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Skeletal Muscle Adaptability: Significance for Metabolism and Performance

Bengt Saltin, Philip D. Gollnick

10.1002/cphy.cp100119

Source: Supplement 27: Handbook of Physiology, Skeletal Muscle

Originally published: 1983

Published online: January 2011

Full Article on Wiley Online Library



Abstract

The sections in this article are:

1 Motor Unit
1.1 Fibers per Motor Unit
1.2 Contractile Properties
1.3 Biochemical Basis for Differences in Twitch Properties
1.4 Histochemical Differentiation of Muscle Fibers
1.5 Ultrastructural Basis for Skeletal Muscle Fiber Typing
1.6 Maximal Contractile Force
1.7 Speed of Contraction
1.8 Fatigue Characteristics
1.9 Metabolic Characteristics
1.10 Ionic Composition of Skeletal Muscle
1.11 Summary
2 Muscle Fiber Composition in Human Skeletal Muscle
3 Motor‐Unit Recruitment
4 Adaptive Response in Skeletal Muscle
4.1 Muscle Size
4.2 Metabolic Capacity
5 Connective Tissue
6 Capillaries
6.1 Methodology
6.2 Anatomy
6.3 Capillary Density
6.4 Capillary Length and Diameter
6.5 Use and Disuse
6.6 Regulation
7 Significance of Adaptation
7.1 Muscular Size
7.2 Substrate Stores
7.3 Enzyme Activities
7.4 Summary
Figure 1. Figure 1.

Relationship between maximal speed of shortening and actin‐activated ATPase of myosin from a variety of animal species. Equation from the regression line is y = 0.34 + 1.37 x, and for the 2 variables, r = 0.97. [Plotted from original data published by Bárány 31.]
Figure 2. Figure 2.

Influence of pH on Ca2+‐activated ATPase activites of myosin from white [fast‐twitch, glycolytic (FG)] and red [fast‐twitch, oxidative, glycolytic (FOG)] portions of the vastus muscle and soleus [slow‐twitch, oxidative (SO)] muscle of the sedentary (○) and endurance‐trained (•) rats. ATPase activities were determined at 25°C. [From Watrus 715.]
Figure 3. Figure 3.

A: rat diaphragm, serial transverse sections. Left stained with antibody specific for alkali 1 light chain (anti‐Δ1); right stained with antibody for alkali 2 light chain (anti‐Δ2). Both antibodies react with same fibers (W, I, black R) that react with antibodies against whole white myosin. However, level of response to anti‐Δ2 is lower in fast‐twitch red fibers (black R) than in other fast‐twitch fibers (W, I). B: cat flexor digitorum longus, serial sections. Left, anti‐Δ1; right, anti‐Δ2. Response of most fast‐twitch fibers (W) is weak; compare with unreactive fibers (white R). However, level of response to anti‐Δ1 (left) is more intense in one type of red fibers (black R) than in other fast‐twitch fibers. Response to anti‐Δ2 is less intense in this fiber (black R) than in other fast‐twitch fibers. [From Gauthier 241.]
Figure 4. Figure 4.

Serial transverse‐sectioned frozen skeletal muscle from the lateral head of the gastrocnemius muscle of man (A) and the same muscle from rat (B). From top to bottom are the following stains (myofibrillar ATPase stained at pH 9.4 and preincubated at pH 10.3, 4.6, 4.3): nicotinamide adenine dinucleotide, reduced‐tetrazolium reductase (NADH); α‐GPDH, glycogen (periodic acid‐Schiff, PAS); capillaries (man = amylase‐treated sections stained with PAS; rat = alkaline phosphatase); and hematoxylin‐eosin.
Figure 5. Figure 5.

Part of a sarcomere from slow‐twitch, ST (micrograph and top panel), fast‐twitch, subtype a, FTa (middle panel), and fast‐twitch, subtype b, FTb (bottom panel) fibers in combination with a schematic drawing of the respective fiber types. [From Ängquist 9.]
Figure 6. Figure 6.

Important features of organization of motor units in medial gastrocnemius muscle of cat. Diameters of muscle fibers and unit mechanical responses are scaled appropriately for respective groups, representing typical observations. Shading in muscle fiber outlines denotes relative staining intensities found for each histochemical reaction (identified in the FF unit fibers). Note differences in pattern as well as intensity of staining in the oxidative enzyme reaction (3rd fiber from left in each unit sequence). Note also the somewhat smaller motoneuron innervating type S unit and relation between number of group la synapses and cell size; a low density of terminals (as in the FF unit) produces a relatively small la excitatory postsynaptic potential (EPSP), whereas increasing densities (in the FR and higher still in the type S unit) produce larger EPSPs. Motor unit type nomenclature: FF, fast twitch, fatiguable; FR, fast twitch, fatigue resistant; S, slow twitch. Histochemical profiles: FG, fast twitch, glycolytic; FOG, fast twitch, oxidative, glycolytic; SO, slow twitch, oxidative. These 2 systems are essentially interchangeable. [From Burke and Edgerton 98.]
Figure 7. Figure 7.

Examples of the 3 motor unit types found in human medial gastrocnemius. A, isometric twitch; B, isometric tetanus 10 pulses/s; C, isometric tetanus 20 pulses/s; and D, fatigue test, control and after 3,000 stimuli, expressed as a percentage of initial isometric tension. [From Garnett et al. 238.]
Figure 8. Figure 8.

Ca2+‐activated, K+‐activated, and actin‐activated ATPase activities of myosin from heart, soleus, red vastus, and white vastus muscles of sedentary and trained rats. Temperature, 37°C; pH 7.4. Vertical lines, SEM. *Sedentary vs. trained, P < 0.05. Ht, heart; SO, slow‐twitch, oxidative type from soleus; FOG, fast‐twitch, oxidative, glycolytic type from red vastus lateralis; FG, fast‐twitch, glycolytic type from white vastus lateralis.

Adapted from Watrus 715
Figure 9. Figure 9.

Predicted Vmax and apparent Km of actin‐activated ATPase activity of myosin from white vastus, red vastus, and soleus muscles of sedentary and trained rats. Vertical lines, SEM. FG, fast‐twitch, glycolytic type from white vastus; FOG, fast‐twitch, oxidative, glycolytic from red vastus; SO, slow‐twitch, oxidative type from soleus.

Adapted from Watrus 715
Figure 10. Figure 10.

The distribution of relative occurrence of ST fibers in vastus lateralis in young men and women.

Adapted from a study by Hedberg and Jansson 320; some results are presented in Saltin et al. 603
Figure 11. Figure 11.

Intrapair comparison of slow‐twitch fiber distribution of m. vastus lateralis in monozygous (•) and dizygous (○) twins. [From Komi et al. 432.]
Figure 12. Figure 12.

Relative occurrence of ST fibers in some muscles of the body. A: muscle samples are obtained by multiple needle biopsy samples or (B) postmortem within 24 h after death. [A from Sjøgaard 642 and G. Sjøgaard, unpublished material. B from Johnson et al. 407.]
Figure 13. Figure 13.

Schematic illustration of intensity of periodic acid‐Schiff (PAS) stain (glycogen) in human skeletal muscle fibers at rest and after various times during prolonged exercise at relative work intensities ranging from 31% to 85% of the subject's maximal oxygen uptake. Graph is a summary of several studies. Findings at 74% o2 max show the PAS stain evaluated by microphotometry, whereas in the other studies results are based on a subjective rating (dark = filled; and white = unfilled, with various levels between as crosshatched and hatched). [Data from Gollnick, Saltin, et al. 263,264,271,272. Findings at 74% o2 max from K. Vøllestad, unpublished material.]
Figure 14. Figure 14.

Changes in the percent water and concentration of protein in the sarcoplasmic and fibrillar fractions of human skeletal muscle as a result of growth and development.

Adapted from Dickerson and Widdowson 154
Figure 15. Figure 15.

Intracellular ion concentrations for human skeletal muscle from fetal life to adulthood. The data points marked (′) are averages of samples collected from the triceps brachii, vastus lateralis, and soleus of 6 male and 6 female adults. [Data from Dickerson and Widdowson 154, except those marked (′) from Sjøgaard 642.]
Figure 16. Figure 16.

Data are for muscle from human subjects ranging in age from 2 mo to 18 yr. Fiber areas for infants less than 1 yr are not plotted. A: relationship between age and muscle fiber cross‐sectional area in the lower limb muscles of humans. Equation of the regression line y = 115 + 111x. Between age and fiber area r = 0.92; between age and body height r = 0.98. B: relationship between age and muscle fiber cross‐sectional area in the upper limb muscles of humans. Equation of the regression line is y = 112 + 56x. Between age and fiber area r = 0.85 [Data from Aherne et al. 2.]
Figure 17. Figure 17.

A summary description of the relative occurrence of various fiber types in human skeletal muscle during gestation and 1st year of life. The slow‐twitch (ST) fibers are divided by size with the small fraction of Wohlfart's B fiber above the dashed line 727. [Data from Colling‐Saltin 124,126.]
Figure 18. Figure 18.

Relationship between cross‐sectional fiber area and lesser diameter in human skeletal muscle during gestation and 1st years of life (small graph), and adults (large graph). [Small graph from Colling‐Saltin 124; large graph from Sjøgaard 642.]
Figure 19. Figure 19.

Comparison of the number of fibers in a control and enlarged plantaris muscle of the rat. Muscular enlargement was induced either by ablation of the gastrocnemius muscle (•) or a combination of ablation of the gastrocnemius muscle and treadmill exercise (○). [From Gollnick et al. 276.]
Figure 20. Figure 20.

A plot of the number of fibers vs. total wet weight for the plantaris muscles. •, Control muscles (including normal weanling, sham‐operated, thyroidectomized, and control muscles from experimental animals); ○, muscles enlarged by ablation of the gastrocnemius muscle; and , muscles enlarged by ablation of the gastrocnemius muscle and exercise. The smallest muscle weighed 25 mg and the heaviest 712 mg. [From Gollnick et al. 276.]
Figure 21. Figure 21.

Time courses for changes in 2 mitochondrial enzymes and o2 max during physical conditioning and deconditioning. *Significant changes in time (paired t test) for the selected variables.

Adapted from Henriksson and Reitman 339
Figure 22. Figure 22.

Mean change in percent of succinate dehydrogenase (SDH) activity of vastus lateralis with different training procedures. Note that the mean values ± SD for the absolute activities are similar before the training started. N, no training; S, sprint; E, endurance trained; *, significant difference, P < 0.05.

Adapted from Saltin, Gollnick, et al. 604
Figure 23. Figure 23.

Mean values for 2 mitochondrial enzymes [citrate synthase and 3‐hydroxyacyl‐CoA dehydrogenase (HAD)] determined from muscle samples from vastus lateralis in 9 sea‐level residents at sea level and after an average 32‐wk stay (6–52 wk) at elevation 3,700 m and 16 men born and permanently living at this altitude. Note that high‐altitude residents are divided into 2 groups, those who were physically inactive (job and leisure time) and those who were active. Maximal oxygen uptake (ml · kg−1 · min−1) for the sea‐level residents was 39 ml and 36 ml · kg−1 · min−1 at sea level and high altitude, respectively; inactive high‐altitude residents had 28 ml and active 46 ml · kg−1 · min−1.

Adapted from Saltin et al. 605
Figure 24. Figure 24.

A: schematic representation of the vascular arrangement in the tenuissimus muscle. CA, central artery; CV, central vein; TA, transverse arteriole; TV, transverse venule. B: detailed schematic representation of the vascular architecture of the tenuissimus muscle. Arterial vessels, open; venous vessels, filled. Sections of different depth are made into the muscle at II, III, and IV. At I a projection of the pre‐ and postcapillary vessels is shown. The section at II shows the vessels above, at III at the same, and IV under the level of the central vessels. C: graphic representation of a small arteriole (ART) subdividing into capillaries. Capillaries then run parallel to the muscle fibers. [A adapted from Eriksson and Myrhage 197.]
Figure 25. Figure 25.

Capillaries per muscle fiber related to maximal oxygen uptake. Diagram includes mean values obtained from the following: PAS method, light microscopy (PAS + LM) studies, open symbols 5,6,522,524, and electron microscopy (EM) studies, closed symbols 74,386,387,388. Circles, females; triangles, males. P = 0.001; r = 0.917. [From E. Nygard and H. Schmalbruch, unpublished observations.]
Figure 26. Figure 26.

Mean values for number of capillaries per 1,000 μm2 of muscle fiber area. Bar A shows results from a group of sedentary subjects 603. Bars B and C show values before and after 8 wk of conditioning 6,426. Bar D shows values from well‐trained men 368,399,524,603. Bars M and N are values from subjects deconditioned for 7–14 days (ref. 426; B. Saltin, unpublished observations). Vo2 max below bars M and N was estimated from heart rate response to submaximal exercise (subjects were recovering from minor knee injury).
Figure 27. Figure 27.

Capillaries per fiber and fiber area in sea‐level residents at sea level and after an average 32 wk (6–52 wk) at elevation 3,500 m and in high‐altitude residents. For further details see Fig. 23.

Adapted from Saltin et al. 605
Figure 28. Figure 28.

A schematic summary with indication of relative importance of various energy stores and metabolic pathways for performance in strength, sprint, and endurance events. Included in the scheme are also indications of how oxygen delivery and the nervous system are interacting.
Figure 29. Figure 29.

A representation of the influence of changing the total enzyme concentration on the specific activity based on the rate (Vr). The velocity and any substrate concentration [S] can be estimated from the Michaelis constant (Km) and the maximal velocity (Vmax) for the equation . With a doubling of enzyme concentration, velocity of the reaction will be doubled at any substrate concentration. This relationship would be most important at low substrate concentrations where substrate could thereby be more efficiently directed into end‐terminal oxidative pathways. Conversely with a reduction in enzyme concentration such control would be lost. [From Gollnick and Saltin 257.]
Figure 30. Figure 30.

Summary of changes associated with a moderate (panel A) and a large (panel B) increase in o2max in response to physical conditioning. A: from longitudinal studies in which sedentary subjects were conditioned for 2–3 mo. B: (also longitudinal studies) subjects participated either in a conditioning program for 2–3 yr starting from a sedentary level [o2max 45 ml · kg−1 · min−1 185] or in an intense conditioning program for some months starting from very low o2max [34 ml O2‐kg−1 · min−1 602]. [A: circulatory data: 185,595,602. Leg blood flow and arteriovenous O2 differences are collected from several studies: 409,604,713 and B. Saltin, unpublished observations. Muscle data: 339 for enzymes, 8 for capillaries. B: central circulatory data: 185,602. Leg arteriovenous O2 differences: 602; muscle capillarization and enzyme data are from unpublished studies by B. Saltin, J. Halkjær‐Kristensen, and T. Ingemann‐Hansen.]
Figure 31. Figure 31.

Succinate dehydrogenase activity (μmol · g−1 wet wt · min−1) in trained (T) and nontrained (NT) leg (left), respiratory quotient (RQ) values (middle), and release/uptake of lactate (right) for both legs during a posttraining metabolic study. Means ± SE are given. * Significant difference between trained and nontrained leg (P < 0.05).

Adapted from Henriksson 333


Figure 1.

Relationship between maximal speed of shortening and actin‐activated ATPase of myosin from a variety of animal species. Equation from the regression line is y = 0.34 + 1.37 x, and for the 2 variables, r = 0.97. [Plotted from original data published by Bárány 31.]



Figure 2.

Influence of pH on Ca2+‐activated ATPase activites of myosin from white [fast‐twitch, glycolytic (FG)] and red [fast‐twitch, oxidative, glycolytic (FOG)] portions of the vastus muscle and soleus [slow‐twitch, oxidative (SO)] muscle of the sedentary (○) and endurance‐trained (•) rats. ATPase activities were determined at 25°C. [From Watrus 715.]



Figure 3.

A: rat diaphragm, serial transverse sections. Left stained with antibody specific for alkali 1 light chain (anti‐Δ1); right stained with antibody for alkali 2 light chain (anti‐Δ2). Both antibodies react with same fibers (W, I, black R) that react with antibodies against whole white myosin. However, level of response to anti‐Δ2 is lower in fast‐twitch red fibers (black R) than in other fast‐twitch fibers (W, I). B: cat flexor digitorum longus, serial sections. Left, anti‐Δ1; right, anti‐Δ2. Response of most fast‐twitch fibers (W) is weak; compare with unreactive fibers (white R). However, level of response to anti‐Δ1 (left) is more intense in one type of red fibers (black R) than in other fast‐twitch fibers. Response to anti‐Δ2 is less intense in this fiber (black R) than in other fast‐twitch fibers. [From Gauthier 241.]



Figure 4.

Serial transverse‐sectioned frozen skeletal muscle from the lateral head of the gastrocnemius muscle of man (A) and the same muscle from rat (B). From top to bottom are the following stains (myofibrillar ATPase stained at pH 9.4 and preincubated at pH 10.3, 4.6, 4.3): nicotinamide adenine dinucleotide, reduced‐tetrazolium reductase (NADH); α‐GPDH, glycogen (periodic acid‐Schiff, PAS); capillaries (man = amylase‐treated sections stained with PAS; rat = alkaline phosphatase); and hematoxylin‐eosin.



Figure 5.

Part of a sarcomere from slow‐twitch, ST (micrograph and top panel), fast‐twitch, subtype a, FTa (middle panel), and fast‐twitch, subtype b, FTb (bottom panel) fibers in combination with a schematic drawing of the respective fiber types. [From Ängquist 9.]



Figure 6.

Important features of organization of motor units in medial gastrocnemius muscle of cat. Diameters of muscle fibers and unit mechanical responses are scaled appropriately for respective groups, representing typical observations. Shading in muscle fiber outlines denotes relative staining intensities found for each histochemical reaction (identified in the FF unit fibers). Note differences in pattern as well as intensity of staining in the oxidative enzyme reaction (3rd fiber from left in each unit sequence). Note also the somewhat smaller motoneuron innervating type S unit and relation between number of group la synapses and cell size; a low density of terminals (as in the FF unit) produces a relatively small la excitatory postsynaptic potential (EPSP), whereas increasing densities (in the FR and higher still in the type S unit) produce larger EPSPs. Motor unit type nomenclature: FF, fast twitch, fatiguable; FR, fast twitch, fatigue resistant; S, slow twitch. Histochemical profiles: FG, fast twitch, glycolytic; FOG, fast twitch, oxidative, glycolytic; SO, slow twitch, oxidative. These 2 systems are essentially interchangeable. [From Burke and Edgerton 98.]



Figure 7.

Examples of the 3 motor unit types found in human medial gastrocnemius. A, isometric twitch; B, isometric tetanus 10 pulses/s; C, isometric tetanus 20 pulses/s; and D, fatigue test, control and after 3,000 stimuli, expressed as a percentage of initial isometric tension. [From Garnett et al. 238.]



Figure 8.

Ca2+‐activated, K+‐activated, and actin‐activated ATPase activities of myosin from heart, soleus, red vastus, and white vastus muscles of sedentary and trained rats. Temperature, 37°C; pH 7.4. Vertical lines, SEM. *Sedentary vs. trained, P < 0.05. Ht, heart; SO, slow‐twitch, oxidative type from soleus; FOG, fast‐twitch, oxidative, glycolytic type from red vastus lateralis; FG, fast‐twitch, glycolytic type from white vastus lateralis.

Adapted from Watrus 715


Figure 9.

Predicted Vmax and apparent Km of actin‐activated ATPase activity of myosin from white vastus, red vastus, and soleus muscles of sedentary and trained rats. Vertical lines, SEM. FG, fast‐twitch, glycolytic type from white vastus; FOG, fast‐twitch, oxidative, glycolytic from red vastus; SO, slow‐twitch, oxidative type from soleus.

Adapted from Watrus 715


Figure 10.

The distribution of relative occurrence of ST fibers in vastus lateralis in young men and women.

Adapted from a study by Hedberg and Jansson 320; some results are presented in Saltin et al. 603


Figure 11.

Intrapair comparison of slow‐twitch fiber distribution of m. vastus lateralis in monozygous (•) and dizygous (○) twins. [From Komi et al. 432.]



Figure 12.

Relative occurrence of ST fibers in some muscles of the body. A: muscle samples are obtained by multiple needle biopsy samples or (B) postmortem within 24 h after death. [A from Sjøgaard 642 and G. Sjøgaard, unpublished material. B from Johnson et al. 407.]



Figure 13.

Schematic illustration of intensity of periodic acid‐Schiff (PAS) stain (glycogen) in human skeletal muscle fibers at rest and after various times during prolonged exercise at relative work intensities ranging from 31% to 85% of the subject's maximal oxygen uptake. Graph is a summary of several studies. Findings at 74% o2 max show the PAS stain evaluated by microphotometry, whereas in the other studies results are based on a subjective rating (dark = filled; and white = unfilled, with various levels between as crosshatched and hatched). [Data from Gollnick, Saltin, et al. 263,264,271,272. Findings at 74% o2 max from K. Vøllestad, unpublished material.]



Figure 14.

Changes in the percent water and concentration of protein in the sarcoplasmic and fibrillar fractions of human skeletal muscle as a result of growth and development.

Adapted from Dickerson and Widdowson 154


Figure 15.

Intracellular ion concentrations for human skeletal muscle from fetal life to adulthood. The data points marked (′) are averages of samples collected from the triceps brachii, vastus lateralis, and soleus of 6 male and 6 female adults. [Data from Dickerson and Widdowson 154, except those marked (′) from Sjøgaard 642.]



Figure 16.

Data are for muscle from human subjects ranging in age from 2 mo to 18 yr. Fiber areas for infants less than 1 yr are not plotted. A: relationship between age and muscle fiber cross‐sectional area in the lower limb muscles of humans. Equation of the regression line y = 115 + 111x. Between age and fiber area r = 0.92; between age and body height r = 0.98. B: relationship between age and muscle fiber cross‐sectional area in the upper limb muscles of humans. Equation of the regression line is y = 112 + 56x. Between age and fiber area r = 0.85 [Data from Aherne et al. 2.]



Figure 17.

A summary description of the relative occurrence of various fiber types in human skeletal muscle during gestation and 1st year of life. The slow‐twitch (ST) fibers are divided by size with the small fraction of Wohlfart's B fiber above the dashed line 727. [Data from Colling‐Saltin 124,126.]



Figure 18.

Relationship between cross‐sectional fiber area and lesser diameter in human skeletal muscle during gestation and 1st years of life (small graph), and adults (large graph). [Small graph from Colling‐Saltin 124; large graph from Sjøgaard 642.]



Figure 19.

Comparison of the number of fibers in a control and enlarged plantaris muscle of the rat. Muscular enlargement was induced either by ablation of the gastrocnemius muscle (•) or a combination of ablation of the gastrocnemius muscle and treadmill exercise (○). [From Gollnick et al. 276.]



Figure 20.

A plot of the number of fibers vs. total wet weight for the plantaris muscles. •, Control muscles (including normal weanling, sham‐operated, thyroidectomized, and control muscles from experimental animals); ○, muscles enlarged by ablation of the gastrocnemius muscle; and , muscles enlarged by ablation of the gastrocnemius muscle and exercise. The smallest muscle weighed 25 mg and the heaviest 712 mg. [From Gollnick et al. 276.]



Figure 21.

Time courses for changes in 2 mitochondrial enzymes and o2 max during physical conditioning and deconditioning. *Significant changes in time (paired t test) for the selected variables.

Adapted from Henriksson and Reitman 339


Figure 22.

Mean change in percent of succinate dehydrogenase (SDH) activity of vastus lateralis with different training procedures. Note that the mean values ± SD for the absolute activities are similar before the training started. N, no training; S, sprint; E, endurance trained; *, significant difference, P < 0.05.

Adapted from Saltin, Gollnick, et al. 604


Figure 23.

Mean values for 2 mitochondrial enzymes [citrate synthase and 3‐hydroxyacyl‐CoA dehydrogenase (HAD)] determined from muscle samples from vastus lateralis in 9 sea‐level residents at sea level and after an average 32‐wk stay (6–52 wk) at elevation 3,700 m and 16 men born and permanently living at this altitude. Note that high‐altitude residents are divided into 2 groups, those who were physically inactive (job and leisure time) and those who were active. Maximal oxygen uptake (ml · kg−1 · min−1) for the sea‐level residents was 39 ml and 36 ml · kg−1 · min−1 at sea level and high altitude, respectively; inactive high‐altitude residents had 28 ml and active 46 ml · kg−1 · min−1.

Adapted from Saltin et al. 605


Figure 24.

A: schematic representation of the vascular arrangement in the tenuissimus muscle. CA, central artery; CV, central vein; TA, transverse arteriole; TV, transverse venule. B: detailed schematic representation of the vascular architecture of the tenuissimus muscle. Arterial vessels, open; venous vessels, filled. Sections of different depth are made into the muscle at II, III, and IV. At I a projection of the pre‐ and postcapillary vessels is shown. The section at II shows the vessels above, at III at the same, and IV under the level of the central vessels. C: graphic representation of a small arteriole (ART) subdividing into capillaries. Capillaries then run parallel to the muscle fibers. [A adapted from Eriksson and Myrhage 197.]



Figure 25.

Capillaries per muscle fiber related to maximal oxygen uptake. Diagram includes mean values obtained from the following: PAS method, light microscopy (PAS + LM) studies, open symbols 5,6,522,524, and electron microscopy (EM) studies, closed symbols 74,386,387,388. Circles, females; triangles, males. P = 0.001; r = 0.917. [From E. Nygard and H. Schmalbruch, unpublished observations.]



Figure 26.

Mean values for number of capillaries per 1,000 μm2 of muscle fiber area. Bar A shows results from a group of sedentary subjects 603. Bars B and C show values before and after 8 wk of conditioning 6,426. Bar D shows values from well‐trained men 368,399,524,603. Bars M and N are values from subjects deconditioned for 7–14 days (ref. 426; B. Saltin, unpublished observations). Vo2 max below bars M and N was estimated from heart rate response to submaximal exercise (subjects were recovering from minor knee injury).



Figure 27.

Capillaries per fiber and fiber area in sea‐level residents at sea level and after an average 32 wk (6–52 wk) at elevation 3,500 m and in high‐altitude residents. For further details see Fig. 23.

Adapted from Saltin et al. 605


Figure 28.

A schematic summary with indication of relative importance of various energy stores and metabolic pathways for performance in strength, sprint, and endurance events. Included in the scheme are also indications of how oxygen delivery and the nervous system are interacting.



Figure 29.

A representation of the influence of changing the total enzyme concentration on the specific activity based on the rate (Vr). The velocity and any substrate concentration [S] can be estimated from the Michaelis constant (Km) and the maximal velocity (Vmax) for the equation . With a doubling of enzyme concentration, velocity of the reaction will be doubled at any substrate concentration. This relationship would be most important at low substrate concentrations where substrate could thereby be more efficiently directed into end‐terminal oxidative pathways. Conversely with a reduction in enzyme concentration such control would be lost. [From Gollnick and Saltin 257.]



Figure 30.

Summary of changes associated with a moderate (panel A) and a large (panel B) increase in o2max in response to physical conditioning. A: from longitudinal studies in which sedentary subjects were conditioned for 2–3 mo. B: (also longitudinal studies) subjects participated either in a conditioning program for 2–3 yr starting from a sedentary level [o2max 45 ml · kg−1 · min−1 185] or in an intense conditioning program for some months starting from very low o2max [34 ml O2‐kg−1 · min−1 602]. [A: circulatory data: 185,595,602. Leg blood flow and arteriovenous O2 differences are collected from several studies: 409,604,713 and B. Saltin, unpublished observations. Muscle data: 339 for enzymes, 8 for capillaries. B: central circulatory data: 185,602. Leg arteriovenous O2 differences: 602; muscle capillarization and enzyme data are from unpublished studies by B. Saltin, J. Halkjær‐Kristensen, and T. Ingemann‐Hansen.]



Figure 31.

Succinate dehydrogenase activity (μmol · g−1 wet wt · min−1) in trained (T) and nontrained (NT) leg (left), respiratory quotient (RQ) values (middle), and release/uptake of lactate (right) for both legs during a posttraining metabolic study. Means ± SE are given. * Significant difference between trained and nontrained leg (P < 0.05).

Adapted from Henriksson 333
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Article Title: Skeletal Muscle Adaptability: Significance for Metabolism and Performance
 

How to Cite

Bengt Saltin, Philip D. Gollnick. Skeletal Muscle Adaptability: Significance for Metabolism and Performance. Compr Physiol 2011, Supplement 27: Handbook of Physiology, Skeletal Muscle: 555-631. First published in print 1983. doi: 10.1002/cphy.cp100119