Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: 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)

The histoenzymatic characteristics of regenerating myofibers of rat masseter muscle following injection of 1% lidocaine, as well as morphometric and histochemical characteristics of the typical myofibers, were investigated. Myoblasts appeared initially by day 1 among numerous macrophages within the confines of degenerating myofibers. Myotubes predominated by the 3rd day. Complete regeneration of the muscle occurred by at least 45 days. Phosphorylase activity was absent at day 1 and reappeared by the 5th day when the regenerating myofibers showed slight activity. By the 15th day the myofiber types had partly differentiated; red myofibers were smaller and stained less intensely than the white myofibers. Myotubes stained uniformly for succinic dehydrogenase activity from 3 until 5 days. After 5 days this staining increased gradually. Myofiber types began differentiation by 15 days and were fully differentiated by 45 days. ATPase activity was barely evident by 1-3 days. This activity appeared uniformly low up to 5 days and increased to an intensity comparable with that of the typical myofiber by 15 days. Slight leucine aminopeptidase activity occurred in macrophages 1 day following injection. By 3 days this activity appeared in the remaining myoblasts and in the myotubes. Some activity was found in the fibroblasts. This staining intensity at 5 days was equal to that of earlier lesions. A trace of this activity was found at 7 days, and none at 15 days. Glucose-6-phosphate dehydrogenase activity was present in the macrophages by day 1. It increased by 3 days and occurred mainly in myoblasts and myotubes. This activity decreased by 5 days, and none was found by 7 days.
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PMID:Regeneration of masseter muscle following lidocaine-induced degeneration. A histochemical study. 14 12

Changes in succinic dehydrogenase, adenosine triphosphatase, and phosphorylase activities occurred in masseter muscle by 15 minutes following injection of 2% lidocaine. Abolishment of phosphorylase activity suggested an effect on the sarcoplasmic reticulum. Increased staining for succinic dehydrogenase and adenosine triphosphatase activities suggested damage to mitochondria and myofibrils, respectively. Leucine aminopeptidase and glucose-6-phosphate dehydrogenase activities appeared in macrophages.
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PMID:Degenerative changes in masseter muscle following injection of lidocaine: a histochemical study. 14 69

A reduction in the content of neutral mucopolysaccharides in mucous cells of the neck, a slight decrease in the activity of succinate dehydrogenase and NAD-diaphorase in parietal cells, a decrease in the DNA synthesis rate, and an increase in the area of mitochondria and cristae were detected in the gastric mucosa of rats which were in a long-term space flight. In the small intestine, an increase in the activity of glucose-6-phosphate dehydrogenase and leucine aminopeptidase were found. Morphological changes in the liver consisted in infiltrative adiposity. A similar morphological picture was demonstrated in a synchronous experiment on the earth. These changes, however, were nonspecific and reversible (25 days after rehabilitation the picture did not differ from the animal house control).
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PMID:[Morphological changes in the digestive organs during prolonged space flight on the Kosmos-782 biosatellite]. 15

56 human liver biopsy specimens with insignificant or no histological changes, but with abnormally strong canalicular alkaline phosphatase activity, were studied histochemically for other enzyme changes. In comparison with normal specimens, more extensive and increased canalicular activity of gamma-glutamyl transferase, and increase of canalicular leucine aminopeptidase, was found, while the sinusoidal activity of the latter enzyme was decreased. Staining for adenosine triphosphatase regularly desclosed the normal pattern of sinusoidal and canalicular activity. The lysosomal enzymes, acid phosphatase and beta-glucuronidase, stained more intensely than ordinarily, while the reactions for enzymes present in the cytosol (lactic dehydrogenase), in the mitochondria (succinic dehydrogenase, imonoamine oxidase) and in the endoplasmic reticulum (glucose-6-phosphatase) were normal.
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PMID:On histochemical enzyme changes in association with canalicular activity of alkaline phosphatase in human liver. 24 Dec 3

The myoepithelium of developing, lactating, and involuting mammary gland of the mouse exhibits a high alkaline phosphatase activity. The content of the alveoli and the apical plasma membrane of gland cells histochemically show enzyme activity before and after lactation but not during milk secretion. In the course of involution the alveoli shrink in size and the reaction of alkaline phosphatase becomes stronger in the gland tissue. In whole breast tissue the enzyme activity decreases, because in this time a great part of the alveoli are degraded and replaced by connective tissue and fat. As measured by a scanning microdensitometer the activity of some oxydoreductases (3-hydroxybutyrate dehydrogenase, lactate dehydrogenase, malate dehydrogenase, and succinate dehydrogenase) increase in proceeding development of the mammary gland and reach their highest level at the time of lactation. Already 12 h after the start of involution the oxydoreductases loose 30 to 50% of their activity and undergo a further reduction 3 to 4 days later. On the other side the activity of lysosomal enzymes increase during involution. beta-Glucuronidase and leucine aminopeptidase have their highest activity in the early stage of involution, whereas acid phosphatase predominate in the late period of gland degradation.
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PMID:[Microdensitometric measurement enzyme activities in the mammary gland of the mouse]. 83 21

Intravillous, microcrater, and macroscopic invasive lesions induced in the mouse duodenum by N-ethyl-N'-nitro-N-nitrosoguanidine were examined histochemically. The cells of these neoplastic lesions and the proliferative zones of the normal crypts showed similar staining reactions in leucine aminopeptidase, alkaline and acid phosphatases, adenosine 5'-triphosphatase, and glucose-6-phosphate dehydrogenase. However, a slight decrease in succinic dehydrogenase activity and a slight increase in lactic dehydrogenase activity were observed in the intravillous and microcrater lesions compared to the activity in the proliferative zones of the crypts. The neoplastic cells of these lesions showed no mucus secretion. We discussed the origin of the neoplastic lesions using these and other findings.
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PMID:Histochemical patterns in early lesions and infiltrating adenocarcinomas induced in mouse duodenum by n-ethyl-n'-nitro-n-nitrosoguanidine. 125 98

Bestatin, one of the biological response modifiers (BRMs), is an inhibitor of aminopeptidase B (AP-B), leucine aminopeptidase (LAP) and aminopeptidase M (AP-M). In this report, we investigated the direct effect of bestatin on the growth of cancer cells in vitro using established four choriocarcinoma cell lines. In vitro chemosensitivity was evaluated by the succinate dehydrogenase inhibition (SDI) test. Bestatin showed the growth-inhibitory effect on all the choriocarcinoma cell lines dose-dependently, especially on NaUCC-4 cells. Both an isomer of bestatin with no inhibitory activity against aminopeptidases, (2R, 3S)-AHPA-(R)-Leu, and another isomer with stronger inhibitory activity against AP-B than bestatin, (2S, 3S)-AHPA-(R)-Leu, did not show growth inhibition on NaUCC-4 cells. So it is suggested that one of the possible mechanisms responsible for the direct action of bestatin on the choriocarcinoma cells may be related to the inhibition of activity of LAP or AP-M rather than that of AP-B. Furthermore, cytotoxicity of actinomycin D on the choriocarcinoma cells was significantly enhanced by combination with bestatin. These results suggest that bestatin has not only an indirect host-mediated anti-tumor activity, but also a direct growth-inhibitory effect on some kinds of cancer cell lines.
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PMID:Growth inhibitory effect of bestatin on choriocarcinoma cell lines in vitro. 178 99

Canalicular and mitochondrial membranes were investigated as early foci of hepatocyte injury in fed and fasted male Sprague-Dawley rats given 50 mg of 1,1-dichloroethylene (DCE)/kg. Staining of the bile canaliculi localized enzymes, leucine aminopeptidase (LAP), and Mg++-dependent ATPase (Mg++-ATPase), was examined by histochemistry in frozen sections. Mitochondrial membrane enzymes, including succinate dehydrogenase, also were examined by histochemistry. Staining of two monoclonal antibodies, C-1 and 9-B1, whose binding is localized in the bile canalicular region, was examined by immunofluorescence in frozen sections. Fasted rats treated with DCE developed moderate liver damage by 4 hours as evidenced by increases in serum transaminase and bilirubin, whereas fed rats developed only slight cell damage. Centrolobular loss of immunocytochemical and histochemical canalicular staining, especially for C-1 and Mg++-ATPase, was evident as early as 1 hour after DCE and was striking by 2 hours in both fed and fasted rats. Decreases in mitochondrial enzymes were not evident histochemically in fed animals at any time after DCE and were found only at the later times in fasted animals given the toxin. Thus, DCE administration to fed rats provides a new model system of selective bile canaliculi injury.
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PMID:Histochemical and immunocytochemical evidence of early, selective bile canaliculi injury after 1,1-dichloroethylene in rats. 254 11

High HCO3(-)-ATPase activity is known to exist in mitochondria of renal tubular cells. In brush border membrane (BBM) preparations of proximal tubules such an anion-stimulated enzyme was also found. However, these preparations always contained mitochondrial markers. The putative localization and the role of this ATPase in BBM is still controversial. Some authors consider the HCO3(-)-ATPase in the BBM to be a mitochondrial contamination; others attribute to this ATPase a key role in H+ transport in the proximal tubule. To reinvestigate this problem, BBMs from rat kidney cortex were isolated by a simple, rapid (1.5-h) Ca2+-precipitation method, yielding a BBM fraction enriched 12.4-fold with respect to the marker enzyme leucine aminopeptidase (LAP). There was no basolateral Na+-K+-ATPase and no mitochondrial succinate dehydrogenase detectable. Cytochrome c oxidase was drastically reduced to 7 +/- 1% of that observed in the homogenate (TH). The activity of HCO3(-)-ATPase in the BBM fraction was 19 +/- 4 IU/g protein, i.e., 27% that of the homogenate. As sonication of the TH exclusively increases the activity of HCO3(-)-ATPase, its relative activity was 7.5% and thus equal to that of the mitochondrial marker. In many BBM preparations no HCO3(-)-ATPase was detectable. In those BBM preparations in which traces of HCO3(-)-ATPase were found, this activity coincided with that of cytochrome c oxidase in the respective preparation. There was a constant activity ratio of cytochrome c oxidase/HCO3(-)-ATPase in the TH, BBM, and pellet 1. The activity of HCO3(-)-ATPase in BBM did not depend on the activity of LAP.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Evidence for mitochondrial origin of the HCO3(-)-ATPase in brush border membranes of rat proximal tubules. 298 70

Within the uterine glands, the following enzymes were demonstrated by histochemical methods after 30, 58, 80, 100, and 110 d of pregnancy, respectively: beta-N-acetyl-hexosaminidase, beta-galactosidase, beta-glucuronidase, alpha-mannosidase, acid phosphatase, alkaline phosphatase, esterases, cytochrome oxidase, 5-nucleotidase, leucine aminopeptidase, adenosine triphosphatase, diaphorases (NADH, NADPH), glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, succinate dehydrogenase, isocitrate dehydrogenase (NAD, NADP), beta-hydroxybutyrate dehydrogenase, glycero-3-phosphate dehydrogenase, NAD-glycero-3-phosphate dehydrogenase, glutamate dehydrogenase (NAD, NADP), lactate dehydrogenase. The results show that the activities of G-6-PDH, 6-PGDH, and cytochrome oxidase increase within secreting cells during the 2nd half of pregnancy. The activities of the other enzymes remained almost unchanged during the period of investigation. The description of our results distinguishes between gland neck, middle, and distal part of the secretory unit, respectively. In general, the enzyme activities are similar within the middle and distal gland segments, but lower in the epithelia of the neck region. The activity of dehydrogenases was medium to intensive within the middle and distal gland segments, but only low to medium within the neck portion. Of the hydrolases, the acid phosphatase, ATPase, leucine aminopeptidase, and beta-galactosidase demonstrated an intensive activity within activity secreting cells. The enzyme activities of the gland epithelia are compared with these of the uterine surface epithelia and the histochemical results are discussed in context with their significance in histiotrophic nutrition.
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PMID:[Enzyme histochemistry of the pig placenta. III. Histotopics of enzymes in the uterine epithelium]. 309 49


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