scholarly journals A monoclonal antibody to the Ca2+ -ATPase of cardiac sarcoplasmic reticulum cross-reacts with slow type I but not with fast type II canine skeletal muscle fibers: An immunocytochemical and immunochemical study

1988 ◽  
Vol 9 (2) ◽  
pp. 164-174 ◽  
Author(s):  
Annelise O. Jorgensen ◽  
Wayne Arnold ◽  
David R. Pepper ◽  
Steven D. Kahl ◽  
Frederick Mandel ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Monoclonal Antibody ◽  
Sarcoplasmic Reticulum ◽  
Muscle Fibers ◽  
Type I ◽  
Type Ii ◽  
Cardiac Sarcoplasmic Reticulum ◽  
Immunochemical Study ◽  
Skeletal Muscle Fibers ◽  
Slow Type

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.

Isoform-dependent Effects of Halothane in Human Skinned Striated Fibers

1996 ◽  
Vol 84 (5) ◽  
pp. 1138-1147 ◽  
Author(s):  
Benoit M. Tavernier ◽  
Elie Haddad ◽  
Pascal J. Adnet ◽  
Toussaint S. Etchrivi ◽  
Dominique Lacroix ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Muscle Fibers ◽  
Contractile Proteins ◽  
Hill Coefficient ◽  
Type I ◽  
Type Ii ◽  
Maximal Force ◽  
Skeletal Muscle Fibers ◽  
Type Ii Fibers ◽  
Ca Sensitivity

Background Reports of the effects of halothane on isoform contractile proteins of striated muscles are conflicting. To determine whether halothane affects cardiac and skeletal contractile proteins differently, the authors examined the effects of two doses of halothane (0.44 and 1.26 mM, equivalent to 0.75 and 2.25 vol%, respectively) on the Ca++ sensitivity and maximal force in human skinned cardiac, type I (slow twitch), and type II (fast twitch) skeletal muscle fibers. Methods Left ventricular muscle strips and skeletal muscle biopsy specimens were obtained from eight and ten patients undergoing cardiac and orthopedic surgery, respectively. Sarcolemma and sarcoplasmic reticulum were destroyed with ethylene glycol bis (beta-aminoethyl ether)-N,N,N',N'-tetraacetic acid plus Brij 58. Ca++ sensitivity was studied by observing the isometric tension developed by skinned fibers challenged with increasing concentrations of Ca++. Muscle fiber type was determined in each skeletal fiber by the difference in strontium-induced tension measurements. Results Halothane shifted the Ca++ tension curves toward higher Ca++ concentrations and increased the Ca++ concentrations for half-maximal activation in both cardiac and type I skeletal muscle fibers (from 1.96 microM and 1.06 microM under control conditions to 2.92 microM and 1.71 microM in presence of 0.75 vol% halothane, respectively) without changing the slope of this relationship (Hill coefficient). In contrast, no significant effect was observed in type II fibers. Halothane also decreased the maximal activated tension in the three groups of fibers with a lesser effect in type II fibers. Conclusions Halothane decreases Ca++ sensitivity and maximal force in human skinned cardiac and type I fibers at 20 degrees C. It is concluded that the negative inotropic effects of halothane depend on contractile proteins isoforms.

scholarly journals Effects of high-intensity intermittent exercise on the contractile properties of human type I and type II skeletal muscle fibers

2020 ◽  
Vol 128 (5) ◽  
pp. 1207-1216 ◽  
Author(s):  
Cedric. R. Lamboley ◽  
David M. Rouffet ◽  
Travis L. Dutka ◽  
Michael J. McKenna ◽  
Graham D. Lamb
Keyword(s):  
Skeletal Muscle ◽  
High Intensity ◽  
Intermittent Exercise ◽  
Muscle Fibers ◽  
Muscle Performance ◽  
Type I ◽  
Type Ii ◽  
Contractile Apparatus ◽  
Skeletal Muscle Fibers ◽  
Type Ii Fibers

This study identified important cellular changes occurring in human skeletal muscle fibers following high-intensity intermittent exercise: 1) a decrease in contractile apparatus Ca2+ sensitivity in type I but not type II fibers, 2) a decrease in specific force only in type II muscle fibers, and 3) a redox-dependent increase in Ca2+ sensitivity occurring only in type II fibers, which would help maintain muscle performance by countering the normal metabolite-induced decline in Ca2+ sensitivity.

Functional effects of uridine triphosphate on human skinned skeletal muscle fibers

1998 ◽  
Vol 76 (2) ◽  
pp. 110-117 ◽  
Author(s):  
R Vianna-Jorge ◽  
C F Oliveira ◽  
Y Mounier ◽  
G Suarez-Kurtz
Keyword(s):  
Skeletal Muscle ◽  
Sarcoplasmic Reticulum ◽  
Muscle Fibers ◽  
Fiber Types ◽  
Release Channel ◽  
Uridine Triphosphate ◽  
Skinned Muscle ◽  
Skeletal Muscle Fibers ◽  
Slow Type ◽  
Relationship Of

Chemically skinned human skeletal muscle fibers were used to study the effects of uridine triphosphate (UTP) on the tension-pCa relationship and on Ca2+ uptake and release by the sarcoplasmic reticulum (SR). Total replacement (2.5 mM) of adenosine triphosphate (ATP) with UTP (i) displaced the tension-pCa relationship to the left along the abcissae and increased maximum Ca2+-activated tension, both effects being larger in slow- than in fast-type fibers; (ii) markedly reduced Ca2+ uptake by the SR (evaluated by the caffeine-evoked tension) in both fiber types; (iii) had no effect on the rate of depletion of caffeine-sensitive Ca2+ stores during soaking in relaxing solutions; (iv) induced tension in slow- but not in fast-type fibers. The effects on the SR functional properties are consistent with the notion that UTP is a poor substitute for ATP as a substrate for the Ca ATPase pump and as an agonist of the ryanodine-sensitive Ca2+-release channel. The UTP-induced tension in human slow-type fibers is attributed to effect(s) of the nucleotide on the tension-pCa relationship of the contractile machinery. The present data reveal important differences between the effects of UTP on human versus rat muscle fibers.Key words: skinned muscle fiber, UTP-induced tension, tension-pCa relationship, sarcoplasmic reticulum, calcium transport.

scholarly journals BFR Exercise Increases S6K1 Phosphorylation in Type‐I and Type‐II Skeletal Muscle Fibers

2011 ◽  
Vol 25 (S1) ◽  
Author(s):  
David M Gundermann ◽  
Dillon K Walker ◽  
Christopher S Fry ◽  
Jared M Dickinson ◽  
Micah J Drummond ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Muscle Fibers ◽  
Type I ◽  
Type Ii ◽  
Skeletal Muscle Fibers

scholarly journals Catalase in skeletal muscle fibers.

1979 ◽  
Vol 27 (4) ◽  
pp. 814-819 ◽  
Author(s):  
K N Christie ◽  
P J Stoward
Keyword(s):  
Skeletal Muscle ◽  
Hydrogen Peroxide ◽  
Sarcoplasmic Reticulum ◽  
Skeletal Muscles ◽  
Thin Filament ◽  
Muscle Fibers ◽  
Type I ◽  
Skeletal Muscle Fibers ◽  
Type I Fibers

Catalase has been localized immunocytochemically with anti-bovine catalase in long thin filament structures in aerobic type I fibers in the skeletal muscles of normal and genetically dystrophic hamsters. The filaments range in length from 1 to 60 micron, are orientated regularly along the long axis of the fibers, and also seem to surround and project from muscle nuclei. The enzyme thus appears to be more prominent in the sarcoplasmic reticulum than in peroxisomes, and in this situation is suitably placed for destroying toxic hydrogen peroxide which may be continously generated in aerobic fibers.

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.

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