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.

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.

ATP and phosphocreatine changes in single human muscle fibers after intense electrical stimulation

1991 ◽  
Vol 261 (6) ◽  
pp. E737-E741 ◽  
Author(s):  
K. Soderlund ◽  
E. Hultman
Keyword(s):  
Electrical Stimulation ◽  
Adenine Nucleotides ◽  
Vastus Lateralis ◽  
Anaerobic Exercise ◽  
Vastus Lateralis Muscle ◽  
Type I ◽  
Fiber Types ◽  
Type Ii ◽  
Type I Fibers ◽  
Type Ii Fibers

The recovery pattern of adenine nucleotides and glucolytic intermediates after short-lasting anaerobic exercise was studied. Biopsies were obtained from the vastus lateralis muscle at rest, immediately after intermittent electrical stimulation with occluded circulation (total time 166 s), and after 20 s, 60 s, 5 min, and 15 min of recovery. ATP in single fibers decreased from 23.9 +/- 1.41 to 14.2 +/- 3.20 in type I fibers and from 25.01 +/- 1.20 to 13.1 +/- 2.65 mmol/kg dry muscle in type II fibers postexercise. After 15 min of recovery, ATP was resynthesized to 95 and 76% in type I and type II fibers, respectively. The phosphocreatine (PCr) content in type I fibers at rest was 72.3 +/- 4.50 and 83.3 +/- 9.76 mmol/kg dry muscle in type II fibers. After exercise, PCr was depleted in both fiber types. After the 60 s of recovery the PCr content in type I fibers was significantly higher (P less than 0.05) compared with type II fibers, but, after 5 min of oxidative recovery, the PCr levels were equal in the two fiber types. Fifteen minutes postexercise, type II fibers demonstrated a significantly higher content (97.8 mmol/kg dry muscle) compared with its resting value (P less than 0.05).

Recruitment of single muscle fibers during submaximal cycling exercise

2007 ◽  
Vol 103 (5) ◽  
pp. 1752-1756 ◽  
Author(s):  
T. M. Altenburg ◽  
H. Degens ◽  
W. van Mechelen ◽  
A. J. Sargeant ◽  
A. de Haan
Keyword(s):  
Cross Sections ◽  
Vastus Lateralis ◽  
Periodic Acid ◽  
Ratio Method ◽  
Vastus Lateralis Muscle ◽  
Type I ◽  
Type Ii ◽  
Periodic Acid Schiff ◽  
Cycling Exercise ◽  
Type Ii Fibers

In literature, an inconsistency exists in the submaximal exercise intensity at which type II fibers are activated. In the present study, the recruitment of type I and II fibers was investigated from the very beginning and throughout a 45-min cycle exercise at 75% of the maximal oxygen uptake, which corresponded to 38% of the maximal dynamic muscle force. Biopsies of the vastus lateralis muscle were taken from six subjects at rest and during the exercise, two at each time point. From the first biopsy single fibers were isolated and characterized as type I and II, and phosphocreatine-to-creatine (PCr/Cr) ratios and periodic acid-Schiff (PAS) stain intensities were measured. Cross sections were cut from the second biopsy, individual fibers were characterized as type I and II, and PAS stain intensities were measured. A decline in PCr/Cr ratio and in PAS stain intensity was used as indication of fiber recruitment. Within 1 min of exercise both type I and, although to a lesser extent, type II fibers were recruited. Furthermore, the PCr/Cr ratio revealed that the same proportion of fibers was recruited during the whole 45 min of exercise, indicating a rather constant recruitment. The PAS staining, however, proved inadequate to fully demonstrate fiber recruitment even after 45 min of exercise. We conclude that during cycling exercise a greater proportion of type II fibers is recruited than previously reported for isometric contractions, probably because of the dynamic character of the exercise. Furthermore, the PCr/Cr ratio method is more sensitive in determining fiber activation than the PAS stain intensity method.

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 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.

scholarly journals Velocity, force, power, and Ca2+ sensitivity of fast and slow monkey skeletal muscle fibers

1998 ◽  
Vol 84 (5) ◽  
pp. 1776-1787 ◽  
Author(s):  
Robert H. Fitts ◽  
Sue C. Bodine ◽  
Janell G. Romatowski ◽  
Jeffrey J. Widrick
Keyword(s):  
Peak Power ◽  
Fiber Type ◽  
Medial Gastrocnemius ◽  
Type I ◽  
Fiber Types ◽  
Type Ii ◽  
Shortening Velocity ◽  
Hybrid Fibers ◽  
Slow Type ◽  
Type Ii Fibers

In this study, we determined the contractile properties of single chemically skinned fibers prepared from the medial gastrocnemius (MG) and soleus (Sol) muscles of adult male rhesus monkeys and assessed the effects of the spaceflight living facility known as the experiment support primate facility (ESOP). Muscle biopsies were obtained 4 wk before and immediately after an 18-day ESOP sit, and fiber type was determined by immunohistochemical techniques. The MG slow type I fiber was significantly smaller than the MG type II, Sol type I, and Sol type II fibers. The ESOP sit caused a significant reduction in the diameter of type I and type I/II (hybrid) fibers of Sol and MG type II and hybrid fibers but no shift in fiber type distribution. Single-fiber peak force (mN and kN/m2) was similar between fiber types and was not significantly different from values previously reported for other species. The ESOP sit significantly reduced the force (mN) of Sol type I and MG type II fibers. This decline was entirely explained by the atrophy of these fiber types because the force per cross-sectional area (kN/m2) was not altered. Peak power of Sol and MG fast type II fiber was 5 and 8.5 times that of slow type I fiber, respectively. The ESOP sit reduced peak power by 25 and 18% in Sol type I and MG type II fibers, respectively, and, for the former fiber type, shifted the force-pCa relationship to the right, increasing the Ca2+ activation threshold and the free Ca2+concentration, eliciting half-maximal activation. The ESOP sit had no effect on the maximal shortening velocity ( V o) of any fiber type. V o of the hybrid fibers was only slightly higher than that of slow type I fibers. This result supports the hypothesis that in hybrid fibers the slow myosin heavy chain would be expected to have a disproportionately greater influence on V o.

scholarly journals Histochemical, biochemical, and ultrastructural analyses of single human muscle fibers, with special reference to the C-fiber population.

1992 ◽  
Vol 40 (4) ◽  
pp. 563-568 ◽  
Author(s):  
R S Staron ◽  
R S Hikida
Keyword(s):  
Fiber Type ◽  
Vastus Lateralis ◽  
Oxidative Capacity ◽  
Vastus Lateralis Muscle ◽  
Type I ◽  
Fiber Types ◽  
Heavy Chains ◽  
C Fibers ◽  
C Fiber ◽  
Ph Range

A muscle biopsy from the vastus lateralis muscle of a strength-trained woman was found to contain an unusual fiber type composition and was analyzed by histochemical, biochemical, and ultrastructural techniques. Special attention was given to the C-fibers, which comprised over 15% of the total fiber number in the biopsy. The mATPase activity of the C-fibers remained stable to varying degrees over the pH range normally used for routine mATPase histochemistry. Although a continuum existed, the C-fibers were histochemically subdivided into three main fiber types: IC, IIC, and IIAC. The IC fibers were histochemically more similar to the Type I, the IIAC were more similar to the Type IIA, and the IIC were darkly stained throughout the pH range. Biochemical analysis revealed that all C-fibers coexpressed myosin heavy chains (MHC) I and IIa in variable ratios. The histochemical staining intensity correlated with the myosin heavy chain composition such that the Type IC fibers contained a greater ratio of MHCI/MHCIIa, the IIAC contained a greater ratio of MHCIIa/MHCI, and the Type IIC contained equal amounts of these two heavy chains. Ultrastructural data of the C-fiber population revealed an oxidative capacity between fiber Types I and IIA and suggested a range of mitochondrial volume percent from highest to lowest such that I greater than IC greater than IIC greater than IIA-C greater than IIA. Under physiological conditions, it appears that the IC fibers represent Type I fibers that additionally express some fast characteristics, whereas the Type IIAC are Type IIA fibers that additionally express some slow characteristics. Fibers expressing a 50:50 mixture of MHCI and MHCIIa (IIC fibers) were rarely found. It is not known whether C-fibers represent a distinct population between the fast- and slow-twitch fibers that is specifically adapted to a particular usage or whether they are transforming fibers in the process of going from fast to slow or slow to fast.

scholarly journals Myoglobin levels in individual human skeletal muscle fibers of different types.

1984 ◽  
Vol 32 (11) ◽  
pp. 1211-1216 ◽  
Author(s):  
P M Nemeth ◽  
O H Lowry
Keyword(s):  
Lactate Dehydrogenase ◽  
Citrate Synthase ◽  
Vastus Lateralis ◽  
Muscle Fibers ◽  
Human Muscle ◽  
Oxidative Enzymes ◽  
Vastus Lateralis Muscle ◽  
Type I ◽  
Trained Athlete ◽  
Fiber Types

An attempt was made to determine the relationship of myoglobin content to specific fiber types in human muscle. Biopsies were obtained from biceps brachii, vastus lateralis, and gastrocnemius muscles of untrained subjects and from the vastus lateralis muscle of a highly trained athlete at peak training and at intervals of no training (detraining). Individual muscle fibers were assayed, by quantitative microanalytical methods, for myoglobin, lactate dehydrogenase, malate dehydrogenase, citrate synthase, beta-hydroxyacyl-coenzyme A dehydrogenase, and adenylokinase activities all on the same fiber. The enzyme levels were used to classify the fibers into type I or II. The results show that the content of myoglobin in human muscle does not differ greatly between fiber types in contrast to other species. The type II fibers contained, on the average, at least two-thirds as much myoglobin as type I fibers. The concentration of myoglobin did not change in either fiber type during detraining (84 days), despite marked changes in lactate dehydrogenase, adenylokinase and the three oxidative enzymes.

Oxidative capacity of human muscle fiber types: effects of age and training status

1995 ◽  
Vol 78 (6) ◽  
pp. 2033-2038 ◽  
Author(s):  
D. N. Proctor ◽  
W. E. Sinning ◽  
J. M. Walro ◽  
G. C. Sieck ◽  
P. W. Lemon
Keyword(s):  
Succinate Dehydrogenase ◽  
Vastus Lateralis ◽  
Muscle Fibers ◽  
Oxidative Capacity ◽  
Muscle Fiber Types ◽  
Type I ◽  
Fiber Types ◽  
Training Status ◽  
Type Ii ◽  
And Training

Morphometry and oxidative capacity of slow-twitch (type I) and fast-twitch (type IIa and IIb) muscle fibers obtained from vastus lateralis needle biopsies were compared between younger (21-30 yr) and older (51-62 yr) normal fit (maximal O2 uptake = 47.0 vs. 32.3 ml.kg-1.min-1) and endurance-trained (66.3 vs. 52.7 ml.kg-1.min-1) men (n = 6/group). The older groups had smaller type IIa (31%) and IIb (40%) fiber areas and fewer capillaries surrounding these fibers than did younger groups. The reduced type II fiber areas and capillary contacts associated with aging were also observed in the older trained men. However, the capillary supply per unit type II fiber area was not affected by age but was enhanced by training. Additionally, on the basis of quantitative histochemical analysis, succinate dehydrogenase activities of type IIa fibers in the older trained men [4.07 +/- 0.68 (SD) mmol.min-1.l-1] were similar to those observed in younger trained men (4.00 +/- 0.48 mmol.min-1.l-1) and twofold higher than in older normal fit men (2.01 +/- 0.65 mmol.min-1.l-1; age x fitness interaction, P < 0.05). Type I muscle fibers were unaffected by age but were larger and had more capillary contacts and higher succinate dehydrogenase activities in the trained groups. The findings of this study suggest that aging results in a decrease in type II fiber size and oxidative capacity in healthy men and that this latter effect can be prevented by endurance training. Conclusions regarding the effects of age and training status on muscle capillarization depend largely on how these data are expressed.

Effect of swim exercise training on human muscle fiber function

1989 ◽  
Vol 66 (1) ◽  
pp. 465-475 ◽  
Author(s):  
R. H. Fitts ◽  
D. L. Costill ◽  
P. R. Gardetto
Keyword(s):  
Exercise Training ◽  
Training Program ◽  
Fiber Type ◽  
Type I ◽  
Fiber Types ◽  
Marker Enzyme ◽  
Type Ii ◽  
Intensive Training ◽  
Type I Fibers ◽  
Type Ii Fibers

This study examined the effect of a typical collegiate swim-training program and an intensified 10-day training period on the peak tension (Po), negative log molar Ca2+ concentration (pCa)-force, and maximal shortening speed (Vmax) of the slow-twitch type I and fast-twitch type II fibers of the deltoid muscle. Over a 10-wk period, the swimmers averaged 4,266 +/- 264 m/day swimming intermittent bouts of front crawl, kicking, or pulling. The training program induced an almost twofold increase in the mitochondrial marker enzyme citrate synthase. Po of the single fibers was not altered by either the training or 10-day intensive training programs, and no significant differences were observed in the Po (kg/cm2) of type I compared with the type II fibers. The type II fiber diameters were significantly larger than the type I fibers (94 +/- 4 vs. 80 +/- 2 microns), and although fiber diameters were unaffected by the training, the 10-day intensive training significantly reduced the type II fiber diameter. The type I fibers from the trained swimmers showed pCa-force curves shifted to the right such that higher free Ca2+ levels were required to elicit a given percent of Po (for values less than 0.5 Po). The activation threshold (pCa) for the onset of tension and the pCa required to elicit one-half maximal tension were not altered by the training in either fiber type. Fiber Vmax (measured by the slack test) was fivefold higher in type II compared with type I fibers (4.85 +/- 0.50 vs. 0.86 +/- 0.04 fiber lengths/s). The exercise-training program significantly increased and decreased the Vmax of the slow and fast fibers, respectively. The 10 days of intensified training produced a further significant decrease in the Vmax of the type II fibers. After a period of detraining, the Vmax of both fiber types returned to the control level. The force-velocity relation was not significantly altered in either fiber type by the swim training; however, the intensified training significantly depressed the velocity of the type II fiber at all loads studied. The Vmax changes with exercise training are likely explained by an exercise-induced expression of fast myosin in slow fibers and slow myosin in fast fibers.

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