Stretch-induced enhancement of mechanical work production in frog single fibers and human muscle

Takarada, Yudai, Hiroyuki Iwamoto, Haruo Sugi, YuichiHirano, and Naokata Ishii. Stretch-induced enhancement ofmechanical work production in frog single fibers and human muscle.J. Appl. Physiol. 83(5):1741-1748, 1997.The relations between the velocity of prestretchand the mechanical energy liberated during the subsequent isovelocityrelease were studied in contractions of frog single fibers and humanmuscles. During isometric contractions of frog single fibers, a rampstretch of varied velocity (amplitude, 0.02 fiber length; velocity,0.08-1.0 fiber length/s) followed by a release (amplitude, 0.02 fiber length; velocity, 1.0 fiber length/s) was given, and the amountof work liberated during the release was measured. For human muscles,elbow flexions were performed with a prestretch of variedvelocity (range, 40°; velocity, 30-180°/s) followed by anisokinetic shortening (velocity, 90°/s). In both frog single fibersand human muscles, the work production increased with both the velocityof stretch and the peak of force attained before the release up to acertain level; thereafter it declined with the further increases ofthese variables. In human muscles, the enhancement of work productionwas not associated with a significant increase in integratedelectromyogram. This suggests that changes in intrinsic mechanicalproperties of muscle fibers play an important role in thestretch-induced enhancement of work production.

     

Calf muscle work and segment energy changes in human treadmill walking

The relation between changes in potential and kinetic energy in a seven-segment model of the human body and the work of m. triceps surae was investigated in four subjects walking on a treadmill at speeds between 0.5 and 2.0 m/s. Segment energy levels were determined by means of tachometers attached with strings to various points on the subject's body. Muscle work was assessed by electromyogram to force processing. M. triceps surae is active during stance, first doing negative (eccentric) work and ending with a short period of positive (concentric) work at “push-off”. It turned out that in normal walking these muscles provide the major part of positive work for the initiation of swing at push-off. Only at large step lengths, when push-off starts well before contralateral heel contact, is there a minor pushing forward of the trunk. In the negative work phase, m. triceps surae seem to check the forward speed of the trunk. A related decrease of trunk kinetic energy is not present, however, but this may be obscured by the simultaneous action of m. quadriceps femoris and, in a later stage, by a transfer of energy from the decelerating contralateral (swing) leg to the trunk. Energy of the trunk segment shows a sharp decline in double stance and a more gradual increase in the first half of single stance. Evidence is given that this effect is due to quadriceps action in the knee flexion-extension movement during stance. The presented results are incorporated in a general picture of energy flows in human walking.     

Hypertrophy of rat plantaris muscle fibers after voluntary running with increasing loads

There have been no systematic comparisons ofskeletal muscle adaptations in response to voluntary wheel runningunder controlled loading conditions. To accomplish this, a voluntaryrunning wheel for rats and mice was developed in which a known load canbe controlled and monitored electronically. Five-week-old maleSprague-Dawley rats (10 rats/group) were assigned randomly to either a1) sedentary control group(Control); 2) voluntary exercisedwith no load (Run-No-Load) group; or3) voluntary exercised withadditional load (Run-Load) group for 8 wk. The load for the Run-Loadgroup was progressively increased to reach ~60% of body weightduring the last week of training. The proportions of fast glycolytic(FG), fast oxidative glycolytic (FOG), or slow oxidative (SO) fibers inthe plantaris were similar in all groups. The absolute and relativeplantaris weights were greater in the Run-Load group compared with theControl and Run-No-Load groups. The mean fiber cross-sectional areas of FG, FOG, and SO fibers were 20, 25, and 15% greater in the Run-Load than in Control rats. In addition, these fiber types were 16, 21, and12% larger in Run-Load than in Run-No-Load rats. The muscle weightsand mean cross-sectional areas of each fiber type were highlycorrelated with the average running distances and total work performedin the Run-Load, but not the Run-No-Load, group. The slope of therelationship between fiber size and running distance and total workperformed was significant for each fiber type but was higher for FG andFOG fibers compared with SO fibers. These data show that the load on arat running voluntarily can determine the magnitude of a hypertrophicresponse and the population of motor units that are recruited toperform at a given loading condition.

     

Myosin types in human skeletal muscle fibers

By combining enzyme histochemistry for fiber typing with immunohistochemistry for slow and fast myosin a correlation between fiber type and myosin type was sought in human skeletal muscle. Fiber typing was done by staining for myofibrillar ATPases after preincubation at discriminating pH values. Myosin types were discriminated using type specific anti-rabbit myosin antibodies shown to cross-react with human myosin and were visualized by a protein A-peroxidase method. Type I fibers were shown to contain slow myosin only, type IIA and IIB fibers fast myosin only, and type IIC fibers both myosins in various proportions. When muscle biopsies from well-trained athletes were investigated essentially the same staining pattern was observed. However, rarely occurring type I fibers with high glycolytic activity were detected containing additional small amounts of fast myosin and occasional type IIA fibers had small amounts of slow myosin. Based on the observation of various fiber types in which slow and fast myosin coexist we propose a dynamic continuum of fibers encompassing all fiber types.     

Myosin types in human skeletal muscle fibers

Summary By combining enzyme histochemistry for fiber typing with immunohistochemistry for slow and fast myosin a correlation between fiber type and myosin type was sought in human skeletal muscle. Fiber typing was done by staining for myofibrillar ATPases after preincubation at discriminating pH values. Myosin types were discriminated using type specific anti-rabbit myosin antibodies shown to cross-react with human myosin and were visualized by a protein A-peroxidase method. Type I fibers were shown to contain slow myosin only, type IIA and IIB fibers fast myosin only, and type IIC fibers both myosins in various proportions. When muscle biopsies from well-trained athletes were investigated essentially the same staining pattern was observed. However, rarely occurring type I fibers with high glycolytic activity were detected containing additional small amounts of fast myosin and occasional type IIA fibers had small amounts of slow myosin. Based on the observation of various fiber types in which slow and fast myosin coexist we propose a dynamic continuum of fibers encompassing all fiber types.     

Effect of microgravity on metabolic enzymes of individual muscle fibers

Eleven enzymes were measured in individual fibers of soleus and tibialis anterior (TA) muscles from two flight and two control (synchronous) animals. There were five enzymes of glycogenolytic metabolism: phosphorylase, glucose-6-phosphate isomerase, glycerol-3-phosphate dehydrogenase, pyruvate kinase, and lactate dehydrogenase (group GLY); five of oxidative metabolism: citrate synthase, malate dehydrogenase, beta-hydroxyacyl-CoA dehydrogenase, 3-ketoacid CoA-transferase, and mitochondrial thiolase (group OX); and hexokinase, subserving both groups. Fiber size (dry weight per unit length) was reduced about 35% in both muscles. On a dry weight basis, hexokinase levels were increased 100% or more in flight fibers from both soleus and TA. Group OX enzymes increased 56-193% in TA without significant change in soleus. Group GLY enzymes increased an average of 28% in soleus fibers but underwent, if anything, a modest decrease (20%) in TA fibers. These changes in composition of TA fibers were those anticipated for a conversion of about half of the originally predominant fast glycolytic fibers into fast oxidative glycolytic fibers. Calculation on the basis of fiber length, rather than dry weight, gave an estimate of absolute enzyme changes: hexokinase was still calculated to have increased in both soleus and TA fibers, but only by 50 and 25%, respectively. Three of the OX enzymes were, on this basis, unchanged in TA fibers, but 3-ketoacid CoA-transferase and thiolase had still nearly doubled, whereas TA GLY enzymes had fallen about 40%. In soleus fibers, absolute levels of OX enzymes had decreased an average of 25% and GLY enzymes were marginally decreased.     

Changes in muscle free carnitine and acetylcarnitine with increasing work intensity in the Thoroughbred horse

Treadmill exercise in Thoroughbred horses of 2 min duration and increasing intensity resulted in increased formation and accumulation of acetylcarnitine in the working middle gluteal muscle. At high work intensities a plateau in acetylcarnitine formation was reached corresponding to approximately 70% of the total carnitine pool (approx. 30 mmol.kg-1 dry muscle). Formation of acetylcarnitine was mirrored by an equal fall in the free carnitine content, which stabilised, at the highest work intensities, at around 8 mmol.kg-1 dry muscle. Acetylcarnitine and carnitine reached their point of maximum change at a work intensity just below that resulting in the rapid production and accumulation of lactate and glycerol 3-phosphate. It is possible that the formation of acetylcarnitine is important in the regulation of the intramitochondrial acetyl CoA/CoA ratio; equally these changes may represent a blocking mechanism aimed at preventing the transfer of unwanted free fatty acids (as acylcarnitines) into the mitochondria at work intensities where they could contribute little to energy production.     

Polarization changes in light diffracted from contracting muscle fibers

Single fibers were isolated from the semitendinosus muscle of frog and illuminated with an He-Ne laser. The polarization of the laser beam was varied by a photoelastic modulator. The time course of the degree of polarization of light diffracted from the muscle fiber during an isometric contraction was measured directly with a time resolution of 1 ms. Tension, sarcomere length, and diffraction intensity were also measured. During the contraction cycle, the degree of polarization of the active fiber exhibited a biphasic variation relative to that of the resting fiber. Analysis identifies the movement of heavy meromyosin toward actin and the rise in myoplasmic calcium ion concentration as the main contributors to the polarization transient of active fibers. A quantitative theory describing the polarized diffraction from muscle fibers is formulated. There is good agreement between the theory and measurements.     

Polarization changes in light diffracted from contracting muscle fibers

Single fibers were isolated from the semitendinosus muscle of frog and illuminated with an He-Ne laser. The polarization of the laser beam was varied by a photoelastic modulator. The time course of the degree of polarization of light diffracted from the muscle fiber during an isometric contraction was measured directly with a time resolution of 1 ms. Tension, sarcomere length, and diffraction intensity were also measured. During the contraction cycle, the degree of polarization of the active fiber exhibited a biphasic variation relative to that of the resting fiber. Analysis identifies the movement of heavy meromyosin toward actin and the rise in myoplasmic calcium ion concentration as the main contributors to the polarization transient of active fibers. A quantitative theory describing the polarized diffraction from muscle fibers is formulated. There is good agreement between the theory and measurements.     

Lattice shrinkage with increasing resting tension in stretched, single skinned fibers of frog muscle.

The 1,0 lattice spacing d1,0 in chemically and mechanically skinned single fibers of frog muscle was measured at various sarcomere lengths, L, in the range from L = 2.1 to 6.0 microns by an x-ray diffraction method. In chemically skinned fibers, d1,0 decreased with a similar slope to that of mechanically skinned fibers up to L congruent to 3 microns, but beyond this point d1,0 steeply decreased with further stretching. This steep decrease in d1,0 could be ascribed mainly to an increase in the compressing force associated with the longitudinal extension of a remnant of the sarcolemma. In mechanically skinned fibers, the gradual decrease in d1,0 continued beyond filament overlap (L greater than or equal to 3.5 microns) and was highly proportional to a resting tension. This decrease in d1,0 at L greater than or equal to 3.5 microns could be ascribed to an increase in the force exerted by lateral elastic components, which is proportional to the longitudinal resting tension. A conceptual model is proposed of a network structure of elastic components in a sarcomere.