scholarly journals Effect of 23-day muscle disuse on sarcoplasmic reticulum Ca2+ properties and contractility in human type I and type II skeletal muscle fibers

2016 ◽  
Vol 121 (2) ◽  
pp. 483-492 ◽  
Author(s):  
C. R. Lamboley ◽  
V. L. Wyckelsma ◽  
B. D. Perry ◽  
M. J. McKenna ◽  
G. D. Lamb
Keyword(s):  
Skeletal Muscle ◽  
Sarcoplasmic Reticulum ◽  
Muscle Fibers ◽  
Type I ◽  
Fiber Types ◽  
Specific Force ◽  
Type Ii ◽  
Muscle Disuse ◽  
Type I Fibers ◽  
Type Ii Fibers

Inactivity negatively impacts on skeletal muscle function mainly through muscle atrophy. However, recent evidence suggests that the quality of individual muscle fibers is also altered. This study examined the effects of 23 days of unilateral lower limb suspension (ULLS) on specific force and sarcoplasmic reticulum (SR) Ca2+ content in individual skinned muscle fibers. Muscle biopsies of the vastus lateralis were taken from six young healthy adults prior to and following ULLS. After disuse, the endogenous SR Ca2+ content was ∼8% lower in type I fibers and maximal SR Ca2+ capacity was lower in both type I and type II fibers (−11 and −5%, respectively). The specific force, measured in single skinned fibers from three subjects, decreased significantly after ULLS in type II fibers (−23%) but not in type I fibers (−9%). Western blot analyses showed no significant change in the amounts of myosin heavy chain (MHC) I and MHC IIa following the disuse, whereas the amounts of sarco(endo)plasmic reticulum Ca2+-ATPase 1 (SERCA1) and calsequestrin increased by ∼120 and ∼20%, respectively, and the amount of troponin I decreased by ∼21%. These findings suggest that the decline in force and power occurring with muscle disuse is likely to be exacerbated in part by reductions in maximum specific force in type II fibers, and in the amount of releasable SR Ca2+ in both fiber types, the latter not being attributable to a reduced calsequestrin level. Furthermore, the ∼3-wk disuse in human elicits change in SR properties, in particular a more than twofold upregulation in SERCA1 density, before any fiber-type shift.

scholarly journals Myoglobin concentration in skeletal muscle fibers of chronic heart failure patients

2009 ◽  
Vol 107 (4) ◽  
pp. 1138-1143 ◽  
Author(s):  
Martijn A. Bekedam ◽  
Brechje J. van Beek-Harmsen ◽  
Willem van Mechelen ◽  
Anco Boonstra ◽  
Willem J. van der Laarse
Keyword(s):  
Heart Failure ◽  
Skeletal Muscle ◽  
Chronic Heart Failure ◽  
Muscle Fibers ◽  
Type I ◽  
Fiber Types ◽  
Type Ii ◽  
Skeletal Muscle Fibers ◽  
Type I Fibers ◽  
Type Ii Fibers

The purpose of this study was to determine the myoglobin concentration in skeletal muscle fibers of chronic heart failure (CHF) patients and to calculate the effect of myoglobin on oxygen buffering and facilitated diffusion. Myoglobin concentration, succinate dehydrogenase (SDH) activity, and cross-sectional area of individual muscle fibers from the vastus lateralis of five control and nine CHF patients were determined using calibrated histochemistry. CHF patients compared with control subjects were similar with respect to myoglobin concentration: type I fibers 0.69 ± 0.11 mM (mean ± SD), type II fibers 0.52 ± 0.07 mM in CHF vs. type I fibers 0.70 ± 0.09 mM, type II fibers 0.49 ± 0.07 mM in control, whereas SDH activity was significantly lower in CHF in both fiber types ( P < 0.01). The myoglobin concentration in type I fibers was higher than in type II fibers ( P < 0.01). Consequently, the oxygen buffering capacity, calculated from myoglobin concentration/SDH activity was increased in CHF: type I fibers 11.4 ± 2.1 s, type II fibers 13.6 ± 3.9 s in CHF vs. type I fibers 7.8 ± 0.9 s, type II fibers 7.5 ± 1.0 s in control, all P < 0.01). The calculated extracellular oxygen tension required to prevent core anoxia (Po2crit) in muscle fibers was similar when controls were compared with patients in type I fibers 10.3 ± 0.9 Torr in CHF and 11.5 ± 3.3 Torr in control, but was lower in type II fibers of patients 6.1 ± 2.8 Torr in CHF and 14.7 ± 6.2 Torr in control, P < 0.01. The lower Po2crit of type II fibers may facilitate oxygen extraction from capillaries. Reduced exercise tolerance in CHF is not due to myoglobin deficiency.

scholarly journals Differential regulation of the fiber type-specific gene expression of the sarcoplasmic reticulum calcium-ATPase isoforms induced by exercise training

2014 ◽  
Vol 117 (5) ◽  
pp. 544-555 ◽  
Author(s):  
Marc P. Morissette ◽  
Shanel E. Susser ◽  
Andrew N. Stammers ◽  
Kimberley A. O'Hara ◽  
Phillip F. Gardiner ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Sarcoplasmic Reticulum ◽  
Exercise Training ◽  
Calcium Atpase ◽  
Specific Gene ◽  
Type I ◽  
Fiber Types ◽  
Type Ii ◽  
Type Ii Fibers ◽  
Sarcoplasmic Reticulum Calcium

The regulatory role of adenosine monophosphate-activated protein kinase (AMPK)-α2 on sarcoplasmic reticulum calcium-ATPase (SERCA) 1a and SERCA2a in different skeletal muscle fiber types has yet to be elucidated. Sedentary (Sed) or exercise-trained (Ex) wild-type (WT) and AMPKα2-kinase dead (KD) transgenic mice, which overexpress a mutated and inactivated AMPKα2 subunit, were utilized to characterize how genotype or exercise training influenced the regulation of SERCA isoforms in gastrocnemius. As expected, both Sed and Ex KD mice had >40% lower AMPK phosphorylation and 30% lower SERCA1a protein than WT mice ( P < 0.05). In contrast, SERCA2a protein was not different among KD and WT mice. Exercise increased SERCA1a and SERCA2a protein content among WT and KD mice, compared with their Sed counterparts. Maximal SERCA activity was lower in KD mice, compared with WT. Total phospholamban protein was higher in KD mice than in WT and lower in Ex compared with Sed mice. Exercise training increased phospholamban Ser16 phosphorylation in WT mice. Laser capture microdissection and quantitative PCR indicated that SERCA1a mRNA expression among type I fibers was not altered by genotype or exercise, but SERCA2a mRNA was increased 30-fold in WT+Ex, compared with WT+Sed. In contrast, the exercise-stimulated increase for SERCA2a mRNA was blunted in KD mice. Exercise upregulated SERCA1a and SERCA2a mRNA among type II fibers, but was not altered by genotype. Collectively, these data suggest that exercise differentially influences SERCA isoform expression in type I and type II fibers. Additionally, AMPKα2 influences the regulation of SERCA2a mRNA in type I skeletal muscle fibers following exercise training.

Acute effects of taurine on sarcoplasmic reticulum Ca2+ accumulation and contractility in human type I and type II skeletal muscle fibers

2014 ◽  
Vol 117 (7) ◽  
pp. 797-805 ◽  
Author(s):  
T. L. Dutka ◽  
C. R. Lamboley ◽  
R. M. Murphy ◽  
G. D. Lamb
Keyword(s):  
Sarcoplasmic Reticulum ◽  
Fiber Type ◽  
Vastus Lateralis ◽  
Muscle Fibers ◽  
Vastus Lateralis Muscle ◽  
Type I ◽  
Fiber Types ◽  
Type Ii ◽  
Contractile Apparatus ◽  
Type Ii Fibers

Taurine occurs in high concentrations in muscle and is implicated in numerous physiological processes, yet its effects on many aspects of contractility remain unclear. Using mechanically skinned segments of human vastus lateralis muscle fibers, we characterized the effects of taurine on sarcoplasmic reticulum (SR) Ca2+ accumulation and contractile apparatus properties in type I and type II fibers. Prolonged myoplasmic exposure (>10 min) to taurine substantially increased the rate of accumulation of Ca2+ by the SR in both fiber types, with no change in the maximum amount accumulated; no such effect was found with carnosine. SR Ca2+ accumulation was similar with 10 or 20 mM taurine, but was significantly slower at 5 mM taurine. Cytoplasmic taurine (20 mM) had no detectable effects on the responsiveness of the Ca2+ release channels in either fiber type. Taurine caused a small increase in Ca2+ sensitivity of the contractile apparatus in type I fibers, but type II fibers were unaffected; maximum Ca2+-activated force was unchanged in both cases. The effects of taurine on SR Ca2+ accumulation 1) only became apparent after prolonged cytoplasmic exposure, and 2) persisted for some minutes after complete removal of taurine from the cytoplasm, consistent with the hypothesis that the effects were due to an action of taurine from inside the SR. In summary, taurine potentiates the rate of SR Ca2+ uptake in both type I and type II human fibers, possibly via an action from within the SR lumen, with the degree of potentiation being significantly reduced at low physiological taurine levels.

Diaphragm muscle fatigue resistance during postnatal development

1991 ◽  
Vol 71 (2) ◽  
pp. 458-464 ◽  
Author(s):  
G. C. Sieck ◽  
M. Fournier ◽  
C. E. Blanco
Keyword(s):  
Postnatal Development ◽  
Fatigue Resistance ◽  
Muscle Fibers ◽  
Diaphragm Muscle ◽  
Fatigue Properties ◽  
Type I ◽  
Type Ii ◽  
Cross Sectional ◽  
Type I Fibers ◽  
Type Ii Fibers

postnatal development. Both twitch contraction time and half-relaxation time decreased progressively with age. Correspondingly, the force-frequency curve was shifted to the left early in development compared with adults. The ratio of peak twitch force to maximum tetanic force decreased with age. Fatigue resistance of the diaphragm was highest at birth and then progressively decreased with age. At birth, most diaphragm muscle fibers stained darkly for myofibrillar adenosinetriphosphatase after alkaline preincubation and thus would be classified histochemically as type II. During subsequent postnatal development, the proportion of type I fibers (lightly stained for adenosinetriphosphatase) increased while the number of type II fibers declined. At birth, type I fibers were larger than type II fibers. The size of both fiber types increased with age, but the increase in cross-sectional area was greater for type II fibers. On the basis of fiber type proportions and mean cross-sectional areas, type I fibers contributed 15% of total muscle mass at birth and 25% in adults. Thus postnatal changes in diaphragm contractile and fatigue properties cannot be attributed to changes in the relative contribution of histochemically classified type I and II fibers. However, the possibility that these developmental changes in diaphragm contractile and fatigue properties correlated with the varying contractile protein composition of muscle fibers was discussed.

Effects of ACE inhibition and beta-blockade on skeletal muscle fiber types in dogs with moderate heart failure

1996 ◽  
Vol 270 (1) ◽  
pp. H115-H120 ◽  
Author(s):  
H. N. Sabbah ◽  
H. Shimoyama ◽  
V. G. Sharov ◽  
T. Kono ◽  
R. C. Gupta ◽  
...  
Keyword(s):  
Heart Failure ◽  
Skeletal Muscle ◽  
Exercise Intolerance ◽  
Beta Blockade ◽  
Muscle Fiber Types ◽  
Type I ◽  
Fiber Types ◽  
Type Ii ◽  
Early Therapy ◽  
Type I Fibers

The proportion of slow-twitch, fatigue-resistant type 1 skeletal muscle (SM) fibers is often reduced in heart failure (HF), while the proportion of fatigue-sensitive type-II fibers increases. This maladaptation may be partially responsible for the exercise intolerance that characterize HF. In this study, we examined the effects of early monotherapy with the angiotensin-converting enzyme inhibor, enalapril, and the beta-blocker, metoprolol, on SM fiber type composition in 18 dogs with moderate HF produced by intracoronary microembolizations. HF dogs were randomized to 3 mo therapy with enalapril (10 mg twice daily), metoprolol (25 mg twice daily), or no treatment. Triceps muscle biopsies were obtained at baseline, before randomization, and at the end of 30 mo of therapy. Type I and type II SM fibers were differentiated by myofibrillar adenosinetriphosphatase (pH 9.4). In untreated dogs, the proportion of type I fibers was 27 +/- 1% before randomization and decreased to 23 +/- 1% (P < 0.05) at the end of 3 mo of follow up. In dogs treated with enalapril or metoprolol, the proportion of type I fibers was 30 +/- 4 and 28 +/- 2% before randomization and 33 +/- 4 and 33 +/- 1%, respectively, after 3 mo of therapy. In conclusion, in dogs with moderate HF, early therapy with enalapril or metoprolol prevents the progressive decline in the proportion of type I SM fibers.

Energy metabolism in single human muscle fibers during contraction without and with epinephrine infusion

1991 ◽  
Vol 260 (5) ◽  
pp. E713-E718 ◽  
Author(s):  
P. L. Greenhaff ◽  
J. M. Ren ◽  
K. Soderlund ◽  
E. Hultman
Keyword(s):  
Electrical Stimulation ◽  
Muscle Fibers ◽  
Type I ◽  
Type Ii ◽  
Short Term ◽  
Epinephrine Infusion ◽  
Before And After ◽  
Type I Fibers ◽  
Type Ii Fibers ◽  
Femoris Muscle

The concentrations of glycogen, ATP, and phosphocreatine were analyzed in types I and II muscle fibers separated from biopsy samples of the quadriceps femoris muscle in five healthy volunteers. Muscle samples were obtained before and after 64 s of intermittent electrical stimulation. The experiment was carried out without and with epinephrine (Epi) infusion. Before stimulation the glycogen concentration was 11% higher in type II than in type I fibers (P less than 0.05). During electrical stimulation, rapid glycogenolysis occurred in type II fibers with hardly any detectable glycogenolysis in type I fibers. The calculated rates of glycogenolysis were 0.18 +/- 0.14 and 3.54 +/- 0.53 mmol glucose.kg dry muscle-1.s-1 in types I and II fibers, respectively. Epi infusion increased the rate of glycogenolysis during electrical stimulation in type I fibers (10-fold) but did not enhance the rate in type II fibers (P greater than 0.05). It is considered that, during short-term maximal muscle contraction, rapid muscle glycogenolysis occurs predominantly in type II fibers even though types I and II fibers are recruited and that, when Epi stimulation of glycogenolysis occurs, this is predominantly limited to type I fibers.

scholarly journals Denervation and reinnervation of fast and slow muscles. A histochemical study in rats.

1975 ◽  
Vol 23 (11) ◽  
pp. 808-827 ◽  
Author(s):  
M M Jaweed ◽  
G J Herbison ◽  
J F Ditunno
Keyword(s):  
Fiber Diameter ◽  
Histochemical Study ◽  
Fiber Type ◽  
Type I ◽  
Fiber Types ◽  
Type Ii ◽  
Type I Fibers ◽  
Type Ii Fibers ◽  
Fast Muscles ◽  
Slow And Fast Muscles

A histochemical study, using myosin-adenosine triphosphatase activity at pH 9.4, was conducted in soleus and plantaris muscles of adult rats, after bilateral crushing of the sciatic nerve at the sciatic notch. The changes in fiber diameter and per cent composition of type I and type II fibers plus muscle weights were evaluated along the course of denervation-reinnervation curve at 1, 2, 3, 4 and 6 weeks postnerve crush. The study revealed that in the early denervation phase (up to 2 weeks postcrush) both the slow and fast muscles, soleus and plantaris, resepctively, atrophied similarly in muscle mass. Soleus increased in the number of type II fibers, which may be attributed to "disuse" effect. During the same period, the type I fibers of soleus atrophied as much or slightly more than the type II fibers; whereas the type II fibers of plantaris atrophied significantly more than the type I fibers, reflecting that the process of denervation, in its early stages, may affect the two fiber types differentially in the slow and fast muscles. It was deduced that the type I fibers of plantaris may be essentially different in the slow (soleus) and fast (plantaris) muscles under study. The onset of reinnervation, as determined by the increase in muscle weight and fiber diameter of the major fiber type, occurred in soleus and plantaris at 2 and 3 weeks postcrush, respectively, which confirms the earlier hypotheses that the slow muscles are reinnervated sooner than the fast muscles. It is suggested that the reinnervation of muscle after crush injury may be specific to the muscle type or its predominant fiber type.

scholarly journals Functional and structural adaptations of skeletal muscle to microgravity

2001 ◽  
Vol 204 (18) ◽  
pp. 3201-3208 ◽  
Author(s):  
Robert H. Fitts ◽  
Danny R. Riley ◽  
Jeffrey J. Widrick
Keyword(s):  
Skeletal Muscle ◽  
Muscle Atrophy ◽  
Peak Force ◽  
Type I ◽  
Type Ii ◽  
Shortening Velocity ◽  
Slow Type ◽  
Fiber Atrophy ◽  
Type I Fibers ◽  
Type Ii Fibers

SUMMARY Our purpose is to summarize the major effects of space travel on skeletal muscle with particular emphasis on factors that alter function. The primary deleterious changes are muscle atrophy and the associated decline in peak force and power. Studies on both rats and humans demonstrate a rapid loss of cell mass with microgravity. In rats, a reduction in muscle mass of up to 37% was observed within 1 week. For both species, the antigravity soleus muscle showed greater atrophy than the fast-twitch gastrocnemius. However, in the rat, the slow type I fibers atrophied more than the fast type II fibers, while in humans, the fast type II fibers were at least as susceptible to space-induced atrophy as the slow fiber type. Space flight also resulted in a significant decline in peak force. For example, the maximal voluntary contraction of the human plantar flexor muscles declined by 20–48% following 6 months in space, while a 21% decline in the peak force of the soleus type I fibers was observed after a 17-day shuttle flight. The reduced force can be attributed both to muscle atrophy and to a selective loss of contractile protein. The former was the primary cause because, when force was expressed per cross-sectional area (kNm−2), the human fast type II and slow type I fibers of the soleus showed no change and a 4% decrease in force, respectively. Microgravity has been shown to increase the shortening velocity of the plantar flexors. This increase can be attributed both to an elevated maximal shortening velocity (V0) of the individual slow and fast fibers and to an increased expression of fibers containing fast myosin. Although the cause of the former is unknown, it might result from the selective loss of the thin filament actin and an associated decline in the internal drag during cross-bridge cycling. Despite the increase in fiber V0, peak power of the slow type I fiber was reduced following space flight. The decreased power was a direct result of the reduced force caused by the fiber atrophy. In addition to fiber atrophy and the loss of force and power, weightlessness reduces the ability of the slow soleus to oxidize fats and increases the utilization of muscle glycogen, at least in rats. This substrate change leads to an increased rate of fatigue. Finally, with return to the 1g environment of earth, rat studies have shown an increased occurrence of eccentric contraction-induced fiber damage. The damage occurs with re-loading and not in-flight, but the etiology has not been established.

Histochemical and Morphometric Evaluation of Skeletal Muscle of Cachectic Sheep

1981 ◽  
Vol 18 (3) ◽  
pp. 279-298 ◽  
Author(s):  
T. J. Hulland
Keyword(s):  
Skeletal Muscle ◽  
Muscle Fiber ◽  
Succinic Dehydrogenase ◽  
Adult Life ◽  
Biological Behavior ◽  
Type I ◽  
Fiber Types ◽  
Type Ii ◽  
Atrophy And Hypertrophy ◽  
Type I Fibers

Skeletal muscle of sheep was examined histochemically in an attempt to define muscle fiber populations capable of distinctive biological behavior. ATPase at alkaline and acid pH, NADH-TR, and succinic dehydrogenase showed at least 12 fiber types, but only three often enough to be considered biologically important muscle fiber populations. The proportions of the three major types altered during early life, but not perceptibly during adult life. Proportions of Type I and Type II fibers were different, sometimes significantly, from breed to breed. Histochemical techniques and morphometric analyses of fiber cross-sectional area were used to study muscle fiber changes in moderate to marked cachectic atrophy. Progressive reduction of gross muscle volume was attended by complex interrelationships between the two major muscle fiber types, including alternate episodes of atrophy and hypertrophy, resulting in marked inequality of mean fiber size between the fiber types. The patterns appeared to be different but characteristic for each muscle. The usual pattern of cachectic atrophy shows atrophy resistance of Type I fibers, but here a Type II-dominant atrophy also was seen. It is concluded that the large muscle fibers often seen in advanced cachectic atrophy are those Type I fibers that are more labile in both atrophy and hypertrophy than most.

Effects of carnosine on contractile apparatus Ca2+ sensitivity and sarcoplasmic reticulum Ca2+ release in human skeletal muscle fibers

2012 ◽  
Vol 112 (5) ◽  
pp. 728-736 ◽  
Author(s):  
T. L. Dutka ◽  
C. R. Lamboley ◽  
M. J. McKenna ◽  
R. M. Murphy ◽  
G. D. Lamb
Keyword(s):  
Skeletal Muscle ◽  
Human Muscle ◽  
Muscle Performance ◽  
Type I ◽  
Type Ii ◽  
Contractile Apparatus ◽  
Muscle Carnosine ◽  
Ec Coupling ◽  
Type I Fibers ◽  
Type Ii Fibers

There is considerable interest in potential ergogenic and therapeutic effects of increasing skeletal muscle carnosine content, although its effects on excitation-contraction (EC) coupling in human muscle have not been defined. Consequently, we sought to characterize what effects carnosine, at levels attained by supplementation, has on human muscle fiber function, using a preparation with all key EC coupling proteins in their in situ positions. Fiber segments, obtained from vastus lateralis muscle of human subjects by needle biopsy, were mechanically skinned, and their Ca2+ release and contractile apparatus properties were characterized. Ca2+ sensitivity of the contractile apparatus was significantly increased by 8 and 16 mM carnosine (increase in pCa50 of 0.073 ± 0.007 and 0.116 ± 0.006 pCa units, respectively, in six type I fibers, and 0.063 ± 0.018 and 0.103 ± 0.013 pCa units, respectively, in five type II fibers). Caffeine-induced force responses were potentiated by 8 mM carnosine in both type I and II fibers, with the potentiation in type II fibers being entirely explicable by the increase in Ca2+ sensitivity of the contractile apparatus caused by carnosine. However, the potentiation of caffeine-induced responses caused by carnosine in type I fibers was beyond that expected from the associated increase in Ca2+ sensitivity of the contractile apparatus and suggestive of increased Ca2+-induced Ca2+ release. Thus increasing muscle carnosine content likely confers benefits to muscle performance in both fiber types by increasing the Ca2+ sensitivity of the contractile apparatus and possibly also by aiding Ca2+ release in type I fibers, helping to lessen or slow the decline in muscle performance during fatiguing stimulation.

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