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2 edition of Myofibrillar ATPase activity in rat heart and skeletal muscle following exercise found in the catalog.

Myofibrillar ATPase activity in rat heart and skeletal muscle following exercise

William Frederick Schaffer

Myofibrillar ATPase activity in rat heart and skeletal muscle following exercise

by William Frederick Schaffer

  • 141 Want to read
  • 35 Currently reading

Published .
Written in English

    Subjects:
  • Exercise -- Physiological aspects -- Research.,
  • Rats as laboratory animals.

  • Edition Notes

    Statementby William Frederick Schaffer.
    The Physical Object
    Paginationvii, 54 leaves, bound :
    Number of Pages54
    ID Numbers
    Open LibraryOL16568833M

      Myofibrillar myopathy is a muscular disease and part of a group of disorders called muscular dystrophies. The condition is characterized by improper functioning of muscle . *recruit large muscles or muscle groups during an activity *increase the cross-sectional area of muscles involved in the desired activity *preload a muscle just before a concentric action to enhance force production during the subsequent muscle action *use preloading during training to develop strength early in the range of motion.

    Effects of a long-term, high intensity training program upon histochemically assessed myofibrillar actomyosin ATPase, myosin composition, peptide pattern of sarcoplasmic reticulum (SR), and parvalbumin content were analysed in muscles from the same rats which were used in a previous study (Green et al. ). Following 15 weeks of extreme training, an increase in type I and type IIA fibres . Increase in myofibrillar ATPase intermediate human skeletal muscle fibers in response to endurance training Article (PDF Available) in Muscle & Nerve 6(8) October with 42 Reads.

    The size, succinate dehydrogenase (SDH) and alpha-glycerolphosphate dehydrogenase (GPD) activities, and alkaline myofibrillar adenosinetriphosphatase (ATPase) staining properties were determined from quantitative histochemical analyses of single fibers from five hindlimb muscles of six male rats exposed to a 7-day National Aeronautics and Space Administration spaceflight mission (SL-3). Skeletal muscle fibers characterized by their expression of the Type II MYOSIN HEAVY CHAIN isoforms which have high ATPase activity and effect | Explore the latest full-text research PDFs.


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Myofibrillar ATPase activity in rat heart and skeletal muscle following exercise by William Frederick Schaffer Download PDF EPUB FB2

Bárány M. ATPase activity of myosin correlated with speed of muscle shortening. J Gen Physiol. Jul; 50 (6 Suppl)– [PMC free article] []Bottinelli R, Betto R, Schiaffino S, Reggiani C. Unloaded shortening velocity and myosin heavy chain and alkali light chain isoform composition in rat skeletal muscle by: recent study on single muscle fibres from the rat at C (Bottinelli et al.

), myofibrillar ATPase activity has been found to be mainly dependent on the myosin heavy chain (MHC)isoform composition, whereasthe influence of myosin light chain (MLC) isoform composition was negligible. In this study we therefore focus on the Cited by:   Kurebayashi N, Ogawa Y.

Discrimination of Ca(2+)-ATPase activity of the sarcoplasmic reticulum from actomyosin-type ATPase activity of myofibrils in skinned mammalian skeletal muscle fibres: distinct effects of cyclopiazonic acid on the two ATPase activities.

J Muscle Res Cell Motil. Aug; 12 (4)– Levy RM, Umazume Y, Kushmerick MJ. correlated with the contractile velocity of whole skeletal muscle (Barany, ) and is the basis for the histochemical classification of individual muscle fibers as either fast or slow, as proposed by Brooke and Kaiser ().

The difference in myofibrillar ATPase (mATPase) activity between fast and slow muscles of mammals and. The mechanism behind the increased SR ATPase activity in CHF is not known.

It is known that shifts in SR ATPase activity as well as myofibrillar ATPase activity can be induced by thyroid hormone. Thus, it is a possibility that the changes are related to thyroid hormone receptor activation in skeletal muscle of CHF by: 8.

Myofibrillar ATPase activity, isometric tension (Po) and unloaded shortening velocity (Vo) were determined in single skinned fibres isolated from rat hindlimb muscles during maximal calcium activation at 12 degrees C.

In each fibre, myosin heavy chain (MHC) isoforms were identified using electrophoresis and immunocytochemistry. Myofibrillar ATP consumption and isometric tension (P0) were determined in chemically skinned skeletal muscle fibres from human rectus abdominis and vastus lateralis muscle.

Fibres were classified in four groups (I, IIA, IIB, IIA/B or mixed) based on myosin heavy chain composition. With regard to the skeletal muscles exhausted group, the myofibril ATPase activity were not different than control under the maximal activating conditions (e.g.

5 mM Mg-ATP and 10/xM Ca). This finding is consistent with a previous report on myofibril ATPase activity of skeletal muscle isolated from rats swum to exhaustion (Fitts et al., ). The purpose of this study was to examine the Ca2+-Mg2+ myofibrillar ATPase and protein composition of cardiac and skeletal muscle following strenuous activity to voluntary exhaustion.

Sprague-Dawley rats ( g) were assigned to a control and exercised group, with the run group completing 25 mmin−1 and 8% grade for 1 hour. Following activity, the myocardial Ca2+−Mg2+ myofibrillar ATPase. Myofibrillar ATPase: Identifying Fast and Slow Fibers The histochemical assay for myofibrillar ATPase activity is used to distinguish between fast- and slow-contracting muscle fibers.

Recall that the during the cross-bridge cycle, the myosin molecule itself binds and hydrolyzes ATP during force generation. 9 Drexler H, Reide U, Just H. Alterations of skeletal muscle in chronic heart failure.

Circulation. ; Crossref Medline Google Scholar; 10 Massie BM, Simonini A, Sahgal P, Wells L, Dudley GA. Relationship of systemic and local muscle exercise capacity to skeletal muscle characteristics in patients with congestive heart failure.

Changes in myofibrillar proteins occur in relation to acclimation temperature in skeletal muscle (see Guderley and Blier, ; Johnston et al., ). Johnston et al. () demonstrated that goldfish skeletal myofibrillar ATPase activity is fold higher in fish acclimated to 1°C than to 26°C.

Kentish JC, Stienen GJ. Differential effects of length on maximal force production in myofibrillar ATPase activity in rat skinned cardiac muscle. J Physiol. ; – [PMC free article] Kentish JC, ter Keurs HEDJ, Ricciardi L, Bucx JJJ, Noble MIM.

The effect of high-intensity exercise on the respiratory capacity of skeletal muscle was studied in horses which ran five m bouts on a track with 2 min of rest between exercise bouts, or once. In permeabilized single fibers of fast (psoas) and slow (soleus) muscle from the rabbit, the effect of pH on isometric myofibrillar ATPase activity and force was studied at 15 degrees C, in the pH range – ATPase activity was measured photometrically by enzymatic coupling of the regeneration of ATP to the oxidation of NADH, present in the bathing solution.

Myofibrillar ATPase activity during isometric contraction and isomyosin composition in rat single skinned muscle fibres. J Physiol. Dec 15; (Pt 3)– [PMC free article] Burchfield DM, Rall JA. Temperature dependence of the crossbridge cycle during unloaded shortening and maximum isometric tetanus in frog skeletal muscle.

Myofibrillar myopathy (MFM) primarily affects skeletal muscles, which are muscles that the body uses for movement. In some cases, the heart (cardiac) muscle is also affected.

The signs and symptoms of MFM vary among affected individuals, typically depending on the exact genetic cause of. The return to normal activity after 6 weeks without endurance training, provide evidence that the adaptations of the myofibril ATPase are not main- tained into adulthood.

Moreover, the degree of Table 3. Ca2+ uptake activity in the rat fast-twitch skeletal muscle as a function of growth and endurance training.

chronic heart failure (CHF) is associated with limited exercise capacity, as is reflected by a decrease in the maximum rate of oxygen consumption (V̇ o 2 max) (41, 46).Previous studies have shown abnormalities of skeletal muscle, including atrophy, impaired function, changes in fiber-type composition, and altered metabolism (10, 31, 33, 36, 40).These abnormalities could contribute to the.

Background— Patients with chronic heart failure (HF) frequently experience skeletal muscle weakness that limits physical function. The mechanisms underlying muscle weakness, however, have not been clearly defined.

Methods and Results— This study examined the hypothesis that HF promotes a loss of myosin protein from single skeletal muscle fibers, which in turn reduces contractile performance. With this background, we addressed the effect of aerobic exercise on the skeletal muscle of ethanol-treated rats.

The experimental design included study of muscle metabolism, capillary distribution, myofibrillar distribution and fibre morphometry.

2. Materials and .Myofibrillar myopathies are a group of conditions called myopathies that affect muscle function and cause weakness. They primarily affect skeletal muscles.

A weakening of the heart muscle (cardiomyopathy) is also common and may manifest as arrhythmia, conduction defects or congestive heart .The maximal isotonic shortening velocity was highly correlated with the myofibrillar ATPase activity, and both were relatively resistant to fatigue.

Furthermore, the Ca2+ sensitivity of the myofibrils was unaffected by exercise in both fast and slow muscle.