Mechanical properties and myosin heavy chain isoform composition of skinned skeletal muscle fibres from a human biopsy sample

 Experiments were conducted to investigate the mechanics of contraction of chemically skinned muscle fibre segments of a biopsied sample of single human quadriceps muscle. Subsequently, the isoforms of the myosin heavy chain (MHC) were analysed by sodium dodecyl sulphate (SDS) gel electrophoresis.Of the 41 fibres, 26 contained MHCI (type I), 11 of the fibres contained MHCIIa (type IIA), and 4 of the fibres contained both MHCI and MHCIIa (of which MHCIIa was always slightly predominant (type IIC)). Distinct differences between fibre types were found in terms of the kinetics of force responses following stepwise length changes (order of velocity: IIA > IIC > I). The differences in maximal shortening velocity and in the kinetics of Ca²⁺-dependent activation were of the same order, but much less pronounced. Type I fibres had significantly greater fibre diameters than type IIA fibres. No significant differences were found among different fibre types in terms of isometric tension, resting sarcomere length or the length change needed to discharge the elasticity of maximally Ca²⁺-activated fibres (y _o value). The distribution of shortening velocity and kinetics of stretch activation values suggest that two muscle fibre subtypes may exist in human type I fibres. Received: 15 April 1997 / Received after revision 19 May 1997 / Accepted: 20 May 1997     

Changes in the myosin heavy chain isoform profile of the triceps brachii muscle following 12 weeks of resistance training

The purpose of this investigation was to determine whether 12 weeks of resistance training, which increased arm girth (5%) and forearm extensor strength (39%), also altered the myosin heavy chain (MHC) characteristics of the triceps brachii muscle. Fifteen healthy, active men volunteered to participate under experimental (n = 11) or control (n = 4) conditions. The experimental group completed four sets of eight to 12 repetitions for each exercise (i.e. triceps pushdown, close grip bench press, triceps kickbacks and biceps curl) with loads of between 70–75% of one repetition maximum (1RM) three times a week. The inter-set and inter-exercise recovery period was only 90 s. Skeletal muscle tissue was removed from the triceps brachii muscle prior to (W0) and following 4 (W4), 8 (W8) and 12 (W12) weeks of the investigation. Samples were analysed for MHC isoform content using 6% sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE). MHC isoform composition in the control group did not change significantly. However, the percentage of MHC type IIb isoform decreased significantly from W0 to W4 and again from W4 to W12 [W0: 39.7 (9.2); W12: 29.2 (8.2)%] in the experimental condition. The increments in MHC type IIa [W0: 34.0 (9.9); W12: 41.5 (10.4)] and type I [W0: 26.3 (7.9); W12: 29.3 (9.6)] isoforms were not significant for the experimental group. However, the effect size (ES) transformation of changes in types IIa MHC content was moderate (ES = 0.75). Changes in MHC isoform content were not significantly correlated with changes in 1RM strength for the triceps pushdown exercise. These data indicated that resistance training rapidly, and in an ongoing manner, changed the contractile protein profile of trained skeletal muscle. However, changes in MHC isoform composition in the first 12 weeks of training were not implicated in the development of 1RM triceps pushdown strength.     

Exercise training induces transitions of myosin isoform subunits within histochemically typed human muscle fibres

Fibre type composition based on histochemical myosin ATPase reaction was studied in cross section of biopsies from the vastus lateralis muscle of men. In addition, protein composition as well as peptide patterns of isolated myosin heavy chains were examined in batches of individually classified fibres from the same biopsies. High intensity endurance training during 8 weeks induces significant decreases by 31–70% of the type IIB fibre population in 3 of 4 subjects (in one case no change was observed). These decreases were offset by corresponding increases in either type I or type IIA fibres with the type IIC fibres remaining always below 3%. A total of 13 professional cyclists with training periods over several years have a 20 times lower content of type IIB fibres than 4 sedentary controls and a concomitant high content of 80% of type I fibres. The content of type I and type IIB fibres of 8 sprinter athletes did almost not differ from that of controls. Thus the type IIB fibres respond most sensitively with a decrease to aerobic endurance training. Since both type IIA and IIB fibres were identical in protein composition containing the same fast variety of myosin light chains and heavy chains as well as troponin-I, their interconversion could not be seen at the molecular level. However, the slow variety of myosin light chains and of troponin-I started accumulating after 8 weeks of training in type IIA fibres. Furthermore, the myosin heavy chain isoform started shifting by producing new peptide patterns that resemble the digestion pattern of slow myosin heavy chains in fibres which still classified as type IIA. These changes on the molecular level in type IIA fibres mark the beginning of their transition over the intermediate and variable type IIC fibres, towards the slow type I fibre.Abbreviations VLM vastus lateralis muscle - maximal oxygen uptake capacity - MVD total mitochondrial volume density - I slow-twitch fibre type - IIA IIB, fast-twitch fibre types - IIC intermediate fibre type - HC myosin heavy chain - LC myosin light chain - TN-I troponin-I - ATPase adenosine 5-triphosphatase (EC 3.6.1.3) - SAV-8 Staphylococcus aureus V-8 proteinase (EC 3.4.21.19) - SDS sodium dodecyl sulfate - kD kilo Dalton     

Effects of low-resistance/high-repetition strength training in hypoxia on muscle structure and gene expression

To test the hypothesis that severe hypoxia during low-resistance/high-repetition strength training promotes muscle hypertrophy, 19 untrained males were assigned randomly to 4 weeks of low-resistance/high-repetition knee extension exercise in either normoxia or in normobaric hypoxia (FiO₂ 0.12) with recovery in normoxia. Before and after the training period, isokinetic strength tests were performed, muscle cross-sectional area (MCSA) measured (magnetic resonance imaging) and muscle biopsies taken. The significant increase in strength endurance capacity observed in both training groups was not matched by changes in MCSA, fibre type distribution or fibre cross-sectional area. RT-PCR revealed considerable inter-individual variations with no significant differences in the mRNA levels of hypoxia markers, glycolytic enzymes and myosin heavy chain isoforms. We found significant correlations, in the hypoxia group only, for those hypoxia marker and glycolytic enzyme mRNAs that have previously been linked to hypoxia-specific muscle adaptations. This is interpreted as a small, otherwise undetectable adaptation to the hypoxia training condition. In terms of strength parameters, there were, however, no indications that low-resistance/high-repetition training in severe hypoxia is superior to equivalent normoxic training.     

Reproducibility of isokinetic leg strength and endurance characteristics of adult men and women

Summary Day-to-day variability and single-measurement reliability of selected isokinetic knee extension-flexion strength and endurance indices were assessed in 10 adult men and 8 adult women. On three occasions separated by at least 5 days, the subjects completed 4 reciprocal maximal voluntary contractions (MVC) at different angular velocities (1.05 rad · s^–1 and 3.14 rad · s^–1). The men also completed a muscular endurance test consisting of 30 reciprocal, MVC at 3.14 rad ·^–1. Coefficient of variation, intra-class correlation coefficient and standard error of single-measurement scores support the continued use of gravity corrected peak torque (PT) and average peak torque (APT) as indices of isokinetic leg strength. Similarly, gravity corrected APT and total work should be the recommended indices of isokinetic leg muscular endurance in men. The results suggest that these isokinetic indices must be assessed using multiple day-to-day trial protocols adequately to describe performance capacity. Composite indices such as the ratio of Knee flexion to extension PT and fatigue measurements offer considerably reduced reliability and a greater potential for misinterpretation. The reliability of knee extension indices generally exceeds that of flexion indices. Similar variability and reproducibility of responses were observed between men and women and between reciprocal contractions performed at angular velocities of 1.05 rad · s^–1 and 3.14 rad · s^–1.     

Skeletal muscle adaptations in elastic resistance-trained young men and women

Skeletal muscle adaptations (fiber-type composition, cross-sectional area, myosin heavy chain (MHC) content, and capillarity) were assessed in the vastus lateralis muscle of young men and women after 8 weeks of training with the Sportcord, an elastic resistance device. Ten men [mean (SD) age 20 (1.1) years] and 13 women [20 (1.2) years] performed two sets each to failure of single leg squats and leg extensions at approximately 50 repetitions x min(-1). Biopsy samples were taken from the right vastus lateralis muscle before and after training. Six fiber types (I, IC, IIC, IIA, IIAB, and IIB) were classified using myofibrillar ATPase histochemistry. Training with the Sportcord caused a small, but significant, increase in one-repetition maximum using free weights and a large increase in repetitions to failure. In addition, elastic resistance training caused an increase in the percentage of fibers classified as type IIAB for both men and women, and a decrease in the percentage of type IIB fibers in the men. MHC analysis supported these findings (a significant increase in the percentage of MHCIIa for the men). The cross-sectional areas ofboth the type I and IIAB + IIB fibers increased after training for the men, whereas no area changes were found for the women. The capillary:fiber ratio and capillary contacts per fiber type increased significantly for the men, and similar trends were noted for the women. Capillary density did not change in either the men or the women. These data suggest minor changes in fiber type composition (IIB-->IIAB), fiber size, and capillarization following short-term training with elastic resistance. Although muscular changes did occur using the Sportcord, the extent of these changes was less than those reported previously for short-term resistance-training programs using free weights.     

Co-existence of myosin heavy chain I and IIa isoforms in human skeletal muscle fibres with endurance training

The myosin heavy chain (MHC) composition of single fibres from m. vastus lateralis was analysed by one-dimensional electrophoresis and immunoblotting in three groups of young men with distinct difference in physical activity patterns. No major co-existence of MHC isoforms was found in the group with some daily physical activity. In the very sedentary group, however, 19±5% (P<0.05) of the fibres exhibited coexistence of MHC type IIa and IIb. Further, in the endurance trained group co-existence of MHC type I and IIa was manifested in 36±4% (P<0.05) of the fibres. Disuse and extreme usage of muscle both give rise to an elevation in co-expression of MHC isoforms in single muscle fibres but of markedly different combination of isoforms.     

Favourable associations between the myosin heavy-chain and light-chain isoforms in human skeletal muscle

Histochemical and biochemical analyses were performed in order to examine the relationship between myosin light-chain (LC) isoforms and fibre-type distributions in whole human skeletal muscle. Muscle biopsies were obtained from the vastus lateralis muscle in six healthy men, and analysed for the relative area occupied by each fibre type (percentage of fibre type area) and the molar ratio of each LC isoform. The percentage of type I fibre area was positively correlated with the molar ratio of slow LC (LC1s and LC2s) to total LC. The regression line was located below the line of unity. Also, the ratio of percentage of type II fibre area to that of type II fibre area was positively correlated with the molar ratio of the fast alkali LC LC1f to fast alkali LCs LC1f and LC3f. These results support previous study, having shown that in human skeletal muscle some type I fibres express various amounts of fast LC in addition to slow LC and suggest that fast myosin heavy-chain HCII a is favourably associated with LC1f, whereas HCIIb is favourably associated with LC3f.     

Postnatal expression of myosin heavy chains in muscle spindles of the rat

Summary The immunocytochemical expression of two myosin isoforms in intrafusal muscle fibers was examined in soleus muscles of neonatal (zero to six days postpartum) and adult rats. Monoclonal antibodies specific for myosin heavy chains of the slow-tonic anterior latissimus dorsi (ALD58) and fast-twitch pectoralis (MF30) muscles of the chicken were used. In adults ALD58 bound to the intracapsular regions of bag₁ and bag₂ fibers and MF30 bound to the intracapsular regions of bag₂ and chain fibers. The extracapsular regions of intrafusal fibers and all extrafusal fibers did not react to ALD58 or MF30. Bag₁ and bag₂ fibers of neonatal rats expressed immature myosin patterns but chain fibers did not. The adult pattern of immunoreactivity of intrafusal fibers developed by the fourth postnatal day, when the patterns of motor but not sensory innervation in the spindle are still immature. Data suggest that the expression and maintenance of the specific anti-myosin immunoreactivity of intrafusal fibers during postnatal development of rat spindles is dependent upon sensory but not motor innervation. Moreover, afferents might regulate the gene expression responsible for synthesis of myosins isoforms specific to intrafusal fibers only in those myonuclei located within the capsule, but not in the myonuclei in extracapsular regions of intrafusal fibers.     

Muscular adaptations in response to three different resistance-training regimens: specificity of repetition maximum training zones

Thirty-two untrained men [mean (SD) age 22.5 (5.8) years, height 178.3 (7.2) cm, body mass 77.8 (11.9) kg] participated in an 8-week progressive resistance-training program to investigate the "strength–endurance continuum". Subjects were divided into four groups: a low repetition group (Low Rep, n=9) performing 3–5 repetitions maximum (RM) for four sets of each exercise with 3 min rest between sets and exercises, an intermediate repetition group (Int Rep, n=11) performing 9–11 RM for three sets with 2 min rest, a high repetition group (High Rep, n=7) performing 20–28 RM for two sets with 1 min rest, and a non-exercising control group (Con, n=5). Three exercises (leg press, squat, and knee extension) were performed 2 days/week for the first 4 weeks and 3 days/week for the final 4 weeks. Maximal strength [one repetition maximum, 1RM), local muscular endurance (maximal number of repetitions performed with 60% of 1RM), and various cardiorespiratory parameters (e.g., maximum oxygen consumption, pulmonary ventilation, maximal aerobic power, time to exhaustion) were assessed at the beginning and end of the study. In addition, pre- and post-training muscle biopsy samples were analyzed for fiber-type composition, cross-sectional area, myosin heavy chain (MHC) content, and capillarization. Maximal strength improved significantly more for the Low Rep group compared to the other training groups, and the maximal number of repetitions at 60% 1RM improved the most for the High Rep group. In addition, maximal aerobic power and time to exhaustion significantly increased at the end of the study for only the High Rep group. All three major fiber types (types I, IIA, and IIB) hypertrophied for the Low Rep and Int Rep groups, whereas no significant increases were demonstrated for either the High Rep or Con groups. However, the percentage of type IIB fibers decreased, with a concomitant increase in IIAB fibers for all three resistance-trained groups. These fiber-type conversions were supported by a significant decrease in MHCIIb accompanied by a significant increase in MHCIIa. No significant changes in fiber-type composition were found in the control samples. Although all three training regimens resulted in similar fiber-type transformations (IIB to IIA), the low to intermediate repetition resistance-training programs induced a greater hypertrophic effect compared to the high repetition regimen. The High Rep group, however, appeared better adapted for submaximal, prolonged contractions, with significant increases after training in aerobic power and time to exhaustion. Thus, low and intermediate RM training appears to induce similar muscular adaptations, at least after short-term training in previously untrained subjects. Overall, however, these data demonstrate that both physical performance and the associated physiological adaptations are linked to the intensity and number of repetitions performed, and thus lend support to the "strength–endurance continuum". Electronic Publication     

Effects of hypobaric hypoxia on histochemical fibre-type composition and myosin heavy chain isoform component in the rat soleus muscle

Histochemical fibre-type composition and myosin heavy chain isoform component in the soleus muscle were studied in normoxic rats at postnatal ages of 5, 10, 15, and 20 weeks and in rats exposed to hypobaric hypoxia (460 torr) for 5 weeks from postnatal ages of 5, 10, and 15 weeks. The increase in the percentage of type I fibres and the concomitant decrease in that of type IIa fibres in the soleus muscle of normoxic rats were observed until 15 weeks of age. On the other hand, no change in the fibre-type composition of the muscle during postnatal development was observed in hypoxic rats, irrespective of the age at which they were exposed to hypoxia. The changes in the myosin heavy chain isoform component (MHC I and MHC IIa) of the muscle during postnatal development and by hypoxia corresponded well with those in the muscle fibre-type composition. It is concluded that hypobaric hypoxia inhibits the growth-related shift of muscle fibre-types from type IIa to type I and of myosin heavy chain isoforms from MHC IIa to MHC I in the rat soleus muscle, and that there are no changes in the muscle fibre-type composition or the myosin heavy chain isoform component caused by hypoxia after the shifts in these parameters which occur during postnatal development are completed.     

Slowing effects of Mg2+ on contractile kinetics of skinned preparations of rat hearts depending on myosin heavy chain isoform content

The effects of changes in Mg²⁺ concentration on the kinetics of stretch activation were investigated on skinned rat heart preparations under maximal Ca²⁺ activation. Muscle strips of hyper- and hypothyroid rat hearts were investigated at 0.5 and 1 mM free Mg²⁺; the total ATP concentration was 8 mM which resulted in saturating MgATP^2– concentrations above 5 mM. Preparations containing exclusively the cardiac -myosin heavy chain (hyper- and hypothyroid atria, hyperthyroid ventricles) showed an acceleration of the kinetics of stretch activation by a factor of about 1.5 (P<0.01, paired t-test) when free Mg²⁺ was decreased from 1 to 0.5 mM. Conversely, preparations containing exclusively the -myosin heavy chain isoform showed only a small acceleration by a factor of 1.05 (P<0.05, paired t-test) under the same conditions. The fact that the Mg²⁺ sensitivity was dependent on the myosin heavy chain isoform excludes the possibility that Mg²⁺ exhibits only unspecific effects on contractile proteins. Several hypotheses for explaining the observed Mg²⁺ effects are discussed. The conditions used in our experiments might be close to the physiological situation and, thus, changes of Mg²⁺ concentration must be considered as possible factors modulating the contractile kinetics especially of atrial muscle tissue.     

mRNA expression of fibroblast growth factors and hepatocyte growth factor in rat plantaris muscle following denervation and compensatory overload

We addressed the question of whether hypertrophy induced by compensatory overload differs according to innervation status, and how fibroblast growth factors (FGF) and hepatocyte growth factor (HGF) mRNAs are expressed in the rat plantaris muscle during overload (OL) and/or denervation. Male Wistar rats were divided into four groups (Normal-Cont, Normal-OL, Denervated-Cont, and Denervated-OL). according to the plantaris denervation and/or overload. Three weeks later, plantaris weight in Denervated-Cont and Denervated-OL was significantly lower than in the Normal-Cont. The muscle weights in the Normal-OL were higher than in the Normal-Cont. The muscle weights in the Denervated-OL were higher than in the Denervated-Cont. Three days after the treatment, FGF-2, FGF-6, FGF-7 and HGF mRNAs in the Normal-OL were significantly higher than those in the Normal-Cont. FGF-2, FGF-6, FGF-7 and HGF mRNAs in the Denervated-OL were also significantly higher after 3 days than those in the Denervated-Cont. After 7 days, FGF-2, FGF-5, FGF-6, FGF-7 and HGF mRNAs were significantly higher in the Normal-OL than those in the Normal-Cont. At 21 days, FGF-1, FGF-6 and HGF mRNA levels were significantly increased. In the Denervated-OL, FGF-2, FGF-7 and HGF mRNAs at 7 days, and FGF-2 mRNA at 21 days were significantly higher than those in the Denervated-Cont. FGF-2 and FGF-6 mRNA levels decreased significantly following denervation; however, FGF-1, FGF-5, FGF-7 and HGF mRNA levels increased and maintained this increase for the 21-days treatment period. Muscle hypertrophy was thus induced by compensatory overload irrespective of innervation status, possibly in association with certain FGFs and HGF. The differential mRNA expression patterns of FGFs and HGF observed following compensatory overload and/or denervation suggest distinct roles for individual FGFs and HGF in muscle hypertrophy and/or atrophy.     

Gender- and age-related differences in the regulatory influence of thyroid hormone on the contractility and myosin composition of single rat soleus muscle fibres

 The effects of 4 weeks of thyroid hormone (3,5,3′-triiodothyronine, T₃) treatment on the myosin isoform composition and maximum velocity of unloaded shortening (V ₀) of single soleus muscle fibres of young (3–6 months) and old (20–24 months) female (149 fibres) and male (200 fibres) rats were studied. Gender-related differences in the up-regulation of fast myosin heavy chain (MyHC) and myosin light chain (MyLC) isoforms were observed. In the female hyperthyroid rats, pure type I fibres and fibres co-expressing type I and type IIA MyHC (type I/IIA fibres) predominated. Some fibres expressed an α cardiac-like MyHC isoform either purely (α cardiac-like fibre type) or in co-expression with IIA MyHC (α cardiac-like/IIA fibre type). In the male hyperthyroid rats, on the other hand, all fibres were either type I/IIA or type I/IIAX. The relative quantities of fast MyLC isoforms in type I/IIA and type I/IIAX fibres was higher in female than in male hyperthyroid rats. V ₀ was similar in male and female control rats, and decreased with age in both genders (P<0.001). After T₃ treatment, the average V ₀ increased (P<0.001) in females with a concomitant up-regulation of fast MyHC and fast MyLC isoforms irrespective of age. The average V ₀ of the pooled fibres was higher (P<0.001) in female than in male hyperthyroid rats at both ages. In conclusion, gender- and age-related differences were observed in the regulatory influence of 4 weeks’ T₃ treatment on myosin isoform composition and V ₀ in soleus fibres. These differences are presumably related to an interaction of thyroid and sex hormones in the regulation of myosin gene expression. Received: 10 March 1998 / Received after revision 3 June 1998 / Accepted: 14 August 1998     

Expression of myosin heavy and light chains changes during pregnancy in the rat uterus

We investigated the in vivo expression of myosin heavy chains (MHC) and myosin light chains (MLC) in the rat uterus during pregnancy and post parturn (p. p.). According to their antigenic reactivity, we observed two smooth-muscle-specific MHC (SM-MHC) of 204 kDa and 200 kDa (SM1 and SM2 respectively) and one non-muscle-specific MHC band of 198 kDa (NM-MHC). Adult virgin female rats expressed SM1 and NM-MHC (65/35) but no SM2. During the first pregnancy NM-MHC expression decreased in favour of the SM1 form, the SM1/NM-MHC ratio being 82/12 after 20 days of pregnancy. SM2 is newly expressed in the first p. p. state, the SM1/SM2/NM-MHC ratio being 58/28/14 between 3 and 33 days p. p. During the second pregnancy, starting 34 days p. p., both SM2 and NM-MHC expression decreased, the SM1/SM2/NM-MHC ratio being 85/0/15 after 20 days of pregnancy. Two protein bands of approximately 154 kDa and 145 kDa (sodium dodecylsulphate electrophoresis), designated SMP1 and SMP2 respectively, with the same immunoreactivity as the SM-MHC were observed in vivo in the pregnant but not in the non-pregnant uterus. In addition, a Ca²⁺-independent protease, which uses MHC as substrate, is expressed in the pregnant but not in the non-pregnant rat uterus. Two isoforms of the 17-kDa MLC (LC_17a and LC_17b) exist in the rat uterus. Expression of the LC_17a isoform increased during the first pregnancy from 46% in virgin rats to 65% in uteri of rats 20 days pregnant. During the first p. p. state LC_17a expression decreased to 42% at 19 days p. p. then remained constant up to 33 days p. p. Again, during the second pregnancy LC_17a expression increased to the same extent as observed in the first pregnancy. Phosphorylation of the 20-kDa MLC forms of skinned uterus fibres derived from 6-days- and 20-days-pregnant rats (first and second pregnancy) increased upon Ca²⁺ activation but the phosphorylation levels were the same in both groups. As extrapolated from the force/velocity relation, the maximal shortening velocity (V _max) of chemically skinned uteri from 6-days pregnant-rats was 0.104 muscle length (ML) s^–1 and increased up to 0.201 ML s^–1 in uteri from 20-days-pregnant animals (first pregnancy). V _max remained high 2 days p. p. (0.2 ML s^–1) and decreased to 0.09 ML s^–1 19 days p. p. During the second pregnancy V _max was 0.1 ML for 6-days-pregnant uteri and increased up to 0.21 ML s^–1 after 20 days of pregnancy. Our results suggest a correlation between LC_17a expression and V _max rather than between MHC and V _max.     

Differential titin isoform expression in human skeletal muscle

Mammalian skeletal muscle expresses at least two isoforms of the cytoskeletal protein titin (connectin; MW ≈ 3000 kDa). These isoforms are associated with different passive force curves, and thus may affect physical performance. To study the distribution of titin and its possible influence on performance in humans, muscle biopsies were obtained from 15 males (X ± SE; age = 25.4 ± 2.9 years, height = 177.7 ± 1.8 cm, weight = 76.5 ± 2.2 kg). Two biopsies were obtained on separate occasions from both the right and left vastus lateralis, and one biopsy each from the lateral head of the right gastrocnemius and the right soleus, with all biopsies handled identically. Fibre type analyses were performed via mATPase histochemistry. Expression of titin and myosin heavy chain isoforms were determined by SDS-PAGE. Titin bands in the resulting gels were highly repeatable and were verified by migration patterns, as well as Western blot analysis. Two groups of subjects were identified: group 1 (n=10) expressed only one titin isoform (titin-1) in all biopsies, and group 2 (n=5) expressed two titin isoforms (titin-1 and titin-2) in all biopsies. No significant differences (P> 0.05) between groups were observed for percentage fibre types, percentage fibre type areas, fibre type cross-sectional areas, and percentage myosin heavy chain expression when comparing individual muscles, sampling times or bilateral comparisons. This is the first report of differential titin isoform expression in healthy, mature human skeletal muscle, but it is not clear why this occurs or what influence this may have on performance.     

Correlation between isoform composition of the 17 kDa myosin light chain and maximal shortening velocity in smooth muscle

The relation between the isoform distribution of the myosin 17 kDa essential light chain (LC₁₇) and the mechanical properties of smooth muscle was investigated. The relative content of the basic (LC_17b) and acidic (LC_17a) isoelectric variants of the 17 kDa myosin light chain was determined in different mammalian smooth muscle tissues. The relative content of LC_17b varied between muscles: rabbit rectococcygeus 0%, rabbit trachea 5%, guinea-pig taenia coli 21%, rat uterus 38%, rabbit aorta 56% and rat aorta 60%. The rate of tension development was determined following photolysis of cagedadenosine triphosphate (ATP) in skinned fibres activated with thiophosphorylation of the regulatory light chains. The half-time for force development was 0.67 s in rabbit rectococcygeus, 1.6 s in rabbit trachea, 1.13 s in guineapig taenia coli and 1.38 s in rabbit aorta. The maximal shortening velocity (v _max) was determined with the isotonic quick release technique in skinned fibre preparations activated with thiophosphorylation. v _max was 0.25 muscle lengths per second (ML/s) in rabbit rectococcygeus, 0.24 ML/s in rabbit trachea, 0.17 ML/s in guinea-pig taenia coli, 0.11 ML/s in rat uterus and 0.03 ML/s in rabbit aorta. The range of variation in v _max between muscles was larger than in the half-time for force development. The inverse relationship between v _max and the relative content of LC_17b in the investigated muscles suggests that the type of essential myosin light chain influences the v _max in smooth muscle.     

Myosin heavy chain isoform transition in ageing fast and slow muscles of the rat

Sugiura , T., Matoba , H., Miyata , H., Kawai , Y. & Murakami , N. 1992. Myosin heavy chain isoform transition in ageing fast and slow muscles of the rat. Acta Physiol Scand 144 , 419423. Received 26 August 1 991 , accepted 3 December 1991. ISSN 0001–6772. Laboratory of Biomechanics and Physiology, Faculty of Liberal Arts, Yamaguchi University, Yamaguchi, Faculty of Integrated Arts and Sciences, Tokushima University, Tokushima, and Department of Physiology, Yamaguchi University School of Medicine, Ube, Yamaguchi, Japan. Using gradient sodium dodecyl sulphate-polyacrylamide gel electrophoresis, myosin heavy chain (MHC) isoforms were studied in the extensor digitorum longus (EDI,) and the soleus muscles of male Wistar rats at different ages ( 5, 10 , 20 weeks, 1 and 2 years). In the EDL muscle, four types of MHC isoforms were observed in all age groups. There was an increase in the percentage of HCIId and a concomitant decrease in the percentage of HCIIb with increasing age. No significant difference was observed in the percentages of HCI and HCIIa isoforms in all the age groups. In contrast, the soleus muscle contained two MHC isoforms, HCI and HCIIa. There was an increase in the percentage of HCI and a concomitant decrease in the percentage of HCIIa with increasing age. These results suggest that age-related changes in the MHC isoforms in both the fast-twitch EDI, and the slow-twitch soleus muscles are one factor underlying the age-related decrease in the speed of muscle contraction.