Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.6.1.3 (ATPase)
65,361 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Muscle mass, fiber area, total fiber number, fiber population and capillarity were assessed in 6- and 25-month-old animals trained by treadmill running at 75% mean maximal capacity for 10 weeks. Serial cross-sections were stained for ATPase activity to differentiate fiber types and expose capillaries. Aging and training effects were demonstrated in maximal running speed and endurance running time. Soleus muscle mass increased in the aged, however, soleus and EDL total fiber number were declining. When adjusted for muscle weight, a significant reduction existed in fiber number for the aged soleus. Fiber area increased in the old soleus compared to young. All changes in the EDL were specific to the deep region. While there was a tendency for the capillaries/fiber and fiber area to be higher with training in the Type I fibers of the soleus, it was only significant for the young animals. Thus, while the majority of variables that showed a training effect did so across both age groups, this was not the case for vascularity. Age-associated changes in muscle morphology appear to be both muscle and fiber specific.
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PMID:A comparison of skeletal muscle morphology with training between young and old Fischer 344 rats. 203 12

The effect of a wide range of temperature on the development of twitch and tetanic tension was investigated in directly stimulated rat fast (EDL) and slow (SOL) twitch muscle preparations. When increasing the temperature from 6 to 30 degrees C the maximum tetanic tension rose steadily. The Q10 was 2.3 (EDL) and 2.7 (SOL) for temperatures between 12 and 22 degrees C. The twitch tension output of SOL muscle increased up to 36-38 degrees C, whereas the EDL muscle exhibited a distinct maximum at 22 degrees C followed by a 50% decrease at 34 degrees C. Post-tetanic potentiation was observed in EDL muscle at temperatures higher than 20 degrees C. In SOL muscle neither posttetanic potentiation nor cold potentiation could be observed. The twitch/tetanus ratio was 0.2-0.3 at 35 degrees C but 0.7-0.8 at 6 degrees C. In both muscle types the most characteristic effect of temperature was the prolongation of the time to peak and the relaxation time in parallel to cooling. The tension rise of fast twitch rat muscle during cooling from 35 degrees C downwards can be compared to the cold potentiation of frog sartorius muscle. It is suggested that the main effect of temperature on muscle function concerns the process of Ca2+ release and of Ca2+ uptake. The different response of SOL muscle may be related to the less developed sarcoplasmic reticulum and the lower Ca2+ ATPase activity.
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PMID:Contractile properties of fast and slow twitch muscles of the rat at temperatures between 6 and 42 degrees C. 344 7

1. The isometric properties and related biochemical properties of a developing rat fast muscle (extensor digitorum longus, EDL) have been determined during the 21 days after birth.2. At birth the maximum rate of rise of tension in a tetanus, a measure of speed of contraction, is slow; it begins to increase only after the 5th day and reaches adult values by 21 days.3. The increase in actomyosin ATPase activity of the rat EDL correlates closely (P << 0.001) with the changes in the maximum rate of rise during the same period of development.4. The relaxation phase of a tetanic response begins to increase in speed promptly after birth, and reaches adult values by the 21st day. The rate of calcium accumulation by the isolated sarcoplasmic reticulum (SR) increases with a similar time course.5. The separate contributions of contraction and relaxation mechanisms to the changes in the more conventional isometric properties of maturing muscles have been analysed.
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PMID:Development of a mammalian fast muscle: dynamic and biochemical properties correlated. 427 1

The rate of splitting of energy-rich phosphate compounds and the extent of myosin light chain phosphorylation in contracting mouse extensor digitorum longus (EDL, fast twitch) and soleus (slow twitch) muscles were studied at 20 degrees C. The rate of high energy phosphate-splitting during a maintained isometric tetanus was 1.44 +/- 0.21 mumol . g-1 . s-1 in soleus. In EDL, the splitting rate was higher, 3.71 +/- 0.62 mumol . g-1 . s-1, during the first several seconds and thereafter was reduced to a rate of 1.63 +/- 0.35 mumol . g-1 . s-1 between 12 and 15 s of stimulation. Light chains identified on 2-dimensional gel electrophoretograms from EDL corresponded to the light chain composition of fast twitch muscle (LC1f, LC2f, and LC3f). Soleus is composed of fast twitch and slow twitch fibers because 2 additional light chains were found: LC1s and LC2s. In unstimulated EDL and soleus muscles, 0.1 of the LC1f and LC2s were phosphorylated. Upon stimulation, only LC2f, and only in EDL, increased its extent of phosphorylation. The time course of increase in phosphorylation of LC2f and decrease in rate of high energy phosphate-splitting correspond so that the 2 processes may be mechanistically related. If so, it appears that myosin LC2f phosphorylation represents a thick filament regulatory system capable of downward modulation of actomyosin ATPase in vivo during a maintained contraction.
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PMID:Myosin light chain phosphorylation is associated with a decrease in the energy cost for contraction in fast twitch mouse muscle. 706 10

Hindlimb skeletal muscles of the rat express two isoforms of the alpha (alpha 1 and alpha 2) and two isoforms of the beta (beta 1 and beta 2) subunits of the Na+,K(+)-ATPase. Because several muscles constitute the hindlimb, we investigated if specific isoforms are expressed in particular muscles. Northern blot analysis using isoform-specific cDNA probes demonstrated that soleus muscle expressed only the beta 1 transcript, whereas EDL or white gastrocnemius muscles expressed only the beta 2 transcript, and red gastrocnemius muscle expressed both mRNAs. All muscles tested expressed both alpha 1 and alpha 2 transcripts, albeit to various degrees: alpha 1 transcripts were present to about the same extent in all muscles but alpha 2 mRNA was 4-fold more abundant in soleus than in EDL for the same amount of total RNA. Beta subunit protein levels were investigated in purified plasma membrane fractions of pooled red (soleus + red gastrocnemius + red quadriceps) or white (white gastrocnemius + white quadriceps) muscles using isoform-specific antibodies. Red muscles expressed mostly the beta 1 protein while white muscles expressed mostly the beta 2 subunit. Both muscle groups had similar levels of alpha 1 or alpha 2 subunits, and crude membranes isolated from red muscles had 30% higher Na+,K(+)-ATPase activity than white muscle membranes. We conclude that oxidative muscles (slow and fast twitch) express beta 1 subunits, whereas glycolytic, fast twitch muscles express beta 2 subunits, and that both beta isoforms support the Na+,K(+)-ATPase activity of the alpha subunits.
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PMID:Expression of beta subunit isoforms of the Na+,K(+)-ATPase is muscle type-specific. 839 48

Based on the MHC isoform pattern, adult mammalian limb skeletal muscles contain two and, in some species, three types of fast fibers (Type IIa, IIx, and IIb), and one slow fiber (Type I). Slow muscles, such as the soleus, contain primarily the slow Type I fiber, whereas fast-twitch muscles are composed primarily of a mixture of the fast myosin isozymes. Force generation involves cross-bridge interaction and transition from a weakly bound, low-force state (AM-ADP-P(i)) to the strongly bound, high-force state (AM-ADP). This transition is thought to be rate limiting in terms of dP/dt, and the high-force state is the dominant cross-bridge form during a peak isometric contraction. Intact fast and slow skeletal muscles generate approximately the same amount of peak force (Po) of between 200 and 250 kN.m-2. However, the rate of transition from the low- to high-force state shows Ca2+ sensitivity and is 7-fold higher in fast-twitch, as compared to slow-twitch, skeletal muscle fibers. Fiber Vo or the maximal cross-bridge cycle rate is highly correlated with and thought to be dependent on the specific activity of the myosin or myofibrillar ATPase. The hierarchy for Vo is the Type IIb > IIx > IIa > I. This functional difference for the fast fiber types explains the higher Vo observed in the predominantly Type IIb SVL vs. the mixed fast Type IIa and IIb EDL muscle. A plot of Vo vs. species size demonstrates that an inverse relationship exists between Vo and body mass. From the standpoint of work capacity, the important property is power output. An analysis of individual muscles indicates that peak power is obtained at loads considerably below 50% of Po. Individuals with a high percentage of fast-twitch fibers generate a greater torque and higher power at a given velocity than those with predominantly slow-twitch fibers. In humans, mean peak power occurred in a ratio of 10:5:1 for the Type IIb, IIa, and I fibers. The in vivo measurement of the torque-velocity relationship and Vmax in human muscle is difficult because of limitations inherent in the equipment used and the inability to study the large limb muscles independently. Nevertheless, the in vivo torque-velocity relationships are similar to those measured in vitro in animals. This observation suggests that little central nervous system inhibition exists and that healthy subjects are able to achieve maximal activation of their muscles. Although peak isometric tension is not dependent on fiber type distribution, a positive correlation exists between the percentage of fast fibers and peak torque output at moderate-to-high angular isokinetic velocities. Consequently, peak power output is substantially greater in subjects possessing a predominance of fast fibers. The mechanical properties of slow and fast muscles do adapt to programs of regular exercise. Endurance exercise training has been shown to increase the Vo of the slow soleus by 20%. This increase could have been caused by either a small increase in all, or most, of the fibers, or to a conversion of a few fibers from slow to fast. Recently, the increase was shown to be caused by the former, as the individual slow Type I fibers of the soleus showed a 20% increase in Vo, but there was little or no change in the percentage of fast fibers. The increased Vo was correlated with, and likely caused by, an increased fiber ATPase. We hypothesize that the increased ATPase and cross-bridge cycling speed might be attributable to an increased expression of fast MLCs in the slow Type I fibers (Fig. 14.10). This hypothesis is based on the fact that light chains have been shown to be involved in the power stroke, and removal of light chains depresses force and velocity. Regular endurance exercise training had no effect on fiber size, but with prolonged durations of daily training it depressed Po and peak power. When the training is maintained over prolonged periods, it may even induce atrophy of the slow Type I and fast Type IIa fibers. (ABSTRACT TRUNCATED)
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PMID:Muscle mechanics: adaptations with exercise-training. 874 58

The present study was carried out to investigate the contribution of the Ca2+-transport ATPase of the sarcoplasmic reticulum (SR) to caffeine-induced Ca2+ release in skinned skeletal muscle fibres. Chemically skinned fibres of balb-C-mouse EDL (extensor digitorum longus) were exposed for 1 min to a free Ca2+ concentration of 0.36 microM to load the SR with Ca2+. Release of Ca2+ from the SR was induced by 30 mM caffeine and recorded as an isometric force transient. For every preparation a pCa/force relationship was constructed, where pCa = -log10 [Ca2+]. In a new experimental approach, we used the pCa/force relationship to transform each force transient directly into a Ca2+ transient. The calculated Ca2+ transients were fitted by a double exponential function: Y0 + A1 . (-t/t1) + A2 . exp(t/t2), with A1 < 0 < A2, t1 < t2 and Y0, A1, A2 in micromolar. Ca2+ transients in the presence of the SR Ca2+-ATPase inhibitor cyclopiazonic acid (CPA) were compared to those obtained in the absence of the drug. We found that inhibition of the SR Ca2+-ATPase during caffeine-induced Ca2+ release causes an increase in the peak Ca2+ concentration in comparison to the control transients. Increasing CPA concentrations prolonged the time-to-peak in a dose-dependent manner, following a Hill curve with a half-maximal value of 6.5 +/- 3 microM CPA and a Hill slope of 1.1 +/- 0.2, saturating at 100 microM. The effects of CPA could be simulated by an extended three-compartment model representing the SR, the myofilament space and the external bathing solution. In terms of this model, the SR Ca2+-ATPase influences the Ca2+ gradient across the SR membrane in particular during the early stages of the Ca2+ transient, whereas the subsequent relaxation is governed by diffusional loss of Ca2+ into the bathing solution.
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PMID:The contribution of the sarcoplasmic reticulum Ca2+-transport ATPase to caffeine-induced Ca2+ transients of murine skinned skeletal muscle fibres. 876 74

We have presented an assay for measuring the rate of sarcoplasmic reticulum (SR) Ca2+ uptake and Ca2+ release in skeletal muscle homogenates using the fluorescent Ca2+ probe Fura-2. Using this assay, we investigated the effects of an elevated temperature (40 degrees C) and lowered pH (6.8), two factors proposed to be involved in skeletal muscle fatigue, on SR Ca2+ uptake. The EDL muscle was found to have a higher rate of Ca2+ uptake than the soleus (34%). Exposure of the muscles to a raised temperature, but not a reduced pH, resulted in a reduction in the rate of Ca2+ uptake in both the EDL and soleus homogenates. This uptake process was blocked by cyclopiazonic acid (CPA) a specific inhibitor of the major transport protein of the sarcoplasmic reticulum, the Ca(2+)-ATPase. Calcium release was induced using AgNO3 after loading of the vesicles during the uptake process. It was found that AgNO3 was only effective in producing Ca2+ release in the EDL muscles. The soleus muscles did not release Ca2+ under varying [Mg2+] or with Hg2+ substitution for Ag+, suggesting that fast- and slow-twitch muscle fibres require different conditions for maximum Ca2+ release, or that different isoforms of the Ca2+ release channels are present in the different fibres.
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PMID:A method for measuring sarcoplasmic reticulum calcium uptake in the skeletal muscle using Fura-2. 886 73

: To elucidate the pathogenesis of chronic compartment syndrome, we examined pathological changes in the soleus (red) and extensor digitorum longus (EDL; white) muscles in Japanese white rabbits after repeated compression with a pneumatic tourniquet. Repeated tourniquet compression via cuff inflation was carried out on the rabbits, calves daily, for 2 h, then stopped for 30 min, and then applied for another 2 h. The contralateral hindlimb, which was not compressed, served as a control. Animals were allocated to 15 groups, with pressures of 40, 80, and 120 mmHg for periods of 1 day, 3 days, 1 week, 2 weeks, and 4 weeks. Skeletal muscle specimens in each group were studied by histopathological and histochemical (ATPase) methods. After compression for 1 day, regardless of pressure, and compression for 3 days in the 40-mmHg pressure group, edematous changes in regions with mild inflammation and increases in fiber diameter were observed in the muscles. After compression for 3 days in the 80- and 120-mmHg pressure groups, and after 1, 2, or 4 weeks in the 40-mmHg pressure group, a few necrotic fibers and scattered fibers with some mononuclear cell infiltrates indicative of early-stage necrosis were detected. In the groups with 80 or 120 mmHg pressure for 1, 2, or 4 weeks, muscle fibers exhibited marked degenerative changes, which were more pronounced in the 120-mmHg group than in the 80-mmHg group. The pathological changes were more pronounced in the soleus than in the EDL muscles, indicating that these two muscles differed in sensitivity to repeated compression. Additionally, average muscle wet weight and average fiber diameter for both types of muscle were increased in the 1-day and 3-day compression groups and decreased in the 1-week, 2-week, and 4-week compression groups. These findings clearly differ from those of previously reported single-compression experiments. Our findings indicate that repeated compression may cause serious muscle degeneration, particularly in red muscles.
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PMID:Pathology study of rabbit calf muscles after repeated compression. 966 64

The aim of this study was to investigate if the Na(+)-channel activating alkaloid veratrine is able to change the oxidative and m-ATPase activities of a fast-twitch glycolytic muscle (EDL, extensor digitorum longus) and slow-twitch oxidative muscle (SOL, soleus) in mice. Oxidative fibers and glycolytic fibers were more sensitive to veratrine than oxidative-glycolytic fibers 15, 30 and 60 min after the i.m. injection of veratrine (10 ng/kg) with both showing an increase in their metabolic activity in both muscles. In EDL, the m-ATPase reaction revealed a significant (p < 0.001) decrease (50%) in the number of type IIB fibers after 30 min while the number of type I fibers increased by 550%. Type I fibers decreased from 34% in control SOL to 17% (50% decrease) in veratrinized muscles, with a 10% decrease in type IIA fibers within 15 min. A third type of fiber appeared in SOL veratrinized muscle, which accounted for 28% of the fibers. Our work gives evidence that the changes in the percentage of the fiber types induced by veratrine may be the result, at least partially, from a direct effect of veratrine on muscle fibers and else from an interaction with the muscle type influencing distinctively the response of a same fiber type. Based on the results obtained in the present study the alterations in EDL may be related to the higher number of Na(+) channels present in this muscle whereas those in SOL may involve an action of veratrine on mitochondria. Although it is unlikely that the shift of enzymes activities induced by veratrine involves genotypic expression changes an alternative explanation for the findings cannot be substantiated by the present experimental approach.
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PMID:Histochemical differences in the responses of predominantly fast-twitch glycolytic muscle and slow-twitch oxidative muscle to veratrine. 1236 17


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