scholarly journals A Histochemical Study of Normal and Denervated Red and White Muscles of the Rat

1958 ◽  
Vol 4 (1) ◽  
pp. 47-54 ◽  
Author(s):  
Vivianne T. Nachmias ◽  
Helen A. Padykula
Keyword(s):  
Adenosine Triphosphatase ◽  
Histochemical Study ◽  
Muscle Fibers ◽  
Succinic Dehydrogenase ◽  
Biceps Femoris ◽  
Fiber Types ◽  
Albino Rat ◽  
Whole Muscle ◽  
Red And White Muscles

The distribution and characterization of the fibers of normal and denervated red and white muscles of the albino rat are reported in this study. Histochemical procedures for succinic dehydrogenase, lipides, adenosinetriphosphatase, esterase, and glycogen were utilized to differentiate muscle fibers, and these methods facilitated the study of the distribution of fiber types within whole muscle. Muscle fibers of the granular type (dark or red fibers) can be clearly distinguished from those with clearer sarcoplasm (light or white fibers) by methods for demonstrating succinic dehydrogenase, lipides, and esterase. The method for adenosine-triphosphatase reveals differences only under the special conditions described in the text. Additional fiber types are described in the cat's diaphragm and in the extrinsic ocular muscles of the rat. Succinic dehydrogenase and adenosinetriphosphatase activities of the soleus and biceps femoris were studied 14 days after denervation of these muscles. The histochemical findings are discussed principally in the light of current biochemical knowledge of these enzymes.

Intracellular distribution of succinate dehydrogenase activity in skeletal muscle fibers of geese

1984 ◽  
Vol 62 (2) ◽  
pp. 235-240 ◽  
Author(s):  
H. J. Swatland
Keyword(s):  
Skeletal Muscle ◽  
Succinate Dehydrogenase ◽  
Dehydrogenase Activity ◽  
Adenosine Triphosphatase ◽  
Muscle Fibers ◽  
Fiber Types ◽  
Succinate Dehydrogenase Activity ◽  
Individual Muscle ◽  
Concentric Zone ◽  
Pectoralis Muscles

Samples of iliotibialis anterior and pectoralis muscles were taken from five ganders (Anser domesticus). Serial transverse sections were reacted for succinate dehydrogenase (SDH) and alkali-stable adenosine triphosphatase (ATPase). The distribution of SDH activity within individual muscle fibers was measured with a scanning photometer. In many individual fibers, SDH activity was stronger in the periphery than in the axis. This gradient was steepest (−0.034 ± 0.019 absorbance units per concentric zone of 2 μm diameter measurements) in pectoralis fibers with strong SDH activity. In the pectoralis, radial gradients were correlated with fiber area so that the smallest fibers tended to have the steepest gradients of SDH activity. However, this relationship was reversed in fibers with strong ATPase and weak SDH activity in the iliotibialis anterior, and the largest fibers tended to have the steepest gradients. In all fiber types of both muscles, fibers with greater mean SDH activity tended to have steeper gradients.

scholarly journals Quantitative electrophoretic analysis of myosin heavy chains in single muscle fibers

2001 ◽  
Vol 90 (5) ◽  
pp. 1927-1935 ◽  
Author(s):  
Boris A. Tikunov ◽  
H. Lee Sweeney ◽  
Lawrence C. Rome
Keyword(s):  
Muscle Fibers ◽  
Electrophoretic Analysis ◽  
Single Fiber ◽  
Fiber Types ◽  
Single Muscle ◽  
Myosin Heavy Chains ◽  
Single Fibers ◽  
Heavy Chains ◽  
Cross Bridges ◽  
Whole Muscle

To better understand the molecular basis of the large variation in mechanical properties of different fiber types, there has been an intense effort to relate the mechanical and energetic properties measured in skinned single fibers to those of their constituent cross bridges. There is a significant technical obstacle, however, in estimating the number of cross bridges in a single fiber. In this study, we have developed a procedure for extraction and quantification of myosin heavy chains (MHCs) that permits the routine and direct measurement of the myosin content in single muscle fibers. To validate this method, we also compared MHC concentration measured in single fibers with the MHC concentration in whole fast-twitch (psoas and gracilis) and slow-twitch (soleus) muscles of rabbit. We found that the MHC concentration in intact psoas (184 μM) was larger than that in soleus (144 μM), as would be expected from their differing mitochondrial content and volume of myofibrils. We obtained excellent agreement between MHC concentration measured at the single fiber level with that measured at the whole muscle level. This not only verifies the efficacy of our procedure but also shows that the difference in concentration at the whole muscle level simply reflects the concentration differences in the constituent fiber types. This new procedure should be of considerable help in future attempts to determine kinetic differences in cross bridges from different fiber types.

scholarly journals CHANGES IN ENZYME ACTIVITIES OF VARIOUS MUSCLE FIBER TYPES IN RAT INDUCED BY DIFFERENT EXERCISES

1969 ◽  
Vol 17 (9) ◽  
pp. 601-607 ◽  
Author(s):  
K. KOWALSKI ◽  
E. E. GORDON ◽  
A. MARTINEZ ◽  
J. ADAMEK
Keyword(s):  
Endurance Exercise ◽  
Enzyme Activities ◽  
Succinic Dehydrogenase ◽  
Weight Lifting ◽  
Muscle Fiber Types ◽  
Fiber Types ◽  
Phosphorylase Activity ◽  
Succinic Dehydrogenase Activity ◽  
Whole Muscle ◽  
Enzyme Patterns

Mutability of enzyme activities (phosphorylase, succinic dehydrogenase, cytochrome oxidase) of red and white fibers was studied in rat quadriceps subjected to normal physiologic chronic exercises. A rise in phosphorylase activity was found in weight lifting and to a greater extent in running rats when muscle was taken as a whole, but both exercises resulted in equal increments for succinic dehydrogenase and cytochrome oxydase activities. Intraregional comparisons, however, revealed the greatest relative rise of succinic dehydrogenase activity in those fibers that were regarded as predominantly anaerobic in type. This effect was seen only with running and not with weight lifting. Statistically unproved but frequently observed after running in some of the preparations was a rise of phosphorylase activity in red fibers, although to a lesser degree than in white. Thus, in contrast to the dichotomy apparent in electrophysiologic events in nerve and its dependent muscle, metabolic demands may alter what is regarded normally as fixed fiber enzyme patterns. Whole muscle cannot be studied as a biochemical entity because of diverse regional responses to the same stimuli. Endurance exercise (running) and brief, forceful exercise (weight lifting) produced quantitatively different regional changes in succinic dehydrogenase and probably in phosphorylase activities.

scholarly journals HISTOCHEMISTRY OF MUSCLE SPINDLES IN SNAKES OF NATRIX SPECIES

1974 ◽  
Vol 22 (9) ◽  
pp. 881-886 ◽  
Author(s):  
D. J. PALLOT ◽  
JANIS TABERNER
Keyword(s):  
Adenosine Triphosphatase ◽  
Muscle Fibers ◽  
Succinic Dehydrogenase ◽  
Muscle Spindles ◽  
Intermediate Level ◽  
The Other ◽  
Intrafusal Fiber ◽  
Intrafusal Fibers ◽  
Low Levels

The muscle spindles of snakes consist of a single intrafusal fiber; in addition to this, two types of spindles are found. We have studied the histochemistry of the snake intrafusal fibers. One type of spindle, the long capsule spindle intrafusal fiber, is characterized by high levels of the enzymes myosin adenosine triphosphatase, succinic dehydrogenase and phosphorylase; the other type, the short capsule spindle intrafusal fiber, is characterized by low levels of myosin adenosine triphosphatase and phosphorylase and an intermediate level of succinic dehydrogenase. The short capsule spindle intrafusal fiber is thus histochemically similar to the tonic extrafusal fibers, whereas the long capsule spindle intrafusal fiber is similar to the twitch extrafusal muscle fibers. The long capsule spindle is concerned mainly with monitoring static length, the short capsule spindle with monitoring changes in length. It is interesting that the histochemical profiles of long and short capsule spindle intrafusal fibers are similar to the mammalian bag and chain fibers, respectively.

scholarly journals ULTRASTRUCTURE AND ADENOSINE TRIPHOSPHATASE ACTIVITY OF RED AND WHITE MUSCLE FIBERS OF THE CAUDAL REGION OF A FISH, SALMO GAIRDNERI

1972 ◽  
Vol 55 (1) ◽  
pp. 42-57 ◽  
Author(s):  
Asish C. Nag
Keyword(s):  
Electron Microscopy ◽  
Sarcoplasmic Reticulum ◽  
Adenosine Triphosphatase ◽  
White Muscle ◽  
Muscle Fibers ◽  
Salmo Gairdneri ◽  
Fiber Types ◽  
Surface Areas ◽  
Biochemical Studies ◽  
T System

Electron microscopy, together with quantitation using a tracing device linked to a digital computer, reveals that the red and white muscle fibers of Salmo gairdneri differ in diameter, organization of myofibrils, dimensions of myofilaments, volumes and surface areas of T system and sarcoplasmic reticulum, morphology of mitochondria, and content of mitochondria, lipid, and glycogen. Biochemical studies show that the ATPase activity of white fibers is three times that of the red fibers. Actomyosin content of red fibers is higher than that of the white fibers. The functional significance of these differences between two fiber types is discussed.

scholarly journals Revisiting the peculiar regional distribution of muscle fiber types in rat Sternomastoid Muscle

2018 ◽  
Vol 28 (1) ◽  
Author(s):  
Barbara Ravara ◽  
Valerio Gobbo ◽  
Damiana Incendi ◽  
Andrea Porzionato ◽  
Veronica Macchi ◽  
...  
Keyword(s):  
Cross Sections ◽  
Muscle Fibers ◽  
Regional Distribution ◽  
Absolute Number ◽  
Muscle Fiber Types ◽  
Fiber Types ◽  
Types Of Muscle Fibers ◽  
Deep Region ◽  
Whole Muscle

The sternomastoid (SM) muscle in rodents is known to have a peculiar distribution of fiber types with a steep gradient from surface to deep region. We here further characterize this peculiar regional distribution by quantitative histochemical morphometrys. In Hematoxylin-Eosin (H-E) stained transverse cryosections harvested in the medial portion of the muscle we counted around 10.000 myofibers with a mean diameter of 51.3±12.6 (μm). Cryisections of the SM stained by SDH reaction clearly show two distinct regions, toward the deep surface of the muscle a 40% area that contains packed SDH-positive myofibers, while the remaining area of the SM toward the external surface presents a more checker-board appearance. On the other hand, in the deep region of SM type 1 (slow contracting) muscle fibers, caracterized by positive acidic ATPase pH 4.35 reaction, are only the 24.5% of the fibers in the deep area of SM muscles, being restricted to the deepest region. The 75.5% of the myofibers in the deep region are of the fast contracting types (either 48.4% 2A, SDH –positive fibers or 27.1% 2B, SDH-negative fibers, respectively). As expected the 2B muscle fibers, acidic ATPase pH 4.3-negative and SDH-negative, present the largest size, while Type 1 fibers, acidic ATPase pH 4.3-positive and SDH-positive, present the smallest size in rat SM muscle. Based on present and previous observations, comparison of change in absolute number and/or percentage of the fiber types in any experimental model of muscle atrophy/hypertrophy/plasticity/pathology /recovery in the rat SM, and possibly of all mammals, will ask for morphometry of the whole muscle cross-sections, muscle sampling by bioptic approches will provide only comparable data on the size of the different types of muscle fibers.

The avian pectoralis: histochemical characterization and distribution of muscle fiber types

1986 ◽  
Vol 64 (5) ◽  
pp. 1174-1185 ◽  
Author(s):  
Benjamin W. C. Rosser ◽  
John C. George
Keyword(s):  
Adenosine Triphosphatase ◽  
Muscle Fibers ◽  
Muscle Fiber Types ◽  
Fiber Types ◽  
Fast Twitch ◽  
Superficial Area ◽  
Acid Stable ◽  
Acid Labile ◽  
Histochemical Characterization ◽  
Deep Area

The muscle fibers of superficial (ventral) and deep (dorsal) samples from the pectoralis muscle of 43 species of carinate birds are characterized histochemically on the basis of their myofibrillar adenosine triphosphatase (mATPase) activity after acidic and alkaline preincubations. Muscle fibers are described as slow tonic (alkali-labile/acid-stable mATPase activity) or fast twitch (alkali-stable/acid-labile mATPase activity). Three varieties of fast-twitch fibers are recognized histochemically on the basis of their succinate dehydrogenase (SDH) activity: white (low SDH), intermediate (moderate SDH), and red (high SDH). Slow-tonic fibers are restricted to the deep distal area of the muscle in three species studied. All other muscle is fast twitch. In those species studied, there is a significantly (p ≤ 0.0001) higher proportion of red fibers in the deep area of the muscle as compared with the superficial area. The nature and distribution of the fiber types is characteristic of those vertebrate locomotory muscles most specialized for the rapid output of power. The nomenclature of avian extrafusal skeletal muscle fibers is discussed.

Physiological, morphological, and histochemical properties of cat external anal sphincter

1988 ◽  
Vol 255 (6) ◽  
pp. G772-G778 ◽  
Author(s):  
J. Krier ◽  
T. Adams ◽  
R. A. Meyer
Keyword(s):  
Muscle Fiber ◽  
Fiber Type ◽  
Muscle Fibers ◽  
Succinic Dehydrogenase ◽  
Muscle Fiber Types ◽  
Fiber Types ◽  
Motor Axons ◽  
Fast Twitch Muscle ◽  
Fast Twitch ◽  
Stimulation Of

The contractile properties, morphology, and the distribution of striated muscle fiber types of the external and sphincter (EAS) were determined using axial force measurements, fiber size cross-sectional area measurements, and histochemistry. Electrical stimulation of motor axons in pudendal nerve at supramaximal intensities (10 V, 0.05 ms duration) elicited twitch contractions of EAS. The time to peak force after a single pulse ranged from 37 to 42 ms. The time for relaxation to half-maximal twitch force ranged from 20 to 29 ms. Repetitive stimulation of motor axons (0.1-3.0 Hz) produced potentiation and fatigue of single twitch contractile force, suggesting that the EAS of the cat is comprised predominantly of fast-twitch muscle fibers. Confirmation of skeletal muscle fiber types was determined by histochemistry. Frozen serial cross sections of EAS were incubated to demonstrate succinic dehydrogenase (SDH) and myosin adenosine triphosphatase after alkaline preincubation (pH 10.4). Based on these reactions, muscle fibers were classified as fast glycolytic (FG) (high ATPase, low SDH), fast oxidative-glycolytic (FOG) (high ATPase, high SDH), and slow oxidative (SO) (low ATPase, high SDH). The mean percentage +/- SE of each histochemical type was the following: FG, 73.5 +/- 3.9; FOG, 22.8 +/- 3.7; and SO, 3.7 +/- 0.6. These results indicate that the predominant fiber type for the EAS is FG. The EAS of the cat is considered a nominally fast-twitch muscle.

Patterns of succinate dehydrogenase activity in a leg muscle of the domestic duck during postnatal development

1985 ◽  
Vol 63 (1) ◽  
pp. 55-57 ◽  
Author(s):  
H. J. Swatland
Keyword(s):  
Succinate Dehydrogenase ◽  
Adenosine Triphosphatase ◽  
Muscle Fibers ◽  
Histochemical Demonstration ◽  
Fiber Types ◽  
Succinate Dehydrogenase Activity ◽  
Cross Sectional ◽  
Computer Controlled ◽  
Leg Muscle ◽  
Muscovy Ducks

Transverse sections of iliotibialis cranialis from male Muscovy ducks were reacted for histochemical demonstration of myofibrillar adenosine triphosphatase (ATPase) and for succinate dehydrogenase (SDH) activities. The distribution of SDH activity within muscle fibers was measured with a microscope photometer and a computer-controlled scanning stage. From 1 to 10 weeks after hatching, the average SDH activity across muscle fiber areas decreased. All fiber types exhibited a decline of SDH activity in their central axis. However, fibers with strong ATPase and weak SDH concurrently developed stronger SDH activity in their subsarcolemmal zone. Thus, centripetal radial gradients of SDH activity within fibers became more negative as muscle fibers grew in cross-sectional area.

Deep proteomic characterization of fiber types of murine muscles by laser microdissection and mass spectrometry

2019 ◽  
Author(s):  
B Eggers ◽  
K Schork ◽  
R Schröder ◽  
CS Clemen ◽  
C Berwanger ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Laser Microdissection ◽  
Fiber Types
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