Profiles of connectin (titin) in atrophied soleus muscle induced by unloading of rats

2003 ◽  
Vol 94 (3) ◽  
pp. 897-902 ◽  
Author(s):  
Katsumasa Goto ◽  
Ryoko Okuyama ◽  
Masanori Honda ◽  
Hiroshi Uchida ◽  
Tatsuo Akema ◽  
...  
Keyword(s):  
Extensor Digitorum Longus ◽  
Contractile Function ◽  
Muscle Fibers ◽  
Extensor Digitorum ◽  
Hindlimb Suspension ◽  
Molecular Weights ◽  
Band Region ◽  
Wet Weight ◽  
Fast Twitch ◽  
Significant Increment

Responses of the properties of connectin molecules in the slow-twitch soleus (Sol) and fast-twitch extensor digitorum longus muscles of rats to 3 days of unloading with or without 3-day reloading were investigated. The wet weight (relative to body wt) of Sol, not of extensor digitorum longus, in the unloaded group was significantly less than in the age-matched control ( P < 0.05). Immunoelectron microscopic analyses showed that a monoclonal antibody against connectin (SM1) bound to the I-band region close to the edge of the A band at resting length and moved reversibly away from the Z line as the muscle fibers were stretched. In Sol, the displacement of the SM1-bound dense spots in response to stretching decreased after hindlimb suspension. There were no changes in the molecular weights and the percent distributions of α- and β-connectin in both muscles after hindlimb suspension. A significant increment of percent β-connectin in Sol was observed after 3 days of reloading after hindlimb suspension ( P < 0.05). It is suggested that the elasticity of connectin filaments in the I-band region of the atrophied Sol fibers was reduced relative to that of the control fibers. The lack of the elasticity in atrophied muscle fibers may cause a decrease in contractile function.

scholarly journals Carbonic anhydrase activity in skeletal muscle fiber types, axons, spindles, and capillaries of rat soleus and extensor digitorum longus muscles.

1982 ◽  
Vol 30 (12) ◽  
pp. 1275-1288 ◽  
Author(s):  
D A Riley ◽  
S Ellis ◽  
J Bain
Keyword(s):  
Carbonic Anhydrase ◽  
Extensor Digitorum Longus ◽  
Muscle Fibers ◽  
Extensor Digitorum ◽  
Female Rats ◽  
Male Rats ◽  
Muscle Fiber Types ◽  
Fiber Types ◽  
Slow Twitch ◽  
Fast Twitch

Carbonic anhydrase (CA) activities were studied in soluble extracts and cryostat sections of skeletal muscles from prepubertal and postpubertal rats. Acetazolamide inhibition was utilized to distinguish between activities of the acetazolamide-sensitive (CA I and II) and acetazolamide-resistant (CA III) forms of the enzyme. The inhibition studies indicated that fast-twitch oxidative-glycolytic muscle fibers contained both the sensitive and resistant forms of CA. Acetazolamide-sensitive activity was localized within muscle fibers, axons, myelin, and capillaries. Axoplasmic staining was restricted to subpopulations of myelinated axons in both the dorsal and ventral roots. Soleus muscles exhibited significantly greater activity of CA III than extensor digitorum longus muscles at all ages examined. CA III was richest in slow-twitch oxidative and intrafusal fibers. During puberty, soleus muscle fibers matured and converted from fast-twitch oxidative-glycolytic to slow-twitch oxidative fibers. There was a shift from the sensitive to the resistant form of CA; CA III activity increased about sevenfold. This activity peaked earlier in the muscles of female rats than male rats. These results demonstrated a complex distribution of CA isozymes in the neuromuscular system and pointed out that isozyme content depends on both the type of muscle and the age and sex of the animal.

Contractile function of single muscle fibers after hindlimb suspension

1989 ◽  
Vol 66 (6) ◽  
pp. 2739-2749 ◽  
Author(s):  
P. R. Gardetto ◽  
J. M. Schluter ◽  
R. H. Fitts
Keyword(s):  
Contractile Function ◽  
Fiber Type ◽  
Muscle Fibers ◽  
Hindlimb Suspension ◽  
Type I ◽  
Single Muscle ◽  
Peak Tension ◽  
Slow Twitch ◽  
Slow Twitch Fibers ◽  
Fast Twitch

The purpose of this investigation was to determine how muscle atrophy produced by the hindlimb suspension (HS) model alters the contractile function of slow- and fast-twitch single muscle fibers. After 2 wk of HS, small bundles of fibers were isolated from the soleus and the deep and superficial regions of the lateral and medial heads of the gastrocnemius, respectively. The bundles were placed in skinning solution and stored at -20 degrees C until studied. Single fibers were isolated and suspended between a motor arm and force transducer, the functional properties were studied, and subsequently the fiber type was established by myosin heavy chain (MHC) analysis on 1-D sodium dodecyl sulfate polyacrylamide gel electrophoresis. After HS, slow-twitch fibers of the soleus showed a significant reduction in fiber diameter (68 +/- 2 vs. 41 +/- 1 micron) and peak tension (1.37 +/- 0.01 vs. 0.99 +/- 0.06 kg/cm2), whereas the maximal shortening speed (Vmax) increased [1.49 +/- 0.11 vs. 1.92 +/- 0.14 fiber lengths (FL)/s]. A histogram showed two populations of fibers: one with Vmax values identical to control slow-twitch fibers and a second with significantly elevated Vmax values. This latter group frequently contained both slow and fast MHC protein isoforms. The pCa-force relation of the soleus slow-twitch fibers was shifted to the right; consequently, the free Ca2+ required for the onset of tension and for 50% of peak tension was significantly higher after HS. Slow-twitch fibers isolated from the gastrocnemius after HS showed a significant reduction in diameter (67 +/- 4 vs. 44 +/- 3 microns) and peak tension (1.2 +/- 0.06 vs. 0.96 +/- 0.07 kg/cm2), but Vmax was unaltered (1.70 +/- 0.13 vs. 1.65 +/- 0.18 FL/s). Fast-twitch fibers from the red gastrocnemius showed a significant reduction in diameter (59 +/- 2 vs. 49 +/- 3 microns) but no change in peak tension or Vmax. Fast-twitch fibers from the white superficial region of the medial head of the gastrocnemius were unaffected by HS. Collectively, these data suggest that the effects of HS on fiber function depend on the fiber type and location. Both slow-twitch type I and fast-twitch type IIa fibers atrophied; however, only slow-twitch fibers showed a decline in peak tension, and the increase in Vmax was restricted to a subpopulation of slow-twitch soleus fibers.

Glycogenesis and glyconeogenesis in skeletal muscle: effects of pH and hormones

1990 ◽  
Vol 258 (4) ◽  
pp. E693-E700 ◽  
Author(s):  
A. Bonen ◽  
J. C. McDermott ◽  
M. H. Tan
Keyword(s):  
Skeletal Muscle ◽  
Soleus Muscle ◽  
Extensor Digitorum Longus ◽  
Muscle Fibers ◽  
Extensor Digitorum ◽  
Effects Of Ph ◽  
Slow Twitch ◽  
Highly Correlated ◽  
Fast Twitch

We examined the effects of selected hormones and pH on the rates of glyconeogenesis (L-[U-14C]-lactate----glycogen) and glycogenesis (D-[U-14C]glucose----glycogen) in mouse fast-twitch (FT) and slow-twitch muscles incubated in vitro (37 degrees C). Glyconeogenesis and glycogenesis increased linearly with increasing concentrations of lactate (5-20 mM) and glucose (2.5-10 mM), respectively, in both muscles. Glyconeogenesis was approximately three- to fourfold greater in the extensor digitorum longus (EDL) than in the soleus, whereas basal glycogenesis was twofold greater in the soleus muscle than in the EDL. Lactate accounted for up to 5% of the glycogen formed in the soleus and up to 32% in the EDL relative to the rates of glycogenesis (i.e., 5 mM glucose + 10 nM insulin) in each muscle. Corticosterone (10(-12)-10(-6) M) failed to alter glyconeogenesis, whereas this hormone reduced glycogenesis. Insulin (10 nM) markedly stimulated glycogenesis but failed to stimulate glyconeogenesis. The rates of both glycogenesis and glyconeogenesis were pH sensitive, with optimal rates at pH 6.5-7.0 in both muscles. Glyconeogenesis increased by 49% in the soleus and by 39% EDL at pH 6.5 compared with pH 7.4. Glycogenesis increased in the soleus (SOL) and EDL in the absence (SOL: +22%; EDL: +52%) and presence of insulin (SOL: +22%; EDL: +51%) at pH 6.5 when compared with pH 7.4. In additional experiments with the perfused rat hindquarter, rates of glyconeogenesis were shown to be highly correlated with proportion of FT muscle fibers in a muscle.(ABSTRACT TRUNCATED AT 250 WORDS)

Spaceflight on STS-48 and earth-based unweighting produce similar effects on skeletal muscle of young rats

1993 ◽  
Vol 74 (5) ◽  
pp. 2161-2165 ◽  
Author(s):  
M. E. Tischler ◽  
E. J. Henriksen ◽  
K. A. Munoz ◽  
C. S. Stump ◽  
C. R. Woodman ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Extensor Digitorum Longus ◽  
Space Shuttle ◽  
Weight Bearing ◽  
Similar Rate ◽  
Extensor Digitorum ◽  
Hindlimb Suspension ◽  
Albino Rats ◽  
Sprague Dawley ◽  
Ambient Temperatures

Our knowledge of the effects of unweighting on skeletal muscle of juvenile rapidly growing rats has been obtained entirely by using hindlimb-suspension models. No spaceflight data on juvenile animals are available to validate these models of simulated weightlessness. Therefore, eight 26-day-old female Sprague-Dawley albino rats were exposed to 5.4 days of weightlessness aboard the space shuttle Discovery (mission STS-48, September 1991). An asynchronous ground control experiment mimicked the flight cage condition, ambient shuttle temperatures, and mission duration for a second group of rats. A third group of animals underwent hindlimb suspension for 5.4 days at ambient temperatures. Although all groups consumed food at a similar rate, flight animals gained a greater percentage of body mass per day (P < 0.05). Mass and protein data showed weight-bearing hindlimb muscles were most affected, with atrophy of the soleus and reduced growth of the plantaris and gastrocnemius in both the flight and suspended animals. In contrast, the non-weight-bearing extensor digitorum longus and tibialis anterior muscles grew normally. Earlier suspension studies showed that the soleus develops an increased sensitivity to insulin during unweighting atrophy, particularly for the uptake of 2-[1,2–3H]deoxyglucose. Therefore, this characteristic was studied in isolated muscles within 2 h after cessation of spaceflight or suspension. Insulin increased uptake 2.5- and 2.7-fold in soleus of flight and suspended animals, respectively, whereas it increased only 1.6-fold in control animals. In contrast, the effect of insulin was similar among the three groups for the extensor digitorum longus, which provides a control for potential systemic differences in the animals.

Effects of unweighting and clenbuterol on myosin light and heavy chains in fast and slow muscles of rat

2000 ◽  
Vol 279 (5) ◽  
pp. C1558-C1563 ◽  
Author(s):  
Laurence Stevens ◽  
Carole Firinga ◽  
Bärbel Gohlsch ◽  
Bruno Bastide ◽  
Yvonne Mounier ◽  
...  
Keyword(s):  
Light Chain ◽  
Extensor Digitorum Longus ◽  
Extensor Digitorum ◽  
Hindlimb Suspension ◽  
Adrenergic Agonist ◽  
Heavy Chains ◽  
Fast And Slow Muscles ◽  
Induced Changes ◽  
Fast Muscles ◽  
Slow And Fast Muscles

To investigate the plasticity of slow and fast muscles undergoing slow-to-fast transition, rat soleus (SOL), gastrocnemius (GAS), and extensor digitorum longus (EDL) muscles were exposed for 14 days to 1) unweighting by hindlimb suspension (HU), or 2) treatment with the β2-adrenergic agonist clenbuterol (CB), or 3) a combination of both (HU-CB). In general, HU elicited atrophy, CB induced hypertrophy, and HU-CB partially counteracted the HU-induced atrophy. Analyses of myosin heavy (MHC) and light chain (MLC) isoforms revealed HU- and CB-induced slow-to-fast transitions in SOL (increases of MHCIIa with small amounts of MHCIId and MHCIIb) and the upregulation of the slow MHCIa isoform. The HU- and CB-induced changes in GAS consisted of increases in MHCIId and MHCIIb (“fast-to-faster transitions”). Changes in the MLC composition of SOL and GAS consisted of slow-to-fast transitions and mainly encompassed an exchange of MLC1s with MLC1f. In addition, MLC3f was elevated whenever MHCIId and MHCIIb isoforms were increased. Because the EDL is predominantly composed of type IID and IIB fibers, HU, CB, and HU-CB had no significant effect on the MHC and MLC patterns.

scholarly journals Contraction-induced injury to the extensor digitorum longus muscles of rats: the role of vitamin E

1997 ◽  
Vol 83 (3) ◽  
pp. 817-823 ◽  
Author(s):  
Jack H. Van Der Meulen ◽  
Anne McArdle ◽  
Malcolm J. Jackson ◽  
John A. Faulkner
Keyword(s):  
Creatine Kinase ◽  
Vitamin E ◽  
Pyruvate Kinase ◽  
Extensor Digitorum Longus ◽  
Muscle Fibers ◽  
Extensor Digitorum ◽  
Intravenous Injections ◽  
Antioxidant Function ◽  
The Difference

Van der Meulen, Jack H., Anne McArdle, Malcolm J. Jackson, and John A. Faulkner. Contraction-induced injury to the extensor digitorum longus muscles of rats: the role of vitamin E. J. Appl. Physiol. 83(3): 817–823, 1997.—Three days after a protocol of 225 pliometric (lengthening) contractions was administered to in situ extensor digitorum longus muscles of rats, the force deficit was 64 ± 7% and the percentage of damaged muscle fibers was 38 ± 5% of the control values. We then tested the hypothesis that at 3 h and 3 days after the protocol an elevation in the muscle vitamin E content would decrease the force deficit, the percentage of damaged muscle fibers, and the serum activities of creatine kinase and pyruvate kinase. The 5–8 days of intravenous injections of α-tocopherol increased muscle vitamin E content threefold compared with vehicle (ethanol)-treated rats. Despite the difference in vitamin E content, the force deficit and number of damaged fibers were not different. After the contraction protocol, the serum creatine kinase and pyruvate kinase activities of the vehicle-treated rats increased fourfold at 3 h and twofold at 3 days, whereas the vitamin E-treated rats showed no change. We conclude that vitamin E treatment did not ameliorate either the induction of the injury or the more severe secondary injury at 3 days. Despite the absence of evidence for an antioxidant function, the lack of any increase in serum enzyme activities for vitamin E-treated rats at 3 h and 3 days supported a role for vitamin E in the prevention of enzyme loss after muscle damage.

Myosin light chain phosphorylation-dephosphorylation in mammalian skeletal muscle

1982 ◽  
Vol 242 (3) ◽  
pp. C234-C241 ◽  
Author(s):  
D. R. Manning ◽  
J. T. Stull
Keyword(s):  
Skeletal Muscle ◽  
Light Chain ◽  
Extensor Digitorum Longus ◽  
Myosin Light Chain ◽  
Extensor Digitorum Longus Muscle ◽  
Extensor Digitorum ◽  
Mammalian Skeletal Muscle ◽  
Phosphate Content ◽  
Longus Muscle ◽  
Fast Twitch

Phosphorylation of the myosin light chain 2 (LC2) subunit was examined in rat fast-twitch and slow-twitch skeletal muscles in response to repetitive stimulation at 23 and 35 degrees C and on incubation of fast-twitch skeletal muscle with isoproterenol. After a 1-s tetany at 35 degrees C, LC2 phosphate content in extensor digitorum longus muscle increased rapidly and transiently from 0.21 to 0.51 mol phosphate/mol LC2. This pattern of phosphorylation was similar to that observed at 23 degrees C. Increases in LC2 phosphate content were dependent on the frequency and duration of stimulation. In soleus muscle LC2 phosphate content was minimal following a 1-s tetany but increased markedly following more prolonged tetanies. On incubation of extensor digitorum longus muscle with isoproterenol (20 microM), LC2 phosphate content did not change, whereas phosphorylase a levels increased. A positive correlation existed between LC2 phosphate content and potentiation of peak twitch tension in both types of muscles, suggesting a physiological function for LC2 phosphorylation.

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