Short-time recovery skeletal muscle from dexamethasone-induced atrophy and weakness in old female rats.

Background: Several pathological conditions (atrophy, dystrophy, spasticity, inflammation) can change muscle biomechanical parameters. Our previous works have shown that dexamethasone treatment changes skeletal muscle tone, stiffness, elasticity. Exercise training may oppose the side effects observed during dexamethasone treatment.

Changes in Body Composition of Old Rats at Different Time Points After Dexamethasone Administration.

Background: Aging leads to changes in skeletal muscle quantity and quality and is accompanied with increase in body mass and fat mass, whereas fat-free mass either decreases or remains unchanged. The body composition of rodents has been an important factor for clinical trials in the laboratory. Glucocorticoids such as dexamethasone are widely used in clinical medicine, but may induce myopathy, characterized by muscle weakness, atrophy, and fatigue.

Glucocorticoid-Induced Changes in Rat Skeletal Muscle Biomechanical and Viscoelastic Properties: Aspects of Aging.

Objectives: The purpose of this study was to estimate the state of tension (tone) and the biomechanical and viscoelastic properties of skeletal muscle in aging rats during the administration of different doses of dexamethasone and to find the relationships among the state of muscle atrophy, muscle strength, and the abovementioned muscle properties.

Methods: Muscle state of tension, biomechanical (elasticity, dynamic stiffness) and viscoelastic (mechanical stress relaxation time, Deborah number) properties (using MyotonPRO, Myoton Ltd, Tallinn, Estonia), lean body mass (BM), and hind limb grip strength were measured before and after the administration of a 10-day treatment with dexamethasone 100 μg/100 g BM (young and old group) and 50 μg/100 g BM (old group).

Results: Muscle elasticity (logarithmic decrement) was lower in old animals (1.

Morphological peculiarities of neuromuscular junctions among different fiber types: Effect of exercise.

The aim of our research was to examine whether there are differences in the morphology of neuromuscular junctions of different types of muscle fibers in rodents, and after their adaptation to six weeks endurance exercise training. After 5-day acclimation, Wistar rats were subjected to run with the speed 35 m/min during 6 week, 5 days per week and the training volume reached 60 min per day. Muscle samples for ultrastructural studies were fixed, dehydrated and embedded in Epon-812.

Role of Myofibrillar Protein Catabolism in Development of Glucocorticoid Myopathy: Aging and Functional Activity Aspects.

Muscle weakness in corticosteroid myopathy is mainly the result of the destruction and atrophy of the myofibrillar compartment of fast-twitch muscle fibers. Decrease of titin and myosin, and the ratio of nebulin and MyHC in myopathic muscle, shows that these changes of contractile and elastic proteins are the result of increased catabolism of the abovementioned proteins in skeletal muscle. Slow regeneration of skeletal muscle is in good correlation with a decreased number of satellite cells under the basal lamina of muscle fibers.

Exercise myopathy: changes in myofibrils of fast-twitch muscle fibres.

The purpose of the present study was to determine the relationships between the changes of myofibrils in fast-twitch oxidative-glycolytic (type IIA) fibres and fast-twitch glycolytic (type IIB) muscle fibres, protein synthesis and degradation rate in exercise-induced myopathic skeletal muscle. Exhaustive exercise was used to induce myopathy in Wistar rats. Intensity of glycogenolysis in muscle fibres during exercise, protein synthesis rate, degradation rate and structural changes of myofibrils were measured using morphological and biochemical methods.

Aging and regenerative capacity of skeletal muscle in rats.

The objective of the study was to examine skeletal muscle regeneration capacity of young and very old rats during autotransplantation. In 3.5 and 30 month-old Wistar rats, gastrocnemius muscle was removed and grafted back to its original bed.

Role of exercise therapy in prevention of decline in aging muscle function: glucocorticoid myopathy and unloading.

Changes in skeletal muscle quantity and quality lead to disability in the aging population. Physiological changes in aging skeletal muscle are associated with a decline in mass, strength, and inability to maintain balance. Glucocorticoids, which are in wide exploitation in various clinical scenarios, lead to the loss of the myofibrillar apparatus, changes in the extracellular matrix, and a decrease in muscle strength and motor activity, particularly in the elderly.

Myosin heavy chain pattern in the Akhal-Teke horses.

This study investigates the myosin heavy chain (MyHC) isoform composition in the gluteus medius muscle of the Akhal-Teke horses using SDS-PAGE (sodium dodecyl sulfate polyacrylamide gel electrophoresis). Fifteen horses aged between 1.5 and 23.

Muscle protein turnover in endurance training: a review.

There has been much debate about skeletal muscle capacity to adapt to long-lasting endurance exercise. Exercise in the aerobic zone of metabolism does not result in hypertrophy of skeletal muscle fibres but increases their oxidative capacity. The duration and intensity of an exercise session determines the time period of depressed muscle protein synthesis and increased degradation rate during the recovery period after exercise.

Review on aging, unloading and reloading: changes in skeletal muscle quantity and quality.

Aging and muscle unloading are associated with a decline in muscle mass, structure, force and changes in the mechanical properties of skeletal muscle. There is a perception that reloading restores muscle architecture and function but differences in the regeneration capacity of intra- and extra-cellular compartments, age dependent susceptibility to muscle damage, particularly in the contractile machinery, make it difficult to attribute the main role of the above mentioned components. This review briefly summarizes studies that examine aging skeletal muscle during unloading and reloading.

Extracellular matrix and myofibrils during unloading and reloading of skeletal muscle.

The aim of the study was to elucidate the effect of unloading and reloading on the collagen expression and synthesis rate of myofibrillar proteins in fast-twitch (FT) muscle in relation to changes in muscle strength and motor activity. Northern blot analysis was used for testing the specificity of cDNA probes and protein synthesis rate was measured according to incorporation of radioactive leucine into different protein fractions. Unloading depresses collagen type I and III (p<0.

Impaired oxidative phosphorylation in overtrained rat myocardium.

The present study was undertaken to characterize and review the changes in energy metabolism in rat myocardium in response to chronic exhaustive exercise. It was shown that a treadmill exercise program applied for six weeks led the rats into a state characterized by decreased performance, loss of body weight and enhanced muscle catabolism, indicating development of overtraining syndrome. Electron microscopy revealed disintegration of the cardiomyocyte structure, cellular swelling and appearance of peroxisomes.

Structural rearrangements in contractile apparatus and resulting skeletal muscle remodelling: effect of exercise training.

This review briefly summarizes studies that examine fast- and slow-twitch skeletal muscles and the ultra- and molecular structure of fibre types, including intrafusal fibres, during adaptation to exercise training. Adaptation capability of skeletal muscle to different types of exercise training depends on rearrangements in the contractile apparatus, mitochondria, other fibre organelles and neuromuscular junctions. Skeletal muscle functional capacity depends on structural changes in fibre organelles and is related to higher centres of motor control as the adaptation process needs information about muscle length and speed of contraction at any time during the training process.

Relationship between extracellular matrix, contractile apparatus, muscle mass and strength in case of glucocorticoid myopathy.

The purpose of this study was to evaluate the effect of dexamethasone on the contractile apparatus and extracellular matrix (ECM) components of slow-twitch (ST) soleus (Sol) and fast-twitch (FT) extensor digitorum longus (EDL) muscle. The specific aim was to assess the development of glucocorticoid-induced myopathy on the level of contractile apparatus and ECM, paying attention to the expression of fibrillar forming collagen types I and III and nonfibrillar type IV collagen expression in extracellular compartment of muscle. Degradation of myofibrillar proteins increased from 2.

Ageing and dexamethasone associated sarcopenia: peculiarities of regeneration.

The purpose of this study was to assess the development of ageing- and glucocorticoid-related sarcopenia on the level of myofibrillar apparatus, paying attention to the synthesis (SR) and degradation rate (DR) of contractile proteins, muscle strength, and daily motor activity. We also wanted to test the effect of ageing and dexamethasone (Dex) excess on the regeneration peculiarities of skeletal muscle autografts. Four and 30-month-old male rats of the Wistar strain were used.

Changes in fast-twitch muscle oxidative capacity and myosin isoforms modulation during endurance training.

Aim: The purpose of this study was to investigate the effect of endurance training on changes in myosin heavy (MyHC) and light (MyLC) chains expression, their turnover rate in fast-twitch (FT) skeletal muscles, and relations with changes in contractile proteins degradation rate and muscle oxidative capacity.

Methods: Wistar rats were run at 35 m/min for 6 weeks (from 10 min to 60 min per day, from 1.8 kJ to 7 kJ per training session and power of work was 1.

The profile and distribution of myosin heavy chain isoforms in middle-aged sedentary persons.

Aim: Human lifestyle has drastically changed during the past century as the share of physical work in daily life has decreased. The purpose of the present study was to examine the distribution of myosin heavy chain (MHC) isoforms in middle-aged sedentary persons, to compare the proportion of MHC isoforms of middle-aged and young sedentary persons and to demonstrate the effect of physical activity of MHC isoforms in middle-aged sedentary persons.

Methods: Eighty-nine middle-aged sedentary and 13 young sedentary persons volunteered for the study.

Adaptive changes of Myosin isoforms in response to long-term strength and power training in middle-aged men.

The purpose of the study was to examine the adaptive changes in myosin heavy chain (MHC) and light chain (MLC) isoforms in human vastus lateralis muscle caused by long-term strength and power training (54 weeks, approximately 3 times a week) in untrained middle- aged men (16 in the training and 6 in the control group). Muscular MHC and MLC isoforms were determined by means of SDS-PAGE gel electrophoresis. During the training period, maximal anaerobic cycling power increased by 64 W (p < 0.

Altered mitochondrial apparent affinity for ADP and impaired function of mitochondrial creatine kinase in gluteus medius of patients with hip osteoarthritis.

The cellular energy metabolism in human musculus gluteus medius (MGM) under normal conditions and hip osteoarthritis (OA) was explored. The functions of oxidative phosphorylation and energy transport systems were analyzed in permeabilized (skinned) muscle fibers by oxygraphy, in relation to myosin heavy chain (MHC) isoform distribution profile analyzed by SDS-PAGE, and to creatine kinase (CK) and adenylate kinase (AK) activities measured spectrophotometrically in the intact muscle. The results revealed high apparent Km for ADP in regulation of respiration that decreased after addition of creatine in MGM of traumatic patients (controls).

Endurance training: volume-dependent adaptational changes in myosin.

The purpose of this study was to find the effect of different endurance training volumes on the composition and turnover of myosin. Sixteen-week-old male rats of the Wistar strain were divided into three different volume-based training groups. Changes in myosin heavy chain (MyHC), myosin light chain (MyLC) isoforms' composition, their synthesis rate, as well as myosin binding C-protein synthesis rate, and muscle protein degradation rate were measured.

Composition and turnover of contractile proteins in volume-overtrained skeletal muscle.

The purpose of this study was to find the composition shift of myosin heavy chain (MyHC) isoforms in overtraining in fast- and slow-twitch skeletal muscles and different changes in MyHC isofom composition, synthesis and turnover rate between 4-week and 6-week overtraining. Male Wistar rats were randomly assigned to 4-week and 6-week endurance training, 4-week and 6-week overtraining groups. Plantaris (Pla), extensor digitorum longus (EDL), and soleus (Sol) muscles were studied.

The effect of mechanical loading on the MyHC synthesis rate and composition in rat plantaris muscle.

The aim of this study was to investigate the response of protein synthesis rate, particularly myosin heavy chain (MyHC) isoforms synthesis and the magnitude of its isoform transformation in fast-twitch plantaris muscle, to different modes of prolonged mechanical loading. Different protocols of mechanical loading were used: resistance training (RT), compensatory hypertrophy (CH) of m. plantaris after tenotomy of m.

Age-related changes in skeletal-muscle myosin heavy-chain composition: effect of mechanical loading.

The purpose of this study was to investigate the effect of compensatory hypertrophy (CH), heavy-resistance exercise training (HRET), and simultaneous CH and HRET on fast-twitch skeletal-muscle myofibrillar-protein synthesis, myosin heavy-chain (MHC) turnover rate, and MHC-isoform composition in young and old rats. In young animals all treatments intensified myofibrillar-protein synthesis, whereas in old animals with CH protein synthesis remained unchanged. The relative content of MHC I and IID in plantaris muscle increases with age, and the relative content of MHC IIB decreases.

The effect of glucocorticoids on the myosin heavy chain isoforms' turnover in skeletal muscle.

The purpose of this study was to find the effect of dexamethasone on the myosin heavy chain (MyHC) isoforms' composition in different skeletal muscles and glycolytic (G) fibres in relation with their synthesis rate and degradation of MyHC isoforms by alkaline proteinases. Eighteen-week-old male rats of the Wistar strain were treated with dexamethasone (100 microg/100 g bwt) during 10 days. The forelimb strength decreased from 9.