Distribution Of Succinate Dehydrogenase Activity Research Articles

Myofibrillar distribution of succinate dehydrogenase activity and lipid stores differs in skeletal muscle tissue of paraplegic subjects

Lack of physical activity has been related to an increased risk of developing insulin resistance. This study aimed to assess the impact of chronic muscle deconditioning on whole body insulin sensitivity, muscle oxidative capacity, and intramyocellular lipid (IMCL) content in subjects with paraplegia. Nine subjects with paraplegia and nine able-bodied, lean controls were recruited. An oral glucose tolerance test was performed to assess whole body insulin sensitivity. IMCL content was determined both in vivo and in vitro using (1)H-magnetic resonance spectroscopy and fluorescence microscopy, respectively. Muscle biopsy samples were stained for succinate dehydrogenase (SDH) activity to measure muscle fiber oxidative capacity. Subcellular distributions of IMCL and SDH activity were determined by defining subsarcolemmal and intermyofibrillar areas on histological samples. SDH activity was 57 ± 14% lower in muscle fibers derived from subjects with paraplegia when compared with controls (P < 0.05), but IMCL content and whole body insulin sensitivity did not differ between groups. In muscle fibers taken from controls, both SDH activity and IMCL content were higher in the subsarcolemmal region than in the intermyofibrillar area. This typical subcellular SDH and IMCL distribution pattern was lost in muscle fibers collected from subjects with paraplegia and had changed toward a more uniform distribution. In conclusion, the lower metabolic demand in deconditioned muscle of subjects with paraplegia results in a significant decline in muscle fiber oxidative capacity and is accompanied by changes in the subcellular distribution patterns of SDH activity and IMCL. However, loss of muscle activity due to paraplegia is not associated with substantial lipid accumulation in skeletal muscle tissue.

The effect of aerobic exercise training on the distribution of succinate dehydrogenase activity throughout muscle fibres.

We evaluated the effect of endurance training (cycling 3 times per week for 12 weeks) on succinate dehydrogenase (SDH) activity in the subsarcolemmal (SS) and intermyofibrillar (IMF) regions of vastus lateralis muscle fibres in 7 individuals (4 females and 3 males). SDH activity of the SS region increased 9.4% and 12.8% in type I and II fibres, respectively (p < .05). SDH activity of the IMF region increased 4.7% and 6.7% in type I and II fibres, respectively (p < .05). This was less than the increase in the SS region (p < .05). No significant changes were observed in a control group (4 females and 3 males). These data suggest that mitochondria in the SS and IMF regions of human vastus lateralis muscle fibres are sensitive to endurance training. The greater response in the SS region suggests that the metabolic requirements of SS mitochondria were stressed to a greater extent than IMF mitochondria with endurance training.

Altered distribution of mitochondria in rat soleus muscle fibers after spaceflight.

The influence of spaceflight on the distribution of succinate dehydrogenase (SDH) activity throughout the cross section of fibers in the soleus was studied in five male rats and in five rats maintained under ground-based simulated flight conditions (control). The flight (COSMOS 1887) was 12.5 days in duration, and the animals were killed approximately 2 days after return to 1 G. Fibers were classified as slow-twitch oxidative or fast-twitch oxidative-glycolytic in histochemically prepared tissue sections. The distribution of SDH activity throughout the cross section of 20-30 fibers (each type) was determined using quantitative histochemical and computer-assisted image analysis techniques. In all the fibers, the distribution of SDH activity was significantly higher in the subsarcolemmal than in intermyofibrillar region. After spaceflight the entire regional distribution of SDH activity was significantly altered in the slow-twitch oxidative fibers. The fast-twitch oxidative-glycolytic fibers of the spaceflight muscles exhibited a significantly lower SDH activity only in their subsarcolemmal region. These data suggest that when determining the influence of spaceflight on muscle fiber oxidative metabolism enzymes, it is important to consider the location of the enzyme throughout the cross section of a fiber. Furthermore the functional properties of the soleus that depend on the metabolic support of mitochondria in the subsarcolemmal region may be primarily affected by exposure to microgravity.

Intrafibre distribution of succinate dehydrogenase in cat tibialis anterior motor units.

Using isolated ventral root filament stimulation and glycogen depletion techniques, 14 motor units from the cat tibialis anterior were studied. Based on their mechanical properties, the units were classified as either slow-fatigue resistant, fast-fatigue resistant, fast-fatigue intermediate, or fast-fatigable. Quantitative histochemical and computer assisted image analysis techniques were used to determine the activity of succinate dehydrogenase in a population of fibres in each unit. In addition, the intrafibre distribution of succinate dehydrogenase activity was measured in those same fibres by calculating the enzymatic activity of circumferential layers every 0.5 microns starting from the fibre edge to its centre. It was established that enzymatic activity and radial distance were linearly related in the fibres. A range in succinate dehydrogenase activity (mean coefficient of variation, 29%) was observed among the fibres of a unit. In contrast, the intrafibre distribution of that activity was rather consistent (mean variation, 4%) across the fibres of a unit. Further, the intrafibre distribution was similar among the fibres of units classified as the same type. However, the intrafibre distribution was disparate among the different unit types. These data suggest that the intrafibre distribution of mitochondrial enzymes may contribute to the mechanical properties of a motor unit. In this regard, a hypothesis is proposed that describes how the absolute activity of a mitochondrial enzyme, and the intrafibre distribution of that activity, may interactively contribute to the fatigue resistance of a unit.

Gentamicin-induced alterations of succinic dehydrogenase activity in the organ of Corti as revealed by non-decalcified frozen sections of the guinea pig's cochlea

The distribution of succinic dehydrogenase (SDH) activity and the changes of SDH activity after injection of gentamicin (GM) were observed in the organ of Corti using non-decalcified frozen sections of the guinea pig's cochlea. The distribution of SDH activity was found to increase from the apex to the basal turn. At each turn, SDH activity of the inner hair cells, the inner supporting cells and the nerve endings surrounding the supporting cell and on the hair cells presented a greater activity than that found in the outer hair cells, adjacent Deiter's cells and associated nerve endings. It was further observed that GM had a greater effect on SDH activity in the basal turn than the other turns. At each turn, a more sensitive area of response to GM was found on the nerve endings one each hair cell, especially on the outer hair cells of the basal turn.

Fibre-optic spectrophotometry of immature bovine skeletal muscles and the cellular distribution of myoglobin and succinate dehydrogenase.

Samples of diaphragm and pectoralis profundus were taken from nine calves with a range of blood haemoglobin levels of 4 to 8.5 g/100 ml. In both muscles, fibres with strong succinate dehydrogenase activity contained myoglobin, but in the pectoralis there were many fibres with strong alkaline ATPase activity and weak succinate dehydrogenase activity that had low or undetected levels of myoglobin. The whole cross-sectional area of individual fibres was scanned to map the distribution of succinate dehydrogenase activity. Among fibres with similar levels of ATPase activity, those from the diaphragm had greater succinate dehydrogenase activity than those from the pectoralis. Subsarcolemmal succinate dehydrogenase activity was greater than the axial succinate dehydrogenase activity, and radial gradients of succinate dehydrogenase activity were steepest in the diaphragm. For pectoralis fibres with weak ATPase, the mean and the axial succinate dehydrogenase activities were correlated with blood haemoglobin levels (r = 0.62 and r = 0.61, respectively; P less than 0.05 with a Student's t-test). Muscle colour was measured directly by fibre-optic spectrophotometry and correlations of absorbance with succinate dehydrogenase activity were obtained. Absorbance at 620 nm 24 h post-mortem was correlated with succinate dehydrogenase activity in pectoralis fibres with weak ATPase (r = 0.81; P less than 0.005).

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

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.

The radial distribution of succinate dehydrogenase activity in porcine muscle fibres

A microscope photometer with a computer-controlled scanning stage was used to map the distribution of succinate dehydrogenase (SDH) activity in transverse sections of skeletal muscle fibres of pigs from 9 to 29 weeks of age. Absorbance due to SDH activity was measured in successive concentric zones that converged on the central axis of the muscle fibre. In all fibres, there was less SDH activity in the axis of the fibre than in the periphery of the fibre. In fibres with strong adenosine triphosphatase (ATPase) activity and weak overall SDH activity, the radial gradient of SDH activity remained constant as fibres grew in cross-sectional area. However, in fibres with weak ATPase and strong SDH and in fibres with strong ATPase and strong SDH, the radial gradient of SDH activity increased as fibres grew larger. Changes in radial gradients were due to both decreased SDH activity in the axis and to increased SDH activity in the periphery. In all three fibre types, the overall SDH activity per fibre increased with age.

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

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.

Do enzyme activities vary along muscle fibres?

Distribution of succinate dehydrogenase activity along muscle fibres has been studied qualitatively by histochemistry on single micro-dissected rat muscle fibres and quantitatively by comparative kinetic microphotometry on longitudinal muscle sections. Qualitative staining reactions showed no appreciable variations in enzyme activity along the fibres regardless of fibre type. By quantitative assessment, minor variations were found along fibres but were within the range of the experimental error. These variations are of the same magnitude as those observed in enzyme activities of pieces of the same fibre by means of quantitative microchemical methods, performed in our laboratory (Spamer and Pette 1979; Nemeth et al. 1980a, b). Our results provide evidence that the enzyme levels are the same along the course of a muscle fibre.

Muscle weights and succinic dehydrogenase distribution in the hind limb musculature of two rodents (Thryonomys gregorianus and Pedetes capensis) with different locomotory habits.

The hind limb muscles of the spring hare (Pedetes capensis) were found to be relatively heavier than the hind limb muscles of the cane rat (Thryonomys gregorianus). The distribution of succine dehydrogenase activity was investigated in four of these muscles (m. gluteus superficialis, m.semimembranosus, m. biceps femoris and m.rectus femoris) from both animals. It was found that the spring hare had a higher proportion of low-activity fibres in all four muscles than the cane rat. All muscle fibre types were also smaller in diameter in the spring hare than the cane rat. These results are discussed in relation to the different locomotry habits of the two animals.

Succinic Dehydrogenase Distribution in the Pectoralis Muscle of Several East African Birds

AbstractThe distribution of succinic dehydrogenase activity was investigated in the pectoralis muscle of thirteen East African birds, representing five Orders. It was found that the pectoralis muscle of the most primitive birds studied (Galliformes) contained all “white” muscle fibres whereas the more advanced birds (Passeriformes) had all “red” muscle fibres. Intermediate Orders had mostly a mixture of red and white muscle fibres. There also appeared to be a direct relationship between body size and average muscle fibre size. However, it was concluded that the most important factor in relation to the muscle structure is the bird's mode of flight. The relationship with the degree of evolution and body size only held true in so far as the birds which had developed the facility for sustained flight, by increasing their red muscle fibre content, were also smaller in size and constituted the more “evolved” Orders of birds. In support of this it was noted that migratory birds (i.e. engaging in sustained flight) from more primitive Orders also had a high red muscle fibre content in their pectoralis muscles.

The ultrastructural distribution of succinic dehydrogenase activity in the supraoptico-neurohypophyseal system of the rat.

The succinic dehydrogenase (SDH) activity in the supraoptico-neurohypophyseal system of the rat was studied by means of electron microscopic histochemistry aiming at the explanation of earlier findings pointing out the consistently negative reaction of this enzyme in the axon terminals. SDH activity was found to be localized in the mitochondria of neurosecretoy neurons and pituicytes. The hypothalamic as well as the neurohypophyseal portions of neurosecretory axons have markedly stained mitochondria. In contrast to this, axon terminals devoid of neurosecretory material contain non-reacting mitochondria similarly to the previously described distribution of SDH activity in other regions of the nervous system. Accordingly SDH activity could be revealed neither in the mitochondria of axon terminals synapsing on the neurosecretory perikarya nor in the mitochondria of those neurohypophyseal boutons lacking neurosecretory granules. The more uniform distribution of SDH-activity in neurosecretory than in non-neurosecretory neurons points to the possible role of axoplasmic flow in causing within the neurons the described proximodistal decrease of SDH-activity.

Bio- and histochemical studies on enzymes in steroidogenesis in the adrenal cortex of maturing rats.

The developmental process of adrenal function in maturing rats was observed by histo-and biochemical procedures. The activity of Δ5-3β-OH steroid dehydrogenase capable of oxidizing Δ5-3β-OH steroids to Δ4-3-keto steroids, was bio-and histochemically investigated. The distribution of DPNH-diaphorase, glucose-6-phosphate dehydrogenase, succinic dehydrogenase, acid phosphatase and lipid was determined by histochemical methods. The body and adrenal weight were markedly increased between 20 and 40 days of age. At the same time, Δ5-3β-OH steroid dehydrogenase activity was gradually increased in the fascicular and reticular zones. This enzyme activity in females was higher than in males at the age of 30 days. The lipid free subglomerular zone, a transitional zone, disappeared at 40 days of age only in females. Histochemically, glucose-6-phosphate dehydrogenase activity was distributed in a similar way to Δ5-3β-OH steroid dehydrogenase except in the intramedullary cortical cells at all ages; this finding might indicate a close relationship between the two enzymes in steroidogenesis. Though the intramedullary cortical cells (Van Dorp and Deane, 1950) were morphologically similar to the reticular zone, the function might be different, since both were different in the distribution of enzymes and lipid. The distribution of succinic dehydrogenase activity paralleled that of acid phosphatase in all age groups. The distribution of DPNH-diaphorase activity was characteristic in its high concentration in the glomerular zone. While the layer highest in succinic dehydrogenase activity gradually moved to the inner part of the fascicular zone with maturation of animals, that in glucose-6-phosphate dehydrogenase and Δ5-3β-OH steroid dehydrogenase activities shifted to the outer part and the layer rich in lipid as well.

Histochemical and cytochemical studies on the succinic dehydrogenase in the developing cerebellum

1. A study was done on the distribution of succinic dehydrogenase activity (SDA) in the developing cerebella of cats and mice, from the middle fetal life to the adult, using fresh frozen sections prepared by the use of carbowax (polyethylene glycol).2. Although extremely weak, the SDA was already recognized at the middle stage of embryonic life. The activity was seen to be intensified at the later stage (near term). There was a remarkable difference on the distribution of SDA between the embryos and the adults.3. The pronounced increase in the activities with the development of all the components of cerebellum were seen from about the 6th day after birth on again (mouse 5th day). Observations on the 65th day (mouse 19th day) revealed that they showed the adult pattern.4. Cytologically, the SDA was beautifully demonstrated in the external granule cells, the cells in the molecular layer, the PURKINJE cells, and their satellite cells, basket cell fibers, the inner granule cells and other cells in the granule layer. The activities were, also, observed in the cells of the white matter during the development.5. In the inner granule layer, the activities were at first restricted mainly to the region adjacent to the PURKINJE cell layer with the gradual decrease towards the white matter.6. By the 6th day after birth (mouse 8th day), the PURKINJE cell nuclei were located towards the bottom of cell bodies showing the eccentrical localization of the activity in the area of dendritic origin. Thereafter, they were located in the center of racket-shaped cytoplasm showing perinuclear staining of the cytoplasm.7. Except for the above mentioned results, findings were essentially the same to those reported by FRIEDE (957) in the developing cerebellum of the rat.

Histology and cytochemistry of human skin. VII. The distribution of succinic dehydrogenase activity.

Histology and cytochemistry of human skin. VII. The distribution of succinic dehydrogenase activity.

Comparative distribution of succinic dehydrogenase in six mammals and modification in the histochemical technic.

The distribution of succinic dehydrogenase activity was compared in the organs of six mammals. The histochemical localization of the enzyme was improved so as to enable the use of thin frozen sections (10 µ) by the addition of the following ions:bicarbonate, calcium, magnesium and aluminum. The distribution of enzymatic activity by this technic in the organs of the rat was compared with the earlier method.