Functional properties of skinned rabbit skeletal and cardiac muscle preparations containing α-cardiac myosin heavy chain

Contractile properties of skinned muscle fibres from the masseter muscle and strips of heart atrium muscle from rabbits, both containing the -cardiac myosin heavy chain isoform (-cardiac MHC), were investigated and compared with those of other skeletal muscle fibre types. The stretch-induced delayed force increase (stretch activation) was investigated on maximally Ca²⁺-activated skinned preparations as an index of the kinetic properties of the myosin heads of various MHC isoforms. Skeletal muscle fibres containing exclusively -cardiac MHC (type ) and muscle strips of heart atrium showed specific kinetics of stretch activation intermediate between those of types IIA and I fibres. In agreement with available data the unloaded shortening velocity V _u of type fibres was also intermediate between that of types IIA and I fibres. Compared with skeletal muscle type fibres, muscle strips of heart atrium exhibited significantly (P<0.001) faster kinetics of both stretch activation and V _u. We conclude that type fibres have characteristic kinetic properties that fill the gap between the fast type II and the slow type I fibres, and the following order of velocity can be established: IIB>IID(X)>IIA>>I.     

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     

Influence of fast and slow alkali myosin light chain isoforms on the kinetics of stretch-induced force transients of fast-twitch type IIA fibres of rat

This study contributes to understand the physiological role of slow myosin light chain isoforms in fast-twitch type IIA fibres of skeletal muscle. These isoforms are often attached to the myosin necks of rat type IIA fibres, whereby the slow alkali myosin light chain isoform MLC1s is much more frequent and abundant than the slow regulatory myosin light chain isoform MLC2s. In the present study, single-skinned rat type IIA fibres were maximally Ca²⁺ activated and subjected to stepwise stretches for causing a perturbation of myosin head pulling cycles. From the time course of the resulting force transients, myosin head kinetics was deduced. Fibres containing MLC1s exhibited slower kinetics independently of the presence or absence of MLC2s. At the maximal MLC1s concentration of about 75%, the slowing was about 40%. The slowing effect of MLC1s is possibly due to differences in the myosin heavy chain binding sites of the fast and slow alkali MLC isoforms, which changes the rigidity of the myosin neck. Compared with the impact of myosin heavy chain isoforms in various fast-twitch fibre types, the influence of MLC1s on myosin head kinetics of type IIA fibres is much smaller. In conclusion, the physiological role of fast and slow MLC isoforms in type IIA fibres is a fine-tuning of the myosin head kinetics.     

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.     

Store and recoil of elastic energy in slow and fast types of human skeletal muscles

Stretch-shortening cycle refers to the mechanical condition in which store and recoil of elastic energy occur in the skeletal muscle. This leads to a greater work output when compared to a simple shortening contraction. The subjects performed vertical jumps with and without preliminary counter-movement and with small and large knee angular displacement. The results indicated that those subjects who had more fast twitch (FT) fibers benefited more from the stretching phase performed with high speed and short angular displacement. The amounts of elastic energy stored in this phase were 30 and 26 N × kgBW^-1, respectively, for FT and slow twitch (ST) type subjects. The recoil of elastic energy was proportional to the amount of energy storage. In large amplitude jumps where transient period between stretch and shortening is long the both types of subjects demonstrated similar amount of storage of elastic energy (17 and 16 N × kgBW^-1, respectively). However, the re-use of this elastic energy was greater in ST group (24%) as compared to the FT group (17%). The results can be interpreted through differences in sarcomere cross-bridge life times between fast and slow muscle fibers. The slow type muscle may be able to retain the cross-bridge attachment for a longer period of time and therefore it may utilize elastic energy better in a slow type ballistic motion.     

Scaling of skeletal muscle shortening velocity in mammals representing a 100,000-fold difference in body size

To fully understand the effect of scaling on skeletal muscle shortening velocity (V ₀), it is important to know which phenotypic characteristics drive the changes between species. The purpose of the current investigation was to compare the effects of body mass and femur length, as an estimate of total limb length, on V ₀ in species that cover a 100,000-fold range of body masses. Using the slack test procedure, V ₀ was determined for fibers expressing types I and IIa myosin heavy chain (MyHC) isoforms in the mouse, rat, dog, human, horse, and rhinoceros under identical experimental conditions. A significant scaling effect on V ₀ was detected when compared to body mass (type I fibers, r=0.95, p<0.01; type IIa fibers, r=0.83, p<0.05). However, the horse’s V ₀ for both fiber types was faster than the human’s, despite having a 5-fold greater body mass than the human. When V ₀ was scaled vs limb length, the strength of the relationships improved in fibers expressing both types I and IIa MyHC (r=0.98, p<0.001, and r=0.89, p<0.05, respectively) and scaled with the expected relationship, with the species with the shorter femur, the horse, having the faster V ₀. A similar effect can be seen with stride frequency scaling more closely with limb length than body mass. These results suggest that limb length, not body mass, is a more relevant factor driving the scaling effect on skeletal muscle shortening velocity.     

Functional characteristics of the rat jaw muscles: daily muscle activity and fiber type composition

Skeletal muscles have a heterogeneous fiber type composition, which reflects their functional demand. The daily muscle use and the percentage of slow‐type fibers have been shown to be positively correlated in skeletal muscles of larger animals but for smaller animals there is no information. The examination of this relationship in adult rats was the purpose of this study. We hypothesized a positive relationship between the percentage of fatigue‐resistant fibers in each muscle and its total duration of use per day. Fourteen Wistar strain male rats (410–450 g) were used. A radio‐telemetric device was implanted to record muscle activity continuously from the superficial masseter, deep masseter, anterior belly of digastric and anterior temporalis muscles. The degree of daily muscle use was quantified by the total duration of muscle activity per day (duty time) exceeding specified levels of the peak activity (2, 5, 20 and 50%). The fiber type composition of the muscles was examined by the myosin heavy chain content of the fibers by means of immunohistochemical staining. At lower activity levels (exceeding 2 and 5% of the peak activity), the duty time of the anterior belly of digastric muscle was significantly (P < 0.01) longer than those of the other muscles. The anterior belly of digastric muscle also contained the highest percentage of slow‐type fibers (type I fiber and hybrid fiber co‐expressing myosin heavy chain I + IIA) (ca. 11%; P < 0.05). By regression analysis for all four muscles, an inter‐muscular comparison showed a positive relationship between the duty time (exceeding 50% of the peak activity) and the percentage of type IIX fibers (P < 0.05), which demonstrate intermediate physiological properties relative to type IIA and IIB fibers. For the jaw muscles of adult male rats, the variations of fiber type composition and muscle use suggest that the muscle containing the largest amounts of slow‐type fibers (the anterior belly of digastric muscle) is mainly involved in low‐amplitude activities and that the amount of type IIX fibers is positively related to the generation of large muscle forces, validating our hypothesis.     

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.     

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.     

Effects of anabolic/androgenic steroids on regenerating skeletal muscles in the rat

We have examined the effect of male sexual hormones on the regeneration of skeletal muscles. Degeneration/regeneration of the left soleus and extensor digitorum longus muscles (EDL) of Wistar male rats was induced by an injection of snake venom (2 μg, Notechis scutatus scutatus). During the muscle regeneration (25 days), rats were treated with either oil (CON), nandrolone (NAN), NAN combined with exercise (NAN + EXE) or were castrated (CAS). Muscle growth and myosin heavy chain (MyHC) isoform content of regenerating muscles were studied. Castration altered the concentrations of MyHC in venom-treated EDL (P < 0.01) and soleus (P < 0.05). NAN increased the mass (P < 0.01) of regenerating soleus and decreased the relative amount of fast MyHC protein (% of total, P < 0.05). The effect of NAN + EXE on the fast MyHC proteins of venom-treated soleus was opposite (P < 0.05). NAN and NAN + EXE were without effect on the regenerating EDL (P > 0.05). In conclusion, it is possible that male sexual hormones play a role in the growth (synthesis of contractile proteins) of regenerating muscles in rat. In addition, contrary to NAN + EXE, NAN could be beneficial to soleus regeneration.     

Structure-function relationship of soleus muscle fibres from the rhesus monkey

Functional and structural properties of rhesus monkey skinned fibres were studied in order to examine the relationship between calcium/strontium (Ca/Sr) activation characteristics and protein composition. The fibres were classified according to their Ca/Sr affinity into slow (61%) and fast groups (39%). According to the myosin isoform composition, two additional hybrid types were defined. Thus, four profiles were characterized: two corresponding to slow (S) and fast (F) isoforms and two corresponding to a mixed proportion of slow and fast isoforms. They were called hybrid slow (HS) or hybrid fast (HF) based on the predominant myosin isoform. Tension/pCa parameters and maximal shortening velocities were determined. S fibres showed a higher pCa threshold and affinity as well as shallower slopes of their tension/pCa curve than did F fibres. HS and HF fibres exhibited tension/pCa curves which were positioned close to those of S and F fibres, respectively. No significant difference was observed between S and HS fibres or between F and HF fibres. Maximal shortening velocity values were higher for fibres expressing predominantly fast myosin isoforms. We suggest than when both S and F isoforms of myofibrillar proteins are expressed in a muscle fibre, the functional properties are mainly governed by the predominant isoform.     

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     

限食8周对大鼠不同类型骨骼肌收缩功能及线粒体生物合成的影响

目的:探讨限食对不同类型骨骼肌收缩功能和线粒体生物合成的影响,为阐明限食的有益作用及机制提供实验依据。方法:每天按正常大鼠摄食量的60%饲养动物以制备限食8周大鼠模型,麻醉下分离比目鱼肌和趾长伸肌,记录电刺激诱导骨骼肌单次、强直和疲劳收缩,观测线粒体基因细胞色素C氧化酶I亚基(COX I)和核基因β-actin拷贝数的比值以反映线粒体生物合成,检测骨骼肌ATP含量以反映线粒体功能。结果:限食8周对电刺激诱导的比目鱼肌和趾长伸肌的单次和强直收缩均有增强作用,但仅提高比目鱼肌的抗疲劳作用;限食也增加两种肌肉的ATP含量,但对比目鱼肌更明显;限食虽对2种肌肉腺苷酸活化蛋白激酶(AMPK)的磷酸化具有增加作用,但只上调比目鱼肌内线粒体生物合成及其调节基因PGC-1α和NRF的转录。结论:限食8周增强大鼠比目鱼肌和趾长伸肌对电刺激的收缩反应,尤其对富含氧化型肌纤维的比目鱼肌更明显;其机制除与限食促进这2种肌肉AMPK活化、增加ATP供应以外,还与上调比目鱼肌线粒体生物合成及其调控因子有关。     

Shortening velocity and force/pCa relationship in skinned crab muscle fibres of different types

Single fibres of three different types, which had been characterized histochemically with regard to differences in myofibrillar adenosine triphosphatase (ATPase) activity and its pH stability, were microdissected from freeze dried preparations of the closer muscle in walking legs of the crab Eriphia spinifrons. Shortening velocities were determined in slack tests and under constant load conditions in maximally Ca²⁺-activated skinned muscle fibres. Force/pCa relationships were also measured for the different types of fibres. Compared with data on vertebrate muscles, all crab muscle fibres required large length changes to reach zero force and showed low Ca²⁺ sensitivity for isometric force generation. The length/time relationship obtained from slack tests had a biphasic course. Maximal velocity of filament sliding differed in the three types of fibres investigated. The filament sliding of type IV fibres was about 3 times faster than that of type I fibres. The values obtained for type II fibres ranged in between. These data are positively correlated with myofibrillar ATPase activity determined histochemically. Ca²⁺ sensitivity of force generation was lowest in the fast type IV fibres. It was high in the slow type I and the faster contracting type II fibres. Ca²⁺ sensitivity in crab muscle seems not to be correlated with speed of shortening.     

Different adaptations of alpha‐actinin isoforms to exercise training in rat skeletal muscles

Aim: Alpha (α)‐actinins are located in the skeletal muscle Z‐line and form actin–actin cross‐links. Mammalian skeletal muscle has two isoforms: α‐actinin‐2 and α‐actinin‐3. However, the response of α‐actinin to exercise training is little understood. Therefore, the current study examined the effects of exercise training on the expression level of two α‐actinin isoforms in skeletal muscles. Methods: Twelve male Wistar rats were assigned randomly to a control (C; n = 6) or exercise training (T; n = 6) group. After T animals were trained on an animal treadmill for 9 weeks, α‐actinin‐2 and α‐actinin‐3 levels in the plantaris, white and red gastrocnemius muscles were analysed. In addition, changes in the myosin heavy chain (MyHC) composition were assessed, and muscle bioenergetic enzyme activities were measured. Results: Results show that exercise training increased α‐actinin‐2 expression levels in all muscles (P < 0.05). However, no significant difference was found in α‐actinin‐3 expression levels between C and T animals. Subsequent MyHC analyses of all muscle showed an MyHC shift with direction from IIb to IIa. Furthermore, enzymatic analysis revealed that exercise training improved enzyme activities related to aerobic metabolism. Conclusion: The results of this study demonstrate that exercise training alters the expression level of α‐actinin at the isoform level. Moreover, the increase in expression levels of α‐actinin‐2 is apparently related to alteration of skeletal muscle: its aerobic capacity is improved.     

Collagen of slow twitch and fast twitch muscle fibres in different types of rat skeletal muscle

Summary The appearance of collagen around individual fast twitch (FT) and slow twitch (ST) muscle fibres was investigated in skeletal muscles with different contractile properties using endurance trained and untrained rats as experimental animals. The collagenous connective tissue was analyzed by measuring hydroxyproline biochemically and by staining collagenous material histochemically in M. soleus (MS), M. rectus femoris (MRF), and M. gastrocnemius (MG). The concentration of hydroxyproline in the ST fibres dissected from MS (2.72±0.35 g·mg^–1 d.w.) was significantly higher than that of the FT fibres dissected from MRF (1.52±0.33 g·mg^–1 d.w.). Similarly, the concentration of hydroxyproline was higher in ST (2.54±0.51 g·mg^–1 d.w.) than in FT fibres (1.60±0.43 g·mg^–1 d.w.), when the fibres were dissected from the same muscle, MG. Histochemical staining of collagenous material agreed with the biochemical evidence that MS and the slow twitch area of MG are more collagenous than MRF and the fast twitch area of MG both at the level of perimysium and endomysium. The variables were not affected by endurance training. When discussing the role of collagen in the function of skeletal muscle it is suggested that the different functional demands of different skeletal muscles are also reflected in the structure of intramuscular connective tissue, even at the level of endomysial collagen. It is supposed that the known differences in the elastic properties of fast tetanic muscle compared to slow tonic muscle as, e.g., the higher compliance of fast muscle could at least partly be explained in terms of the amount, type, and structure of intramuscular collagen.This study was supported by grants from the Finnish Research Council for Physical Education and Sport (Ministry of Education) and the Academy of Finnland     

Functional significance of collateral blood flow in working skeletal muscle of the dog

Summary The semitendinosus muscle of the dog is supplied by two separate arteries and drained by two corresponding veins. In the muscles used in this study no blood entering via the distal artery was found to leave via the proximal vein during perfusion through both arteries (orthograde perfusion). Therefore, collateral flow (CF) could be determined as proximal venous outflow during occlusion of the proximal artery. During orthograde perfusion total blood flow averaged 12 ml × min⁻¹ × 100 g⁻¹ at rest and 58.4 ml × min⁻¹ × 100 g⁻¹ during exercise. CF was found to average 6.2 ml × min⁻¹ × 100 g⁻¹ at rest and increased to 9.2 ml × min⁻¹ × 100 g⁻¹ during exercise. CF was sufficient to cover the metabolic demand of resting muscle. During exercise the O₂-uptake ( ) of the distal muscle portion was increased 13.4 fold in comparison to a 3.1 fold increase in the proximal muscle portion. The average contractile power decreased by 46%. Additional infusion of adenosine into the distal artery resulted in an increase of CF to 11.4 ml × min⁻¹ × 100 g⁻¹ and of orthograde flow to 71 ml × min⁻¹ × 100 g⁻¹. The average contractile power of the muscle increased by 13%. Both orthograde flow and CF were found to decrease with increasing muscle load. But this decrease was significantly more pronounced in the case of CF especially at a. lower range of loads. It is concluded that after acute occlusion of orthograde flow, CF is limited by the number, the size and the dilatory capacity of precapillary network vessels. Furthermore, CF is influenced considerably by changes of extravascular support. Presented in part at the 43rd Meeting of the Deutsche Physiologische Gesellschaft [9] and at the XXVI International Congress of Physiological Sciences, New Delhi [6] Supported by the Deutsche Forschungsgemeinschaft (Hi 137/6)     

Effect of endurance training and acute exercise on sarcoplasmic reticulum function in rat fast- and slow-twitch skeletal muscles

Following 10 weeks of endurance training and in age-matched sedentary rats, sarcoplasmic reticulum (SR) Ca²⁺-uptake, Ca²⁺-release, and Ca²⁺-stimulated adenosinetriphosphatase (ATPase) activity were examined in homogenates of the plantaris and soleus muscles from rats subjected to moderate-intensity treadmill running to exhaustion. In order to examine the effects of acute exercise and/or training on SR Ca²⁺-handling capacity, comparisons between exhausted and non-exercised rats and between trained and untrained rats were performed. Our data confirm that Ca²⁺-sequestration by the SR from fast-twitch muscles is depressed after training. Immediately after exhaustive running, decreases in SR function occurred in both muscles, but were more pronounced in the soleus. In the plantaris, reductions in SR Ca²⁺-uptake rate and Ca²⁺-ATPase activity were observed in untrained rats only, while in the soleus they were adversely affected irrespective of training status. Although the average run time to exhaustion varied markedly between untrained and trained animals (untrained: 253.0 min; trained: 559.4 min), no differences existed with regard to the magnitude of decreases in SR function in the soleus after exercise. The mean rate of decline in SR Ca²⁺-handling capacity during acute exercise, as estimated from the run time and the extent of the decline, was more than twofold higher in untrained than in trained soleus. From the present study, it is unclear whether there exists a causal relationship between muscular fatigue and SR function because the run time to exhaustion was not significantly correlated with any of parameters indicative of SR Ca²⁺-handling capacity, but suggested that endurance training may be capable of delaying a progression of the deterioration in SR function that occurs during exercise. Electronic Publication     

Myosin heavy chains in skeletal muscles of the common shrew (Sorex araneus): absence of a slow isoform and transitions of fast isoforms with ageing

Myosin heavy chain (MHC) composition in seven skeletal muscles of the common shrew (Sorex araneus) was analysed by gradient SDS-PAGE and immunoblotting with monoclonal antibodies. Characteristic for the studied muscles (diaphragm, lateral gastrocnemius, medial gastrocnemius, masseter, plantaris, soleus and tibialis anterior) was a total absence of the slow isoform, MHCI; all muscles were exclusively composed of two fast isoforms MHCIId and MHCIIb. In young adults the amount of MHCIId varied between 34% (tibialis anterior) and 97% (masseter). In over-wintered senescent individuals MHCIId was clearly the dominant isoform in all muscles studied; the lowest MHCIId content was measured for tibialis anterior (69%), while in diaphragm, masseter and soleus it was practically the sole isoform (over 96%). Ageing associated isoform transition from MHCIIb to MHCIId occurred in all seven muscles studied (P< 0.05).