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Alterations in Myofibril Size and Structure During Growth, Exercise, and Changes in Environmental Temperature

Geoffrey Goldspink

10.1002/cphy.cp100118

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 Changes in Myofibrils During Growth
1.1 Increase in Length of Myofibrils
1.2 Increase in Myofibrillar Cross‐Sectional Area
1.3 Synthesis and Assembly of Myofibrillar Proteins
1.4 Changes in Myofibrillar Proteins During Differentiation
2 Muscle Fiber Types in Adult Muscle
2.1 Tonic Muscle Fibers
2.2 Phasic Muscle Fibers
2.3 Structural Differences Between Myofibrils of Different Fiber Types
3 Changes in Muscle Fiber Types During Growth
4 Effect Of Exercise and Inactivity on Myofibrillar Content of Muscle Fibers
5 Ultrastructural Changes Associated with Cross Innervation and Artificial Stimulation
6 Temperature Adaptation in Myofibrils of Ectothermic Animals
7 Conclusion
Figure 1. Figure 1.

Increase in sarcomere number in mouse soleus with age and effect of immobilization of muscle at different ages in different ways. Recovery from effects of plaster cast immobilization is shown by dashed lines. [Data from Williams and Goldspink 115,117.]
Figure 2. Figure 2.

Level of labeling in end and middle regions of young (top) and mature (center) muscles after a single injection of tritiated adenosine (adenosine is incorporated into structural ADP of actin monomers). Bottom: level of labeling for adult muscles recovering from immobilization in shortened position is also given. In top and bottom, end regions are more heavily labeled than middle ones, indicating that the site of longitudinal growth is at end regions.
Figure 3. Figure 3.

Autoradiograph of tail muscle from Xenopus tadpole reared for a few days in a medium containing [3H]leucine. Muscle fibers are arranged in myotomes and ends of fibers show bands of heavy labeling. This is further evidence that new sarcomeres are added serially to ends of existing myofibrils.
Figure 4. Figure 4.

Myofibrils in process of splitting longitudinally. Position of split is marked by white arrow. Some Z disks in myofibrils are still intact, whereas others have split, and there are already elements of the sarcoplasmic reticular system and some mitochondria in the fork of each split.
Figure 5. Figure 5.

Mechanism of myofibril splitting seems to depend on oblique pull of peripheral actin filaments. This oblique pull is due to mismatch in actin and myosin lattices. Obliqueness of actin filaments increases as myofibrils grow and also as sarcomeres shorten during contraction. When force is developed very rapidly, this oblique pull of actin filaments is believed to result in splitting of Z disks.
Figure 6. Figure 6.

Method of distinguishing different fiber types with myofibrillar ATPase stain (left) and oxidative enzymes such as succinic dehydrogenase (right). With these methods, at least 3 fiber types can be distinguished in most mammalian muscles. The ATPase method includes preincubation at pH 9.4, and therefore alkaline‐resistant fibers stain more darkly. Three fiber types—slow twitch, oxidative (SO), fast twitch, glycolytic (FG), and fast twitch, oxidative, glycolytic (FOG)—are indicated. (Photomicrographs by P. Watt of Muscle Research Unit, University of Hull, England.)
Figure 7. Figure 7.

Change in number of fast (•) and slow (○) fibers in mouse biceps brachii and soleus muscles during growth. Because total number of fibers does not change, change in number of different types means that there is some interconversion of types. Predominant fiber type is the one that tends to increase, and this may be the result of some reinnervation. [From Goldspink and Ward 44.]
Figure 8. Figure 8.

Plots of ATPase activity (mol P1 · mg−1 · min−1) and rate of temperature denaturation for myofibrils of antarctic and tropical fish (top) and warm‐ and cold‐acclimated carp (bottom). Plots on left show specific ATPase activity of myofibrils at different temperatures; those on the right show residual ATPase activity after preincubation for different periods of time at 37°C. Production of different kinds of myofibril according to environmental temperature is seen from results of warm‐ and cold‐adapted fish. [From Johnston, Goldspink, et al. 61.]


Figure 1.

Increase in sarcomere number in mouse soleus with age and effect of immobilization of muscle at different ages in different ways. Recovery from effects of plaster cast immobilization is shown by dashed lines. [Data from Williams and Goldspink 115,117.]



Figure 2.

Level of labeling in end and middle regions of young (top) and mature (center) muscles after a single injection of tritiated adenosine (adenosine is incorporated into structural ADP of actin monomers). Bottom: level of labeling for adult muscles recovering from immobilization in shortened position is also given. In top and bottom, end regions are more heavily labeled than middle ones, indicating that the site of longitudinal growth is at end regions.



Figure 3.

Autoradiograph of tail muscle from Xenopus tadpole reared for a few days in a medium containing [3H]leucine. Muscle fibers are arranged in myotomes and ends of fibers show bands of heavy labeling. This is further evidence that new sarcomeres are added serially to ends of existing myofibrils.



Figure 4.

Myofibrils in process of splitting longitudinally. Position of split is marked by white arrow. Some Z disks in myofibrils are still intact, whereas others have split, and there are already elements of the sarcoplasmic reticular system and some mitochondria in the fork of each split.



Figure 5.

Mechanism of myofibril splitting seems to depend on oblique pull of peripheral actin filaments. This oblique pull is due to mismatch in actin and myosin lattices. Obliqueness of actin filaments increases as myofibrils grow and also as sarcomeres shorten during contraction. When force is developed very rapidly, this oblique pull of actin filaments is believed to result in splitting of Z disks.



Figure 6.

Method of distinguishing different fiber types with myofibrillar ATPase stain (left) and oxidative enzymes such as succinic dehydrogenase (right). With these methods, at least 3 fiber types can be distinguished in most mammalian muscles. The ATPase method includes preincubation at pH 9.4, and therefore alkaline‐resistant fibers stain more darkly. Three fiber types—slow twitch, oxidative (SO), fast twitch, glycolytic (FG), and fast twitch, oxidative, glycolytic (FOG)—are indicated. (Photomicrographs by P. Watt of Muscle Research Unit, University of Hull, England.)



Figure 7.

Change in number of fast (•) and slow (○) fibers in mouse biceps brachii and soleus muscles during growth. Because total number of fibers does not change, change in number of different types means that there is some interconversion of types. Predominant fiber type is the one that tends to increase, and this may be the result of some reinnervation. [From Goldspink and Ward 44.]



Figure 8.

Plots of ATPase activity (mol P1 · mg−1 · min−1) and rate of temperature denaturation for myofibrils of antarctic and tropical fish (top) and warm‐ and cold‐acclimated carp (bottom). Plots on left show specific ATPase activity of myofibrils at different temperatures; those on the right show residual ATPase activity after preincubation for different periods of time at 37°C. Production of different kinds of myofibril according to environmental temperature is seen from results of warm‐ and cold‐adapted fish. [From Johnston, Goldspink, et al. 61.]

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Article Title: Alterations in Myofibril Size and Structure During Growth, Exercise, and Changes in Environmental Temperature
 

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Geoffrey Goldspink. Alterations in Myofibril Size and Structure During Growth, Exercise, and Changes in Environmental Temperature. Compr Physiol 2011, Supplement 27: Handbook of Physiology, Skeletal Muscle: 539-554. First published in print 1983. doi: 10.1002/cphy.cp100118