Search PubMed⌕ Search

Biomedical subjects

F W Booth

Publications and source records attributed to F W Booth.

At least 109 records · Page 6Linked to original sources
PubMed1984

Changes in actin synthesis and alpha-actin-mRNA content in rat muscle during immobilization.

The fractional rates of actin synthesis in adult rat gastrocnemius muscle from control and 6-h hindlimb-immobilized animals were determined by the constant-infusion technique. The rate of actin synthesis in gastrocnemius muscle was significantly decreased from control values during the 6th h of hindlimb immobilization. The content of alpha-actin-specific mRNA was then estimated in adult rat gastrocnemius muscle from control, 6-h, 72-h, and 7-day immobilized animals by "dot blot" hybridization. RNA extracted from control and immobilized animals was secured on nitrocellulose filters and hybridized to 32P-labeled plasmid p749 (containing a cDNA sequence produced from rat alpha-actin mRNA). The relative content of alpha-actin-specific mRNA in gastrocnemius muscle was significantly decreased at 7 days of immobilization but not at 6 or 72 h of immobilization. It is concluded that a change in the content of alpha-actin mRNA does not contribute significantly to the rapid onset of the decrease in actin synthesis rate observed after 6 h of immobilization. An alteration in the translation of alpha-actin-specific mRNA must occur to account for the early decline in actin synthesis during immobilization.

Actins↗
PubMed1984

Glucose uptake and glycogen synthesis in muscles from immobilized limbs.

The purposes of this study were to determine whether the defects in glucose metabolism in muscles of immobilized limbs of mice were related to alterations in insulin binding, insulin responsiveness, glucose supply, and insulin activation of glycogen synthase. These were tested by in vitro methodology. A significant lessening in the insulin-induced maximal response of 2-deoxyglucose uptake into the mouse soleus muscle occurred between the 3rd and 8th h of limb immobilization, suggesting a decreased insulin responsiveness. Lack of change in the specific binding of insulin to muscles of 24-h immobilized limbs indicates that a change in insulin receptor number did not play a role in the failure of insulin to stimulate glucose metabolism. It's inability to stimulate glycogen synthesis in muscle from immobilized limbs is due, in part, to a lack of glucose supply to glycogen synthesis and also to the ineffectiveness of insulin to increase the percentage of glycogen synthase in its active form in muscles from 24-h immobilized limbs.

Animals↗
PubMed1983

Effects of disuse on the structure and function of skeletal muscle.

The purpose of this paper is to briefly review some of the effects of reduced muscle use on the structure and function of human and animal skeletal muscle. A loss in muscle strength has been observed in astronauts after space flight. On Earth joint fixation of human limbs results in losses in muscle mass, in the cross-sectional area of both fiber types, and in the activities of mitochondrial enzymes. Methods that reduce muscular activity of animals also produce muscle atrophy. Fixation of the limb joints in position where the muscles are maintained less than resting length results in an atrophy in slow-twitch muscle. Associated with this atrophy are decreases in sarcomere number, fiber cross-sectional area, protein synthesis, and insulin responsiveness for the uptake of 2-deoxyglucose by muscle. Suspension of animals in a horizontal or head-down position is also a method being used currently for unloading muscles and producing alterations in development. In the future, the animal and human model should identify the mechanisms responsible for a decrease in muscle function when the muscle undergoes a decrease in usage.

Animals↗
PubMed1982

Insulin resistance for glucose metabolism in disused soleus muscle of mice.

Our hypothesis was that insulin resistance for carbohydrate metabolism develops after a single day of muscular disuse. The immobilization of the mouse hindlimb for 24 h was used to produce muscular disuse (group c). As food intake was voluntarily decreased during the immobilization, two additional groups were used: group A was untreated and ate ad libitum, whereas group B was anesthetized with group C and was fed amounts of food similar to those eaten by group C. Because groups B and C differed only by limb immobilization, group B was used as the reference group. When insulin was present in the incubation media, the rates of 2-deoxyglucose uptake and glycogen synthesis were always significantly decreased in soleus muscles from group C (anesthetized, ate less, immobilized) as compared to group B (anesthetized, pair-fed food that group C ate). Significant interaction between the factors of insulin and muscular disuse for the rates of 2-deoxyglucose uptake and glycogen synthesis support the concept that disuse of skeletal muscle attenuates insulin action. These observations are a direct demonstration of a decrease in insulin responsiveness in skeletal muscle as the result of a single day of muscular inactivity. Because plasma insulin concentrations were significantly lower in groups B and C than in the untreated group, it seems likely that the development of insulin resistance in disused skeletal muscle is independent of plasma insulin levels.

Anesthesia, General↗
PubMed1982

Effect of limb immobilization on skeletal muscle.

The immobilization of limbs resulted in atrophy of those muscles that are fixed either at or less than resting length. The loss in protein in these muscles can be described by a first-order equation. Decreases in protein synthesis rate in muscles of immobilized limbs occur during the first 6 h of immobilization, and this decrease probably played a role in initiating muscular atrophy. After weeks of immobilization, muscles composed predominately of slow-twitch fibers took on properties characteristic of fast twitch muscles. The EMG activity of muscles in immobilized limbs was reduced to 5--15% of control levels. Insulin responsiveness for 2-deoxyglucose uptake into the soleus muscle of a limb is decreased at the 24th h of limb immobilization. Muscles of immobilized limbs have either no change or a decrease in resting membrane potential, an increase in extrajunctional acetylcholine receptors of lesser magnitude than the increase that occurred in denervated muscle, and no change in acetylcholinesterase activity in neuromuscular junctions. Immobilizing muscles at stretched lengths prevented the decrease in nerve afterhyperpolarization that was seen in muscles immobilized at shortened positions. These observations suggested that metabolic changes in muscles have a retrograde trophic influence on motor nerves. The model of limb immobilization permits the study of many fundamental problems concerned with mechanisms by which a muscle adapts so that it can meet the requirements of the external environment.

Animals↗
PubMed1981

Protein synthesis rates in atrophied gastrocnemius muscles after limb immobilization.

Fractional rates of protein synthesis in rats were determined by the constant-infusion technique. Rates of protein synthesis in the gastrocnemius muscle were significantly reduced from control values throughout a 7-day period of hindlimb immobilization and 1) significantly increased to control values during the first 6 h following the 7-day period of hindlimb immobilization; 2) remained at control values for the next 2 days; and 3) then significantly increased to about twice control values on the 4th day following immobilization. Exercise of sufficient duration and/or intensity affected a further increase in the protein synthesis rate during recovery from atrophy. For example, running on a motor-driven treadmill 1 h daily for 3 days after ending limb immobilization resulted in a significant increase in the fractional rate of protein synthesis in the gastrocnemius muscle on the 2nd day following immobilization. Also, weight lifting for 200 s on the 2nd day of protein synthesis in the gastrocnemius muscle. Thus increased usage of atrophied muscle was followed by an increased rate of protein synthesis.

Animals↗
PubMed1980

The effects of cutting or of stretching skeletal muscle in vitro on the rates of protein synthesis and degradation.

Rates of protein synthesis were significantly lower in the cut soleus and extensor digitorum longus muscles than in their uncut counterparts. Rates of protein degradation were significantly higher in cut soleus muscles, but not in cut extensor digitorum longus muscles as compared with their uncut controls. Concentrations of ATP and phosphocreatine were significantly lower in cut soleus and extensor digitorum longus muscles after incubation in vitro in contrast with respective control uncut muscles. These data indicate that cutting of muscle fibres alters rates of protein synthesis and degradation, in addition to altering concentrations of high-energy phosphates. Since these findings stressed the importance of using intact muscles to study protein metabolism, additional studies were made on intact muscles in vitro. Stretched soleus muscles had higher concentrations of high-energy phosphates at the end of an incubation period than did unstretched muscles. However, the length of the soleus, extensor digitorum longus and diaphragm muscles during incubation did not affect rates of protein degradation.U

Adenosine Triphosphate↗
PubMed1980

Populations of rat skeletal muscle mitochondria after exercise and immobilization.

We slightly modified an existing procedure (Palmer et al., J. Biol. Chem. 252: 8731-8739, 1977) to isolate two distinct populations of mitochondria from rat skeletal muscle; initial brief Polytron homogenization released the subsarcolemmal mitochondria, and brief exposure of the resultant intact myofibrils to the proteolytic enzyme, Nagarse, extracted the intermyofibrillar mitochondria. The intermyofibrillar mitochondria differed from the subsarcolemmal mitochondr. ia by higher state III respiration measurements and enzymatic activities. These two populations of mitochondria were then isolated from the gastrocnemius muscle that had been induced to perform different amounts of contractile activity. The endurance training program of daily running significantly increased state III respiration and respiratory control index in the subsarcolemmal mitochondria, but the program did not increase these measurements in the intermyofibrillar mitochondria. In addition, 2 days of hindlimb immobilization resulted in a significant decrease in state II respiration and the respiratory control index of the subsarcolemmal mitochondria; however, immobilization did not affect the intermyofibrillar mitochondria. These measurements suggest that the subsarcolemmal mitochondria adapt in response to chronic changes in the level of contractile activity.

Adaptation, Physiological↗
PubMed1980

Longevity of exercising obese hypertensive rats.

The purpose of this study was to determine whether daily running lengthens the life-span of animals dying prematurely due to cardiovascular disease. We used a strain of rat that is genetically hypertensive and obese and is reported to develop atherosclerosis (Exp. Mol. Pathol. 19: 53--60, 1973). These animals were divided into three groups consisting of runners exercised daily on treadmills from an early age life, food-restricted sedentary rats, and libitum eaters that were sedentary. This latter group had significantly higher average daily food intakes and body weights than either of the other two groups. The average life-span of both sedentary groups was significantly longer than the running group. Runners had a greater frequency of focal myocardial necrosis, but atherosclerosis was absent in all three groups. We speculate that daily running may have accentuated the development of factor s that may have contributed to the early death of runners.

Animals↗
PubMed1979

Recovery of skeletal muscle after 3 mo of hindlimb immobilization in rats.

During immobilization, skeletal muscle undergoes decreases in size and strength with concomitant atrophic and degenerative changes in slow-twitch muscle fibers. Currently there are no objective data in slow-twitch muscle demonstrating recovery of biochemical or physiological indices following termination of immobilization. The purpose of this study was to determine whether the soleus, a slow-twitch muscle, could recover normal biochemical or physiological levels following termination of immobliization. Adenosine triphosphate, glycogen, and protein concentration (mg/g wet wt) all significantly decreased following 90 days of hindlimb immobilization, but these three values returned to control levels by the 60th recovery day. Similarly, soleus muscle wet weight and protein content (mg protein/muscle) returned to control levels by the 14th recovery day. In contrast, maximal isometric tension did not return to normal until the 120th day. These results indicate that following muscular atrophy, which was achieved through 90 days of hindlimb immoblization, several biochemical and physiological values in skeletal muscle are recovered at various times after the end of immobilization.

Adenosine Triphosphate↗
PubMed1979

Early change in skeletal muscle protein synthesis after limb immobilization of rats.

The atrophy of skeletal muscle accruing from disuse, or limb immobilization, is caused by a decreased rate of protein synthesis and an increased rate of protein degradation. Currently, little information is available regarding the initial time of the decline in the rate of protein synthesis in skeletal muscle. The purpose of the present study was to determine, as precisely as possible, the time at which the protein synthesis rate first begins to decline in skeletal muscle, utilizing immobilized limbs of rats for a model. A constant-infusion technique employing [14C]tyrosine was used to estimate protein synthesis rates. During the first 6 h of immobilization, a significant decline of 37% in the fractional rate of protein synthesis from the control level of 5.7%/day was observed. These results suggest that very early changes are occurring in molecular events that regulate protein synthesis in disused or immobilized skeletal muscle.

Animals↗
PubMed1978

Inability of myoglobin to increase in dystrophic skeletal muscle during daily exercise.

An exercise program consisting of 80-min daily runs on a treadmill was performed by normal and dystrophic hamsters. Subgroups were sacrificed at various times during the 45-day program. Daily exercise resulted in a significant increase in the myoglobin concentration of gastrocnemius muscles in normal animals but not in dystrophic animals. In the exercise groups of hamsters, there were significant increases in the concentration of cytochrome c, a marker for respiratory capacity, in the gastrocnemius of both normal and dystrophic hamsters.

Animals↗
PubMed1978

Regrowth of atrophied skeletal muscle in adult rats after ending immobilization.

The recovery time course of muscle atrophied by immobilization was followed after removal of hindlimb casts from adult female rats. Increases of only 9% in body weight, 4% in gastrocnemius weight, and 10% in soleus weight occurred in controls during the 78-day duration of the experiment. There were no increases in the amounts of total protein or of citrate synthase activities in gastrocnemius or soleus during the first 3 days after removal of hindlimb casts; thereafter, there were increases in these paramters. Citrate synthase activities per mg of gastrocnemius protein were significantly higher at the 16th and 50th day of recovery. No significant differences for citrate synthase activity per mg of soleus occurred during recovery. Until the 50th day of recovery, no significant differences for total protein in soleus and for total protein and wet weight of gastrocnemius were observed between control and recovery values. However, the wet weight of the soleus returned rapidly during recovery and was not significantly different from control during recovery.

Aging↗
PubMed1977

Cytochrome c turnover in rat skeletal muscles.

Exercise induces an increase in cytochrome c concentration in skeletal muscle. This adaptation provides an approach to studying the turnover of cytochrome c that avoids the problem of reutilization encountered with isotopic tracers. The half-life of cytochrome c was estimated from the time course of the increase in its concentration to a new, higher, steady state level in response to exercise training, and from the decrease in cytochrome c after cessation of exercise. The half-time of the increase in cytochrome c concentration was approximately 6 days, while the half-time of the decrease was 7 to 8 days in the fast red and slow red types of muscle. The finding that the half-times of the increase and of the decrease in cytochrome c concentration are similar provides evidence that the exercise-induced increase in cytochrome c is due to an increase in its rate of synthesis. These half-times are much shorter than those obtained with isotopic tracers. It had been thought that the heme precursor delta-aminolevulinate is not reutilized. However, the half-time of the decrease in radioactivity of cytochrome c labeled with delta-aminol[14C]levulinate was 45 days, and increased to 60 days in response to exercise, in fast red muscle. The half-time of the decrease in radioactivity of cytochrome c labeled with [(3H)]leucine in gastrocnemius muscle was shorter than with delta-amino[14C]levulinate (18 days compared to 38 days). These results indicate that when delta-amino(14C)levulinate is used to label heme, reutilization is a serious problem in skeletal muscle.

Aminolevulinic Acid↗
PubMed1977

Time course of muscular atrophy during immobilization of hindlimbs in rats.

The hindlimbs of rats were immobilized, in plaster casts, for varying durations, and the time course for atrophy of muscle and of selected proteins in these muscles was determined. In those muscles whose lengths were at less than resting length during the fixation procedures, exponential decay to a new apparent steady state after atrophy was shown by wet and dry muscle weights and by the amounts of biuret protein, cytochrome c, and citrate synthase. The time taken to decrease to one-half of the final decrease at the new apparent steady state level was about 4-6 days for the above parameters which decayed exponentially. In contrast, the myoglobin concentration increased during atrophy and the amount of myoglobin remain unchanged during atrophy. When fixation procedures on limbs were such that muscles were stretched to lengths greater than resting length, then the onset of atrophy was delayed; indeed, in some cases muscles hypertrophied when fixed in the stretched position.

Animals↗
PubMed1975

Depletion of muscle and liver glycogen during exercise. Protective effect of training.

Carbohydrate depletion during exercise was measured in the liver, in the three different types of skeletal muscle, and in the blood of exercise-trained and untrained rats. The acute exercise test consisted of 45 min of treadmill running of progressively increasing intensity. The training program consisted of 6 hrs of swimming per day, 5 days per week for 14 weeks; the training induced an increase of approximately 35 percent in the respiratory capacity of gastrocnemius muscle, and a 14 percent incrase in heart weight. Glycogen stores in fast-twitch red, fast-twitch white, and slow-twitch red types of skeletal muscle, were depleted significantly more slowly in the trained than in the untrained animals during the treadmill exercise test. Resting glycogen stores in the liver were higher and were depleted more slowly during exercise in the trained than the untrained animals. Blood lactate concentration was significantly lower in the trained than in the untrained rats at the end of the exercise test. These results provide evidence that endurance exercise training induces adaptation which protect against the depletion of glycogen from the liver and from the tree types of skeletal muscle during prolonged exercise.

Animals↗