Insulin binding and 2-deoxy-D-glucose uptake in fast- and slow-twitch mouse skeletal muscle at 18 and 37 °C

1984 ◽  
Vol 62 (12) ◽  
pp. 1460-1465 ◽  
Author(s):  
Wendy M. Watson-Wright ◽  
Meng H. Tan ◽  
Arend Bonen
Keyword(s):  
Extensor Digitorum Longus ◽  
Insulin Binding ◽  
Extensor Digitorum ◽  
Insulin Degradation ◽  
Response Curves ◽  
Slow Twitch Muscle ◽  
Two Temperatures ◽  
Higher Temperature ◽  
Slow Twitch ◽  
Insulin Responsiveness

Insulin binding, insulin degradation, and 2-deoxyglucose uptake were examined at 18 and 37 °C in soleus and extensor digitorum longus muscles of mice. Insulin binding and degradation were greater in the soleus than in the extensor digitorum longus at both temperatures (p < 0.05). At 37 °C, binding was decreased in both muscles while percentage degradation was increased in comparison with 18 °C (p < 0.05). Dose–response curves (percentage of binding at 4 nM of insulin) remained the same for both muscles at the two temperatures. Basal (no insulin) 2-deoxyglucose uptake was increased at 37 °C in the extensor digitorum longus but not the soleus. Insulin responsiveness in terms of the amount of 2-deoxyglucose taken up per femtomole of insulin bound was almost identical for the two muscles at 18 °C, whereas at 37 °C it was increased more in the soleus than in the extensor digitorum longus. The results indicate that in the presence of physiological concentrations of insulin (0.2–4 nM), insulin binding trends are minimally affected by increased temperature. In contrast, the ability of insulin to stimulate 2-deoxyglucose uptake varies between the two temperatures, and at the higher temperature between fast- and slow-twitch muscle.

Effect of cross-reinnervation on the expression of GLUT-4 and GLUT-1 in slow and fast rat muscles

1996 ◽  
Vol 270 (6) ◽  
pp. R1355-R1360
Author(s):  
E. Johannsson ◽  
O. Waerhaug ◽  
A. Bonen
Keyword(s):  
Extensor Digitorum Longus ◽  
Extensor Digitorum ◽  
Metabolic Phenotype ◽  
Glut 1 ◽  
Glut 4 ◽  
Slow Twitch Muscle ◽  
Fast Twitch Muscle ◽  
Oxidative Phenotype ◽  
Slow Twitch ◽  
Fast Twitch

We determined whether the twitch-velocity phenotype or the metabolic phenotype of a muscle influences the content of GLUT-4 and GLUT-1 proteins. The soleus (Sol) and extensor digitorum longus (EDL) muscles were cross-reinnervated (X-Sol, X-EDL). After 3 mo the X-EDL had become enriched in slow-twitch oxidative (SO) fibers (70.5% SO) compared with its control (3.8% SO), whereas the X-Sol became enriched in fast-twitch oxidative-glycolytic (FOG) fibers (78.6% FOG) compared with its control (10% FOG). Thus the twitch phenotype of X-Sol shifted to fast-twitch muscle, whereas X-EDL shifted to a slow-twitch muscle. In the X-EDL, the oxidative nature of the X-EDL was increased to 97% oxidative fibers compared with 43% oxidative fibers in the normal EDL. In the Sol the oxidative nature of the X-Sol was retained at 100%. GLUT-4 content was increased 1.6-fold in the X-EDL (P < 0.05) but was not changed in the X-Sol (P > 0.05). GLUT-1 content was increased fourfold in X-EDL but was not altered in the X-Sol. We conclude that GLUT-4 and GLUT-1 content in muscle is related to the oxidative phenotype of the muscle rather than the twitch-velocity phenotype.

scholarly journals Activity of mu- and m-calpain in regenerating fast and slow twitch skeletal muscles.

1996 ◽  
Vol 43 (4) ◽  
pp. 693-700 ◽  
Author(s):  
J Moraczewski ◽  
E Piekarska ◽  
M Zimowska ◽  
M Sobolewska
Keyword(s):  
Intracellular Calcium ◽  
Soleus Muscle ◽  
Muscle Regeneration ◽  
Skeletal Muscles ◽  
Extensor Digitorum Longus ◽  
Extensor Digitorum ◽  
Slow Twitch ◽  
Edl Muscle ◽  
Calpain Ii ◽  
Complete Regeneration

Calpains--non-lysosomal intracellular calcium-activated neutral proteinases, form a family consisting of several distinct members. Two of the isoenzymes: mu (calpain I) and m (calpain II) responded differently to the injury during complete regeneration of Extensor digitorum longus (EDL) muscle and partial regeneration of Soleus muscle. In the crushed EDL the level of m-calpain on the 3rd and 7th day of regeneration was higher than in non-operated muscles, whereas the activity of this calpain in injured Soleus decreased. The level of mu-calpain in EDL oscillated irregularly during regeneration whereas in Soleus of both injured and contralateral muscles its level rapidly rose. Our results support the hypothesis that m-calpain is involved in the process of fusion of myogenic cells whereas mu-calpain plays a significant but indirect role in muscle regeneration.

Simultaneous Assessment of Isometric Forces in Fast- and Slow-Twitch Muscles of Single Rat Hindlimbs in Situ

1996 ◽  
Vol 21 (1) ◽  
pp. 23-34 ◽  
Author(s):  
Andrew J. Carvalho ◽  
Nancy H. McKee
Keyword(s):  
Extensor Digitorum Longus ◽  
Mechanical Performance ◽  
Contractile Function ◽  
Small Strain ◽  
Extensor Digitorum ◽  
Published Data ◽  
Slow Twitch ◽  
Isometric Twitch ◽  
Simultaneous Assessment

An apparatus, consisting of a pair of small strain gauge transducers, was designed for the simultaneous assessment of isometric contractile function in two muscles, composed of a predominance of either fast- or slow-twitch fibers, and within a single rat hindlimb in situ. This facilitates assessment of mechanical performance of two separate muscles under identical conditions. In anesthetized rats (N = 10), the voltages and frequencies required to produce isometric twitch and tetanic forces from the soleus (SOL) and extensor digitorum longus (EDL) muscles were determined. The apparatus was then used to demonstrate the simultaneous assessment of forces produced by the SOL and EDL from the same hindlimbs (n = 5) during 30 min of fatigue and 30 min of recovery. With this apparatus, data collected were comparable to published data. The apparatus can be used for the simultaneous assessment of isometric contractile function and fatigue in both a fast- and a slow-twitch muscle of a single rat hindlimb in situ. Key words: model, fatigue, ischemia, soleus, extensor digitorum longus

scholarly journals Effect of acetoacetate on glucose metabolism in the soleus and extensor digitorum longus muscles of the rat

1977 ◽  
Vol 162 (3) ◽  
pp. 557-568 ◽  
Author(s):  
E Z Maizels ◽  
N B Ruderman ◽  
M N Goodman ◽  
D Lau
Keyword(s):  
Glucose Metabolism ◽  
Glucose Uptake ◽  
Glucose Oxidation ◽  
Extensor Digitorum Longus ◽  
Similar Rate ◽  
Extensor Digitorum ◽  
Lactate Release ◽  
Red Muscle ◽  
Slow Twitch ◽  
Fast Twitch

1. The effect of acetoacetate on glucose metabolism was compared in the soleus, a slow-twitch red muscle, and the extensor digitorum longus, a muscle composed of 50% fast-twitch red and 50% white fibres. 2. When incubated for 2h in a medium containing 5 mM-glucose and 0.1 unit of insulin/ml, rates of glucose uptake, lactate release and glucose oxidation in the soleus were 19.6, 18.6 and 1.47 micronmol/h per g respectively. Acetoacetate (1.7 mM) diminished all three rates by 25-50%; however, it increased glucose conversion into glycogen. In addition, it caused increases in tissue glucose, glucose 6-phosphate and fructose 6-phosphate, suggesting inhibition of phosphofructokinase. The concentrations of citrate, an inhibitor of phosphofructokinase, and of malate were also increased. 3. Rates of glucose uptake and lactate release in the extensor digitorum longus were 50-80% of those in the soleus. Acetoacetate caused moderate increases in tissue glucose 6-phosphate and possibly citrate, but it did not decrease glucose uptake or lactate release. 4. The rate of glycolysis in the soleus was approximately five times that previously observed in the perfused rat hindquarter, a muscle preparation in which acetoacetate inhibits glucose oxidation, but does not alter glucose uptake or glycolysis. A similar rate of glycolysis was observed when the soleus was incubated with a glucose-free medium. Under these conditions, tissue malate and the lactate/pyruvate ratio in the medium were decreased, and acetoacetate did not decrease lactate release or increase tissue citrate or glucose 6-phosphate. An intermediate rate of glycolysis, which was not decreased by acetoacetate, was observed when the soleus was incubated with glucose, but not insulin. 5. The data suggest that acetoacetate glucose inhibits uptake and glycolysis in red muscle under conditions that resemble mild to moderate exercise. They also suggest that the accumulation of citrate in these circumstances is linked to the rate of glycolysis, possibly through the generation of cytosolic NADH and malate formation.

Effect of cyclopiazonic acid on contractile responses in slow and fast bundles of cremaster skeletal muscle from the ferret

1994 ◽  
Vol 72 (8) ◽  
pp. 833-840 ◽  
Author(s):  
Corinne Huchet ◽  
Claude Léoty
Keyword(s):  
Skeletal Muscle ◽  
Sarcoplasmic Reticulum ◽  
Extensor Digitorum Longus ◽  
Cyclopiazonic Acid ◽  
Extensor Digitorum ◽  
Skinned Fibers ◽  
Contractile Apparatus ◽  
Slow Twitch ◽  
Slow Twitch Fibers ◽  
Dose Dependent

The effects of cyclopiazonic acid (CPA) on twitch force, calcium (Ca2+) uptake and release by the sarcoplasmic reticulum (SR), and Ca2+ sensitivity of contractile apparatus were studied using intact and chemically skinned cremaster fibers and compared with those on the extensor digitorum longus and soleus. In cremaster muscles treated with CPA (0.5–5 μM) a potentiation of the twitch was observed, associated with an increase in time to peak and in time of relaxation. In Triton-skinned fibers, CPA, at concentrations less than 10 μM, exerted no significant effect on the contractile apparatus of either slow- or fast-twitch fibers. In slow-twitch fibers, a dose-dependent increase in Ca2+ sensitivity was associated with a decrease in maximal tension, at CPA concentrations > 10 μM. In saponin-skinned fibers, during the uptake phase, CPA at > 10 μM induced a dose-dependent decrease in caffeine contracture. The possibility of an action on the SR Ca2+ release channel was excluded by testing the effect of CPA during the releasing phase. The enhancing effect of CPA (0.5 – 5 μM) on mechanical activity could be explained by an inhibition of the SR Ca2+ ATPase in skeletal muscle cells without an effect on the contractile proteins. Our results strongly suggest that CPA (< 10 μM) has a highly specific effect on the SR Ca2+ pump in the fast- and slow-twitch fibers and therefore could be a good tool to study the mechanisms of Ca2+ regulation in skeletal muscles. Furthermore, the study of the SR properties, using CPA, has shown no significant differences in the SR function of ferret cremaster fibers in comparison with extensor digitorum longus and soleus muscles.Key words: caffeine, skinned fiber, sarcoplasmic reticulum.

Aberrant expression of myosin isoforms in skeletal muscles from mice lacking the rev-erbAα orphan receptor gene

2005 ◽  
Vol 288 (2) ◽  
pp. R482-R490 ◽  
Author(s):  
P. Pircher ◽  
P. Chomez ◽  
F. Yu ◽  
B. Vennström ◽  
L. Larsson
Keyword(s):  
Thyroid Hormone ◽  
Hormone Receptor ◽  
Skeletal Muscles ◽  
Extensor Digitorum Longus ◽  
Thyroid Hormone Receptor ◽  
Extensor Digitorum ◽  
Type I ◽  
Wild Type ◽  
Slow Twitch ◽  
Isoform Expression

The rev-erbAα orphan protein belongs to the steroid nuclear receptor superfamily. No ligand has been identified for this protein, and little is known of its function in development or physiology. In this study, we focus on 1) the distribution of the rev-erbAα protein in adult fast- and slow-twitch skeletal muscles and muscle fibers and 2) how the rev-erbAα protein influences myosin heavy chain (MyHC) isoform expression in mice heterozygous (+/−) and homozygous (−/−) for a rev-erbAα protein null allele. In the fast-twitch extensor digitorum longus muscle, rev-erbAα protein expression was linked to muscle fiber type; however, MyHC isoform expression did not differ between wild-type, +/−, or −/− mice. In the slow-twitch soleus muscle, the link between rev-erbAα protein and MyHC isoform expression was more complex than in the extensor digitorum longus. Here, a significantly higher relative amount of the β/slow (type I) MyHC isoform was observed in both rev-erbAα −/− and +/− mice vs. that shown in wild-type controls. A role for the ratio of thyroid hormone receptor proteins α1 to α2 in modulating MyHC isoform expression can be ruled out because no differences were seen in MyHC isoform expression between thyroid hormone receptor α2-deficient mice (heterozygous and homozygous) and wild-type mice. Therefore, our data are compatible with the rev-erbAα protein playing an important role in the regulation of skeletal muscle MyHC isoform expression.

scholarly journals Carbonic anhydrase activity in skeletal muscle fiber types, axons, spindles, and capillaries of rat soleus and extensor digitorum longus muscles.

1982 ◽  
Vol 30 (12) ◽  
pp. 1275-1288 ◽  
Author(s):  
D A Riley ◽  
S Ellis ◽  
J Bain
Keyword(s):  
Carbonic Anhydrase ◽  
Extensor Digitorum Longus ◽  
Muscle Fibers ◽  
Extensor Digitorum ◽  
Female Rats ◽  
Male Rats ◽  
Muscle Fiber Types ◽  
Fiber Types ◽  
Slow Twitch ◽  
Fast Twitch

Carbonic anhydrase (CA) activities were studied in soluble extracts and cryostat sections of skeletal muscles from prepubertal and postpubertal rats. Acetazolamide inhibition was utilized to distinguish between activities of the acetazolamide-sensitive (CA I and II) and acetazolamide-resistant (CA III) forms of the enzyme. The inhibition studies indicated that fast-twitch oxidative-glycolytic muscle fibers contained both the sensitive and resistant forms of CA. Acetazolamide-sensitive activity was localized within muscle fibers, axons, myelin, and capillaries. Axoplasmic staining was restricted to subpopulations of myelinated axons in both the dorsal and ventral roots. Soleus muscles exhibited significantly greater activity of CA III than extensor digitorum longus muscles at all ages examined. CA III was richest in slow-twitch oxidative and intrafusal fibers. During puberty, soleus muscle fibers matured and converted from fast-twitch oxidative-glycolytic to slow-twitch oxidative fibers. There was a shift from the sensitive to the resistant form of CA; CA III activity increased about sevenfold. This activity peaked earlier in the muscles of female rats than male rats. These results demonstrated a complex distribution of CA isozymes in the neuromuscular system and pointed out that isozyme content depends on both the type of muscle and the age and sex of the animal.

Effects of exercise on insulin binding and glucose metabolism in muscle

1984 ◽  
Vol 62 (12) ◽  
pp. 1500-1504 ◽  
Author(s):  
A. Bonen ◽  
M. H. Tan ◽  
W. M. Watson-Wright
Keyword(s):  
Insulin Sensitivity ◽  
Glucose Metabolism ◽  
Extensor Digitorum Longus ◽  
Glucose Utilization ◽  
Treadmill Exercise ◽  
Insulin Binding ◽  
Glucose Disposal ◽  
Slow Twitch ◽  
Fast Twitch ◽  
Uptake And Metabolism

To elucidate the mechanism of enhanced insulin sensitivity by muscle after exercise, we studied insulin binding, 2-deoxy-D-[1-14C]glucose (2-DOG) uptake and [5-3H]glucose utilization in glycolysis and glycogenesis in soleus and extensor digitorum longus (EDL) muscles of mice after 60 min of treadmill exercise. In the soleus, glycogenesis was increased after exercise (P < 0.05) and remained sensitive to the action of insulin. Postexercise insulin-stimulated glycolysis was also increased in the soleus (P < 0.05). In the EDL, glycogenesis was increased after exercise (P < 0.05). However, this was already maximal in the absence of insulin and was not further stimulated by insulin (0.1–4 nM). The disposal of glucose occurred primarily via the glycolytic pathway (>60%) in the soleus and EDL at rest and after exercise. The uptake of 2-DOG uptake was not altered in the soleus after exercise (4 h incubation at 18 °C). However, with 1-h incubations at 37 °C, a marked increase in 2-DOG uptake after exercise was observed in the soleus (P < 0.05) in the absence (0 nM) and presence of insulin (0.2–4 nM) (P < 0.05). A similar postexercise increase in 2-DOG uptake occurred in EDL. Despite the marked increase in glucose uptake and metabolism, no changes in insulin binding were apparent in either EDL or soleus at 37 °C or 18 °C. This study shows that the postexercise increase of glucose disposal does not appear to be directly attributable to increments in insulin binding to slow-twitch and fast-twitch muscles. Also, after exercise the increments in glucose metabolism differ markedly in the two types of muscle.

Glycogenesis and glyconeogenesis in skeletal muscle: effects of pH and hormones

1990 ◽  
Vol 258 (4) ◽  
pp. E693-E700 ◽  
Author(s):  
A. Bonen ◽  
J. C. McDermott ◽  
M. H. Tan
Keyword(s):  
Skeletal Muscle ◽  
Soleus Muscle ◽  
Extensor Digitorum Longus ◽  
Muscle Fibers ◽  
Extensor Digitorum ◽  
Effects Of Ph ◽  
Slow Twitch ◽  
Highly Correlated ◽  
Fast Twitch

We examined the effects of selected hormones and pH on the rates of glyconeogenesis (L-[U-14C]-lactate----glycogen) and glycogenesis (D-[U-14C]glucose----glycogen) in mouse fast-twitch (FT) and slow-twitch muscles incubated in vitro (37 degrees C). Glyconeogenesis and glycogenesis increased linearly with increasing concentrations of lactate (5-20 mM) and glucose (2.5-10 mM), respectively, in both muscles. Glyconeogenesis was approximately three- to fourfold greater in the extensor digitorum longus (EDL) than in the soleus, whereas basal glycogenesis was twofold greater in the soleus muscle than in the EDL. Lactate accounted for up to 5% of the glycogen formed in the soleus and up to 32% in the EDL relative to the rates of glycogenesis (i.e., 5 mM glucose + 10 nM insulin) in each muscle. Corticosterone (10(-12)-10(-6) M) failed to alter glyconeogenesis, whereas this hormone reduced glycogenesis. Insulin (10 nM) markedly stimulated glycogenesis but failed to stimulate glyconeogenesis. The rates of both glycogenesis and glyconeogenesis were pH sensitive, with optimal rates at pH 6.5-7.0 in both muscles. Glyconeogenesis increased by 49% in the soleus and by 39% EDL at pH 6.5 compared with pH 7.4. Glycogenesis increased in the soleus (SOL) and EDL in the absence (SOL: +22%; EDL: +52%) and presence of insulin (SOL: +22%; EDL: +51%) at pH 6.5 when compared with pH 7.4. In additional experiments with the perfused rat hindquarter, rates of glyconeogenesis were shown to be highly correlated with proportion of FT muscle fibers in a muscle.(ABSTRACT TRUNCATED AT 250 WORDS)

scholarly journals Catalase-positive microperoxisomes in rat soleus and extensor digitorum longus muscle fiber types.

1988 ◽  
Vol 36 (6) ◽  
pp. 633-637 ◽  
Author(s):  
D A Riley ◽  
S Ellis ◽  
J L Bain
Keyword(s):  
Muscle Fiber ◽  
Extensor Digitorum Longus ◽  
Extensor Digitorum ◽  
Muscle Fiber Types ◽  
Fiber Types ◽  
Fiber Area ◽  
Longus Muscle ◽  
Crystalloid Inclusions ◽  
Slow Twitch ◽  
Fast Twitch

The size, distribution, and content of catalase-reactive microperoxisomes were studied cytochemically in slow-twitch oxidative (SO), fast-twitch oxidative glycolytic (FOG), and fast-twitch glycolytic (FG) fibers of soleus and extensor digitorum longus (EDL) rat muscles. Fiber types were classified on the basis of mitochondrial content and distribution, Z-band widths, and myofibril size and shape. Microperoxisomes were generally located between myofibrils at the I-bands. The absence of crystalloid inclusions prevented positive identification of microperoxisomes in nonreacted and aminotriazole-inhibited muscles. EDL and soleus SO fibers possessed the largest microperoxisomes, whereas FOG and FG fibers of the EDL contained small- to medium-sized microperoxisomes. Comparing either microperoxisome number per muscle fiber area or microperoxisome area per fiber area revealed significant differences between fiber types with this ranking: soleus SO greater than EDL SO greater than EDL FOG greater than EDL FG. The present observations demonstrate that the content of catalase-positive microperoxisomes is greatest in the oxidative muscle fiber types. These cytochemical findings account for the higher catalase activity in homogenates of soleus muscles as compared to that of EDL muscles, because the soleus contains more oxidative fibers than EDL.

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