Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:1.3.5.1 (succinate dehydrogenase)
 8,177 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Morphological and enzymatic responses in fibers expressing fast, slow, or both types of myosin heavy chain (MHC) were studied in rats after 14 days of spaceflight (COSMOS 2044) or hindlimb suspension. Although the percentage of slow-twitch fibers was unchanged, a higher percentage of fibers that expressed both slow and fast MHC was observed in flight and suspended rats than in synchronous ground-based controls. The soleus was 25 and 34% smaller than control after 14 days of flight and suspension, with the reduction in fiber cross-sectional area (CSA) being greater in slow- than in fast-twitch fibers in both experimental groups. The activities of succinate dehydrogenase (SDH) and alpha-glycerophosphate dehydrogenase (GPD) were not significantly affected by flight or suspension. The total SDH activity (i.e., SDH activity x CSA) decreased significantly in the slow-twitch fibers of the flight and the fast-twitch fibers of the suspended rats, in large part due to fiber atrophy. A shift in MHC expression in 14 and 9% of the fibers in flight and suspended rats occurred without a change in myosin adenosinetriphosphatase activity. The SDH and GPD activities of the fibers that expressed both slow and fast MHC were slightly higher than the slow-twitch fibers and slightly lower than the fast-twitch fibers. These data indicate that events were initiated within 14 days of spaceflight or suspension that began to reconfigure the protein profiles of 9-14% of the slow-twitch fibers from typical slow-twitch toward those of fast-twitch fibers, while all fibers were dramatically losing total protein.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Rat soleus muscle fiber responses to 14 days of spaceflight and hindlimb suspension. 138 48

The adaptation of single fibers in medial gastrocnemius (MG), a fast-twitch extensor, and tibialis anterior (TA), a fast-twitch flexor, was studied after 14 days of spaceflight (COSMOS 2044) or hindlimb suspension. Cross-sectional area (CSA) and succinate dehydrogenase (SDH), alpha-glycerophosphate dehydrogenase (GPD), and myofibrillar adenosinetriphosphatase (ATPase) activities were determined in fibers identified in frozen serial cross sections. Fibers were categorized as light, dark, or intermediate on the basis of myosin ATPase staining and alkaline preincubation and immunohistochemically as reacting with slow, fast, or both slow and fast myosin heavy chain monoclonal antibodies. Because there was a close relationship between these two means of categorizing fibers, all fibers were categorized on the basis of the immunohistochemical reaction. The percentage of slow- and fast-twitch fibers of the MG and TA were unchanged in either group. Mean fiber size of all fibers, irrespective of type, was unaffected in either muscle after flight or suspension. The fibers that expressed both fast and slow myosin heavy chains were smaller than control in the MG of both experimental groups. Compared with control, the SDH and total SDH activities in the MG were significantly less in suspended rats, with the fast-twitch fibers showing the largest difference. The ATPase activity in the MG was higher in flight than in control or suspended rats. There were no significant effects of flight on fibers of the TA. In contrast, the TA in suspended rats had higher GPD activities than either control or flight rats.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Adaptation of fibers in fast-twitch muscles of rats to spaceflight and hindlimb suspension. 138 49

The present study was designed to determine whether the degree and kind of adaptation of a muscle fiber to a functional overload (FO) are determined by properties that are intrinsic to that fiber. The study also addresses the question of the capability of fibers to maintain a normal level of coordination of proteins per fiber as fiber volume changes dramatically. The plantaris muscle of six adult female cats was overloaded for 12 wk by bilateral synergist removal. Plantaris muscle fiber mean size doubled after FO, although some very small fibers that stained dark for adenosinetriphosphatase (ATPase) were observed in some of the FO muscles. There appeared to be no change in total succinate dehydrogenase activity per fiber. A reduction in succinate dehydrogenase activity per unit volume was observed in a substantial number of fibers, reflecting a disproportionate increase in fiber volume relative to mitochondrial volume. In contrast, total alpha-glycerophosphate dehydrogenase activity and actomyosin ATPase activity increased as fiber size increased, whereas there was no change in alpha-glycerophosphate dehydrogenase and ATPase activities per unit volume. Control and FO muscle fibers generally expressed either a fast or slow myosin heavy chain type, but in some cases FO muscle fibers expressed both fast and slow myosin heavy chains. The persistence of variability in fiber sizes and enzyme activities in fibers of overloaded muscles suggests a wide range in the adaptive potential of individual fibers to FO. These data indicate that a severalfold increase in cell size may occur without significant qualitative changes in the coordination of protein regulation associated with metabolic pathways and ATP utilization.
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PMID:Variation and limitations in fiber enzymatic and size responses in hypertrophied muscle. 139 91

Single motor units in the fast-twitch tibialis anterior muscle were functionally isolated by stimulation of microdissected ventral root filaments. The muscle fibres of 35 fast-twitch single motor units (motor unit fibres), 18 units from 3 to 6-month-old and 17 units from 20 to 24-month-old male rats, were identified by glycogen depletion. Measurements were made of staining intensities for intermyofibrillar succinate dehydrogenase, using microphotometric techniques, and of cross-sectional areas of the motor unit fibres. The average coefficients of variation for succinate dehydrogenase activity of the muscle fibres within each unit, between the different units and for repeated measurements of the same fibre in 10 consecutive cross-sections stained on different glasses were 26, 72 and 14%, respectively. The average coefficients of variation for cross-sectional fibre areas within each unit, between the different units and for repeated measurements were 21, 53 and 7%, respectively. Further, the succinate dehydrogenase activity of muscle fibres within the motor unit differed significantly depending on the position of the fibre along the superficial-deep axis of the muscle. The average succinate dehydrogenase activity in the 35 motor units was 21% lower (P less than 0.001) in the superficial as compared with the deep motor unit fibres. In order to eliminate the influence of altered motoneurone properties related to a transformation process or an age-related motoneurone dysfunction as indicated by a non-homogeneous myosin heavy chain composition in motor unit fibres, cross-sectional fibre areas and enzyme activities were also compared in motor units with a uniform myosin heavy chain composition in young animals. However, the same regional differences were observed in these 16 units as when all the 35 units were pooled together. Thus, in conformity with previous reports, the variability in enzyme activities within single motor unit fibres is small but too large for a motor unit homogeneity to be accepted. In addition, the present results demonstrate that the systematic differences in succinate dehydrogenase activities of motor unit fibres along the superficial-deep axis of the tibialis anterior muscle represent a biological rather than a methodological phenomenon.
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PMID:Is the motor unit uniform? 157 48

1. Physiological, enzyme-histochemical, biochemical and morphometrical properties of fast-twitch single motor units were compared between young (3-6 months) and old rats (20-24 months) using the glycogen depletion technique. Monoclonal antibodies (mAbs) were used to identify the myosin heavy chain (MHC) composition in the muscle fibres of the motor unit (motor unit fibres) in order to facilitate correlative physiological, histochemical, biochemical and morphometrical studies. 2. Earlier observations on effects of age on contractile properties of fast-twitch motor units were confirmed and extended. That is, the duration of the isometric twitch, and the twitch and tetanus forces, were increased. Further, motor unit fibres were rearranged, occupying a larger territory and displaying an increased innervation ratio in old age, indicating a denervation-reinnervation process. 3. Motor units with muscle fibres expressing the novel IIX myosin heavy chain (MHC) were observed in both young and old animals, and they constituted the predominant motor unity type identified in the old animals. In contrast to the type IIX MHC motor units in the young animals, the type IIX MHC units in old age often contained muscle fibres which expressed either the type IIA or type IIB MHC, although type IIX MHC fibres were in the majority (so called 'IIX' MHC motor units), but motor units containing all these three fibre types were never observed. There were also single fibres co-expressing IIX and IIB MHCs in old age. 4. In the young animals the IIX MHC motor units had a higher (P less than 0.001) resistance to fatigue (fatigue ratio 0.45 +/- 0.11) than the type IIB MHC units (0.03 +/- 0.05), a succinate dehydrogenase (SDH) activity (0.62 +/- .007) intermediate (P less than 0.001) between those of type IIA muscle fibres classified according to myofibrillar ATPase activity after acid pre-incubation, i.e. type IIA ATPase, (0.84 +/- 0.13) and type IIB MHC motor unit fibres (0.20 +/- 0.04), and cross-sectional fibre areas (1650 +/- 320 microns 2) which were similar to those of type IIA ATPase muscle fibres (1460 +/- 150 microns 2) but smaller (P less than 0.001) than type IIB MHC motor unit fibres (4650 +/- 1180 microns 2).(ABSTRACT TRUNCATED AT 400 WORDS)
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PMID:Effects of age on physiological, immunohistochemical and biochemical properties of fast-twitch single motor units in the rat. 166 38

The role of neuromuscular activity in maintaining the normal enzyme heterogeneity found in a predominantly fast mixed muscle was studied. Enzymatic profiles of single fibers in the adult cat medial gastrocnemius (MG) were examined after almost complete elimination of neuromuscular activity for 6 mo. Inactivity was achieved by spinal cord isolation (SI), i.e., spinal transection at T12-T13 and L7-S1 combined with bilateral dorsal rhizotomy between the two transection sites. Cross-sectional area and succinate dehydrogenase (SDH) and alpha-glycerophosphate dehydrogenase (GPD) activities were determined in a population of fibers identified in frozen serial cross sections. Each fiber was categorized as light or dark on the basis of its staining characteristics for qualitative myosin adenosinetriphosphatase (ATPase), alkaline preincubation, and its reaction to fast and slow myosin heavy chain (MHC) antibodies. SI resulted in a conversion of nearly all light (approximately 36% in the control) to dark ATPase fibers. Virtually all MG fibers in the SI cats reacted with the fast MHC antibody, whereas very few fibers reacted with slow MHC antibody. On the basis of fiber cross-sectional area, it was estimated that the MG atrophied by approximately 10% after SI. Compared with the mean of the dark and light ATPase fibers in control (weighted by the percent fiber type distribution), mean SDH activity was significantly lower (approximately 70%) and mean GPD activity was significantly higher (approximately 120%) in the SI cats. These data indicate that prolonged electrical silence of a mixed fast hindlimb extensor results in virtually all fibers expressing fast MHC as well as oxidative and glycolytic enzyme profiles normally observed in fast glycolytic fibers.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Enzymatic responses of cat medial gastrocnemius fibers to chronic inactivity. 182 90

After rats were chronically exercised by endurance swimming, an augmentation of succinic dehydrogenase (SDH) activity in the diaphragm and the EDL muscle was observed. In addition, endurance training induced a decrease in the percentage of myosin heavy chain (MHC) IIb in the diaphragm, and a decrease in the percentage of HCIIb concomitant with an increase in the percentage of HCIId in the EDL muscle. These results indicate that endurance training induced not only an increase of the oxidative capacity but also an alteration in the expression of an MHC phenotype in the diaphragm and skeletal muscle.
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PMID:Myosin heavy chain isoform changes in rat diaphragm are induced by endurance training. 208 95

The adaptation of a slow (soleus, Sol) and a fast (medial gastrocnemius, MG) skeletal muscle to spaceflight was studied in five young male rats. The flight period was 12.5 days and the rats were killed approximately 48 h after returning to 1 g. Five other rats that were housed in cages similar to those used by the flight rats were maintained at 1 g for the same period of time to serve as ground-based controls. Fibers were classified as dark or light staining for myosin adenosine triphosphatase (ATPase). On the average, the fibers in the Sol of the flight rats atrophied twice as much as those in the MG. Further, the fibers located in the deep (close to the bone and having the highest percentage of light ATPase and high oxidative fibers in the muscle cross section) region of the MG atrophied more than the fibers located in the superficial (away from the bone and having the lowest percentage of light ATPase and high oxidative fibers in the muscle cross-section) region of the muscle. Based on quantitative histochemical assays of single muscle fibers, succinate dehydrogenase (SDH) activity per unit volume was unchanged in fibers of the Sol and MG. However, in the Sol, but not the MG, the total amount of SDH activity in a 10-microns-thick section of a fiber decreased significantly in response to spaceflight. Based on population distributions, it appears that the alpha-glycerophosphate dehydrogenase (GPD) activities were elevated in the dark ATPase fibers in the Sol, whereas the light fibers in the Sol and both fiber types in the MG did not appear to change. The ratio of GPD to SDH activities increased in the dark (but not light) fibers of the Sol and was unaffected in the MG. Immunohistochemical analyses indicate that approximately 40% of the fibers in the Sol of flight rats expressed a fast myosin heavy chain compared with 22% in control rats. Further, 31% of the fibers in the Sol of flight rats expressed both fast and slow myosin heavy chains compared with 8% in control rats. Immunohistochemical changes in the MG were minimal. These data suggest that the magnitude and direction of enzymatic activity and cell volume changes are dependent on the muscle, the region of the muscle, and the type of myosin expressed in the fibers. Further, the ability of fibers to maintain normal or even elevated activities per unit volume of some metabolic enzymes is remarkable considering the marked and rapid decrease in fiber volume.
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PMID:Metabolic and morphologic properties of single muscle fibers in the rat after spaceflight, Cosmos 1887. 213 39

The metabolic plasticity of single fibers in adult cat medial gastrocnemius (MG) 6 mo after complete spinal cord transection (Sp) at T12-T13 was studied. Some Sp cats were trained to weight support (Sp-WS) 30 min/day beginning 1 mo posttransection. Cross-sectional area, succinate dehydrogenase (SDH), alpha-glycerophosphate dehydrogenase (GPD), and myofibrillar adenosinetriphosphatase (ATPase) activities were determined in fibers identified in frozen serial sections. Fibers were categorized as light or dark based on myosin ATPase staining, alkaline preincubation. The percentage of dark ATPase fibers was higher in Sp and Sp-WS (approximately 85%) than in control (approximately 60%). All dark ATPase fibers reacted positively to a fast myosin heavy chain monoclonal antibody. In both spinal groups, a higher percentage of dark ATPase fibers reacted to both fast and slow myosin heavy chain antibodies than in controls. Neither Sp nor Sp-WS cats showed fiber atrophy. Compared with control, SDH activity was decreased in both fiber types of Sp cats. Daily weight-support training ameliorated this adaptation. There were no differences among the three groups in mean GPD and ATPase activities for either fiber type. There was a slight tendency, however, for spinal cats to have higher GPD and ATPase activities (independent of type) than control, probably reflecting the larger proportion of dark ATPase fibers in these cats. These observations indicate that 6 mo after spinalization in adult cats, some of the fibers of a fast muscle became "faster" and developed oxidative and glycolytic enzyme profiles that normally are exhibited in fast fatigable motor units.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Enzymatic plasticity of medial gastrocnemius fibers in the adult chronic spinal cat. 214 12

This study was designed to determine the effects of reduced neuromuscular activity on the expression of proteins associated with contractile and metabolic functions and the size of single muscle fibers in the cat soleus. Adult cats were spinalized (Sp) at T12-T13 and maintained in a healthy condition for 6 months. Some of the cats were trained to weight-support (Sp-WS) for 30 minutes per day beginning one month posttransection. Cross-sectional area (CSA), succinate dehydrogenase (SDH), alpha-glycerophosphate dehydrogenase (GPD), and myofibrillar adenosine triphosphatase (ATPase) activities were determined in a population of single fibers identified in frozen serial cross-sections. Each fiber was categorized as either light or dark based on its staining density for qualitative myosin ATPase, alkaline preincubation (pH 8.75). The Sp (45%) and Sp-WS (31%) groups had significantly higher percentages of dark ATPase fibers than control (less than 1%). All dark ATPase fibers were shown to react positively for a fast myosin heavy chain monoclonal antibody, while some of these fibers showed a reaction to both fast and slow myosin heavy chain antibodies. Overall mean fiber CSA were significantly smaller (approximately 25%) than control in both Sp groups. In the Sp-WS, but not the Sp cats, the dark fibers were larger than the light fibers (P less than 0.05), suggesting a preferential effect of postural training on the ATPase converted fibers. There were no significant differences among the three groups in any of the mean enzyme activities for either ATPase type fiber. However, there was a general tendency for the Sp cats to have elevated GPD and ATP activities per muscle; this appeared to be directly related to the percentage of fibers staining darkly for myosin ATPase. These data indicate that 6 months after spinalization some of the fibers of the slow muscle developed fast myosin staining patterns and oxidative and glycolytic enzyme profiles that are normally exhibited in fast fatigue-resistant motor units. Periods of daily weight-support appear to ameliorate some of these adaptations to spinalization. Further, the observation that SDH activities are maintained at control values in spinalized adult cats as well as in spinalized kittens (unpublished observations) suggest that, at least in the soleus, skeletal muscle fibers can maintain their oxidative potential even though there is a marked reduction in neuromuscular activity for 6 months.
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PMID:Expression of a fast fiber enzyme profile in the cat soleus after spinalization. 214 97


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