Biomedical subjects

K Alev

Publications and source records attributed to K Alev.

9 recordsLinked to original sources

PubMed2006

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. Thirty middle-aged sedentary subjects participated in strength-conditional exercise program during 9 months. Vertical jumping height and maximal anaerobic work capacity were measured. Muscle samples were taken from vastus lateralis muscle. MHC isoform composition was determined by SDS-PAGE. RESULTS: Variation of MHC I and MHC IIa isoforms in middle-age sedentary persons demonstrated normal distribution. Significant differences of MHC isoform proportions between middle-aged and young sedentary participants were not observed. The proportion of MHC IIx decreased significantly after the exercise period that significantly improved the maximal anaerobic power and jumping height of participants. CONCLUSIONS: Normal distribution illustrated the proportion of MHC I and MHC IIa isoforms in 89 middle-aged sedentary persons while significant differences of MHC isoforms proportion between young and middle-aged sedentary persons were not observed. Even small increase of physical activity improved physical performance and decrease the MHC IIx proportion of middle-aged sedentary persons. Physically active lifestyle in middle age, when age-related changes have not started yet, may delay age-related changes in skeletal muscle.

Adult↗

PubMed2005

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. In slow-twitch (ST) soleus (Sol) muscle MyHC I isoform relative content increased and MyHC IIa isoform decreased during excessive increase in the volume of endurance training (ET). In plantaris (Pla) muscle excessive increase in ET volume decreased MyHC I and IIb isoforms, and increased MyHC IIa and IId relative content. In extensor digitorum longus (EDL) muscle the relative content of MyHC IId isoform increased during ET, but excessive increase in training volume decreased it. In Pla muscle the relative content of MyLC 1 (slow) isoform decreased during ET, but excessive increase in ET volume decreased the relative content of MyLC 3 (fast) isoform in both fast-twitch (FT) muscles. Decrease in MyHC and myosin binding C-protein synthesis rate in Pla muscle had significant correlation with ET volume (r = - 0.537, p < 0.05 and r = - 0.727, p < 0.001 subsequently). MyHC I and IIb isoforms and MyLC 3 (fast) isoform in Pla muscle and MyHC IIb, IId and MyLC 3 (fast) isoforms in EDL muscle are the most sensitive to the increase in ET volume. Excessive increase in ET volume leads to a decrease in physical working capacity. The degradation of muscle protein increased during ET in all groups.

Adaptation, Physiological↗

PubMed2004

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. gastrocnemius and a combination of the two previous loadings (RT + CH). During the different modes of loading, plantaris muscle hypertrophy in RT group was approximately 10 %, CH approximately 40 % and CH + RT approximately 44 %. MyHC I and IID isoform synthesis rate increased in all experimental groups, as well as their relative content. MyHC IIA relative content decreased during RT and RT + CH and increased during CH. MHC IIB isoform relative content decreased in all experimental groups, but compared with CH in CH + RT MyHC IIB isoform content increased in plantaris muscle. These results demonstrate that different modes of mechanical loading resulted in the selective up- and down-regulation of MyHC isoforms in fast-twitch skeletal muscle. The synthesis rate and relative content of the two fastest isoforms of MyHC IIB and IID are regulated to different directions during mechanical loading.

Animals↗

PubMed2004

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. Daily excretion of 3-methylhistidine (3-MeHis) pool as an indicator for protein degradation increased in the 4-week and 6-week overtraining group to 4.04 +/- 0.21 and 4.32 +/- 0.23 %/day subsequently in comparison with the control group (2.16 +/- 14 %/day, p < 0.001). In Pla muscle MyHC I isoform synthesis rate was 33 200 +/- 2150 (after 6-week overtraining 27 100 +/- 1800, p < 0.05), IIa 32 600 +/- 2100; IId 27 300 +/- 1890 and IIb isoform 20 100 +/- 1600 (after 6-week overtraining 15 500 +/- 1400, p < 0.05) dpm/M leucine/min. Actin synthesis rate increased in fast-twitch muscles during 4- and 6-week overtraining, and in soleus muscle during 6-week overtraining. In EDL and Sol muscle MyHC isoform composition during 6-week overtraining did not change significantly. During the 6-week overtraining the relative content of MyHC I and IIb isoforms decreased and IIa and IId isoforms increased in Pla muscle. The initial increase of MyHC IIb isoform after 4-week overtraining shows the higher stability of this isoform in comparison with MyHC I isoform in fast-twitch muscles during high volume exercise.

Animals↗

PubMed1997

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.

Animals↗

PubMed1991

Effect of muscular activity on the turnover rate of actin and myosin heavy and light chains in different types of skeletal muscle.

In endurance-trained rats the myosin HC have a more rapid turnover rate than in control animals in all three types of skeletal muscle fibres, but in sprint-trained rats only in fast-glycolytic and fast-oxidative-glycolytic fibres. A comparison of the actin turnover rate in sprint- and endurance-trained animals shows that in both groups there are more rapid turnover rates in all types of muscle fibres in comparison with control rats. During long-lasting exhaustive exercise the turnover rate of myosin HC decreases. Twelve hours after exercise, myosin LC 2 and 3, and actin have a more rapid turnover than in control rats. Changes in the turnover rate of muscle contractile proteins during exercise and the recovery period after exercise reflect the functional conditions of the contractile apparatus in different types of skeletal muscle fibres and have a physiological significance.

Actins↗

PubMed1988

Effect of glucocorticoids on contractile apparatus of rat skeletal muscle.

Skeletal muscles which have a high oxidative potential are less sensitive to the catabolic action of dexamethasone. In fast-twitch white muscles, where the oxidative capacity is low, the alkaline proteinase activity as well as the rise in the number of lysosomes was more pronounced. It seems that the glucocorticoid-caused myopathy is a result of elevated degradation of contractile proteins. This process of degradation of contractile proteins begins in the myosine filaments and then spreads to the thin filaments and the z-line.

Actin Cytoskeleton↗

PubMed1986

Effect of muscular activity on the turnover rate of actin and myosin heavy and light chains in different types of skeletal muscle. I. Changes in the turnover rate of myosin and actin during and after single-bout physical activity.

During a single-bout of 6-h swimming, myosin heavy chain (HC) and actin in m. gastrocnemius turned over more slowly than they did in the pre-exercise period, whereas the turnover rate of myosin light chain (LC) increased; 48 h after swimming, actin and myosin HC had a significantly higher turnover rate, but the turnover rate of myosin LC remained at the pre-exercise level. Exercise caused a remarkable decrease in the incorporation of the 14C leucine into actin and myosin HC, but an increase in the incorporation into myosin LC. An elevation of the synthesis rate of actin and myosin HC was observed 48 h after exercise. Myofibrillar proteinase activity at alkaline pH reached its maximum level during exercise, but the same was observed for the proteolytic activity at acid pH 6 h and at neutral pH 24 h after exercise.

Actins↗

PubMed1985

Effect of glucocorticoids on the turnover rate of actin and myosin heavy and light chains on different types of skeletal muscle fibres.

The catabolic action of glucocorticoids on the molecular level of the two main muscular proteins, myosin and actin, was found to depend on the type of muscle fibres. The synthesis rate of actin and myosin heavy chain was decreased in all types of muscle fibres, and in myosin light chain only in the slow-twitch red fibres. The turnover rate of actin and myosin heavy chain was also found decreased in all types of muscle fibres. The myosin light chains turned over more rapidly in dexamethasone-treated than in the control rats in all types of muscle fibres except in the case of the slow-twitch red ones as was shown by single and double isotope methods. Dexamethasone treatment enhanced the urinary 3-methylhistidine excretion in rats by 60%.

Actins↗