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

1. The development of the characteristic histochemical appearance of the slow anterior latissimus dorsi (ALD) and fast posterior latissimus dorsi (PLD) was studied in chickens during embryonic development as well as during regeneration of minced muscle. 2. During embryonic development the activity of the oxidative enzyme succinic dehydrogenase (SDH) is higher in the slow ALD muscle already at 16 days of incubation. At this time the fast PLD has a higher activity of the glycolytic enzyme, phosphorylase. Although the histochemical appearance of the two types of muscle is already different at 16 days, their contractile speeds are still similar. No difference in myosin ATP-ase was found in the two muscles in young embryos but in 20-day old embryos the two muscles became distinctly different when stained for this enzyme. 3. When PLD muscles in hatched chickens redeveloped during regeneration in place of ALD the histochemical characteristics of the regenerated muscle resembled ALD, and when ALD regenerated in place of PLD it resembled PLD. 4. It is concluded that the histochemical characteristics of slow and fast muscles become determined during early development, even before any difference in contractile properties can be detected and that they are determined by the nerve.
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PMID:Differentiation of slow and fast muscles in chickens. 14 31

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

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

Recent studies in patients with long-term heart failure have suggested that intrinsic abnormalities in skeletal muscle can contribute to the development of early lactic acidosis and fatigue during exercise. The present study provides an analysis of substrate and enzyme content, fiber typing, and capillarization in skeletal muscle biopsy samples obtained at rest from the vastus lateralis in 11 patients with long-term heart failure (left ventricular ejection fraction, 21 +/- 8%) and nine normal subjects. Patients demonstrated a reduced peak exercise oxygen consumption (13.0 +/- 3.3 ml/kg/min) when compared with normals (30.2 +/- 8.6 ml/kg/min, p less than 0.001) and had an accelerated rise in blood lactate levels during exercise. In mixed fiber skeletal muscle, total phosphorylase and glycolytic enzyme activities were not different in the two groups, whereas mitochondrial enzymes involved in terminal oxidation were decreased in patients as compared with normal subjects as indicated by reductions in succinate dehydrogenase (51 +/- 15 vs. 81 +/- 17 microM/g protein/min, p less than 0.001) and citrate synthetase (26 +/- 7 vs. 43 +/- 20 microM/g protein/min, p less than 0.05). 3-Hydroxyacyl-CoA-dehydrogenase, an important enzyme mediating beta-oxidation of fatty acids, was also reduced in patients as compared with normals (18 +/- 7 vs. 27 +/- 10 microM/g protein/min, p less than 0.05). There was no difference in high-energy phosphagens or lactate concentration of mixed muscle in the two groups, whereas glycogen content was decreased in patients (262 +/- 29 vs. 298 +/- 35 microM glucosyl units/kg dry wt, p = 0.01). Patients demonstrated a reduced percentage of slow twitch type I fibers (36 +/- 7% vs. 52 +/- 22%, p less than 0.05) and had a higher percentage of type IIb fast twitch fibers (24 +/- 9% vs. 11 +/- 12%, p = 0.02), which were smaller than the type IIb fibers seen in normal subjects (p less than 0.05). In patients, the number of capillaries per fiber was decreased for type I and type IIa fibers (both, p less than 0.03), but the ratio of capillaries to cross-sectional fiber area was not different for the two groups. These data demonstrate major alterations in skeletal muscle histology and biochemistry in patients with long-term heart failure, including fiber atrophy, a decrease in percentage of composition of type I fibers, and an increase in type IIb fibers accompanied by a decrease in oxidative enzyme capacity.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Skeletal muscle biochemistry and histology in ambulatory patients with long-term heart failure. 229 59

The number of fibers staining for the oxidative enzyme succinic dehydrogenase (SDH) was measured in the iliotibialis lateralis caudalis muscle of the domestic fowl before treadmill training and after 6 wk and 15 wk of training, respectively. This leg muscle contains exclusively fast-twitch or type II fibers, and before exercise training approximately 40% of these stained intensely for SDH. After 6 and 15 wk training this proportion rose to approximately 50 and 60%, respectively. Most of these highly oxidative fibers also stained weakly for the glycolytic enzyme alpha-glycerophosphate dehydrogenase (alpha-GPDH) and belonged to the fast-twitch oxidative category. Most of the poorly oxidative fibers stained strongly for alpha-GPDH and therefore belonged to the fast-twitch glycolytic category. It is concluded that exercise training in birds can bring about adaptive changes in the oxidative capacity of skeletal muscle similar to those that have been observed in man and other mammals.
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PMID:Treadmill exercise training increases the oxidative capacity of chicken iliotibialis muscle. 252 27

Two muscles involved in locomotion the vastus lateralis and the gastrocnemius, were compared on a variety of histochemical an biochemical properties. Ten active males, age 20 - 24 years, served as subjects. Fibre type distributions, type I, type IIA and type IIB, as determined from samples extracted by muscle biopsy were similar in both muscles. In addition, no significant difference (p greater than 0.05) was found between fibre types in each muscle for fibre size, relative area, capillaries per fibre and the ratio of capillaries per fibre area. The activities of a number of enzymes representative of energy supplying pathways - the citric acid cycle (succinate dehydrogenase, SHD; beta-hydroxyacyl CoA dehydrogenase, HADH), glycogenolysis (total phosphorylase, PHOSP), glycolysis (phosphofructokinase, PFK) - were of similar magnitude between the two muscles. The only exception noted was for the activity of a glycolytic enzyme, lactate dehydrogenase, LDH, where a 16% higher value was observed in the vastus lateralis. The close degree of homogeneity displayed between these two muscles may be of significance in providing for a functional synchrony to occur in locomotor activities of varying intensity.
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PMID:Human vastus lateralis and gastrocnemius muscles. A comparative histochemical and biochemical analysis. 617 18

Normal ankle flexion and extension was inhibited in neonatal rats by applying an adhesive cast on the day of birth such that the tibialis anterior (TA) muscle of one hindlimb was immobilized in a shortened position. Casts were changed daily for 3 weeks, at which time animals were sacrificed. Immobilized TA muscles were significantly lighter in weight, and whole muscle and teased fiber fascicular lengths were significantly shorter. No effects were seen on fiber diameter profiles, total muscle fiber number or muscle cross-sectional area. Immobilized TA muscles had significantly lower phosphofructokinase activities, and lower slow-twitch fibers than contralateral muscles. The mitochondrial enzyme succinic dehydrogenase was unaffected by the reduced activity. It is apparent that, in a developing fast-twitch muscle such as the TA, myofibrillar ATPase histochemical patterns and glycolytic enzyme activity (phosphofructokinase) may be regulated by factors dependent upon neuromuscular activity. Mitochondrial enzymes, such as succinic dehydrogenase, seem to be regulated during development by factors which are not as sensitive to activity.
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PMID:Influence of reduced neuromuscular activity on the development of neonatal rat hindlimb muscle. 645 21

Despite the wealth of literature concerned with muscle fiber biochemical, ultrastructural and physiological characteristics, little information is available regarding the metabolic enzyme activities of alpha-motoneurons. The present study examines the metabolism of alpha-motoneurons located in the lateral cell column of the rat lumbosacral enlargment with a quantitative histochemical technique. Variation in the activities of alpha-glucan phosphorylase, NADH-diaphorase, succinic dehydrogenase and acid phosphatase were detectable with the photographic densitometry and atomic absorption spectrophotometry technique. No difference in the glycolytic enzyme activity (mitochondrial alpha-glycerophosphate dehydrogenase) was observed. Analysis of lactate dehydrogenase isoenzymes demonstrated the existence of H type isoenzyme in alpha-motoneurons, consistent with other observations indicating predominance of aerobic metabolism within these neurons. The activities of the former enzymes in alpha-motoneurons formed a complete spectrum of activities, distributed unimodally. Smaller motoneurons exhibited the greatest NADH-D and acid phosphatase activities; phosphorylase activity was greatest in larger motoneurons. Significant variation in the enzyme activity of similar-sized motoneurons suggests that the metabolism of the motoneuron is regulated by factors other than cell size. Relationships between motoneuron metabolic enzyme activity and motor unit type are under current investigation.
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PMID:Metabolic variation among rat lumbosacral alpha-motoneurons. 668 5

Enzyme activities of energy metabolism were determined in both homogenates and single fibers of immature-normal (IN), adult-normal (AN), and adult-dystrophic (AD) tibialis anterior (TA) muscle of BL6 mice. Mitochondrial enzyme activities were similar in AN and AD, whereas lower activities were found in IN. Creatine kinase, glycogenolytic, and glycolytic enzyme activities were reduced but glucose 6-phosphate dehydrogenase was elevated in AD and IN as compared to AN. IN and AD both showed an increase in the H-subunit of lactate dehydrogenase. Microphotometric measurements of succinate dehydrogenase (SDH) revealed large fiber differences in AN whereas smaller scattering was observed both in IN and AD. Although similarities exist between enzyme and isozyme patterns of anaerobic metabolism in AD and IN, this does not hold for mitochondrial enzymes.
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PMID:Enzyme activities and activity profiles in muscle fibers of dystrophic, immature-normal, and adult-normal BL6 mice. 671 87


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