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S Kristiansen

Publications and source records attributed to S Kristiansen.

At least 19 recordsLinked to original sources
PubMed1998

Biochemical and functional characterization of the GLUT5 fructose transporter in rat skeletal muscle.

Previous work has demonstrated that human skeletal muscle and adipose tissue both express the GLUT5 fructose transporter, but to date the issue of whether this protein is also expressed in skeletal muscle and adipose tissue of rodents has remained unresolved. In the present study we have used a combination of biochemical and molecular approaches to ascertain whether rat skeletal muscle expresses GLUT5 protein and, if so, whether it possesses the capacity to transport fructose. An isoform-specific antibody against rat GLUT5 reacted positively with crude membranes prepared from rat skeletal muscle. A single immunoreactive band of approx. 50 kDa was visualized on immunoblots which was lost when using anti-(rat GLUT5) serum that had been pre-adsorbed with the antigenic peptide. Subcellular fractionation of skeletal muscle localized this immunoreactivity to a single membrane fraction that was enriched with sarcolemma. Plasma membranes, but not low-density microsomes, from rat adipose tissue also displayed a single protein band of equivalent molecular mass to that seen in muscle. Reverse transcription-PCR analyses, using rat-specific GLUT5 primers, of muscle and jejunal RNA revealed a single PCR fragment of the expected size in jejunum and in four different skeletal muscle types. Sarcolemmal vesicles from rat muscle displayed fructose and glucose uptake. Vesicular uptake of glucose was inhibited by nearly 90% in the presence of cytochalasin B, whereas that of fructose was unaffected. To determine whether fructose could regulate GLUT5 expression in skeletal muscle, rats were maintained on a fructose-enriched diet for 4 days. This procedure increased jejunal and renal GLUT5 protein expression by approx. 4- and 2-fold respectively, but had no detectable effects on the abundance of GLUT5 protein in skeletal muscle or on fructose uptake in rat adipocytes. The present results show that GLUT5 is expressed in the sarcolemma of rat skeletal muscle and that it is likely to mediate fructose uptake in this tissue. Furthermore, unlike the situation in absorptive and re-absorptive epithelia, GLUT5 expression in insulin-sensitive tissues is not regulated by increased substrate supply.

Animals↗
PubMed1998

Phosphatidylinositol 4-kinase, but not phosphatidylinositol 3-kinase, is present in GLUT4-containing vesicles isolated from rat skeletal muscle.

Insulin stimulates the rate of glucose transport into muscle and adipose cells by translocation of glucose transporter (GLUT4)-containing vesicles from an intracellular storage pool to the surface membrane. This event is mediated through the insulin receptor substrates (IRSs), which in turn activate phosphatidylinositol (PI) 3-kinase isoforms. It has been suggested that insulin causes attachment of PI 3-kinases to the intracellular GLUT4-containing vesicles in rat adipose cells. Furthermore, it has also been shown that GLUT4-containing vesicles in adipose cells contain a PI 4-kinase. In the present study we investigate whether GLUT4-containing vesicles isolated from rat skeletal muscle display PI 3-kinase and/or PI 4-kinase activities. Insulin stimulation caused a rapid increase (5-15-fold increase compared with control) in the intracellular cytosolic IRS-1-associated PI-3 kinase activity. This PI 3-kinase activity was also present in a membrane preparation containing the insulin-regulatable pool of GLUT4 transporters. However, when GLUT4-containing vesicles were isolated by immunoprecipitation from basal and insulin-stimulated (3 min) skeletal muscle, the vesicles displayed PI 4-kinase, but not PI 3-kinase, activity. Insulin did not regulate the PI 4-kinase activity in the GLUT4-containing vesicles. In conclusion, GLUT4-containing vesicles from rat skeletal muscle contain a PI 4-kinase, but not a PI 3-kinase. It is suggested that, in skeletal muscle, insulin causes activation of the IRS/PI 3-kinase complex in an intracellular membrane compartment associated closely with the GLUT4-containing vesicles, but not in the GLUT4-containing vesicles themselves.

1-Phosphatidylinositol 4-Kinase↗
PubMed1998

Exercise metabolism in human skeletal muscle exposed to prior eccentric exercise.

1. The effects of unaccustomed eccentric exercise on exercise metabolism during a subsequent bout of graded concentric exercise were investigated in seven healthy male subjects. Arterial and bilateral femoral venous catheters were inserted 2 days after eccentric exercise of one thigh (eccentric thigh) and blood samples were taken before and during graded two-legged concentric knee-extensor exercise. Muscle biopsies were obtained from the eccentric and control vastus lateralis before (rest) and after (post) the concentric exercise bout. 2. Maximal knee-extensor concentric exercise capacity was decreased by an average of 23 % (P < 0.05) in the eccentric compared with the control thigh. 3. The resting muscle glycogen content was lower in the eccentric thigh than in the control thigh (402 +/- 30 mmol (kg dry wt)-1 vs. 515 +/- 26 mmol (kg dry wt)-1, means +/- s.e.m., P < 0.05), and following the two-legged concentric exercise this difference substantially increased (190 +/- 46 mmol (kg dry wt)-1 vs. 379 +/- 58 mmol (kg dry wt)-1, P < 0.05) despite identical power and duration of exercise with the two thighs. 4. There was no measurable difference in glucose uptake between the eccentric and control thigh before or during the graded two-legged concentric exercise. Lactate release was higher from the eccentric thigh at rest and, just before termination of the exercise bout, release of lactate decreased from this thigh (suggesting decreased glycogenolysis), whereas no decrease was found from the contralateral control thigh. Lower glycerol release from the eccentric thigh during the first, lighter part of the exercise (P < 0.05) suggested impaired triacylglycerol breakdown. 5. At rest, sarcolemmal GLUT4 glucose transporter content and glucose transport were similar in the two thighs, and concentric exercise increased sarcolemmal GLUT4 content and glucose transport capacity similarly in the two thighs. 6. It is concluded that in muscle exposed to prior eccentric contractions, exercise at a given power output requires a higher relative workload than in undamaged muscle. This increases utilization of the decreased muscle glycogen stores, contributing to decreased endurance.

Adult↗
PubMed1998

Training effects on muscle glucose transport during exercise.

Muscle glucose uptake is increased during exercise compared to rest. In general, muscle glucose uptake increases with increasing exercise intensity and duration. Whereas the arterio-venous concentration difference only increases 2-4-fold during exercise compared with rest the increase in muscle perfusion in 10-20 times and therefore quantitatively very important. During exercise the surface membrane glucose transport capacity increases in skeletal muscle primarily due to an increase in surface membrane GLUT4 protein content. Endurance training decreases muscle glucose uptake during exercise at a given absolute submaximal work-load despite a large increase in muscle GLUT4 protein content. We have shown that this decrease in glucose uptake at least in part is due to a blunted exercise-induced increase in sarcolemmal glucose transport capacity secondary to a blunted increase in sarcolemmal GLUT4 transporter number. Thus, endurance training leads to a marked reduction of the fraction of muscle GLUT4 that is translocated during a given submaximal exercise bout. Whether this is true also during exercise at higher intensities remains to be seen.

Animals↗
PubMed1998

GLUT5 expression and fructose transport in human skeletal muscle.

Biochemical and immunocytochemical studies have revealed that, in addition to GLUT1 and GLUT4, human skeletal muscle also expresses the GLUT5 hexose transporter. The subcellular distribution of GLUT5 is distinct from that of GLUT4, being localised exclusively in the sarcolemmal membrane. The substrate selectivity of GLUT5 is also considered to be different to that of GLUT1 and GLUT4 in that it operates primarily as a fructose transporter. Consistent with this suggestion studies in isolated human sarcolemmal vesicles have shown that fructose transport obeys saturable kinetics with a Vmax of 477 +/- 37 pmol.mg protein-1 min-1 and a Km of 8.3 +/- 1.2 mM. Unlike glucose uptake, fructose transport in sarcolemmal vesicles was not inhibited by cytochalasin B suggesting that glucose and fructose are unlikely to share a common route of entry into human muscle. Muscle exercise, which stimulates glucose uptake through the increased translocation of GLUT4 to the plasma membrane, does not increase fructose transport or sarcolemmal GLUT5 content. In contrast, muscle inactivity, induced as a result of limb immobilisation, caused a significant reduction in muscle GLUT4 expression with no detectable effects on GLUT5. The presence of a fructose transporter in human muscle is compatible with studies showing that this tissue can utilise fructose for both glycolysis and glycogenesis. However, the full extent to which provision of fructose via GLUT5 is important in meeting the energy requirements of human muscle during both physiological and pathophysiological circumstances remains an issue requiring further investigation.

Biological Transport↗
PubMed1998

Molecular mechanisms involved in GLUT4 translocation in muscle during insulin and contraction stimulation.

Studies in mammalian cells have established the existence of numerous intracellular signaling cascades that are critical intermediates in the regulation of various biological functions. Over the past few years considerable research has shown that many of these signaling proteins are expressed in skeletal muscle. However, the detailed mechanisms involved in the regulation of glucose transporter (GLUT4) translocation from intracellular compartments to the cell surface membrane in response to insulin and contractions in skeletal muscle are not well understood. In the present essay we report three different approaches to unravel the GLUT4 translocation mechanism: 1. specific pertubation of the insulin and/or contraction signaling pathways; 2. characterization of the protein composition of GLUT4-containing vesicles with the expectation that knowledge of the constituent proteins of the vesicles may help in understanding their trafficking; 3. degree of co-immunolocalization of the GLUT4 glucose transporters with other membrane marker proteins assessed by immunofluorescense and electron microscopy.

Animals↗
PubMed1998

Sarcolemmal glucose transport and GLUT-4 translocation during exercise are diminished by endurance training.

Glucose utilization during exercise of a given submaximal power output is decreased after endurance training. The aim of the present study was to elucidate the mechanisms behind this phenomenon by utilizing the sarcolemmal giant vesicle technique. Eight healthy young untrained men endurance trained one thigh for 3 wk. They then exercised both thighs simultaneously at the same work load (77% of peak O2 uptake of the untrained thigh) for 40 min. Training increased muscle GLUT-4 protein by 70% (P < 0.05). Glucose uptake during exercise was 38% lower (P < 0.05) in the trained (T) thigh than in the untrained (UT) thigh because of both a lower (P < 0.05) glucose extraction and blood flow in T. During exercise, sarcolemmal GLUT-4 protein content and glucose transport capacity increased significantly less in T than in UT muscle, and muscle glucose concentration was lower in T compared with UT (P < 0.05) at the end of exercise. It is concluded that, despite a large increase in muscle GLUT-4 with endurance training, exercise of a given submaximal power output increases muscle glucose uptake less in T than in UT muscle. It is suggested that the mechanism behind this phenomenon is blunted exercise-induced translocation of GLUT-4 to the sarcolemma, resulting in a blunted increase in sarcolemmal glucose transport in T muscle.

Adult↗
PubMed1998

Palmitate transport and fatty acid transporters in red and white muscles.

We performed studies 1) to investigate the kinetics of palmitate transport into giant sarcolemmal vesicles, 2) to determine whether the transport capacity is greater in red muscles than in white muscles, and 3) to determine whether putative long-chain fatty acid (LCFA) transporters are more abundant in red than in white muscles. For these studies we used giant sarcolemmal vesicles, which contained cytoplasmic fatty acid binding protein (FABPc), an intravesicular fatty acid sink. Intravesicular FABPc concentrations were sufficiently high so as not to limit the uptake of palmitate under conditions of maximal palmitate uptake (i.e., 4.5-fold excess in white and 31.3-fold excess in red muscle vesicles). All of the palmitate taken up was recovered as unesterified palmitate. Palmitate uptake was reduced by phloretin (-50%), sulfo-N-succinimidyl oleate (-43%), anti-plasma membrane-bound FABP (FABPpm, -30%), trypsin (-45%), and when incubation temperature was lowered to 0 degrees C (-70%). Palmitate uptake was also reduced by excess oleate (-65%), but not by excess octanoate or by glucose. Kinetic studies showed that maximal transport was 1.8-fold greater in red vesicles than in white vesicles. The Michaelis-Menten constant in both types of vesicles was approximately 6 nM. Fatty acid transport protein mRNA and fatty acid translocase (FAT) mRNA were about fivefold greater in red muscles than in white muscles. FAT/CD36 and FABPpm proteins in red vesicles or in homogenates were greater than in white vesicles or homogenates (P < 0.05). These studies provide the first evidence of a protein-mediated LCFA transport system in skeletal muscle. In this tissue, palmitate transport rates are greater in red than in white muscles because more LCFA transporters are available.

Animals↗
PubMed1997

Membrane associated fatty acid binding protein (FABPpm) in human skeletal muscle is increased by endurance training.

Endurance training increases the capacity for utilization of fatty acids. Since fatty acids are believed to enter cells via facilitated diffusion a possible mechanism behind this adaptation to training might be a training-induced increase in membrane content of putative fatty acid transporters. We investigated whether the expression of the 40 KD membrane associated fatty acid binding protein (FABPpm) in skeletal muscle is increased with endurance training in man. The FABPpm was detectable in a crude membrane preparation from human skeletal muscle. Three weeks of intense one-legged endurance training increased (p < 0.05) the content of FABPpm by 49% whereas in the untrained control muscle no change was observed. In addition, the activity of citrate synthase was increased (p < 0.05) by 20% in the trained compared with the untrained muscle. It is concluded that expression of FABPpm in human skeletal muscle is increased with endurance training consistent with a role of FABPpm as a sarcolemmal fatty acid transporter.

Adult↗
PubMed1997

Eccentric contractions decrease glucose transporter transcription rate, mRNA, and protein in skeletal muscle.

We have recently shown that eccentric contractions (ECs; forced lengthening of active muscle) elicit a delayed decrease in glucose transporter (GLUT-4) protein content in rat skeletal muscle and a decrease in subsequent contraction-stimulated glucose transport. Here, we investigate whether this decrease in total GLUT-4 protein after prior ECs is due to changes in GLUT-4 gene transcription rate and GLUT-4 mRNA level. Furthermore, the effect of prior ECs on sarcolemmal GLUT-4 protein content in plasma membrane (PM) vesicles isolated from contraction-stimulated muscle was determined. Rat gastrocnemius muscle was electrically stimulated for ECs, and the contralateral muscle served, as unstimulated control (UC). Two days later, the total GLUT-4 protein content was decreased by 50% (P < 0.05) and 32% (P < 0.05) in the white and red gastrocnemius muscle, respectively. Furthermore, the GLUT-4 mRNA concentration was decreased by 41% (P < 0.05) in both the white and red gastrocnemius muscle. Moreover, the GLUT-4 transcription rate, determined by nuclear run-on analysis, was decreased by 75% (P < 0.05) in mixed EC gastrocnemius muscle compared with UC muscle. PM vesicles were isolated from EC and UC muscle after 15 min of isometric contractions. The PM GLUT-4 protein content was reduced by 51% (P < 0.05) in EC muscle compared with UC muscle. In conclusion, 2 days after ECs, the GLUT-4 transcription rate, GLUT-4 mRNA, and GLUT-4 protein content were decreased in rat skeletal muscle. Moreover, the PM GLUT-4 protein content in contraction-stimulated muscle was decreased. We suggest that eccentric muscle contractions decrease muscle GLUT-4 transcription rate, resulting in a lower GLUT-4 protein content, which in turn decreases the number of GLUT-4 transporters translocated to the sarcolemma, ultimately leading to decreased contraction-induced muscle glucose transport.

Animals↗
PubMed1997

Progressive increase in glucose transport and GLUT-4 in human sarcolemmal vesicles during moderate exercise.

Muscle glucose uptake increases progressively during moderate-intensity exercise. To elucidate whether this is due to a progressive increase in sarcolemmal glucose transport capacity, nine men exercised for 40 min at 75% maximal oxygen uptake on a bicycle ergometer. Muscle biopsies were obtained from the vastus lateralis at rest (0 min) and after 5 and 40 min of exercise and used for production of sarcolemmal giant (SG) vesicles. SG vesicle glucose transport at 5 mM increased (P < 0.05) by 38 and 93% after 5 and 40 min of exercise, respectively, compared with glucose transport at rest. The SG vesicle GLUT-4 protein content increased (P < 0.05) by 36 and 91% after 5 and 40 min of exercise, respectively, compared with rest. Thus the increase in vesicle glucose transport was accompanied by a similar increase in SG vesicle GLUT-4 protein content. Muscle glucose and glucose 6-phosphate were low at rest, increased (P < 0.05) 2.2- and 2.3-fold, respectively, after 5 min of exercise, and returned to resting values after 40 min of exercise. It is concluded that the progressive increase in muscle glucose uptake during moderate-intensity exercise may be due at least in part to a progressive increase in sarcolemmal glucose transport and GLUT-4 protein content.

Adult↗
PubMed1997

Fructose transport and GLUT-5 protein in human sarcolemmal vesicles.

Sarcolemmal vesicles were produced from human skeletal muscle biopsy material obtained at rest and immediately after maximal dynamic exercise (100% maximal O2 uptake) for analysis of fructose transport and hexose transporter (GLUT-5) protein concentration. Human sarcolemmal vesicles displayed a time-dependent uptake of D-fructose that displayed saturable Michaelis-Menten type kinetics (maximal transport 477 +/- 37 pmol.min-1.mg protein-1; half-maximal concentration constant 8.3 +/- 1.2 mM). At a hexose concentration of 5 mM, vesicle transport rate was eight times faster for glucose than for fructose. Preincubation of human muscle vesicles with 35 microM cytochalasin B before the uptake assay resulted in > 95% inhibition in D-glucose uptake, whereas transport of D-fructose was unaffected. Sarcolemmal vesicles prepared from exercised human muscle showed a significant increase (49%) in vesicle GLUT-4 content (P < 0.03, n = 10), which accounts for the increase in vesicle glucose transport that we have recently reported [S. Kristiansen, M. Hargreaves, and E.A. Richter. Am. J. Physiol. 270 (Endocrinol. Metab. 33): E197-E201, 1996]. In contrast, exercise did not increase the vesicle GLUT-5 protein content or induce changes in vesicle fructose transport activity. In conclusion, we propose that fructose transport into human skeletal muscle occurs via a mechanism distinct from that utilized by glucose on the basis of differences in sensitivity to cytochalasin B and responsiveness to exercise. Furthermore, our findings signify that uptake of fructose in human skeletal muscle is mediated by the GLUT-5 transporter.

Adult↗
PubMed1996

Eccentric exercise decreases maximal insulin action in humans: muscle and systemic effects.

1. Unaccustomed eccentric exercise decreases whole-body insulin action in humans. To study the effects of one-legged eccentric exercise on insulin action in muscle and systemically, the euglycaemic clamp technique combined with arterial and bilateral femoral venous catheterization was used. Seven subjects participated in two euglycaemic clamps, performed in random order. One clamp was preceded 2 days earlier by one-legged eccentric exercise (post-eccentric exercise clamp (PEC)) and one was without the prior exercise (control clamp (CC)). 2. During PEC the maximal insulin-stimulated glucose uptake over the eccentric thigh was marginally lower when compared with the control thigh, (11.9%, 64.6 +/- 10.3 vs. 73.3 +/- 10.2 mumol kg-1 min-1, P = 0.08), whereas no inter-thigh difference was observed at a submaximal insulin concentration. The glycogen concentration was lower in the eccentric thigh for all three clamp steps used (P < 0.05). The glucose transporter GLUT4 protein content was on average 39% lower (P < 0.05) in the eccentric thigh in the basal state, whereas the maximal activity of glycogen synthase was identical in the two thighs for all clamp steps. 3. The glucose infusion rate (GIR) necessary to maintain euglycaemia during maximal insulin stimulation was lower during PEC compared with CC (15.7%, 81.3 +/- 3.2 vs. 96.4 +/- 8.8 mumol kg-1 min-1, P < 0.05). 4. Our data show that 2 days after unaccustomed eccentric exercise, muscle and whole-body insulin action is impaired at maximal but not submaximal concentrations. The local effect cannot account for the whole-body effect, suggesting the release of a factor which decreases insulin responsiveness systemically.

Adult↗
PubMed1996

Effect of vanadate on glucose transporter (GLUT4) intrinsic activity in skeletal muscle plasma membrane giant vesicles.

Maximally effective concentrations of vanadate (a phosphotyrosine phosphatase inhibitor) increase glucose transport in muscle less than maximal insulin stimulation. This might be due to vanadate-induced decreased intrinsic activity of GLUT4 accompanying GLUT4 translocation. Thus, the effect of vanadate (NaVO3) on glucose transporter (GLUT4) intrinsic activity (V(max) = intrinsic activity x [GLUT4 protein]) was studied in muscle plasma membrane giant vesicles. Giant vesicles (average diameter 7.6 microns) were produced by collagenase treatment of rat skeletal muscle. The vesicles were incubated for 1.5 h with concentrations of vanadate ranging from 3 to 40 mmol l-1 at 34 degrees C before being used for determination of glucose transport. The dose-response curve showed that vanadate decreased the specific D-glucose uptake by a maximum of 70% compared with a control preparation. The vanadate-induced decrease in glucose uptake was not due to a decrease in number of vesicles. To further verify the apparent vanadate-induced decrease in GLUT4 intrinsic activity, the kinetics of glucose transport were also examined. In the presence of 10 mmol l-1 vanadate the V(max) and K(m) were decreased (P < 0.05, n = 6) 55% and 60%, respectively, compared with control. The plasma membrane GLUT4 protein content was not changed in response to vanadate. It is concluded that vanadate decreased glucose transport per GLUT4 (intrinsic activity). This finding suggests that regulation of glucose transport in skeletal muscle can involve changes in GLUT4 intrinsic activity.

Animals↗
PubMed1996

Exercise-induced increase in glucose transport, GLUT-4, and VAMP-2 in plasma membrane from human muscle.

A major effect of muscle contractions is an increase in sarcolemmal glucose transport. We have used a recently developed technique to produce sarcolemmal giant vesicles from human muscle biopsy samples obtained before and after exercise. Six men exercised for 10 min at 50% maximal O2 uptake (Vo2max) and then to fatigue at 100% Vo2max (5.7 +/- 0.2 min). Vesicle glucose transport at 5 mM increased from 3.3 +/- 0.6 pmol.microgram-1.min-1 at rest to 6.6 +/- 1.0 pmol.microgram-1.min-1 at fatigue (mean +/- SE, n = 6, P < 0.05). This increase in glucose transport was associated with a 1.6-fold increase in vesicle GLUT-4 protein content. Glucose transport normalized to GLUT-4 protein content also increased with exercise, suggesting increased intrinsic activity of GLUT-4. Furthermore, exercise resulted in a 1.4-fold increase in sarcolemmal vesicle-associated membrane protein (VAMP-2) content, suggesting that muscle contractions may induce trafficking of GLUT-4-containing vesicles via a mechanism similar to neurotransmitter release. Our results demonstrate for the first time exercise-induced translocation of GLUT-4 and VAMP-2 to the plasma membrane of human muscle and increased sarcolemmal glucose transport.

Adult↗
PubMed1996

Decreased muscle GLUT-4 and contraction-induced glucose transport after eccentric contractions.

Eccentric exercise causes muscle damage and decreased muscle glycogen and glucose transporter isoform (GLUT-4) protein content. We investigated whether the contraction-induced increase in skeletal muscle glucose transport and muscle performance is affected by prior eccentric contractions. The calf muscles from rats were stimulated for eccentric (EC) or concentric (CC) contractions or were passively stretched (ST). Muscles from unstimulated control (CT) rats were also studied. Two days later, all rats had their isolated hindlimbs perfused either at rest or during 15 min of isometric muscle contractions. EC rats had a significantly lower total GLUT-4 protein content in the white gastrocnemius (GW) muscle (55%) and red gastrocnemius (GR) muscle (34%) compared with muscle from the CT, ST, and CC rats. In contrast, GLUT-1 protein content was approximately twofold higher in the GW muscle in EC rats than in CT rats. In the GW and GR muscle, prior eccentric exercise decreased contraction-induced stimulation of glucose transport compared with CT, ST, and CC rats despite no difference in tension development and oxygen uptake among the groups. There was no change in total GLUT-4 content and glucose transport in the soleus (S) muscle among the four group. It is concluded that the GLUT-4 and GLUT-1 protein contents in fast-twitch muscle are decreased and increased, respectively, 2 days after eccentric contractions. The functional consequence of these changes appears to be decreased contraction-induced increase in skeletal muscle glucose transport.

Animals↗
PubMed1995

Eccentric muscle damage transiently decreases rat skeletal muscle GLUT-4 protein.

The effects of concentric and muscle-damaging eccentric contractions on muscle glucose transporter GLUT-4 content were studied in rat muscles. Rats were anesthetized, the calf muscles on one side were stimulated electrically for concentric or eccentric contractions, and bilateral calf muscles were obtained in the postexercise period. Inflammatory and phagocytic cells accumulated in the eccentric white and red gastrocnemius muscles, whereas there were only discrete changes in the eccentric soleus. Glycogen was depleted to the same extent in the white and red gastrocnemius muscles after both types of stimulation, and it remained decreased > 2 days in eccentric muscles. The total GLUT-4 protein content was decreased in the eccentric white and red gastrocnemius muscles 1 and 2 days after the eccentric stimulation, whereas the maximal activity of glycogen synthase was unaffected at these time points. In conclusion, our one-legged stimulation model caused eccentric muscle damage in the white and red gastrocnemius, whereas only minor damage was observed in the soleus muscle. In damaged muscle, muscle glycogen and GLUT-4 protein content were decreased for > 2 days. These findings may suggest (but do not prove) that decreased muscle GLUT-4 protein is involved in the delayed glycogen resynthesis after eccentric exercise.

Animals↗