Response of slow and fast muscle to hypothyroidism: maximal shortening velocity and myosin isoforms

1992 ◽  
Vol 263 (1) ◽  
pp. C86-C94 ◽  
Author(s):  
V. J. Caiozzo ◽  
R. E. Herrick ◽  
K. M. Baldwin
Keyword(s):  
Skeletal Muscles ◽  
Relative Content ◽  
Type I ◽  
Myosin Isoforms ◽  
Velocity Data ◽  
Sprague Dawley ◽  
Shortening Velocity ◽  
Sprague Dawley Rats ◽  
Force Velocity ◽  
Fast Twitch

This study examined both the shortening velocity and myosin isoform distribution of slow- (soleus) and fast-twitch (plantaris) skeletal muscles under hypothyroid conditions. Adult female Sprague-Dawley rats were randomly assigned to one of two groups: control (n = 7) or hypothyroid (n = 7). In both muscles, the relative contents of native slow myosin (SM) and type I myosin heavy chain (MHC) increased in response to the hypothyroid treatment. The effects were such that the hypothyroid soleus muscle expressed only the native SM and type I MHC isoforms while repressing native intermediate myosin and type IIA MHC. In the plantaris, the relative content of native SM and type I MHC isoforms increased from 5 to 13% and from 4 to 10% of the total myosin pool, respectively. Maximal shortening velocity of the soleus and plantaris as measured by the slack test decreased by 32 and 19%, respectively, in response to hypothyroidism. In contrast, maximal shortening velocity as estimated by force-velocity data decreased only in the soleus (-19%). No significant change was observed for the plantaris.

Influence of hyperthyroidism on maximal shortening velocity and myosin isoform distribution in skeletal muscles

1991 ◽  
Vol 261 (2) ◽  
pp. C285-C295 ◽  
Author(s):  
V. J. Caiozzo ◽  
R. E. Herrick ◽  
K. M. Baldwin
Keyword(s):  
Skeletal Muscles ◽  
Significant Shift ◽  
Sprague Dawley ◽  
Fast Skeletal Muscle ◽  
Shortening Velocity ◽  
Control Value ◽  
Fast Myosin ◽  
Sprague Dawley Rats ◽  
Velocity Relationship ◽  
Force Velocity

The objectives of this study were 1) to examine the effects of hyperthyroidism on the myosin isoform distribution in slow and fast skeletal muscle, 2) to explore how these effects were manifested with respect to the force-velocity relationship and maximal shortening velocity, and 3) to contrast two different techniques of measuring maximal shortening velocity under normal and hyperthyroid conditions. Adult female Sprague-Dawley rats were randomly assigned to one of two groups: control (n = 8) or hyperthyroid (n = 8). Hyperthyroidism was induced by injections of 3,3',5-triiodo-L-thyronine every other day for 20 wk. We found that hyperthyroidism produced a significant shift in the myosin isoform distribution of the soleus but not the plantaris. The relative amount of the slow myosin isoform was reduced from a control value of 93 to 69% in the hyperthyroid condition. In contrast, both the intermediate and fast myosin-3 isoform pools were substantially increased (P less than 0.001) by approximately fourfold. Hyperthyroidism produced an increase in the maximal shortening velocity of the soleus as measured either by the slack test (+57%; P less than 0.001) or by extrapolation of force-velocity data (+33%; P less than 0.001). The hyperthyroid condition did not, however, affect the mechanical properties of the plantaris.

Influence of myosin isoforms on contractile properties of intact muscle fibers from Rana pipiens

2002 ◽  
Vol 282 (4) ◽  
pp. C835-C844 ◽  
Author(s):  
Gordon J. Lutz ◽  
Shashank R. Sirsi ◽  
Sarah A. Shapard-Palmer ◽  
Shannon N. Bremner ◽  
Richard L. Lieber
Keyword(s):  
Myosin Light Chain ◽  
Rana Pipiens ◽  
Isometric Tension ◽  
Myosin Isoforms ◽  
Shortening Velocity ◽  
Cross Sectional ◽  
Sds Page ◽  
Intact Muscle ◽  
Force Velocity ◽  
Fast Twitch

The myosin heavy chain (MHC) and myosin light chain (MLC) isoforms in skeletal muscle of Rana pipiens have been well characterized. We measured the force-velocity (F- V) properties of single intact fast-twitch fibers from R. pipiens that contained MHC types 1 or 2 (MHC1 or MHC2) or coexpressed MHC1 and MHC2 isoforms. Velocities were measured between two surface markers that spanned most of the fiber length. MHC and MLC isoform content was quantified after mechanics analysis by SDS-PAGE. Maximal shortening velocity ( V max) and velocity at half-maximal tension ( V P 50) increased with percentage of MHC1 (%MHC1). Maximal specific tension (Po/CSA, where Po is isometric tension and CSA is fiber cross-sectional area) and maximal mechanical power ( W max) also increased with %MHC1. MHC concentration was not significantly correlated with %MHC1, indicating that the influence of %MHC1 on Po/CSA and W max was due to intrinsic differences between MHC isoforms and not to concentration. The MLC3-to-MLC1 ratio was not significantly correlated with V max, V P 50, Po/CSA, or W max. These data demonstrate the powerful relationship between MHC isoforms and F- V properties of the two most common R. pipiensfiber types.

Force-velocity and force-power properties of single muscle fibers from elite master runners and sedentary men

1996 ◽  
Vol 271 (2) ◽  
pp. C676-C683 ◽  
Author(s):  
J. J. Widrick ◽  
S. W. Trappe ◽  
D. L. Costill ◽  
R. H. Fitts
Keyword(s):  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Power Output ◽  
Peak Power ◽  
Isometric Force ◽  
Peak Force ◽  
Peak Power Output ◽  
Type I ◽  
Shortening Velocity ◽  
Force Velocity

Gastrocnemius muscle fiber bundles were obtained by needle biopsy from five middle-aged sedentary men (SED group) and six age-matched endurance-trained master runners (RUN group). A single chemically permeabilized fiber segment was mounted between a force transducer and a position motor, subjected to a series of isotonic contractions at maximal Ca2+ activation (15 degrees C), and subsequently run on a 5% polyacrylamide gel to determine myosin heavy chain composition. The Hill equation was fit to the data obtained for each individual fiber (r2 > or = 0.98). For the SED group, fiber force-velocity parameters varied (P < 0.05) with fiber myosin heavy chain expression as follows: peak force, no differences: peak tension (force/fiber cross-sectional area), type IIx > type IIa > type I; maximal shortening velocity (Vmax, defined as y-intercept of force-velocity relationship), type IIx = type IIa > type I; a/Pzero (where a is a constant with dimensions of force and Pzero is peak isometric force), type IIx > type IIa > type I. Consequently, type IIx fibers produced twice as much peak power as type IIa fibers, whereas type IIa fibers produced about five times more peak power than type I fibers. RUN type I and IIa fibers were smaller in diameter and produced less peak force than SED type I and IIa fibers. The absolute peak power output of RUN type I and IIa fibers was 13 and 27% less, respectively, than peak power of similarly typed SED fibers. However, type I and IIa Vmax and a/Pzero were not different between the SED and RUN groups, and RUN type I and IIa power deficits disappeared after power was normalized for differences in fiber diameter. Thus the reduced absolute peak power output of the type I and IIa fibers from the master runners was a result of the smaller diameter of these fibers and a corresponding reduction in their peak isometric force production. This impairment in absolute peak power production at the single fiber level may be in part responsible for the reduced in vivo power output previously observed for endurance-trained athletes.

Subunit composition of rodent isomyosins and their distribution in hindlimb skeletal muscles

1987 ◽  
Vol 63 (5) ◽  
pp. 2101-2110 ◽  
Author(s):  
R. W. Tsika ◽  
R. E. Herrick ◽  
K. M. Baldwin
Keyword(s):  
Light Chain ◽  
Skeletal Muscles ◽  
Slow Light ◽  
Muscular Activity ◽  
Light Chains ◽  
Fiber Types ◽  
Myosin Isoforms ◽  
Adult Skeletal Muscle ◽  
Physiological Importance ◽  
Fast Twitch

Three adult skeletal muscle sarcomeric myosin heavy chain (MHC) genes have been identified in the rat, suggesting that the expressed native myosin isoforms can be differentiated, in part, on the basis of their MHC composition. This study was undertaken to ascertain whether the five major native isomyosins [3 fast (Fm1, Fm2, Fm3), 1 slow (Sm), and 1 intermediate (Im)], typically expressed in the spectrum of adult rat skeletal muscles comprising the hindlimb, could be further differentiated on the basis of their MHC profiles in addition to their light chain composition. Results show that in muscles comprised exclusively of fast-twitch glycolytic (FG) fibers and consisting of Fm1, Fm2, and Fm3, such as the tensor fasciae latae, only one MHC, designated as fast type IIb, could be resolved. In soleus muscle, comprised of both slow-twitch oxidative and fast-twitch oxidative-glycolytic fibers and expressing Sm and Im, two MHC bands were resolved and designated as slow/cardiac beta-MHC and fast type IIa MHC. In muscles expressing a mixture of all three fiber types and a full complement of isomyosins, as seen in the plantaris, the MHC could be resolved into three bands. Light chain profiles were characterized for each muscle type, as well as for the purified isomyosins. These data suggest that Im (IIa) consists of a mixture of fast and slow light chains, whereas Fm (IIb) and Sm (beta) isoforms consist solely of fast- and slow-type light chains, respectively. Polypeptide mapping of denatured myosin extracted from muscles expressing contrasting isoform phenotypes suggests differences in the MHC primary structure between slow, intermediate, and fast myosin isotypes. These findings demonstrate that 1) Fm, Im, and Sm isoforms are differentiated on the bases of both their heavy and light chain components and 2) each isomyosin is distributed in a characteristic fashion among rat hindlimb skeletal muscles. Furthermore, these data suggest that the ratio of isomyosins in a given muscle or muscle region is of physiological importance to the function of that muscle during muscular activity.

Maximum shortening velocity and myosin isoforms in single muscle fibers from young and old rats

1996 ◽  
Vol 270 (1) ◽  
pp. C352-C360 ◽  
Author(s):  
X. Li ◽  
L. Larsson
Keyword(s):  
Light Chain ◽  
Extensor Digitorum Longus ◽  
Maximum Velocity ◽  
Type I ◽  
Myosin Isoforms ◽  
Single Muscle ◽  
Shortening Velocity ◽  
Single Fibers ◽  
Age Related ◽  
Old Rats

Maximum velocity of unloaded shortening (Vo) and myosin heavy (MHC) and light chain (MLC) isoform compositions were determined in 185 single fibers from the extensor digitorum longus (EDL) and soleus muscles in 3- to 6- and 20- to 24-mo-old rats. In the soleus, fibers expressing the type I MHC isoform dominated in young and old animals. In the EDL, most fibers in the young animals expressed type IIb MHC or a combination of types IIx and IIb (type IIxb), whereas in the old animals type IIxb MHC fibers predominated. Vo was significantly (P < 0.01) lower (0.59 +/- 0.28 ml/s, n = 55) in soleus fibers from old than from young animals (1.12 +/- 0.46 ml/s, n = 48), despite the fact that all fibers expressed the type I MHC and slow MLC isoforms. In the EDL, Vo values in single fibers did not differ between young (2.18 +/- 0.58 ml/s, n = 43) and old animals (2.10 +/- 0.53 ml/s, n = 39). The mechanism underlying age-related slowing in soleus fibers is not known, but it has been suggested that there could be more than one beta/slow MHC isoform and that there is an age-related transition within these isoforms.

Aminophylline increases submaximum power but not intrinsic velocity of shortening of frog muscle

1992 ◽  
Vol 73 (1) ◽  
pp. 71-74 ◽  
Author(s):  
B. M. Block ◽  
S. R. Barry ◽  
J. A. Faulkner
Keyword(s):  
Skeletal Muscles ◽  
Isometric Force ◽  
Frog Muscle ◽  
Measured Parameter ◽  
Shortening Velocity ◽  
Force Development ◽  
Velocity Of Shortening ◽  
Force Velocity ◽  
Maximum Isometric Force ◽  
Frequency Of Stimulation

We hypothesized that methylxanthines, such as aminophylline, increase the power developed by submaximally activated frog skeletal muscles by increasing the force developed at any given velocity of shortening. Frog semitendinosus muscles were excised and tested at 20 degrees C in oxygenated control and aminophylline Ringer solutions. Force-velocity relationships were determined and power was calculated from muscles stimulated at frequencies of 80 and 300 Hz. The 300-Hz frequency of stimulation produced a maximum rate of force development. In 50 and 500 microM aminophylline, twitch force increased by 25 +/- 12 and 75 +/- 13%, respectively. Aminophylline did not affect maximum isometric force generation or the shortening velocity at any relative load. At 80-Hz stimulation and in the presence of 500 microM aminophylline, power increased by an average of 11% at 10 of 14 relative loads. At maximum frequencies of stimulation, aminophylline had no effect on any measured parameter. We conclude that aminophylline increases the power developed by submaximally activated frog muscles through an increase in the force generated particularly at the lower velocities of shortening.

scholarly journals Force-velocity-power and force-pCa relationships of human soleus fibers after 17 days of bed rest

1998 ◽  
Vol 85 (5) ◽  
pp. 1949-1956 ◽  
Author(s):  
J. J. Widrick ◽  
K. M. Norenberg ◽  
J. G. Romatowski ◽  
C. A. Blaser ◽  
M. Karhanek ◽  
...  
Keyword(s):  
Peak Power ◽  
Weight Bearing ◽  
Bed Rest ◽  
Force Transducer ◽  
Hindlimb Suspension ◽  
Peak Power Output ◽  
Type I ◽  
Shortening Velocity ◽  
Adult Men ◽  
Force Velocity

Soleus muscle fibers from the rat display a reduction in peak power and Ca2+ sensitivity after hindlimb suspension. To examine human responses to non-weight bearing, we obtained soleus biopsies from eight adult men before and immediately after 17 days of bed rest (BR). Single chemically skinned fibers were mounted between a force transducer and a servo-controlled position motor and activated with maximal (isotonic properties) and/or submaximal (Ca2+ sensitivity) levels of free Ca2+. Gel electrophoresis indicated that all pre- and post-BR fibers expressed type I myosin heavy chain. Post-BR fibers obtained from one subject displayed increases in peak power and Ca2+ sensitivity. In contrast, post-BR fibers obtained from the seven remaining subjects showed an average 11% reduction in peak power ( P < 0.05), with each individual displaying a 7–27% reduction in this variable. Post-BR fibers from these subjects were smaller in diameter and produced 21% less force at the shortening velocity associated with peak power. However, the shortening velocity at peak power output was elevated 13% in the post-BR fibers, which partially compensated for their lower force. Post-BR fibers from these same seven subjects also displayed a reduced sensitivity to free Ca2+( P < 0.05). These results indicate that the reduced functional capacity of human lower limb extensor muscles after BR may be in part caused by alterations in the cross-bridge mechanisms of contraction.

Shifts in type I fiber proportion in rat hindlimb muscle are accompanied by changes in HSP72 content

1994 ◽  
Vol 266 (5) ◽  
pp. C1240-C1246 ◽  
Author(s):  
M. Locke ◽  
B. G. Atkinson ◽  
R. M. Tanguay ◽  
E. G. Noble
Keyword(s):  
Citrate Synthase ◽  
Oxidative Capacity ◽  
Surgical Removal ◽  
Type I ◽  
Sprague Dawley ◽  
Hsp70 Family ◽  
Hindlimb Muscles ◽  
Sprague Dawley Rats ◽  
Hindlimb Muscle ◽  
Type I Fibers

Heat-shock protein 72 (HSP72), the inducible isoform of the HSP70 family, is constitutively expressed in rat hindlimb muscles in proportion to the content of type I muscle fibers. To determine whether this relationship was maintained after fiber transformation, male Sprague-Dawley rats were treated with 3,5,3'-triiodo-DL-thyronine (T3) for 40 days or underwent surgical removal of the left gastrocnemius muscle, after which the left plantaris muscle was allowed to hypertrophy for 30 days. Hypertrophied plantaris muscles exhibited an increased number of type I fibers, type I myosin heavy-chain (MHC) protein, and HSP72 content compared with contralateral muscles. Soleus muscles from rats administered T3 exhibited an increased number of type II fibers, citrate synthase activity, and decreased HSP72 content compared with soleus muscles from controls. These results indicate that the relationship between HSP72 content and type I muscle fiber-MHC composition is maintained when muscles undergo fiber transformation and substantiate that HSP72 content in rat skeletal muscle is not directly linked to a muscle's oxidative capacity.

scholarly journals Force-velocity and power characteristics of rat soleus muscle fibers after hindlimb suspension

1994 ◽  
Vol 77 (4) ◽  
pp. 1609-1616 ◽  
Author(s):  
K. S. McDonald ◽  
C. A. Blaser ◽  
R. H. Fitts
Keyword(s):  
Isometric Force ◽  
Fiber Type ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Hindlimb Suspension ◽  
Type I ◽  
Shortening Velocity ◽  
Power Characteristics ◽  
Sds Page ◽  
Force Velocity

The effects of 1, 2, and 3 wk of hindlimb suspension (HS) on force-velocity and power characteristics of single rat soleus fibers were determined. After 1, 2, or 3 wk of HS, small fiber bundles were isolated, placed in skinning solution, and stored at -20 degrees C until studied. Single fibers were isolated and placed between a motor arm and force transducer, functional properties were studied, and fiber protein content was subsequently analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Additional fibers were isolated from soleus of control and after 1 and 3 wk of HS, and fiber type distribution and myosin light chain stoichiometry were determined from SDS-PAGE analysis. After 1 wk of HS, percent type I fibers declined from 82 to 74%, whereas hybrid fibers increased from 10 to 18%. Percent fast type II fibers increased from 8% in control and 1 wk of HS to 26% by 3 wk of HS. Most fibers showed an increased unloaded maximal shortening velocity (Vo), but myosin heavy chain remained entirely slow type I. The mechanism for increased Vo is unknown. There was a progressive decrease in fiber diameter (14, 30, and 38%) and peak force (38, 56, and 63%) after 1, 2, and 3 wk of HS, respectively. One week of HS resulted in a shift of the force-velocity curve, and between 2 and 3 wk of HS the curve shifted further such that Vo was higher than control at all relative loads < 45% peak isometric force. Peak absolute power output of soleus fibers progressively decreased through 2 wk of HS but showed no further change at 3 wk.(ABSTRACT TRUNCATED AT 250 WORDS)

scholarly journals Increases in skeletal muscle ATGL and its inhibitor G0S2 following 8 weeks of endurance training in metabolically different rat skeletal muscles

2016 ◽  
Vol 310 (2) ◽  
pp. R125-R133 ◽  
Author(s):  
Patrick C. Turnbull ◽  
Amanda B. Longo ◽  
Sofhia V. Ramos ◽  
Brian D. Roy ◽  
Wendy E. Ward ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Endurance Training ◽  
Skeletal Muscles ◽  
Gene Identification ◽  
Sprague Dawley ◽  
Sprague Dawley Rats ◽  
Hind Limb Muscle ◽  
Sciatic Nerve Stimulation ◽  
Rate Limiting

Adipose triglyceride lipase (ATGL) catalyzes the rate-limiting removal of the first fatty acid from a triglyceride. ATGL is activated by comparative gene identification-58 and inhibited by G(0)/G(1) switch gene-2 protein (G0S2). Research in other tissues and cell culture indicates that inhibition is dependent on relative G0S2-to-ATGL protein content. G0S2 may also have several roles within mitochondria; however, this has yet to be observed in skeletal muscle. The purpose of this study was to determine if muscle G0S2 relative to ATGL content would decrease to facilitate intramuscular lipolysis following endurance training. Male Sprague-Dawley rats ( n = 10; age 51–53 days old) were progressively treadmill trained at a 10% incline for 8 wk ending with 25 m/min for 1 h compared with control. Sciatic nerve stimulation for hind-limb muscle contraction (and lipolysis) was administered for 30 min to one leg, leaving the opposing leg as a resting control. Soleus (SOL), red gastrocnemius (RG), and white gastrocnemius were excised from both legs following stimulation or control. ATGL protein increased in all trained muscles. Unexpectedly, G0S2 protein was greater in the trained SOL and RG. In RG-isolated mitochondria, G0S2 also increased with training, yet mitochondrial G0S2 content was unaltered with acute contraction; therefore, any role of G0S2 in the mitochondria does not appear to be acutely mediated by content alone. In summary, G0S2 increased with training in oxidative muscles and mitochondria but not following acute contraction, suggesting that inhibition is not through relative G0S2-to-ATGL content but through more complicated intracellular mechanisms.

Sign in / Sign up

Export Citation Format

Share Document