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1. Some rabbit masseter fibres express the alpha-cardiac myosin heavy chain (MHC). To compare the biochemical and physiological properties of these fibres with other skeletal fibre types, we examined the histochemical and immunohistochemical staining characteristics, maximum velocity of shortening (V(zero)) and MHC isoform content of fibres from rabbit masseter and soleus muscles. 2. The fibre-type composition of muscle sections was determined with MHC antibodies and myofibrillar ATPase histochemistry. Fibres we designated 'type alpha-cardiac' were different from type I and type II fibres in that they stained positively with the alpha-cardiac MHC antibody and they maintained. ATPase reactivity after acid and alkali pre-incubations. Samples of superficial masseter contained a few type I fibres, with the majority of fibres classified as either type IIA or type alpha-cardiac. Soleus samples contained type I, IIA and IIC fibres. 3. The V(zero) of chemically skinned fibres was determined by the slack-test method. Each fibre was subsequently characterized as type I, IIA, IIC or alpha-cardiac from MHC identification using gel electrophoresis (SDS-PAGE). In masseter fibres the V(zero) values were (in muscle lengths s-1): type I, 0.54 +/- 0.05 (mean +/- S.D., n = 3); type IIA, 1.23 +/- 0.34 (n = 27); type alpha-cardiac, 0.78 +/- 0.08 (n = 9). In soleus fibres V(zero) values were: type I, 0.55 +/- 0.06 (n = 14); type IIA, 0.89 +/- 0.04 (n = 8); type IIC, 0.73 (n = 2). 4. We conclude that the rabbit masseter muscle contains an 'alpha-cardiac' fibre type that is distinct from other skeletal fibres. This fibre type expresses only the alpha-cardiac MHC, has unusual myofibrillar ATPase reactivity and has a V(zero) intermediate between type I and type II fibres.
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PMID:Unloaded shortening velocities of rabbit masseter muscle fibres expressing skeletal or alpha-cardiac myosin heavy chains. 873 79

The contractile characteristics of three human muscle groups (triceps surae, quadriceps femoris and triceps brachii) of seven young male subjects were examined. The contractile properties were determined from electrically evoked isometric responses and compared with fibre type composition determined from needle biopsy samples. Fibre types were identified using myosin heavy chain (MHC) isoforms as molecular markers with gel electrophoresis (SDS-PAGE) and histochemical ATPase staining. Four contractile parameters (twitch time to peak torque, the maximal rate of torque development, frequency response and fatiguability) were found to be related to fibre type composition. From the biopsy samples, single muscle fibres were isolated and chemically skinned. Isometric tension (Po) unloaded shortening velocity (Vo) and rate of tension rise (dP/dt) were determined. Each fibre was classified on the basis of its MHC isoform composition determined by SDS-PAGE. Fibres belonging to the same type showed identical contractile parameters regardless of the muscle of origin, except minor differences in Po of the fast fibres and dP/dt of slow fibres. The results are in favour of the conclusion that fibre type composition, determined using MHC isoforms as markers, is the major determinant of the diversity of contractile properties among human muscle groups.
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PMID:Whole-muscle and single-fibre contractile properties and myosin heavy chain isoforms in humans. 877 43

The myosin heavy chain (MHC) compositions of adult feline limb and diaphragm muscles were determined. Sodium dodecyl sulfate-polyacrylamide gels (SDS-PAGE) were able to separate three different MHC isoforms. This was in contrast to rat muscles, in which four MHC isoforms were separated by SDS-PAGE. The fastest migrating cat MHC migrated similar to rat type I MHC and labeled in Western blots with a monoclonal antibody (mAb) specific for slow MHC and was categorized as type I. The other two MHC isoforms labeled in Western blots with a mAb specific for fast MHC and were categorized as type II. The slowest migrating fast isoform migrated similar to rat type IIa MHC and labeled with mAb N2.261, specific for types I and IIa; therefore, this MHC was categorized as type IIa. The intermediate migrating cat MHC did not migrate similar to either rat type IIx or type IIb and was not reactive with mAbs N2.261, 35 (specific for rat I, IIa, and IIb MHCs), or F3 (specific for rat IIb MHC). In tissue sections, type IIB fibers (based on myofibrillar ATPase histochemistry) were also unstained with mAbs N2.261 and 35. Therefore, the intermediate migrating cat MHC was categorized as type IIx. Consequently, feline limb and diaphragm muscles were composed of fibers containing type I, IIa, or IIx MHCs. The observations that type I and IIa isoforms, but not IIx, had similar electrophoretic mobilities in the cat and rat and that type IIb was absent from cat limb muscles suggest that there is greater diversity in MHC isoforms IIb and IIx compared to I and IIa in cats compared to rats.
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PMID:Myosin heavy chain composition of adult feline (Felis catus) limb and diaphragm muscles. 879 86

Maximal tension generated by gastric muscle is three to four times greater in weanlings than in newborn rabbits. To determine if this functional maturation is accompanied by structural changes, we compared length-tension relationships, myocyte number and size, and actomyosin content in muscle from the gastric body of newborn (1 day) and weanling (12 weeks) rabbits. Passive tension at optimal length (Lo) was six times greater in circular smooth muscle strips from weanling rabbits than from newborn rabbits. Active tension at Lo in weanling rabbits was three times greater than in newborn rabbits. For morphometry, muscle cross-sections stretched to Lo in the circular axis were photographed with electron microscopy (5300x). Cell number/unit area was counted in circular muscle layers from newborns and weanlings. Cross-sectional area of each cell was measured by computerized planimetry. There were 2.5 times more cells per unit area in newborn than in weanling tissue, P < 0.001. However, the mean cell area in newborns (5.4 +/- 4.6 microns2) was less than that in weanlings (13.5 +/- 11.7 microns2). Consequently, the muscle cells occupied similar total areas in newborns and weanlings. We measured actin and myosin heavy chain in full-thickness muscle homogenates using SDS gel electrophoresis and densitometric scanning. Actin and myosin concentrations were lower in newborns (9.6 +/- 1.3 micrograms g-1 wet weight and 5.6 +/- 0.7 micrograms g-1 wet wt, respectively) than in weanlings (17.7 +/- 3.0 micrograms g-1 wet wt and 8.2 +/- 1.6 micrograms g-1 wet wt respectively), each P < 0.01. The proportion of myosin heavy chain isozymes did not change with age. We conclude that there are postnatal increases in cell size and the quantity of actin and myosin in rabbit gastric muscle. The increase in quantity of contractile protein may be in part responsible for age-dependent increases in maximal tension.
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PMID:Postnatal changes in size and actomyosin content of rabbit gastric myocytes. 884 4

Congestive heart failure is often associated with skeletal muscle abnormalities that contribute to early fatigue and acidosis. Up to the present time, however, the mechanisms responsible for these changes are unclear. Myocardial infarctions were produced by coronary ligation in adult Sprague-Dawley rats. At 20 weeks, 10 control rats, and 15 animals with heart failure [defined by elevated LVEDP (26.1 +/- 3.1 v 2.5 +/- 0.5 mmHg) and RV hypertrophy (300 +/- 21 g v 158 +/- 9 mg)] underwent in vivo measurements of total body, and soleus total protein and myosin heavy chain (MHC) synthesis by [3H]leucine constant infusion. Soleus muscle was also analysed for protein content, and MHC isoenzyme content by SDS-PAGE. Northern blotting also was used to determine levels of the mRNA's encoding type I, IIa, IIb, and IIx MHC, alpha-skeletal actin, COX III, SDH and GAPDH. Soleus muscles in heart failure rats were smaller than controls (112 +/- 6 v 126 +/- 5 mg) and the degree of atrophy was significant when corrected for body mass (0.38 +/- 0.02 v 0.46 +/- 0.02 mg/g. P = 0.007). Although there was no significant difference in plasma leucine flux (an index of whole-body protein synthesis), soleus muscle total and MHC synthesis was reduced in heart failure animals. Whereas the Type I MHC isoenzyme (beta MHC) was the only MHC detected in the soleus of control animals, type II MHC isoenzyme comprised 11.8 +/- 3.1% of the MHC in the heart failure group. Furthermore, steady-state mRNA levels encoding beta MHC were significantly depressed in the heart failure rats, where those encoding Types IIb and IIx MHC were increased. Steady-state mRNA levels of alpha-skeletal actin, cytochrome C oxidase (COX III) and succinate dehydrogenase (SDH) were also significantly depressed. This animal model of chronic heart failure is associated with quantitative and qualitative alterations in skeletal muscle gene expression that are similar to those reported in skeletal muscle of patients with chronic heart failure. The altered phenotype and impaired metabolic capacity may contribute to exercise intolerance in CHF.
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PMID:Alterations in skeletal muscle gene expression in the rat with chronic congestive heart failure. 887 78

In adult rat muscles experimentally exposed to various patterns of activation, expression of myosin heavy chain isoforms changes, but only within a certain adaptive range. It is characteristic and different in fast or slow muscles. This may be due either to different intrinsic properties of the myogenic cells of the two types of muscles or to extrinsic factors. To test these assumptions, either rat soleus or extensor digitorum longus muscles were injured and transplanted to the bed of the extensor digitorum longus muscle. They regenerated and were reinnervated by the extensor digitorum longus nerve. Expression of myosin heavy chain isoforms was demonstrated immunohistochemically and by in situ hybridization, and analysed by SDS-gel electrophoresis. Three months after cross-transplantation, regenerated soleus expressed all adult myosin heavy chain isoforms, including the myosin heavy chain-2B. The latter was detected in about 50% of muscle fibres and contributed about 10-20% of all myosin heavy chains. The same percentage of myosin heavy chain-2B was found in regenerated extensor digitorum longus. In this regard therefore, the adaptive range of the regenerated soleus muscle was not significantly different from that of the extensor digitorum longus regenerating under the same conditions. This indicates that restriction of the adaptive range in a mature soleus muscle is not due to intrinsic properties of its myogenic cells. It is probably imposed by an extrinsic factor leading to irreversible shut-down of individual myosin heavy chain genes. On the other hand, myosin heavy chain-1 expression was significantly greater in the regenerated soleus than in the extensor digitorum longus innervated by the same nerve. Myosin heavy chain-1 and myosin heavy chain-2B were co-expressed in some regenerated soleus muscle fibres.
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PMID:Adaptive range of myosin heavy chain expression in regenerating soleus is broader than in mature muscle. 888 96

The hypothesis that the limited adaptive range observed in fast rat muscles in regard to expression of the slow myosin is due to intrinsic properties of their myogenic stem cells was tested by examining myosin heavy chain (MHC) expression in regenerated rat extensor digitorum longus (EDL) and soleus (SOL) muscles. The muscles were injured by bupivacaine, transplanted to the SOL muscle bed and innervated by the SOL nerve. Three months later, muscle fibre types were determined. MHC expression in muscle fibres was demonstrated immunohistochemically and analysed by SDS-glycerol gel electrophoresis. Regenerated EDL transplants became very similar to the control SOL muscles and indistinguishable from the SOL transplants. Slow type 1 fibres predominated and the slow MHC-1 isoform was present in more than 90% of all muscle fibres. It contributed more than 80% of total MHC content in the EDL transplants. About 7% of fibres exhibited MHC-2a and about 7% of fibres coexpressed MHC-1 and MHC-2a. MHC-2x/d contributed about 5-10% of the whole MHCs in regenerated EDL and SOL transplants. The restricted adaptive range of adult rat EDL muscle in regard to the synthesis of MHC-1 is not rooted in muscle progenitor cells; it is probably due to an irreversible maturation-related change switching off the gene for the slow MHC isoform.
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PMID:Regenerated rat fast muscle transplanted to the slow muscle bed and innervated by the slow nerve, exhibits an identical myosin heavy chain repertoire to that of the slow muscle. 895 Jun 5

This study examined the effects of 6 weeks of treatment with the beta(2)-adrenoceptor agonist, clenbuterol, on the soleus muscle of adult female Sprague-Dawley rats. Animals (4 months old) were divided into two groups: clenbuterol treated (CL, n = 7) (2 mg.kg-1 body mass injected subcutaneously every other day), and control (CON, n = 7) (injected with isotonic saline). Post-treatment body weights were approximately 5% greater in the CL group compared to CON (P < 0.05). Polyacrylamide gel electrophoresis (SDS-PAGE) of soleus myofibrillar protein indicated a clenbuterol-induced decrease (P < 0.05) in the relative percentage of type I myosin heavy chain (MHC) with a concomitant increase (P < 0.05) in type IIdx MHC, while the proportion of type IIa MHC was unaffected. ATPase fiber typing revealed increases (P < 0.05) in the proportion of type II fibers expressed both as a percentage of total fiber number and total cross-sectional area (CSA). Finally, mean type II fiber CSA was approximately 25% greater (P < 0.05) in the CL groups as compared to the CON group. These data indicate that clenbuterol treatment results in alterations in the MHC phenotype and an increased proportion of type II fiber CSA in the soleus of adult rats. These observations were due to an increase in the total number of type II fibers, as well as hypertrophy of these fibers. Thus, the relative increase in the number of histochemically determined type II fibers and the emergence of the normally unexpressed type IIdx MHC isoform in the soleus suggest a clenbuterol-induced transition of muscle fiber phenotype as well as selective hypertrophy of the type II fibers.
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PMID:Clenbuterol-induced fiber type transition in the soleus of adult rats. 895 85

Four rabbit muscles (i.e. semimembranosus proprius, psoas major, biceps femoris and longissimus lumborum), differing in their fibre type composition in the adult, were investigated during postnatal development. Muscle samples were taken at 1, 7, 14, 21, 28, 35, 49 and 77 days of age. Complementary techniques were used to characterize myosin heavy chain (MHC) isoform transitions, i.e. SDS-PAGE, immunocytochemistry and conventional histochemistry. Good accordance was found between electrophoretic and immunocytochemical techniques. Our results show that rabbit muscles were phenotypically immature at birth. At 1 day of age, perinatal isoform represented 70-90% of the total isoform content of the muscles. Two generations of myofibres could be observed on the basis of their morphology and reaction to specific antibodies. In all muscles, primary fibres expressed slow MHC. In contrast, secondary generation of fibres never expressed slow MHC in future fast muscles, while half of them expressed slow MHC in the future slow-twitch muscle, the semimembranosus proprius. During the postnatal period, all muscles displayed a transition from embryonic to perinatal MHC isoforms, followed by a transition from perinatal to adult MHC isoforms. These transitions occured mainly during the first postnatal month. The embryonic isoform was no longer expressed after 14 days, except in longissimus where it disappeared after 28 days. On the contrary, large differences were found in the timing of disappearance of the perinatal isoform between the four muscles. The perinatal isoform disappeared between 28 and 35 days in semimembranosus proprius and 35 and 49 days in psoas and biceps femoris. Interestingly, the perinatal isoform was still present in 6% of the fibres in longissimus at 77 days, the commercial slaughter age, denoting a great delay in the maturation. Fate of each generation of fibres differed between muscles.
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PMID:Myosin isoform transitions in four rabbit muscles during postnatal growth. 899 85

Actin and nonmuscle myosin heavy chain (myosin-II) have been identified and localized in the cortex of unfertilized zebrafish eggs using techniques of SDS-polyacrylamide gel electrophoresis, immunoblotting, and fluorescence microscopy. Whole egg mounts, egg fragments, cryosections, and cortical membrane patches probed with rhodamine phalloidin, fluorescent DNase-I, or anti-actin antibody showed the cortical cytoskeleton to contain two domains of actin: filamentous and nonfilamentous. Filamentous actin was restricted to microplicae and the cytoplasmic face of the plasma membrane where it was organized as an extensive meshwork of interconnecting filaments. The cortical cytoplasm deep to the plasma membrane contained cortical granules and sequestered actin in nonfilamentous form. The cytoplasmic surface (membrane?) of cortical granules displayed an enrichment of nonfilamentous actin. An antibody against human platelet myosin was used to detect myosin-II in whole mounts and egg fragments. Myosin-II colocalized with both filamentous and nonfilamentous actin domains of the cortical cytoskeleton. It was not determined if egg myosin was organized into filaments. Similar to nonfilamentous actin, myosin-II appeared to be concentrated over the surface of cortical granules where staining was in the form of patches and punctate foci. The identification of organized and interconnected domains of filamentous actin, nonfilamentous actin, and myosin-II provides insight into possible functions of these proteins before and after fertilization.
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PMID:The cortical actin cytoskeleton of unactivated zebrafish eggs: spatial organization and distribution of filamentous actin, nonfilamentous actin, and myosin-II. 905 46


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