Karin Alev

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. Protein turnover characterizes the renewal processes of muscle proteins and the functional capacity of muscle. The turnover rate of myofibrillar proteins is slow in comparison with mitochondrial proteins and depends on the oxidative capacity of muscle fibres. The turnover rate of myofibrillar proteins in the same muscle is different and is also different within the myosin molecule between myosin heavy and light chain isoforms. The turnover rate of muscle proteins in endurance training shows the adaptation of skeletal muscle to long-lasting exercise via remodelling of muscle structures. Adaptational coordination between myofibrillar and mitochondrial compartments shows the physiological role and adaptational capacity of skeletal muscle to endurance training. It is challenging to use muscle protein turnover for the purposes of monitoring the training process of endurance athletes, optimizing training programs and preventing overtraining.

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. Ageing associated sarcopenia was calculated from gastrocnemius muscle relative mass decrease (from 5.6 +/- 0.08 to 3.35 +/- 0.04; p < 0.001). The SR of MyHC in old rats was approximately 30% and actin approximately 23% lower than in young rats. Dex treatment decreased SR of two main contractile proteins significantly in both age groups (p < 0.001) and increased DR during ageing from 2.11 +/- 0.15 to 4.09 +/- 0.29%/day (p < 0.001). Hindlimb grip strength in young rats was 5.90 +/- 0.35 N/100 g bw and 2.64 +/- 0.2 N/100 g bw (p < 0.001) in old rats. Autografts of old rats have a higher content of adipose tissue 14.9 +/- 1.1% in comparison with young rats 6.8 +/- 0.51% (p < 0.001) and less muscle tissue 39.8 +/- 2.6% and 48.3 +/- 2.8%, respectively (p < 0.05). Both, ageing and dex-caused sarcopenic muscles have diminished capacity for regeneration.

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 23.5 years were used in this study and divided into three age groups: 1.5 to 4 (n = 6), 9 to 13 (n = 5) and 18.5 to 23.5 years (n = 4). The average content of the MyHC I isoform was 11.72 ± 1.07% (variation between individuals: 7.09% to 20.14%). The relative content of the MyHC IIa and IIx isoforms was subsequently 38.20 ± 1.46% (30.73% to 48.78%) and 50.07 ± 1.10% (43.8% to 56.78%) from the total MyHC. The MyHC pattern in the skeletal muscles of the Akhal-Teke horses shows that the muscles of these horses have a high capacity both for endurance and speed.

The effect of autografting on the myosin composition in skeletal muscle fibers

The purpose of the study was to investigate the changes in myosin heavy chain (MHC) and myosin light chain (MLC) isoforms following autotransplantation of extensor digitorum longus muscles. Muscles were grafted in “standard” and “nerve‐intact” conditions. MHC and MLC isoforms were analyzed by sodium dodecyl sulphate gel electrophoresis. Changes in MHC isoforms 10, 30, and 60 days after grafting were similar in the “standard” and the “nerve‐intact” grafts. In contrast to MHC, changes in MLC were different in the 10th day groups, but the same in the 30th day groups. Sixty days after grafting the content of MLC isoforms was the same as the control muscles. These data indicate that transient loss of functional innervation, even for a short time, has permanent effect on the composition of MHC but not MLC isoforms in regenerating skeletal muscle fibers.

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 2.62+/-0.28 to 5.58+/-0.49% per day during glucocorticoids excess. Both fibril- and network-forming collagen-specific mRNA levels decreased at the same time in both types of skeletal muscle. Specific mRNA level for MMP-2 did not change significantly during dexamethasone administration. Hindlimb grip strength simultaneously decreased. The effect of excessive glucocorticoids on the extracellular compartment did not differ significantly in skeletal muscles with different twitch characteristics.

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. Incorporation of 3H leucine into myofibrillar and sarcoplasmic protein fractions, their relative contents in autografts and synthesis rate of MyHC and actin were recorded. The relative muscle mass of old rats was about 67% of that of young rats; the absolute mass of autografted muscle was 61% intact in the young rat group and 51% in the old rat group. Content of myofibrillar protein in the autografts of young rats was 46% of the intact muscle content, and 39% in the old rat group. In conclusion, the difference in skeletal muscle regeneration capacity of young and very old rats is about ten percent. In the autografts of both young and old rats, the regeneration of the contractile apparatus is less effective in comparison with the sarcoplasmic compartment.

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 &mgr;g/100 g BM (young and old group) and 50 &mgr;g/100 g BM (old group). Results: Muscle elasticity (logarithmic decrement) was lower in old animals (1.86 ± 0.03) in comparison with young adult rats (1.38 ± 0.04) (P < .01). After the 10‐day treatment with dexamethasone 100 &mgr;g/100 g BM, young adult rats had 10% lower muscle elasticity (P < .01). The same dose of dexamethasone in old rats increased tone (frequency of natural oscillation) from 29.13 ± 0.51 Hz to 38.50 ± 0.95 Hz (P < .001). There were dose‐dependent differences in dynamic stiffness and tone of muscle; changes in elasticity were independent of the dose in old animals. In old rats, the muscles viscoelastic properties decreased after dexamethasone administration. Significant correlation was found between changes in muscle logarithmic decrement and stiffness (rs = 0.90; P < .05) in old animals. Conclusions: Biomechanical and viscoelastic properties of skeletal muscle indicate changes in the main function of muscle during glucocorticoid‐induced muscle atrophy and are in agreement with changes in hind limb strength. The myometric measurements indicate the direction and magnitude of change in muscle tissue after different doses of dexamethasone administration easily and quickly.