Contraction- and hypoxia-stimulated glucose transport is mediated by a Ca2+-dependent mechanism in slow-twitch rat soleus muscle

2005 ◽  
Vol 288 (6) ◽  
pp. E1062-E1066 ◽  
Author(s):  
David C. Wright ◽  
Paige C. Geiger ◽  
John O. Holloszy ◽  
Dong-Ho Han
Keyword(s):  
Glucose Transport ◽  
Soleus Muscle ◽  
Fold Increase ◽  
High Energy ◽  
Muscle Contractions ◽  
High Energy Phosphates ◽  
Dependent Protein ◽  
Rat Soleus Muscle ◽  
Slow Twitch ◽  
Dependent Mechanism

Increases in contraction-stimulated glucose transport in fast-twitch rat epitrochlearis muscle are mediated by AMPK- and Ca2+/calmodulin-dependent protein kinase (CAMK)-dependent signaling pathways. However, recent studies provide evidence suggesting that contraction-stimulated glucose transport in slow-twitch skeletal muscle is mediated through an AMPK-independent pathway. The purpose of the present study was to test the hypothesis that contraction-stimulated glucose transport in rat slow-twitch soleus muscle is mediated by an AMPK-independent/Ca2+-dependent pathway. Caffeine, a sarcoplasmic reticulum (SR) Ca2+-releasing agent, at a concentration that does not cause muscle contractions or decreases in high-energy phosphates, led to an ∼2-fold increase in 2-deoxyglucose (2-DG) uptake in isolated split soleus muscles. This increase in glucose transport was prevented by the SR calcium channel blocker dantrolene and the CAMK inhibitor KN93. Conversely, 5-aminoimidazole-4-carboxamide-1-β-d-ribofuranoside (AICAR), an AMPK activator, had no effect on 2-DG uptake in isolated split soleus muscles yet resulted in an ∼2-fold increase in the phosphorylation of AMPK and its downstream substrate acetyl-CoA carboxylase. The hypoxia-induced increase in 2-DG uptake was prevented by dantrolene and KN93, whereas hypoxia-stimulated phosphorylation of AMPK was unaltered by these agents. Tetanic muscle contractions resulted in an ∼3.5-fold increase in 2-DG uptake that was prevented by KN93, which did not prevent AMPK phosphorylation. Taken in concert, our results provide evidence that hypoxia- and contraction-stimulated glucose transport is mediated entirely through a Ca2+-dependent mechanism in rat slow-twitch muscle.

Lactate dehydrogenase expression at the onset of altered loading in rat soleus muscle

2004 ◽  
Vol 97 (4) ◽  
pp. 1424-1430 ◽  
Author(s):  
Tyrone A. Washington ◽  
James M. Reecy ◽  
Raymond W. Thompson ◽  
Larry L. Lowe ◽  
Joseph M. McClung ◽  
...  
Keyword(s):  
Lactate Dehydrogenase ◽  
Enzymatic Activity ◽  
Soleus Muscle ◽  
High Energy ◽  
Northern Blotting ◽  
Mrna Abundance ◽  
Hindlimb Suspension ◽  
Sprague Dawley ◽  
Muscle Lactate ◽  
Rat Soleus Muscle

Both functional overload and hindlimb disuse induce significant energy-dependent remodeling of skeletal muscle. Lactate dehydrogenase (LDH), an important enzyme involved in anaerobic glycolysis, catalyzes the interconversion of lactate and pyruvate critical for meeting rapid high-energy demands. The purpose of this study was to determine rat soleus LDH-A and -B isoform expression, mRNA abundance, and enzymatic activity at the onset of increased or decreased loading in the rat soleus muscle. The soleus muscles from male Sprague-Dawley rats were functionally overloaded for up to 3 days by a modified synergist ablation or subjected to disuse by hindlimb suspension for 3 days. LDH mRNA concentration was determined by Northern blotting, LDH protein isoenzyme composition was determined by zymogram analysis, and LDH enzymatic activity was determined spectrophotometrically. LDH-A mRNA abundance increased by 372%, and LDH-B mRNA abundance decreased by 43 and 31% after 24 h and 3 days of functional overload, respectively, compared with that in control rats. LDH protein expression demonstrated a shift by decreasing LDH-B isoforms and increasing LDH-A isoforms. LDH-B activity decreased 80% after 3 days of functional overload. Additionally, LDH-A activity increased by 234% following 3 days of hindlimb suspension. However, neither LDH-A or LDH-B mRNA abundance was affected following 3 days of hindlimb suspension. In summary, the onset of altered loading induced a differential expression of LDH-A and -B in the rat soleus muscle, favoring rapid energy production. Long-term altered loading is associated with myofiber conversion; however, the rapid changes in LDH at the onset of altered loading may be involved in other physiological processes.

scholarly journals Furosemide decreases the sensitivity of glucose transport to insulin in skeletal muscle in vitro

1998 ◽  
Vol 139 (1) ◽  
pp. 118-122 ◽  
Author(s):  
G Dimitriadis ◽  
B Leighton ◽  
M Parry-Billings ◽  
C Tountas ◽  
S Raptis ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Glucose Transport ◽  
Soleus Muscle ◽  
Transport Process ◽  
Glucose Utilization ◽  
Glucose Disposal ◽  
Rat Soleus Muscle ◽  
Lactate Formation

The effects of the diuretic furosemide on the sensitivity of glucose disposal to insulin were investigated in rat soleus muscle in vitro. At basal levels of insulin, the rates of 3-O-methylglucose transport, 2-deoxyglucose phosphorylation and lactate formation were not affected significantly by furosemide (0.5 mmol/l). However, furosemide significantly decreased these rates at physiological and maximal levels of insulin. The contents of 2-deoxyglucose and glucose 6-phosphate in the presence of furosemide were not significantly different from those in control muscles at all levels of insulin studied. It is concluded that furosemide decreases the sensitivity of glucose utilization to insulin in skeletal muscle by directly inhibiting the glucose transport process.

Contractile properties of muscle: control by pattern of muscle activity in the rat

1974 ◽  
Vol 187 (1086) ◽  
pp. 99-103 ◽  
Keyword(s):  
Soleus Muscle ◽  
Muscle Activity ◽  
Stimulation Frequency ◽  
Contractile Properties ◽  
Fast Muscle ◽  
Muscle Control ◽  
Rat Soleus Muscle ◽  
The Mean ◽  
Slow Twitch

The denervated slow twitch rat soleus muscle was stimulated electrically for 3-6 weeks with brief trains of stimuli at 100 Hz or long trains at 10 Hz. In both cases the mean stimulation frequency was 2 Hz. Muscles stimulated at 100 Hz acquired several properties characteristic of fast muscle, whereas muscles stimulated at 10 Hz remained slow. The results demonstrate the importance of pattern of muscle activity in determining the contractile properties of muscle.

scholarly journals Translocation of the brain-type glucose transporter largely accounts for insulin stimulation of glucose transport in BC3H-1 myocytes

1990 ◽  
Vol 269 (3) ◽  
pp. 597-601 ◽  
Author(s):  
D M Calderhead ◽  
K Kitagawa ◽  
G E Lienhard ◽  
G W Gould
Keyword(s):  
Glucose Transport ◽  
Glucose Transporter ◽  
Fold Increase ◽  
The Other ◽  
Insulin Stimulation ◽  
Glut 1 ◽  
Glut 4 ◽  
Rat Soleus Muscle ◽  
The Brain ◽  
Stimulation Of

Insulin-stimulated glucose transport was examined in BC3H-1 myocytes. Insulin treatment lead to a 2.7 +/- 0.3-fold increase in the rate of deoxyglucose transport and, under the same conditions, a 2.1 +/- 0.1-fold increase in the amount of the brain-type glucose transporter (GLUT 1) at the cell surface. It has been shown that some insulin-responsive tissues express a second, immunologically distinct, transporter, namely GLUT 4. We report here that BC3H-1 myocytes and C2 and G8 myotubes express only GLUT 1; in contrast, rat soleus muscle and heart express 3-4 times higher levels of GLUT 4 than GLUT 1. Thus translocation of GLUT 1 can account for most, if not all, of the insulin stimulation of glucose transport in BC3H-1 myocytes. On the other, hand, neither BC3H-1 myocytes nor the other muscle-cell lines are adequate as models for the study of insulin regulation of glucose transport in muscle tissue.

Are tyrosine kinases involved in mediating contraction-stimulated muscle glucose transport?

2006 ◽  
Vol 290 (1) ◽  
pp. E123-E128 ◽  
Author(s):  
David C. Wright ◽  
Paige C. Geiger ◽  
Dong-Ho Han ◽  
John O. Holloszy
Keyword(s):  
Protein Kinase ◽  
Cell Surface ◽  
Tyrosine Kinase ◽  
Glucose Transport ◽  
Tyrosine Kinases ◽  
Kinase Inhibitors ◽  
Kinase Inhibitor ◽  
Muscle Contractions ◽  
Calcium Calmodulin Dependent ◽  
Dependent Protein

Muscle contractions and insulin stimulate glucose transport into muscle by separate pathways. The contraction-mediated increase in glucose transport is mediated by two mechanisms, one involves the activation of 5′-AMP-activated protein kinase (AMPK) and the other involves the activation of calcium/calmodulin-dependent protein kinase II (CAMKII). The steps leading from the activation of AMPK and CAMKII to the translocation of GLUT4 to the cell surface have not been identified. Studies with the use of the tyrosine kinase inhibitor genistein suggest that one or more tyrosine kinases could be involved in contraction-stimulated glucose transport. The purpose of the present study was to determine the involvement of tyrosine kinases in contraction-stimulated glucose transport in rat soleus and epitrochlearis muscles. Contraction-stimulated glucose transport was completely prevented by pretreatment with genistein (100 μM) and the related compound butein (100 μM). However, the structurally distinct tyrosine kinase inhibitors 4-amino-5-(4-chlorophenyl)-7-( t-butyl)pyrazolo[3,4-d]pyridine and herbimycin did not reduce contraction-stimulated glucose transport. Furthermore, genistein and butein inhibited glucose transport even when muscles were exposed to these compounds after being stimulated to contract. Muscle contractions did not result in increases in tyrosine phosphorylation of proteins such as proline-rich tyrosine kinase and SRC. These results provide evidence that tyrosine kinases do not mediate contraction-stimulated glucose transport and that the inhibitory effects of genistein on glucose transport result from direct inhibition of the glucose transporters at the cell surface.

Effect of hypothermia on 2-deoxy-glucose transport, insulin binding and insulin sensitivity of the rat soleus muscle

1997 ◽  
Vol 4 (3) ◽  
pp. 205-212
Author(s):  
Teresa Torlińska ◽  
Józef Langfort ◽  
Paweł Maćkowiak ◽  
Tomasz Hryniewiecki ◽  
Hanna Kaciuba-Uściłko ◽  
...  
Keyword(s):  
Insulin Sensitivity ◽  
Glucose Transport ◽  
Soleus Muscle ◽  
Insulin Binding ◽  
Rat Soleus Muscle

scholarly journals Exhausting treadmill running causes dephosphorylation of sMLC2 and reduced level of myofilament MLCK2 in slow twitch rat soleus muscle

2015 ◽  
Vol 3 (2) ◽  
pp. e12285 ◽  
Author(s):  
Kristin Halvorsen Hortemo ◽  
Jan Magnus Aronsen ◽  
Ida G. Lunde ◽  
Ivar Sjaastad ◽  
Per Kristian Lunde ◽  
...  
Keyword(s):  
Soleus Muscle ◽  
Treadmill Running ◽  
Rat Soleus Muscle ◽  
Slow Twitch

Effects of insulin and epinephrine on Na+-K+ and glucose transport in soleus muscle

1987 ◽  
Vol 252 (4) ◽  
pp. E492-E499 ◽  
Author(s):  
T. Clausen ◽  
J. A. Flatman
Keyword(s):  
Glucose Transport ◽  
Soleus Muscle ◽  
Sugar Transport ◽  
Resting Membrane Potential ◽  
Exchange System ◽  
Glucose Transport System ◽  
Rat Soleus Muscle ◽  
Possible Cause ◽  
K Transport ◽  
Stimulation Of

To identify possible cause-effect relationships between changes in active Na+-K+ transport, resting membrane potential, and glucose transport, the effects of insulin and epinephrine were compared in rat soleus muscle. Epinephrine, which produced twice as large a hyperpolarization as insulin, induced only a modest increase in sugar transport. Ouabain, at a concentration (10(-3) M) sufficient to block active Na+-K+ transport and the hyperpolarization induced by the two hormones, did not interfere with sugar transport stimulation. After Na+ loading in K+-free buffer, the return to K+-containing standard buffer caused marked stimulation of active Na+-K+ transport, twice the hyperpolarization produced by insulin but no change in sugar transport. The insulin-induced activation of the Na+-K+ pump leads to decreased intracellular Na+ concentration and hyperpolarization, but none of these events can account for the concomitant activation of the glucose transport system. The stimulating effect of insulin on active Na+-K+ transport was not suppressed by amiloride, indicating that in intact skeletal muscle it is not elicited by a primary increase in Na+ influx via the Na+/H+-exchange system.

Activation of the A1 adenosine receptor increases insulin-stimulated glucose transport in isolated rat soleus muscle

2007 ◽  
Vol 32 (4) ◽  
pp. 701-710 ◽  
Author(s):  
Farah S.L. Thong ◽  
Jamie S.V. Lally ◽  
David J. Dyck ◽  
Felicia Greer ◽  
Arend Bonen ◽  
...  
Keyword(s):  
Glucose Transport ◽  
Soleus Muscle ◽  
Adenosine Receptor ◽  
Adenosine Diphosphate ◽  
Dependent Manner ◽  
Concentration Dependent Manner ◽  
Endogenous Adenosine ◽  
Selective Agonist ◽  
Rat Soleus Muscle ◽  
Muscle Glucose Transport

The A1 adenosine receptor (A1AR) has been suggested to participate in insulin- and contraction-stimulated glucose transport in skeletal muscle, but the qualitative and quantitative nature of the effect are controversial. We sought to determine if A1AR is expressed in rat soleus muscle and then characterize its role in glucose transport in this muscle. A1AR mRNA and protein expression were determined by RT-PCR and Western blotting, respectively. To examine the role of adenosine in 3-O-methylglucose transport, isolated muscles were exposed to adenosine deaminase and α,β-methylene adenosine diphosphate to remove endogenous adenosine and were left unstimulated (basal) or stimulated with insulin. To assess the functional participation of A1AR in 3-O-methylglucose transport, muscles were incubated with A1-selective agonist and (or) antagonist in the absence of endogenous adenosine and with or without insulin. A1AR mRNA was expressed in soleus muscle and A1AR was present at the plasma membrane. Removal of endogenous adenosine reduced glucose transport in response to 100 μU/mL insulin (~50%). The A1-selective agonist, N6-cyclopentyladenosine, increased submaximal (100 μU/mL) insulin-stimulated glucose transport in a dose-dependent manner (0.001–1.0 μmol/L). This stimulatory effect was inhibited by the A1-selective receptor antagonist 1,3-dipropyl-8-cyclopentylxanthine in a concentration-dependent manner (0.001–1.0 μmol/L). However, neither activation nor inhibition of A1AR altered basal or maximal (10 mU/mL) insulin-stimulated glucose transport. Our results suggest that adenosine contributes ~50% to insulin-stimulated muscle glucose transport by activating the A1AR. This effect is limited to increasing insulin sensitivity, but not to either basal or maximal insulin-stimulated glucose uptake in rat soleus muscle.

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