Biomedical subjects

E Hultman

Publications and source records attributed to E Hultman.

At least 37 records · Page 2Linked to original sources

PubMed1998

Regulation of skeletal muscle glycogen phosphorylase and PDH at varying exercise power outputs.

This study investigated the transformational and posttransformational control of skeletal muscle glycogen phosphorylase and pyruvate dehydrogenase (PDH) at three exercise power outputs [35, 65, and 90% of maximal oxygen uptake (VO2 max)]. Seven untrained subjects cycled at one power output for 10 min on three separate occasions, with muscle biopsies at rest and 1 and 10 min of exercise. Glycogen phosphorylase in the more active (a) form was not significantly different at any time across power outputs (21. 4-29.6%), with the exception of 90%, where it fell significantly to 15.3% at 10 min. PDH transformation increased significantly from rest (average 0.53 mmol . kg wet muscle-1 . min-1) to 1 min of exercise as a function of power output (1.60 +/- 0.26, 2.77 +/- 0.29, and 3.33 +/- 0.31 mmol . kg wet muscle-1 . min-1 at 35, 65, and 90%, respectively) with a further significant increase at 10 min (4.45 +/- 0.35) at 90% VO2 max. Muscle lactate, acetyl-CoA, acetylcarnitine, and free ADP, AMP, and Pi were unchanged from rest at 35% VO2 max but rose significantly at 65 and 90%, with accumulations at 90% being significantly higher than 65%. The results of this study indicate that glycogen phosphorylase transformation is independent of increasing power outputs, despite increasing glycogenolytic flux, suggesting that flux through glycogen phosphorylase is matched to the demand for energy by posttransformational factors, such as free Pi and AMP. Conversely, PDH transformation is directly related to the increasing power output and the calculated flux through the enzyme. The rise in PDH transformation is likely due to increased Ca2+ concentration and/or increased pyruvate. These results demonstrate that metabolic signals related to contraction and the energy state of the cell are sensitive to the exercise intensity and coordinate the increase in carbohydrate use with increasing power output.

Acetyl Coenzyme A↗

PubMed1998

Regulation of muscle glycogenolytic flux during intense aerobic exercise after caffeine ingestion.

This study examined the effects of caffeine (Caf) ingestion on muscle glycogen use and the regulation of muscle glycogen phosphorylase (Phos) activity during intense aerobic exercise. In two separate trials, 12 untrained males ingested either placebo (Pl) or Caf (9 mg/kg body wt) 1 h before cycling at 80% maximum O2 consumption (VO2 max) for 15 min. Muscle biopsies were obtained from the vastus lateralis at 0, 3, and 15 min of exercise. In this study, glycogen "sparing" was defined as a 10% or greater reduction in muscle glycogen use during exercise after Caf ingestion compared with Pl. Muscle glycogen use decreased by 28% (Pl 255 +/- 38 vs. Caf 184 +/- 24 mmol/kg dry muscle) after Caf in six subjects [glycogen sparers (Sp)] but was unaffected by Caf in six other subjects [nonsparers (NSp), Pl 210 +/- 35 vs. Caf 214 +/- 37 mmol/kg dry muscle]. In both groups, Caf significantly increased resting free fatty acid concentration, significantly increased epinephrine concentration by twofold during exercise, and increased the Phos a mole fraction at 3 min of exercise compared with Pl, although not significantly. Caf improved the energy status of the muscle during exercise in the Sp group: muscle phosphocreatine (PCr) degradation was significantly reduced (Pl 47.9 +/- 3.6 vs. Caf 40.4 +/- 6.7 mmol/kg dry muscle at 3 min) and the accumulations of free ADP and free AMP (Pl 6.8 +/- 1.3 vs. Caf 3.1 +/- 1.4 micromol/kg dry muscle at 3 min; Pl 8.7 +/- 0.8 vs. Caf 4.7 +/- 1.1 micromol/kg dry muscle at 15 min) were significantly reduced. Caf had no effect on these measurements in the NSp group. It is concluded that the Caf-induced decrease in flux through Phos (glycogen-sparing effect) is mediated via an improved energy status of the muscle in the early stages of intense aerobic exercise. This may be related to an increased availability of fat and/or ability of mitochondria to oxidize fat during exercise preceded by Caf ingestion. It is presently unknown why the glycogen-sparing effect of Caf does not occur in all untrained individuals during intense aerobic exercise.

Adenosine Diphosphate↗

PubMed1997

Longitudinal changes of biochemical parameters in muscle during critical illness.

The study was undertaken to characterize the time course of biochemical parameters in skeletal muscle during critical illness to gain information for the design of a suitable protocol for interventional studies using metabolic or nutritional manipulation. Critically ill patients in our intensive care unit ([ICU] N = 9) were investigated on two separate sampling occasions with percutaneous muscle biopsies for determination of protein, nucleic acids, free amino acids, energy-rich phosphates, fat, water, and electrolytes. The first biopsy specimen was taken 3 to 11 days after admission and the second biopsy specimen 3 to 7 days later. Protein concentration, expressed as alkali-soluble protein (ASP)/DNA, decreased by 12% (P < .02) between the two biopsies. The total free amino acid content was only 50% of normal, but remained unaltered over time. In particular, the concentration of glutamine remained low, approximately 25% of normal. In contrast, branched-chain amino acid (BCAA) increased by 25% (P < .05) and phenylalanine by 55% (P < .05) between biopsies. The fat content related to fat-free solid (FFS) increased by 130% (P < .001) between the two biopsies. Muscle water did not change during the study period. The extracellular portion was double the normal value when related to FFS. Intracellular water, on the other hand, was outside the 95% confidence interval for normal values in the second biopsy. The concentrations of adenosine triphosphate (ATP), creatine, phosphocreatine, and the phosphorylated fraction of total creatine remained at the same level between the two biopsies. We conclude that in critically ill patients, there is a decrease in protein content over time and increases in BCAA, phenylalanine, and fat content, while the low glutamine level and high extracellular water content remain unaltered. The temporal alterations were well characterized after a 5-day study period.

Adult↗

PubMed1997

Resting membrane potential of skeletal muscle calculated from plasma and muscle electrolyte and water contents.

1. A method is described that enables the calculation of resting membrane potential from the electrolyte and water contents in blood plasma and in a sample of human muscle tissue obtained by the percutaneous needle-biopsy technique. In this calculation, the previously described equations for calculating resting membrane potential via the intra- and extra-cellular distribution of chloride were combined with the equation utilizing potassium distribution over the cell membrane. 2. The method of calculation was applied to 60 healthy subjects divided into three groups aged 19-40, 41-60 and 61-85 years. The calculated resting membrane potential in the subjects as a whole was -88.4 mV (SD 1.35; n = 60). A lower value was observed in the group aged 61-85 years (-87.7 mV, SD 1.0; n = 12) than in the group aged 19-40 years (-88.6 mV; SD 1.4; n = 32). No difference was observed between female and male subjects. 3. The RMP calculated with the present method in 60 healthy subjects was also compared with previously published values in healthy subjects, measured by the Clarke electrode method, and with values calculated from electrolyte and water distribution measured by isotope-dilution techniques. The results obtained in healthy subjects with different techniques were very similar. Data were analysed from earlier published studies in experimental animals in which resting membrane potential ranged from -91 to -65 mV. The resting membrane potential calculated from electrolytes in plasma and muscle showed a very good agreement with resting membrane potential recorded directly.

Adult↗

PubMed1997

Nutritional status affects branched-chain oxoacid dehydrogenase activity during exercise in humans.

We examined the effect of glycogen availability and branched-chain amino acid (BCAA) supplementation on branched-chain oxoacid dehydrogenase (BCOAD) activity during exercise. Six subjects cycled at approximately 75% of their maximal oxygen uptake to exhaustion on three occasions under different preexercise conditions: 1) low muscle glycogen (LOW), 2) low muscle glycogen plus BCAA supplementation (LOW+BCAA), and 3) high muscle glycogen (CON). The LOW trial was performed first, followed by the other two conditions in random order, and biopsies for all trials were obtained at rest, after 15 min of exercise (15 min), and at the point of exhaustion during the LOW trial (49 min). BCOAD activity was not different among the three conditions at rest; however, at 15 min BCOAD activity was higher (P < or = 0.05) for the LOW (31 +/- 5%) and LOW+BCAA (43 +/- 11%) conditions compared with CON (12 +/- 1%). BCOAD activity at 49 min was not different from respective values at 15 min for any condition. These data indicate that BCOAD is rapidly activated during submaximal exercise under conditions associated with low carbohydrate availability. However, there was no relationship between BCOAD activity and glycogen concentration or net glycogenolysis, which suggests that factors other than glycogen availability are important for BCOAD regulation during exercise in humans.

3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide)↗

PubMed1996

Markedly improved skeletal muscle function with local muscle training in patients with chronic heart failure.

BACKGROUND: Reduced heart pump function and skeletal muscle abnormalities are considered important determinants for the low physical exercise capacity in chronic heart failure. Because of reduced ventricular function, traditional physical rehabilitation may cause underperfusion and low local work intensity, thereby producing suboptimal conditions for skeletal muscle training. HYPOTHESIS: The study was undertaken to determine the effects of local exercise training, designed as one- or two-legged knee extensor training, on exercise capacity in patients with moderate chronic heart failure. Because such exercise models use only about one quarter to half the muscle mass used in cycle ergometer training, the influence of a restricted circulatory capacity should therefore be limited. Further, we aimed to determine whether or not chronic heart failure skeletal musculature abnormalities are counteracted with such training. METHODS: Fourteen patients with chronic heart failure [age 58 +/- 3 years, ejection fraction (EF) 28 +/- 4%] were randomized to two different training protocols three times a week for 8 weeks and compared with a nontraining control group (n = 7, age 62 +/- 3, EF 27 +/- 3%). Group 2L (n = 7) underwent simultaneous two-legged knee extensor training (about 4 kg working muscle) for 15 min at 65-75% of VO2 max of the two-legged kick. Group 1L (n = 7) trained each leg at a time for 15 min of continuous one-legged dynamic knee extensor work with the same training load per muscle mass, that is, at 35% of VO2 max of the two-legged kick (about 2 kg working muscle). Peak VO2 of two-legged knee extensor exercise (l/min), two-legged endurance (W), and strength (Nm) were determined before and after the training period. The activity of citrate synthase (CS) was estimated in tissue samples from the quadriceps femoris muscle. RESULTS: Peak VO2 did not change with training. Two-legged knee extensor endurance exercise capacity increased by an average of 40-50% (p < 0.01) in all training patients in both the 2L and 1L groups, while no change was observed in the control group. Depressed skeletal muscle CS activity increased by 25-35% in both training groups (p < 0.01). Strength increased by 16% in the 2L group after training (p < 0.05), while no change was seen in the 1L and control groups. CONCLUSIONS: Skeletal muscle changes in stable moderate chronic heart failure are not entirely irreversible. A major factor contributing to these changes and to exercise limitation is deconditioning. Local muscle training is efficient and can at least partially improve skeletal muscle function in these patients. Different degrees of local activation, that is, one- or two-legged knee extensor exercise, do not seem to differ in terms of their effect on exercise capacity. Depressed skeletal muscle oxidative capacity adapts to such physical training with increased activity to an extent not different from that for healthy volunteers.

Adaptation, Physiological↗

PubMed1996

The effect of repeated muscle biopsy sampling on ATP and glycogen resynthesis following exercise in man.

The present study investigated the effect of repeated biopsy sampling on muscle adenosine 5'-triphosphate (ATP) and glycogen resynthesis following prolonged submaximal exercise. In one group of subjects (Ia, n = 7), biopsy specimens were obtained from the vastus lateralis immediately and 48 h after exhaustive one-legged cycling from both the non-exercised (control) and exercised legs. Additional samples were obtained from the exercised leg at 3, 10 and 24 h post-exercise. In a second group of subjects (Ib, n = 6), biopsy specimens were obtained immediately after exercise from both the control and exercised legs and at 48 h post-exercise from the exercised leg. All muscle biopsies were separated by a distance of 2.5 cm. In group Ia, ATP in the exercised leg was still lower after 48 h of recovery compared with the control leg (P <0.05), but complete restoration had occurred in group Ib (P > 0.05). Glycogen super compensation was not observed in group Ia. However, at the end of recovery, in group Ib glycogen in the exercised leg was 42 percent greater than in the control leg (P <0.01). Thus, following exhaustive dynamic exercise, repeated muscle biopsy sampling impaired ATP and glycogen resynthesis for several days, which may have been a result of the distance separating each biopsy site. The inhibition of ATP resynthesis appeared to be associated mainly with type II muscle fibres. The finding that, in contrast to muscle glycogen, ATP did not return to the basal level during the 48 h of recovery, suggests that the measurement of ATP may be a more sensitive measure of muscle damage than that of glycogen.

Adenosine Triphosphate↗

PubMed1996

No change in insulin mediators in human skeletal muscle during isometric contraction or recovery.

The rapid activation of glycogen synthase in human skeletal muscle during recovery from isometric contraction is dependent on an intact circulation, which suggests the requirement of an activating humoral factor. To determine whether the activating factor is insulin, muscle biopsies were obtained from subjects at rest, at fatigue, 3 min postexercise with an intact circulation, and 3 min postexercise during which circulation to the muscle was occluded. Two inositol phosphoglycan mediators of insulin action were isolated from the biopsies, and bioactivity was measured by determining the effects of the isolated mediators on the activities of purified cyclic AMP-dependent protein kinase, pyruvate dehydrogenase phosphatase and glycogen synthase phosphatase in vitro. Bioactivity was not altered by any condition compared with rest. These data suggest that changes in inositol phosphoglycans are not responsible for the circulation-dependent activation of glycogen synthase during recovery from exercise.

Adult↗

PubMed1996

A descriptive study of skeletal muscle metabolism in critically ill patients: free amino acids, energy-rich phosphates, protein, nucleic acids, fat, water, and electrolytes.

OBJECTIVE: To characterize biochemical changes in skeletal muscle in critically ill patients. DESIGN: Survey of critically ill patients. SETTING: Intensive care unit (ICU) at a university hospital. PATIENTS: Critically ill patients (n = 20) subjected to trauma, surgical complications, and/or bacteremia who were treated in the ICU and showed no risk of bleeding complications were included. Reference groups of metabolically healthy volunteers and patients served as the control/reference groups. INTERVENTIONS: Percutaneous muscle biopsy was obtained from both patients and healthy volunteers. MEASUREMENTS AND MAIN RESULTS: Total free amino acids in skeletal muscle decreased 59% (p < .001) and skeletal muscle glutamine concentration decreased 72% (p < .001) in the critically ill patients. Basic amino acids decreased 49% (p < .001). Branch-chain amino acids increased 39% (p < .01), and aromatic amino acids increased 88% (p < .001) in the patients. Adenosine triphosphate (ATP) was reduced by 12% (p < .01). Total creatine concentration increased by 26% (p < .001) due to an 80% increase in free creatine (p < .001). The phosphorylated creatine fraction of total creatine decreased 22% (p < .001) in the patients. Alkali-soluble protein/DNA decreased 24% (p < .01) and fat free solid/DNA decreased 21% (P <.01) in patients sampled on or after ICU day 5 compared with the reference group. Muscle water increased 10% due to a doubling of the extracellular water fraction. CONCLUSIONS: Although critically ill patients are a very heterogeneous group from a clinical point of view, there is a remarkable homogeneity in many of the biochemical parameters regardless of the severity of illness and the length of the ICU admission. The three most consistent differences were the skeletal muscle low glutamine concentration, the decrease in protein content, and the increase in extracellular water in the patients.

APACHE↗

PubMed1996

Regulation of muscle glycogen phosphorylase activity during intense aerobic cycling with elevated FFA.

This study examined muscle glycogenolysis and the regulation of glycogen phosphorylase (Phos) activity during 15 min of cycling at 85% of maximal O2 consumption (VO2max) in control and high free fatty acid (FFA; Intralipid-heparin) conditions in 11 subjects. Muscle biopsies were sampled at rest and 1, 5, and 15 min of exercise, and glycogen Phos transformation state (%Phos alpha), substrate (Pi, glycogen), and allosteric regulator (ADP, AMP, IMP) contents were measured. Infusion of intralipid elevated plasma FFA from 0.32 +/- 0.04 mM at rest to 1.00 +/- 0.04 mM just before exercise and 1.12 +/- 0.10 mM at 14 min of exercise. In the control trial, plasma FFA were 0.36 +/- 0.04 mM at rest and unchanged at the end of exercise (0.34 +/- 0.03 mM). Seven subjects used less muscle glycogen (46.7 +/- 7.6%, mean +/- SE) during the Intralipid trial, and four did not respond. In subjects who spared glycogen, glycogen Phos transformation into the active (alpha) form was unaffected by high FFA except for a nonsignificant reduction during the initial 5 min of exercise. Total AMP and IMP contents were not significantly different during exercise between trials, but total ADP was significantly lower with Intralipid only at 15 min. The calculated free ADP, AMP, and Pi contents were lower with Intralipid but not significantly different. However, when the present results were pooled with the data from a previous study using the same protocol [Dyck et al., Am. J. Physiol. 265 (Endocrinol, Metab. 28): E852-E859, 1993], the free ADP, AMP, and Pi contents of all subjects who spared glycogen (n = 13) were significantly lower at 15 min in the Intralipid trial. The findings suggest that the elevation of plasma FFA during intense cycling spares muscle glycogen by posttransformational regulation of Phos. This may be due to blunted increases in the contents of AMP, an allosteric activator of Phos alpha, and Pi, a substrate for Phos.

Adult↗

PubMed1996

Creatine ingestion favorably affects performance and muscle metabolism during maximal exercise in humans.

Nine male subjects performed two bouts of 30-s maximal isokinetic cycling before and after ingestion of 20 g creatine (Cr) monohydrate/day for 5 days. Cr ingestion produced a 23.1 +/- 4.7 mmol/kg dry matter increase in the muscle total creatine (TCr) concentration. Total work production during bouts 1 and 2 increased by approximately 4%, and the cumulative increases in both peak and total work production over the two exercise bouts were positively correlated with the increase in muscle TCr. Cumulative loss of ATP was 30.7 +/- 12.2% less after Cr ingestion, despite the increase in work production. Resting phosphocreatine (PCr) increased in type I and II fibers. Changes in PCr before exercise bouts 1 and 2 in type II fibers were positively correlated with changes in PCr degradation during exercise in this fiber type and changes in total work production. The results suggest that improvements in performance were mediated via improved ATP resynthesis as a consequence of increased PCr availability in type II fibers.

Adenosine Triphosphate↗

PubMed1996

Metabolic response of type I and II muscle fibers during repeated bouts of maximal exercise in humans.

Nine male subjects performed two bouts of 30-s maximal isokinetic cycling. Each bout of exercise was performed at 80 revolutions/min and was separated by 4 min of recovery. Mixed-muscle phosphocreatine (PCr) resynthesis during recovery (88.1 +/- 6.1%) was positively correlated with the restoration of total work production during bout 2 (r = 0.80, P < 0.05). During bout 1, ATP and PCr utilization were greater in type II compared with type I fibers (P < 0.01 and P < 0.05, respectively). The subsequent 4-min period of recovery was insufficient to allow total restoration of ATP and PCr in type II fibers, but restoration of ATP and PCr in type I fibers was almost complete. During the second bout of exercise, ATP and PCr utilization were reduced in type II fibers (P < 0.01), without a corresponding change in type I fibers, and performance was also significantly reduced. The reduction in work capacity observed during bout 2 may have been related to a slower resynthesis, and consequently a reduced availability, of ATP and PCr in type II fibers.

Adenosine Triphosphate↗

PubMed1996

Carbohydrate ingestion augments skeletal muscle creatine accumulation during creatine supplementation in humans.

This study investigated the effect of carbohydrate (CHO) ingestion on skeletal muscle creatine (Cr) accumulation during Cr supplementation in humans. Muscle biopsy, urine, and plasma samples were obtained from 24 males before and after ingesting 5 g Cr in solution (group A) or 5 g Cr followed, 30 min later, by 93 g simple CHO in solution (group B) four times each day for 5 days. Supplementation resulted in an increase in muscle phosphocreatine (PCr), Cr, and total creatine (TCr; sum of PCr and Cr) concentration in groups A and B, but the increase in TCr in group B was 60% greater than in group A (P < 0.01). There was also a corresponding decrease in urinary Cr excretion in group B (P < 0.001). Creatine supplementation had no effect on serum insulin concentration, but Cr and CHO ingestion dramatically elevated insulin concentration (P < 0.001). These findings demonstrate that CHO ingestion substantially augments muscle Cr accumulation during Cr feeding in humans, which appears to be insulin mediated.

Adenosine Diphosphate↗

PubMed1996

Muscle creatine loading in men.

The effect of dietary creatine and supplementation on skeletal muscle creatine accumulation and subsequent degradation and on urinary creatinine excretion was investigated in 31 male subjects who ingested creatine in different quantities over varying time periods. Muscle total creatine concentration increased by approximately 20% after 6 days of creatine supplementation at a rate of 20 g/day. This elevated concentration was maintained when supplementation was continued at a rate of 2 g/day for a further 30 days. In the absence of 2 g/day supplementation, total creatine concentration gradually declined, such that 30 days after the cessation of supplementation the concentration was no different from the presupplementation value. During this period, urinary creatinine excretion was correspondingly increased. A similar, but more gradual, 20% increase in muscle total creatine concentration was observed over a period of 28 days when supplementation was undertaken at a rate of 3 g/day. In conclusion, a rapid way to "creatine load" human skeletal muscle is to ingest 20 g of creatine for 6 days. This elevated tissue concentration can then be maintained by ingestion of 2 g/day thereafter. The ingestion of 3 g creatine/day is in the long term likely to be as effective at raising tissue levels as this higher dose.

Adenosine Triphosphate↗

PubMed1995

Glycogen resynthesis in human muscle fibre types following exercise-induced glycogen depletion.

1. Studies investigating muscle glycogen resynthesis in man have usually examined mixed-fibred biopsies or have used histochemical methods to estimate single fibre resynthesis. Since the accuracy of the latter is open to debate, this study investigated glycogen resynthesis in type I and II fibres using biochemical methods of analysis. 2. Seven subjects performed one-legged cycling exercise to exhaustion. During the initial 2 h of recovery, subjects consumed 3 g of glucose (kg body mass (BM))-1, and a high carbohydrate diet thereafter. Muscle biopsy samples were obtained from both legs at exhaustion, and from the exercised leg after 3, 10 and 24 h of recovery. 3. In the initial 3 h of recovery, there was a 25 +/- 8% higher rate of resynthesis in type I compared with type II fibres (41 +/- 3 and 31 +/- 4 mmol glucosyl units (kg dry mass (DM))-1 h-1, respectively; P < 0.05). Between 3 and 10 h of recovery, resynthesis in type I fibres declined by 60 +/- 13% to 15 +/- 4 mmol glucosyl units (kg DM)-1 h-1 (P < 0.01), whilst the rate in type II fibres was maintained. Good agreement was found when relating the mixed-fibred muscle glycogen concentration to the mean concentration found in type I and type II fibres (r = 0.96). 4. A discrepancy was found to exist with histochemically derived data reported in the literature. The higher initial glycogen resynthesis rate in type I fibres may be attributable to fibre-type differences in glucose uptake and disposal.(ABSTRACT TRUNCATED AT 250 WORDS)

Adult↗

PubMed1995

Human skeletal muscle protein: effect of malnutrition, elective surgery and total parenteral nutrition.

1. The concentration of alkali-soluble protein, DNA and RNA in percutaneous muscle biopsy specimens was analysed. Tissue alkali-soluble protein/DNA ratio is a measure of muscle protein concentration, while tissue RNA/DNA ratio may reflect the capacity for protein synthesis. 2. Patients with weight loss due to cancer (n = 6) were compared with metabolically healthy patients before elective surgery (n = 7). Alkali-soluble protein/DNA and RNA/DNA ratios in the weight loss group were 248 (14) g/g and 1.3 (0.1) g/g respectively as compared with 404 (13) g/g and 2.1 (0.1) g/g in otherwise healthy patients. All of the alkali-soluble protein/DNA ratios and 5/6 of the RNA/DNA ratios in the weight loss group were below the 95% confidence interval for the healthy control subjects. 3. Patients undergoing elective open cholecystectomy (n = 7) were studied preoperatively and on days 3, 10, 20 and 30 post-operatively. The alkali-soluble protein/DNA ratio remained unchanged on post-operative day 3 but decreased by 8.7% (P < 0.01), 9.6% (P < 0.05) and 20.4% (P < 0.01) on days 10, 20 and 30 respectively in patients eating at will after the operation. No significant post-operative changes in alkali-soluble protein/DNA ratio were seen in patients given post-operative total parenteral nutrition with (n = 9) or without (n = 7) glycyl-glutamine supplementation for 3 days after surgery. 4. In conclusion, patients with weight loss due to malignant disease have a low muscle protein concentration. Elective surgery of medium magnitude results in a decrease in muscle protein lasting for more than 30 days.(ABSTRACT TRUNCATED AT 250 WORDS)

Aged↗

PubMed1995

Fuel selection, muscle fibre.

The fuel selection of muscle fibres at rest is dependent on substrate availability. Increased lipid availability results in an increase citrate concentration with inhibition of glycolysis. Fat utilization also increases the concentration ratio acetyl-CoA:CoASH, with inhibition of PDH transformation to the active form. The result is an inhibition of carbohydrate utilization in conformity with the classical glucose-fatty acid style. During exercise fuel selection is dependent on the intensity of exercise, the recruitment pattern of fibre type and the availability of fuels. During exercise at maximum intensity the main fuels are PCr and muscle glycogen, the highest energy release occurring with type II fibres. At exercise intensities between 70 and 100% VO2max carbohydrate is the main fuel after the intake of normal mixed or carbohydrate-rich diets. No inhibition of PDHa formation was observed by increased concentration ratio acetyl-CoA:CoASH during the exercise, but the activation and transport of fatty-acyl groups from NEFA may be inhibited by a decrease in the concentration of CoASH. This mechanism may limit the contribution of fat to metabolism during exercise at intensities above 60% VO2max, after an intake of carbohydrate-rich diets. After carbohydrate starvation or an infusion of a fat emulsion, there was a substantial increase in the utilization of fat which, after the infusion, was concomitant with a high PDHa and a high lactate production. This is thought to be due to a decrease in glycolysis and in the catalytic activity of PDHa, especially in type I fibres, while lactate production continues in type II fibres. When exercise intensities fall below 60% VO2max, fat becomes the dominant fuel during prolonged exercise. At the same time the recruitment pattern is shifted toward type I fibres which have the lowest activation threshold and the highest oxidative capacity.

Acetyl Coenzyme A↗

PubMed1995

Effects of epinephrine infusion on muscle glycogenolysis during intense aerobic exercise.

The purpose of this study was to determine whether an epinephrine (Epi) infusion would enhance muscle glycogenolysis during intense aerobic exercise. Epi was infused at rates that produced the same plasma Epi concentrations observed after caffeine (Caf) ingestion. Seven male subjects cycled for 15 min at 80% maximal O2 uptake during four different trials. Trial 1 was preceded by a 9 mg/kg oral dose of Caf to determine resting and exercise plasma Epi concentrations. Trial 2 was used to determine the Epi infusion rates needed to mimic the plasma Epi levels found with Caf. Trials 3 and 4 were randomized and consisted of either an Epi infusion or a saline infusion (control, Con). During Epi and Con trials muscle samples were obtained from the vastus lateralis at 0, 3, and 15 min of exercise. Plasma Epi levels were similar between Caf and Epi and were elevated twofold compared with Con. At 5 min of exercise the plasma Epi concentrations were 1.51 +/- 0.26, 2.61 +/- 0.34, and 2.97 +/- 0.45 nM for the Con, Caf, and Epi trials, respectively. Plasma Epi increased to 3.08 +/- 0.56, 5.45 +/- 1.11, and 5.86 +/- 1.03 nM at 14 min of exercise in the Con, Caf, and Epi trials, respectively. Muscle glycogenolysis was not different between trials (Con 220.5 +/- 25.3 vs. Epi 240.6 +/- 12.1 mmol/kg dry muscle). In addition, the degradation of muscle ATP and phosphocreatine and the accumulation of muscle lactate, ADP, and AMP were similar between trials.(ABSTRACT TRUNCATED AT 250 WORDS)

Adult↗