kinase (ERK1/2) and Akt signaling pathways. Although these pathways are readily stimulated after exercise, little is known about how nutritional status may affect stimulation of these pathways in response to resistance exercise in human skeletal muscle. To investigate this, experienced cyclists performed 30 repetitions of knee extension exercise at 70% of one repetition maximum after a low (2%) or high (77%) carbohydrate (LCHO or HCHO) diet, which resulted in low or high (∼174 or ∼591 mmol/kg dry wt) preexercise muscle glycogen content. Muscle biopsies were taken from the vastus lateralis before, ∼20 s after, and 10 min after exercise. ERK1/2 and p90 ribosomal S6 kinase phosphorylation increased ( P ≤ 0.05) 10 min after exercise, regardless of muscle glycogen availability. Akt phosphorylation was elevated ( P < 0.05) 10 min after exercise in the HCHO trial but was unaffected after exercise in the LCHO trial. Mammalian target of rapamycin phosphorylation was similar to that of Akt during each trial; however, change or lack of change was not significant. In conclusion, the ERK1/2 pathway appears to be unaffected by muscle glycogen content. However, muscle glycogen availability appears to contribute to regulation of the Akt pathway, which may influence cellular growth and adaptation in response to resistance exercise in a low-glycogen state.

scholarly journals Hepatic and skeletal muscle glycogen content in rats treated with metformin and submitted to acute exercise by swimming

2018 ◽  
Vol 31 (2) ◽  
pp. 355
Author(s):  
Vitor Alexandre Pezolato ◽  
Marcos Almeida Marques ◽  
Fabio Marcos Abreu ◽  
Nataly Mendes Silva ◽  
Ronaldo Júlio Baganha ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Muscle Glycogen ◽  
Acute Exercise ◽  
Glycogen Content ◽  
Muscle Glycogen Content ◽  
Skeletal Muscle Glycogen

O objetivo deste estudo foi avaliar o comportamento das reservas glicogênicas de ratos, submetidos a uma condição de exercício agudo (50 minutos de natação na intensidade leve), após o tratamento com metformina. Quarenta ratos Wistar (180-200g) adultos foram divididos em quatro grupos (tratados ou não por quinze dias) e assim representados: Controle; Exercício agudo por natação (realizaram uma sessão de natação, sendo 50 minutos na intensidade leve); Tratado com metformina (receberam o fármaco metformina na dosagem de 1,4 mg/ml, durante o período experimental; Tratados com metformina e submetidos a condição exercício agudo por natação (receberam o fármaco metformina na dosagem de 1,4 mg/ml e realizaram uma sessão de natação, sendo 50 minutos na intensidade leve). O exercício agudo diminuiu as reservas glicogênicas, já os animais tratados com metformina, apresentaram um aumento em suas reservas glicogênicas musculares e hepáticas em relação ao grupo que realizou o exercício sem suplementação (p0,05). O tratamento com metformina promoveu melhora nas condições energéticas e menor resposta ao estresse, sugerindo ser uma importante ferramenta farmacológica para a potencialização da performance.

Transcriptional activation of the IL‐6 gene in human contracting skeletal muscle: influence of muscle glycogen content

2001 ◽  
Vol 15 (14) ◽  
pp. 1-15 ◽  
Author(s):  
Charlotte Keller ◽  
Adam Steensberg ◽  
Henriette Pilegaard ◽  
Takuya Osada ◽  
Bengt Saltin ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Transcriptional Activation ◽  
Muscle Glycogen ◽  
Glycogen Content ◽  
Muscle Glycogen Content
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