Metabolic capacity of individual muscle fibers from different anatomic locations.

1992 ◽  
Vol 40 (6) ◽  
pp. 819-825 ◽  
Author(s):  
B W Rosser ◽  
B J Norris ◽  
P M Nemeth

We studied muscle fibers by quantitative biochemistry to determine whether metabolic capacity varied among fibers of a given type as a function of their anatomic location. Muscles were selected from both contiguous and diverse anatomic regions within the rats studied. The individual fibers, classified into myosin ATPase fiber types by histochemical means, were assessed for fiber diameters and analyzed for the activities of enzymes representing major energy pathways: malate dehydrogenase (MDH, oxidative), lactate dehydrogenase (LDH, glycolytic), and adenylokinase (AK, high-energy phosphate metabolism). We found that neither the average activities of each of the three enzymes nor the fiber diameters varied in Type I or Type IIa fibers selected from superficial to deep portions of the triceps surae of the hindlimb. However, the IIb fibers in the deep region of this muscle group had significantly greater oxidative capacity, less glycolytic capacity, and smaller diameters than the superficially situated IIb fibers. Type IIa fibers in lateral gastrocnemius, extensor digitorum longus, psoas, diaphragm, biceps brachii, superficial masseter, and superior rectus muscles were highly variable in both diameter and enzyme profiles, with a correlation between MDH activity and fiber diameter. Therefore, our results show that both intermuscular and intramuscular metabolic variations exist in muscle fibers of a given type.

2011 ◽  
Vol 301 (4) ◽  
pp. R916-R925 ◽  
Author(s):  
Krystyna Banas ◽  
Charlene Clow ◽  
Bernard J. Jasmin ◽  
Jean-Marc Renaud

It has long been suggested that in skeletal muscle, the ATP-sensitive K+ channel (KATP) channel is important in protecting energy levels and that abolishing its activity causes fiber damage and severely impairs function. The responses to a lack of KATP channel activity vary between muscles and fibers, with the severity of the impairment being the highest in the most glycolytic muscle fibers. Furthermore, glycolytic muscle fibers are also expected to face metabolic stress more often than oxidative ones. The objective of this study was to determine whether the t-tubular KATP channel content differs between muscles and fiber types. KATP channel content was estimated using a semiquantitative immunofluorescence approach by staining cross sections from soleus, extensor digitorum longus (EDL), and flexor digitorum brevis (FDB) muscles with anti-Kir6.2 antibody. Fiber types were determined using serial cross sections stained with specific antimyosin I, IIA, IIB, and IIX antibodies. Changes in Kir6.2 content were compared with changes in CaV1.1 content, as this Ca2+ channel is responsible for triggering Ca2+ release from sarcoplasmic reticulum. The Kir6.2 content was the lowest in the oxidative soleus and the highest in the glycolytic EDL and FDB. At the individual fiber level, the Kir6.2 content within a muscle was in the order of type IIB > IIX > IIA ≥ I. Interestingly, the Kir6.2 content for a given fiber type was significantly different between soleus, EDL, and FDB, and highest in FDB. Correlations of relative fluorescence intensities from the Kir6.2 and CaV1.1 antibodies were significant for all three muscles. However, the variability in content between the three muscles or individual fibers was much greater for Kir6.2 than for CaV1.1. It is suggested that the t-tubular KATP channel content increases as the glycolytic capacity increases and as the oxidative capacity decreases and that the expression of KATP channels may be linked to how often muscles/fibers face metabolic stress.


1989 ◽  
Vol 66 (6) ◽  
pp. 2717-2720 ◽  
Author(s):  
F. S. Apple ◽  
P. A. Tesch

Individual human muscle fibers from the vastus lateralis were isolated from age-matched endurance-trained and strength-trained athletes and untrained controls. Slow- (ST) and fast-twitch (FT) fibers were assayed for total creatine kinase (CK), CK-MB, total lactate dehydrogenase (LD), the LD isozyme that predominates in the heart muscle of most vertebrates (LD1), and citrate synthase (CS). Regardless of training of the athletes, both CK-MB and CS were higher in ST than in FT fibers. Also, irrespective of fiber type, CK-MB and CS were greatest in the endurance-trained group. A positive correlation existed between CK-MB and CS, relating oxidative capacity of individual fibers with CK-MB. Total CK varied little among the fiber types, trained groups, or controls. Total LD in FT fibers was greater than in ST fibers in all groups, with only ST fibers from the endurance-trained group containing substantial amounts of LD1. These findings suggest that specific training, endurance exercise, causes a favorable metabolic adaptation of CK and LD isozymes at the individual fiber level, allowing for the muscle to cope with increased energy demands during prolonged exercise.


1987 ◽  
Vol 63 (3) ◽  
pp. 1076-1082 ◽  
Author(s):  
G. C. Sieck ◽  
R. D. Sacks ◽  
C. E. Blanco

The oxidative capacity and cross-sectional area of muscle fibers were compared between the costal and crural regions of the cat diaphragm and across the abdominal-thoracic extent of the muscle. Succinate dehydrogenase (SDH) activity of individual fibers was quantified using a microphotometric procedure implemented on an image-processing system. In both costal and crural regions, population distributions of SDH activities were unimodal for both type I and II fibers. The continuous distribution of SDH activities for type II fibers indicated that no clear threshold exists for the subclassification of fibers based on differences in oxidative capacity (e.g., the classification of fast-twitch glycolytic and fast-twitch oxidative glycolytic fiber types). No differences in either SDH activity or cross-sectional area were noted between fiber populations of the costal and crural regions. Differences in SDH activity and cross-sectional area were noted, however, between fiber populations located on the abdominal and thoracic sides of the costal region. Both type I and II fibers on the abdominal side of the costal diaphragm were larger and more oxidative than comparable fibers on the thoracic side.


1993 ◽  
Vol 75 (6) ◽  
pp. 2689-2695 ◽  
Author(s):  
B. D. Johnson ◽  
G. C. Sieck

In this study, we examined whether exhaustive activation reduces succinate dehydrogenase (SDH) activity in diaphragm muscle fibers. In adult male rats (approximately 300 g), the costal diaphragm was excised and positioned in a chamber perfused with mammalian Ringer solution kept at 26 degrees C and oxygenated with 95% O2–5% CO2. The muscle was stimulated directly at 10 or 75 Hz in trains of 500 ms duration (1/s) for 8 min. An adjacent unstimulated segment of muscle served as control. The two muscle segments were frozen, and serial sections were stained for myofibrillar adenosinetriphosphatase activity after alkaline and acid preincubation to classify type I, IIa, and IIb fibers. The extent of glycogen utilization was also examined histochemically to confirm exhaustive activation of muscle fibers. SDH activity was quantified using a microdensitometric procedure implemented on an image-processing system. Exhaustive activation at both 10 and 75 Hz caused a significant decrease in SDH activity of all fiber types, with the decrease after 10-Hz stimulation being greater than that after 75-Hz stimulation. At both stimulation frequencies, type IIb fibers demonstrated the greatest decrease in SDH activity (36% after 10-Hz and 27% after 75-Hz stimulation), whereas type I and IIa fibers both displayed reductions of approximately 27 and approximately 19% after 10- and 75-Hz stimulation, respectively. The greater reduction of SDH activity in type IIb fibers indicates an inverse relationship between activation-induced reductions in SDH activity and fiber oxidative capacity.(ABSTRACT TRUNCATED AT 250 WORDS)


1995 ◽  
Vol 78 (6) ◽  
pp. 2033-2038 ◽  
Author(s):  
D. N. Proctor ◽  
W. E. Sinning ◽  
J. M. Walro ◽  
G. C. Sieck ◽  
P. W. Lemon

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.


2019 ◽  
Vol 67 (12) ◽  
pp. 891-900 ◽  
Author(s):  
Lauren Larson ◽  
Jessica Lioy ◽  
Jordan Johnson ◽  
Scott Medler

Skeletal muscles comprise hundreds of individual muscle fibers, with each possessing specialized contractile properties. Skeletal muscles are recognized as being highly plastic, meaning that the physiological properties of single muscle fibers can change with appropriate use. During fiber type transitions, one myosin heavy chain isoform is exchanged for another and over time the fundamental nature of the fiber adapts to become a different fiber type. Within the rat triceps surae complex, the soleus muscle starts out as a muscle comprised of a mixture type IIA and type I fibers. As neonatal rats grow and mature, the soleus undergoes a near complete transition into a muscle with close to 100% type I fibers at maturity. We used immunohistochemistry and single fiber SDS-PAGE to track the transformation of type IIA into type I fibers. We found that transitioning fibers progressively incorporate new myofibrils containing type I myosin into existing type IIA fibers. During this exchange, distinct type I-containing myofibrils are segregated among IIA myofibrils. The individual myofibrils within existing muscle fibers thus appear to represent the functional unit that is exchanged during fiber type transitions that occur as part of normal muscle development:


1999 ◽  
Vol 86 (1) ◽  
pp. 335-340 ◽  
Author(s):  
Varvara P. Grichko ◽  
Gwen J. Gettelman ◽  
Jeffrey J. Widrick ◽  
Robert H. Fitts

Results from the Russian Cosmos program suggest that the rhesus monkey is an excellent model for studying weightlessness-induced changes in muscle function. Consequently, the purpose of this investigation was to establish the resting levels of selected substrate and enzymes in individual slow- and fast-twitch muscle fibers of the rhesus monkey. A second objective was to determine the effect of an 18-day sit in the Spacelab experiment-support primate facility [Experimental System for the Orbiting Primate (ESOP)]. Muscle biopsies of the soleus and medial gastrocnemius muscles were obtained 1 mo before and immediately after an 18-day ESOP sit. The biopsies were freeze-dried, and individual fibers were isolated and assayed for the substrates glycogen and lactate and for the high-energy phosphates ATP and phosphocreatine. Fiber enzyme activity was also determined for the glycolytic enzymes phosphofructokinase and lactate dehydrogenase (LDH) and for the oxidative markers 3-hydroxyacyl-CoA dehydrogenase (β-OAC) and citrate synthase. Consistent with other species, the fast type II fibers contained higher glycogen content than did the slow type I fibers. The ESOP sit had no significant effects on the metabolic profile of the slow fibers of either muscle or the fast fibers of the soleus. However, the fast gastrocnemius fibers showed a significant decline in phosphocreatine and an increase in lactate. Also, similar to other species, the fast fibers contained significantly higher LDH activities and lower 3-hydroxyacyl-CoA dehydrogenase activities. For the muscle enzymes, the quantitatively most important effect of the ESOP sit occurred with LDH where activities increased in all fiber types postsit except the slow type I fiber of the medial gastrocnemius.


1992 ◽  
Vol 263 (5) ◽  
pp. R1093-R1098 ◽  
Author(s):  
S. K. Powers ◽  
D. Criswell ◽  
F. K. Lieu ◽  
S. Dodd ◽  
H. Silverman

Limited data exist concerning the effects of exercise training on cellular oxidative capacity in the diaphragm of senescent animals. In this study we examined the changes in cellular oxidative capacity, muscle cell cross-sectional area (CSA), and capillarity within the costal diaphragm of senescent animals after a 10-wk endurance-training program. Twelve 24-mo-old female Fischer 344 rats were divided into either a sedentary control group (n = 6) or exercise training group (n = 6). The trained animals exercised on a motor-driven treadmill (60 min/day, 5 days/wk) at a work rate equal to approximately 55-65% VO2max. Capillaries were identified histologically and fiber types determined using adenosinetriphosphatase (ATPase) histochemistry. Succinate dehydrogenase (SDH) activity and CSA in individual fibers were measured using a computerized image analysis system. Exercise training did not increase (P > 0.05) the capillary-to-fiber ratio for any fiber type. However, training significantly decreased CSA (P < 0.05) and increased capillary density (capillary number/CSA) (P < 0.05) in type I, type IIa, and type IIb fibers. Furthermore, exercise training resulted in small but significant increase in SDH activity (P < 0.05) in type I and IIa fibers, whereas training did not alter SDH activity (P > 0.05) in type IIb fibers. These data demonstrate that endurance training in senescent animals results in small relative improvements in both oxidative capacity and capillary density in costal diaphragmatic type I and IIa muscle fibers. The increase in both capillary density and fiber SDH activity was largely due to a reduction in fiber CSA.


1985 ◽  
Vol 54 (4) ◽  
pp. 818-836 ◽  
Author(s):  
R. P. Dum ◽  
M. J. O'Donovan ◽  
J. Toop ◽  
R. E. Burke

The properties of flexor digitorum longus (FDL) muscles and of individual motor units were studied in cats 30-50 wk after self-reinnervation by FDL motoneurons (FDL----FDL) or cross-reinnervation by soleus (SOL) motoneurons (SOL----FDL). Individual motor units were functionally isolated by intracellular recording and stimulation of identified SOL alpha-motoneurons. Glycogen-depletion methods permitted histochemical study of muscle fibers belonging to physiologically characterized muscle units. The observations were compared with data from normal cat FDL muscles and motor units (27). Intentionally self-reinnervated FDL muscles (FDL----FDL; n = 5) were normal in size and wet weight. FDL----FDL motor units could be classified into the same physiological categories found in normal FDL [types: fast contracting, fatigable (FF), fast contracting, fatigue resistant (FR), and slow (S); n = 24], with approximately the same proportions as normal. The histochemical muscle fiber types associated with these categories were also qualitatively normal although there was evidence of marked distortion of the normal histochemical mosaic. These data confirm other studies of self-reinnervation and suggest that self-reinnervation can produce complete interconversion of muscle fiber types. Cross-reinnervation of FDL muscle by SOL motoneurons (SOL----FDL; n = 12) produced muscles that were smaller (about half the normal wet weight) and more red than normal. SOL----FDL muscle contracted more slowly than normal or FDL----FDL muscles and had much higher proportions of histochemical type I muscle fibers. In those SOL----FDL muscles, in which little or no unwanted self-reinnervation could be demonstrated, greater than 95% of the muscle fibers were type I. Forty-one individual motor units in SOL----FDL muscles were isolated by intracellular penetration in functionally identified SOL alpha-motoneurons. Their muscle units were all type S by physiological criteria (absence of "sag" in unfused tetani and marked resistance to fatigue). SOL----FDL muscle units had contraction times and fatigue properties that were essentially identical to those of type S units in the normal FDL. All of the seven units, successfully studied by glycogen depletion, exhibited histochemical type I fibers. SOL motoneurons that innervated FDL muscle units had slightly shorter afterhyperpolarization durations than normal SOL cells, but axonal conduction velocities were normal.(ABSTRACT TRUNCATED AT 400 WORDS)


1988 ◽  
Vol 36 (7) ◽  
pp. 775-782 ◽  
Author(s):  
P Frémont ◽  
P M Charest ◽  
C Côté ◽  
P A Rogers

The objectives of the present study were to determine if carbonic anhydrase III (CA III) demonstrated a specific association for any particular organelle or structure of the skeletal muscle cell and to quantify the activity and content of this enzyme in different types of skeletal muscle fibers. Ultrastructural localization of CA III in the soleus (SOL), deep vastus lateralis (DVL), and superficial vastus lateralis (SVL), composed of predominantly type I, IIa, and IIb fibers, respectively, was performed using a high-resolution immunocytochemical technique and antibody specific for CA III on ultra-thin sections of skeletal muscle embedded in the water-soluble medium polyvinyl alcohol (PVA). The results indicated a uniform distribution of CA III within the sarcomere. Mitochondria, nuclei, triads, Z-, and M-bands were not specifically labeled. Immunoblotting of washed myofibril preparations did not show any detectable CA III associated with this structure. In addition to quantification of the immunogold labeling, CA III activity and content were assayed in the post-mitochondrial supernatant of the three muscles. In the SOL, these values were found to be 3.6-7.6 times higher than in the DVL. The SVL showed a labeling intensity slightly higher than background level, while the enzyme activity and content were indistinguishable from background levels. We therefore conclude that CA III is randomly distributed in the cytoplasm of the three muscle fiber types and that the relative CA III content and activity in the three muscles studied is SOL greater than DVL greater than SVL approximately equal to 0.


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