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3 edition of A comparison of rat myosin from fast and slow skeletal muscle and the effect of disuse found in the catalog.

A comparison of rat myosin from fast and slow skeletal muscle and the effect of disuse

Brian R Unsworth

A comparison of rat myosin from fast and slow skeletal muscle and the effect of disuse

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  • 22 Currently reading

Published by National Aeronautics and Space Administration in [Washington, D.C .
Written in English

    Subjects:
  • Biochemistry,
  • Enzymes

  • Edition Notes

    StatementBrian R. Unsworth, Frank A. Witzmann, and Robert H. Fitts
    SeriesPerformance guide -- PG-30, NASA-CR -- 174339, NASA contractor report -- 174339
    ContributionsWitzmann, F. A., Fitts, R. H., United States. National Aeronautics and Space Administration, Marquette University. Dept. of Biology
    The Physical Object
    FormatMicroform
    Pagination1 v.
    ID Numbers
    Open LibraryOL14929288M

      (B and C) Electron-dense tethers, similar to those observed in skeletal muscle (see Figures 1 and 6), are also observed in cardiac muscle between mitochondria and SR (small arrows). Also similar to skeletal muscle, mitochondria are positioned on the SR site opposite to that bearing RyR-feet (arrowheads). Bars, (A–C) μm.   A single myosin heavy chain isoform is typically expressed within an adult skeletal muscle fiber. Fibers classified as Type I, IIa, IIx, and IIb express myosin heavy chain isoform I (or slow), IIa, IIx, and IIb, respectively. Type IIx fibers have been reported in peripheral muscles of humans and animals and in the diaphragm of by:   For example, fiber-type transitions from slow to fast twitch muscle have been implicated in situations of disuse atrophy, while exercise training results in fiber type transitions from fast to slow. The M-line and Z-disk are connected via titin and together constitute the framework of the by: 8.


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A comparison of rat myosin from fast and slow skeletal muscle and the effect of disuse by Brian R Unsworth Download PDF EPUB FB2

Add tags for "A comparison of rat myosin from fast and slow skeletal muscle and the effect of disuse". Be the first. Effects of unweighting and clenbuterol on myosin light and heavy chains in fast and slow muscle of rat Article (PDF Available) in AJP Cell Physiology (5):C.

The gastrocnemius of rat is composed of 76% fast and 24% slow myosins. These values change to 56% and 44% respectively, i.e. the accumulation of slow myosin A comparison of rat myosin from fast and slow skeletal muscle and the effect of disuse book %.

The total fast light chain decreases from 76% to 56%. From the fast light chains, the LC-3 shows a 45% decrease, the LC-2 and LC% and 18% by: 1. Introduction. The biology and pathology of skeletal muscle in laboratory rats has undergone greater study in recent years. This abundant and easily obtainable tissue allows for convenient sampling during toxicologic studies, and new molecular techniques have enabled better understanding of processes such as injury and regeneration.

A histochemical study, using myosin-adenosine triphosphatase activity at pHwas conducted in soleus and plantaris muscles of adult rats, after bilateral crushing of the sciatic nerve at the.

Skeletal muscle atrophy attributable to muscular inactivity has significant adverse functional consequences.

While the initiating physiological event leading to atrophy seems to be the loss of muscle tension and a good deal of the physiology of muscle atrophy has been characterized, little is known about the triggers or the molecular signaling events underlying this by: Andruchov O, Andruchova O, Wang YS, Galler S.

Kinetic properties of myosin heavy chain isoforms in mouse skeletal muscle, comparison with rat, rabbit, and human and correlation with amino acid sequence. Amer J Physiol Cell Physiol ,C–C Google ScholarCited by: 9.

Bär A, Pette D () Three fast myosin heavy chains in adult rat skeletal muscle. FEBS Lett – CrossRef PubMed Google Scholar Bär A, Simoneau J-A, Pette D () Altered expression of myosin light chain isoforms in chronically stimulated fast-twitch muscle of Cited A comparison of rat myosin from fast and slow skeletal muscle and the effect of disuse book A Comparison of Rat Myosin from Fast and Slow Skeletal Muscle and the Effect of Disuse, B.

Unsworth, Frank Arthur Witzmann, and Robert H. Fitts Link A Comparison of Reconstructed Phase Spaces and Cepstral Coefficients for Multi-Band Phoneme Classification, Kevin M. Indrebo, Richard James Povinelli, and Michael T. Johnson. A comparison of rat myosin from fast and slow skeletal muscle and the effect of disuse book observed ∼20% increase in fast type II fibres post‐flight in some crew members demonstrates that in addition to the downregulation of slow muscle protein that fast muscle myosin isoform was upregulated and that the extent of upregulation was directly related to the degree of fibre atrophy.

Sarcopenia. Irwin Rosenberg proposed the term ‘sarcopenia’ in to describe the aging-related decrease of skeletal muscle mass, based on the Greek terms ‘sarx’ for flesh and ‘penia’ for poverty (Rosenberg, ).Later, Evans revised this definition of sarcopenia to include an aging-related loss in skeletal muscle strength (Evans, ; Evans and Campbell, ); a Cited by: It is well known that resistance training (RT) is the most effective stimulus to promote muscle hypertrophy.

Since the early s, many studies have investigated at a cellular and molecular level the effect of RT on skeletal muscle [1,2,3,4] gh the underlying precise mechanism is still elusive [], the efficacy of RT in inducing muscle fiber hypertrophy, especially Cited by: The mass spectrometric analysis of skeletal muscle proteins has used both peptide-centric and protein-focused approaches.

The term ‘top-down proteomics’ is often used in relation to studying purified proteoforms and their post-translational modifications. Two-dimensional gel electrophoresis, in combination with peptide generation for the identification and Cited by: 2.

Primary slow fibers change from expression of embryonic to slow myosin heavy chain; 6 7 secondary slow fibers produce embryonic, neonatal, fast, and slow myosins. 8 9 There are several other proteins, such as the troponins and myosin light chains, which have fast and slow isoforms.

10 DNA sequences with E-box and MEF2-like motifs upstream from. Statin toxicity in human muscle biopsies is associated with atrogin-1 expression. Since the muscle-specific ubiquitin protein ligase atrogin-1 is commonly induced in diverse states of muscle wasting (20, 21), we examined its expression in statin-treated patients with symptoms of muscle pain or measured by real-time PCR atrogin-1 levels in 19 human Cited by: People have fast-twitch muscle fibers and slow-twitch muscle fibers.

The size principle in exercise physiology states that motor units are recruited from smallest to largest; in other words, slow-twitch are recruited before fast-twitch muscle fibers. As intensity increases, so does the recruitment of large fast-twitch muscle fibers.

Muscle (from Latin musculus, diminutive of mus "mouse" [1]) is a contractile tissue of animals and is derived from the mesodermal layer of embryonic germ cells. Muscle cells contain contractile filaments that move past each other and change the size of the cell.

They are classified as skeletal, cardiac, or smooth muscles. Their function is to produce force and cause motion. Inflammation (from Latin: inflammatio) is part of the complex biological response of body tissues to harmful stimuli, such as pathogens, damaged cells, or irritants, and is a protective response involving immune cells, blood vessels, and molecular function of inflammation is to eliminate the initial cause of cell injury, clear out necrotic cells and tissues damaged from the.

skeletal muscle fibers are fantastic molecular and metabolic machines that have developed through evolution a large scope of contractile properties, ranging from slow contracting, low-powered fibers designed for endurance, to fast contracting, high-powered fibers designed for short bursts of high-intensity work.

Such a wide range of functional specialization has emerged. As a result of the loss of motoneurons and of muscle cell apoptosis, the number of muscle fibres considerably decreases with aging (Lexell et al.

).Fibre size also decreases with age (atrophy) and this is probably due both to a decrease satellite cell proliferation due to an age‐related decrease in the level of growth factors such as IGFs (Barton‐Davis et al.

), as Cited by:   Muscle disuse atrophy: characterisation. Skeletal muscle atrophy is characterised by a suite of structural, biochemical, physiological and functional changes, largely prevalent in the muscle tissue itself but also evident at neuromuscular junctions (Fahim, ) and in the microvasculature of the muscle (Oki et al., ).On a gross level, there is a reduction in Cited by: The net result is that between 25 and 46% of the muscle mass can be lost in antigravity muscles of the lower extremity such as the soleus (Sol; a calf muscle) and vastus intermedius (VI; a deep layered quadriceps muscle), which are composed mostly of the slow Type I myofibers containing the slow myosin heavy chain (MHC) protein.

MHC is the most. The slow contracting soleus muscle is rich in myofibers expressing the slow type I myosin heavy chain isoform, whereas the fast contracting plantaris muscle is devoid of slow type I myofibers [].

The most informative methods to delineate muscle fiber types are based on specific myosin profiles, specially the myosin heavy chain (MHC) isoform Cited by: TGF-β is a potent stimulator of fibrosis in the kidneys, liver, heart, and lungs [] and is closely associated with skeletal muscle fibrosis as well where it plays a significant role in both the initiation of fibrosis and the induction of myofibroblastic differentiation of myogenic cells in injured skeletal by:   Incubation of muscle fibres for 30 min in low-salt buffer had no effect on motility speed in the slow (a) and fast (b) myosin preparations.

In contrast, incubation with glucose for 30 min caused a progressive decrease in motility speed both in the slow (a) and fast (b) myosin preparations (pCited by: Changes in muscle function can be both a cause (M1 macrophage polarization could follow reduced endurance from slow-to-fast muscle fiber transformation, leading to lactate accumulation) and a consequence (reduced contractile potential) of the inflammatory response Cited by: 2.

Disuse. Disuse of skeletal muscle from a low level of physical activity is also a factor that most likely contributes to the observed muscle alterations in COPD and CHF.

Hampered by their disease, these patients perform less physical activity, which may have a detraining effect on their peripheral by: Skeletal muscle activity, which can involve either single muscles or muscle groups (for review, see Wilmore and Costill, ), includes fine intricate movements, heavy lifting, long-duration traveling, or very fast (rapid-burst) movements.

As in mammalian muscle cell culture, lovastatin led to clear dose-dependent muscle phenotypes, demonstrated by longitudinal muscle fiber staining with an antibody to myosin heavy chain (Figure 5).

Muscle damage at low lovastatin concentration (– μM) was evidenced by bowing, gap formation, and fiber disruption (class 1 changes).Cited by: Glucocorticoids and muscle protein synthesis Testosterone and muscular mass and strength Thyroid hormone and phenotypic muscle effects Insulin and muscle glucose uptake 6.

Exercise, structural maintenance of skeletal muscle, and aging 7. Skeletal muscle cell changes associated with aging The sarcomeric M-region anchors thick filaments and withstands the mechanical stress of contractions by deformation, thus enabling distribution of physiological forces along the length of thick filaments.

While the role of the M-region in supporting myofibrillar structure and contractility is well established, its role in mediating additional cellular processes has only recently started Cited by: The role of neural and mechanical influences in maintaining normal fast and slow muscle properties.

Cells Tissues Organs ; Cells Tissues Organs ; 40 Borina E, Pellegrino MA, D'Antona G, Bottinelli R. Myosin and actin content of human skeletal muscle fibers following 35 days bed by:   Evaluation of the contractile protein composition of the skeletal muscle provides further evidence supporting that a fast to slow type fiber conversion may occur with endurance training ().

Subpopulations of type II fibers are also modified with endurance training, as evidenced by the transformation of type IIb muscle fiber into type IIa.

Skeletal muscle is the most abundant tissue in the human body and also one of the most adaptable. Vigorous training with weights can double or triple a muscle's size, whereas disuse, as in space travel, can shrink it by 20 percent in two weeks. The fibers are called slow and fast for good reason: the maximum contraction velocity of a single.

EDITORS' NOTE: This is the second of a four part series on the Vertebral Subluxation Complex and its relevance to chiropractic theory and basic chiropractic research, as well as to the practice of chiropractic.

The first part of this series appear ed in CRJ Volume 1, No. It introduced an 8 part model and went on to discuss the kinesiopathological component of the vertebral.

Food withdrawal: animal models. Food withdrawal is a strong trigger of the switch toward oxidative metabolism in skeletal muscle ().This effect occurs through rapid cellular signaling, activating a shift toward fatty acid oxidation via the peroxisome proliferator–activated receptor (PPAR)-δ ().Upon immediate energy deprivation through nocturnal food withdrawal in Cited by: Effect of sarcoplasmic reticulum Ca2+ content on action potential-induced Ca2+ release in rat skeletal muscle fibres Academic Article Effects of 2,3-butanedione monoxime on the contractile activation properties of fast- and slow-twitch rat muscle fibres.

Academic Article. fasting- and exercise-induced PDH regulation in skeletal muscle does not require PGC-1α. In general the relationships between PDH-E1α phosphorylation and PDHa activity were not that obvious as in Study 1, 2 and 3.

These KO and TG mice were surly a good model to elucidate if PGC-1α had a significant role of regulating the PDH regulation. on the Myosin Heavy Chains of the Rat Soleus Muscle School of Biological Sciences California State University C.R., and V.J.

Caiozzo. A comparison of the effect of external loading upon maximal power output in stair climbing and running up a ramp. of blood reflow in slow and fast skeletal muscle following tourniquet induced.

Skeletal muscle plays a key role in the control of blood glucose levels, and the metabolic changes and related signaling pathways in skeletal muscle induced by Cited by:. Myosin content of single muscle fibers following short-term disuse and active recovery in pdf and old healthy men.

Exp. Gerontol. 87, –, Jordan MJ, Aagaard P, Herzog W. Asymmetry and thigh muscle co-activity in fatigued ACL reconstructed Elite Skiers.According to the scarce data connected with the download pdf of skeletal muscles cells to gravity disuse in the literature, one of the first events to occur, after two days of antiorthostatic disuse of the hindlimbs of mice, is the accumulation of calcium ions in the soleus muscle [, ].

Above, we described that the maximal calcium ion Cited by:   We speculate that slow fiber myosin ebook may have initially increased ebook to fast heavy chain myosin production, however with time the slow fiber content may have receded to baseline once the muscle was being used while the fast fiber content increased with over use (resistance training) due to increased tension.