Myosin heavy chain isoforms in histochemically defined fiber types of rat muscle

1989 ◽  
Vol 92 (6) ◽  
pp. 453-457 ◽  
Author(s):  
A. Termin ◽  
R. S. Staron ◽  
D. Pette
Keyword(s):  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Myosin Heavy Chain Isoforms ◽  
Fiber Types ◽  
Rat Muscle

Muscle Fiber Types Expressing Different Myosin Heavy Chain Isoforms. Their Functional Properties and Adaptive Capacity

1990 ◽  
pp. 329-342 ◽  
Author(s):  
S. Schiaffino ◽  
L. Gorza ◽  
S. Ausoni ◽  
R. Bottinelli ◽  
C. Reggiani ◽  
...  
Keyword(s):  
Myosin Heavy Chain ◽  
Adaptive Capacity ◽  
Functional Properties ◽  
Muscle Fiber ◽  
Heavy Chain ◽  
Myosin Heavy Chain Isoforms ◽  
Muscle Fiber Types ◽  
Fiber Types

scholarly journals Stability of myosin heavy chain isoforms in selectively denervated adult rat muscle spindles

1997 ◽  
Vol 249 (1) ◽  
pp. 32-43 ◽  
Author(s):  
Jun Wang ◽  
David L. McWhorter ◽  
Jon M. Walro
Keyword(s):  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Muscle Spindles ◽  
Myosin Heavy Chain Isoforms ◽  
Adult Rat ◽  
Rat Muscle

Diversity in expression of myosin heavy chain isoforms and M-band proteins in rat muscle spindles

1989 ◽  
Vol 92 (3) ◽  
pp. 185-194 ◽  
Author(s):  
F. Pedrosa ◽  
G. S. Butler-Browne ◽  
G. K. Dhoot ◽  
D. A. Fischman ◽  
L. -E. Thornell
Keyword(s):  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Muscle Spindles ◽  
Myosin Heavy Chain Isoforms ◽  
Rat Muscle

Influence of neonatal motor denervation on expression of myosin heavy chain isoforms in rat muscle spindles

1990 ◽  
Vol 94 (3) ◽  
Author(s):  
T. Soukup ◽  
F. Pedrosa ◽  
L.-E. Thornell
Keyword(s):  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Muscle Spindles ◽  
Myosin Heavy Chain Isoforms ◽  
Rat Muscle

Expression of myosin heavy chain isoforms in developing rat muscle spindles

1990 ◽  
Vol 94 (3) ◽  
Author(s):  
F. Pedrosa ◽  
L.-E. Thornell
Keyword(s):  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Muscle Spindles ◽  
Myosin Heavy Chain Isoforms ◽  
Rat Muscle ◽  
Developing Rat

Cellular adaptations of skeletal muscles to cyclosporine

1998 ◽  
Vol 84 (6) ◽  
pp. 1967-1975 ◽  
Author(s):  
Manmohan S. Biring ◽  
Mario Fournier ◽  
David J. Ross ◽  
Michael I. Lewis
Keyword(s):  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Cellular Response ◽  
Myosin Heavy Chain Isoforms ◽  
Male Rats ◽  
Type I ◽  
Solid Organ ◽  
Fiber Types ◽  
Cross Sectional ◽  
Final Body Weight

The aim of this study was to evaluate the cellular response of the diaphragm, extensor digitorum longus (EDL), and soleus (Sol) muscles to clinically relevant doses of cyclosporine administered to male rats over 4 wk. Control rats were provided with vehicle only. Muscle fiber types, cross-sectional areas, indexes of capillarity, and succinate dehydrogenase (SDH) activity were determined by quantitative histochemistry. Myosin heavy chain isoforms were identified by SDS-PAGE, and their proportions were measured by scanning densitometry. Serum cyclosporine level, 20–24 h after the last dose of cyclosporine, was 145 ± 81 ng/ml. Final body weight and muscle mass were similar between the cyclosporine and control groups. In the diaphragm, EDL, and Sol, no differences were observed between the groups with regard to fiber type proportions, fiber cross-sectional areas, and proportions of myosin heavy chain isoforms. In the EDL, reductions, both in SDH activity in type I, IIx, and IIb fibers (−26 to −37%) and in indexes of capillarity (−18 to −37%), were noted. In the Sol, SDH activity and capillarity were similar between the groups. In the diaphragm of cyclosporine-treated rats, there was significant reduction in the number of capillaries around individual fibers (−5%), whereas levels of SDH activity tended to be lower. This suggests that activation history may in part determine muscle-specific responses to cyclosporine. We speculate that reduced oxidative activity and capillarity of some limb muscles contribute to reduced exercise capacity and the “deconditioned state” observed in patients receiving cyclosporine after successful solid-organ transplantation.

Enhancement of hybrid-fiber types in rat soleus muscle after clenbuterol administration during hindlimb unloading

2004 ◽  
Vol 82 (5) ◽  
pp. 311-318 ◽  
Author(s):  
F Picquet ◽  
L De-Doncker ◽  
M Falempin
Keyword(s):  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Fiber Type ◽  
Myosin Heavy Chain Isoforms ◽  
Hindlimb Unloading ◽  
Fiber Types ◽  
Myosin Isoforms ◽  
Fast Myosin ◽  
Contractile Parameters ◽  
Fast Myosin Heavy Chain

Our objective was to determine the effects of a clenbuterol (CB) treatment orally administered (2 mg per kg) to rats submitted to 14 days of hindlimb unloading (HU). The morphological and the contractile properties as well as the myosin heavy chain isoforms contained in each fiber type were determined in whole soleus muscles. As classically described after HU, a decrease in muscle wet weight and in body mass associated with a loss of muscular force, an evolution of the contractile parameters towards those of a fast muscle type, and the emergence of fast myosin heavy chain isoforms were observed. The CB treatment in the HU rats helped reduce the decrease in 1) muscle and body weights, 2) force and 3) the proportion of slow fibers, without preventing the emergence of fast myosin isoforms. Clenbuterol induced a complex remodelling of the muscle typing promoting the combination of both slow and fast myosin isoforms within one fiber. To conclude, our data demonstrate that CB administration partially counteracts the effects produced by HU, and they allow us to anticipate advances in the treatment of muscular atrophy.Key words: β2 agonist, clenbuterol, soleus, contractile parameters, myosin, immunohistochemistry, simulated microgravity, countermeasure.

scholarly journals Myosin heavy-chain isoforms in the flight and leg muscles of hummingbirds and zebra finches

2014 ◽  
Vol 306 (11) ◽  
pp. R845-R851 ◽  
Author(s):  
Brandy P. Velten ◽  
Kenneth C. Welch
Keyword(s):  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Fiber Type ◽  
Myosin Heavy Chain Isoforms ◽  
Contractile Properties ◽  
Morphological Properties ◽  
Fiber Types ◽  
Zebra Finches ◽  
Leg Muscles ◽  
Flight Muscles

Myosin heavy chain (MHC) isoform complement is intimately related to a muscle's contractile properties, yet relatively little is known about avian MHC isoforms or how they may vary with fiber type and/or the contractile properties of a muscle. The rapid shortening of muscles necessary to power flight at the high wingbeat frequencies of ruby-throated hummingbirds and zebra finches (25–60 Hz), along with the varied morphology and use of the hummingbird hindlimb, provides a unique opportunity to understand how contractile and morphological properties of avian muscle may be reflected in MHC expression. Isoforms of the hummingbird and zebra finch flight and hindlimb muscles were electrophoretically separated and compared with those of other avian species representing different contractile properties and fiber types. The flight muscles of the study species operate at drastically different contraction rates and are composed of different histochemically defined fiber types, yet each exhibited the same, single MHC isoform corresponding to the chicken adult fast isoform. Thus, despite quantitative differences in the contractile demands of flight muscles across species, this isoform appears necessary for meeting the performance demands of avian powered flight. Variation in flight muscle contractile performance across species may be due to differences in the structural composition of this conserved isoform and/or variation within other mechanically linked proteins. The leg muscles were more varied in their MHC isoform composition across both muscles and species. The disparity in hindlimb MHC expression between hummingbirds and the other species highlights previously observed differences in fiber type composition and thrust production during take-off.

Myosin Heavy Chain Isoforms in Single Fibers of Transforming Rat Muscle

1990 ◽  
pp. 463-472 ◽  
Author(s):  
A. Termin ◽  
R.S. Staron ◽  
D. Pette
Keyword(s):  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Myosin Heavy Chain Isoforms ◽  
Single Fibers ◽  
Rat Muscle

Expression of myosin heavy chain isoforms and myogenesis of intrafusal fibres in rat muscle spindles

1995 ◽  
Vol 30 (5) ◽  
pp. 390-407 ◽  
Author(s):  
Tomáš Soukup ◽  
Fatima Pedrosa-Domellöf ◽  
Lars-Eric Thornell
Keyword(s):  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Muscle Spindles ◽  
Myosin Heavy Chain Isoforms ◽  
Rat Muscle ◽  
Intrafusal Fibres
Sign in / Sign up

Export Citation Format

Share Document