Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.15.1 (ACE)
 18,300 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Histochemical studies were carried out on some of the glycolytic enzymes viz. phosphorylase, aldose, alpha-glycerophosphate dehydrogenase (alpha-GPDH) and lactic dehydrogenase (LDH) and a key enzyme of the pentose phosphatase cycle, glucose-6-phosphate dehydrogenase (G-6-PDH), in the hepatopancreas of Scylla serrata (Forskal). 1. Weak activities of phosphorylase and aldolase and strong-activities of alpha-GPDH and LDH were noticed mainly in the brush border of the tubules and R-cell cytoplasm. A trace activity of G-6-PDH was noticed in the brush border. 2. Bilateral eyestalk removal results in inhibition of both phosphorylase and aldolase. However, enhanced activities of alpha-GPDH and LDH were noticeable 4 h after the operation. The G-6-PDH activity remained unaltered till 24 h. 3. Injection of eyestalk extract into both intact and destalked crabs activated all the enzymes.
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PMID:Histochemical observations on the occurrence of glycolytic and pentose phosphate cycle enzymes in the hepatopancreas and their possible relation to eyestalk factor(s) in the crab Scylla serrata (Forskal). 0 Aug 64

Treatment of male guinea-pigs daily with an oral dose of 2 mg dehydroepiandrosterone (DHA) sulphate/100 g body weight for 2 weeks significantly reduced the glucose-6-phosphate dehydrogenase (G-6-PDH) activity of erythrocytes, liver, kidney and testis. Lactate dehydrogenase activity in plasma also decreased, but L-aspartate: 2-oxoglutarate aminotransferase (GOT) and L-alanine:2-oxoglutarate aminotransferase (GPT) activity in plasma remained unaffected. In liver and kidney, however, a significant rise in GOT and GPT was observed. A 2- to 3-7-fold increase of C19-steroids was observed in plasma, liver and kidney. In extracts of liver and kidney more than 60% of steroids were isolated from the sulphatide fraction. Only minor changes were detected in the metabolic pattern of C19-steroids, 17-hydroxysteroids prevailing in the free and sulphatide fractions, while 17-oxosteroids predominated in the sulphate and glucuronide fractions. A slight rise of cyclic AMP concentrations in liver and kidney tissue was attributed to the inhibition of phosphodiesterase by the DHA/G-6-PDH system
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PMID:Effects of exogenous dehydroepiandrosterone sulphate on various enzymes and on steroid metabolism in the guinea-pig. 13 7

The activity of the glycolytic enzymes and of the glucose-6-phosphate dehydrogenase (G-6-PDH) were compared with the content of noradrenaline in rat myocardium and the liver after the intraperitoneal injection of high doses of noradrenaline. It was shown that 24 hours after int noradrenaline injection which caused exhaustion of endogenous catecholamine supply, the lactate content and the activities of lactic dehydrogenase were increased in the myocardium; the activity of hexokinase and G-6-PDH in rat myocardium and the liver were also increased, whereas the glucokinase activity was decreased. In these experiments alterations of the enzyme activities were shown to be similar to the alterations in the dystrophic tissues in which the catecholamine content was sharply decreased. The role of the sympathetic nervous system and its mediators in the mechanism of the enzyme regulation of the energy metabolism in the myocardium and the liver is discussed.
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PMID:[Activity of energy metabolism related enzymes in the myocardium and liver following administration of large doses of noradrenaline]. 17 88

Investigations on the activity of three erythrocytic enzymes i.e., glucose-6-phosphate dehydrogenase (G-6-PDH), catalase and lactate dehydrogenase (LDH), in 20 patients with extracorpuscular hemolytic anemias of various origins showed a general tendency to decrease of G-6-PDH and catalase, with a concomitant increase in LDH. These results are interpreted as due to metabolic disturbances induced by hemolysis in the erythroblastic series and/or to possible perturbations specific for each type of anemia.
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PMID:Study of some erythrocytic enzymes in extracorpuscular hemolytic anemias. 28 54

The effects of 5 alpha-dihydrotestosterone (DHT) and thyroxine (T4) on glucose-6-phosphate dehydrogenase (G-6-PDH) activity in mouse submandibular gland were investigated histochemically. A strong positive histochemical reaction for G-6-PDH was observed in the excretory ducts of untreated male and female mice, with a slight reaction in the basal portion of the convoluted tubules (striated ducts) of males. Administration of DHT to female mice increased G-6-PDH activity specifically in the convoluted tubules. T4 increased the enzyme activity in the tubules more than DHT. The induction of G-6-PDH activity by T4 in adrenalectomized mice suggests that T4 has a direct effect on the submandibular gland.
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PMID:Histochemical study on the localization of glucose-6-phosphate dehydrogenase induced by androgen or thyroxine in the convoluted tubules of mouse submandibular gland. 50 Apr 9

To determine the effect of chronic alcohol ingestion, rats were given 15 or 25% v/v of alcohol in water for a period of 6 months. The activities of some key enzymes involved in the metabolism of glucose, mitochondrial respiratory rates, and efficiency of oxidative phosphorylation were studied in the hearts of alcohol-treated and untreated rats. In the group receiving 15% alcohol, glucose-6-phosphate dehydrogenase (G-6-PDH) was elevated. In rats given 25% alcohol, activities of G-6-PDH, aldolase, and glyceraldehyde phosphate dehydrogenase were elevated but isocitrate dehydrogenase was reduced. Mitochondrial respiratory rates and the efficiency of phosphorylation were depressed in rats given 25% of alcohol. Except for mitochondrial oxidation of pyruvate and alpha-ketoglutarate, all biochemical parameters studied were within normal limits a month after alcohol was discontinued.
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PMID:The effect of chronic ethanol ingestion on myocardial glucose and energy metabolism. 56 91

The enzymes delta5-3beta-hydroxysteroid dehydrogenase delta5-3beta-HSD) and glucose-6-phosphate dehydrogenase (G-6-PDH) were demonstrated histochemically in the adrenal cortex of female rat. The activities of these enzymes were increased significantly in the alloxan-treated rats kept in LD (light: darkness) cycles of 10:14 h. Continuous light exposure to diabetic animals appeared to decrease delta5-3beta-HSD and g-6-PDH in comparison to the diabetic rats kept in 10 h illumination. The evidence indicates that suppression of adrenal steroidogenesis in diabetic rats after exposure to continuous light is due to the alteration of pentose phosphate pathway.
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PMID:Adrenal dehydrogenases in alloxan diabetic rats following continuous exposure to light. 60 81

In a detailed study focused on the methodological problems in dehydrogenase histochemistry [e.g., fixation, diffusion of enzymes and of reduced inermediates, conversion of NADPH and NADP to NADH and NAD, respectively, penetration of tetrazolium salt and formazan substantivity, 'nothing dehydrogenase' reaction, use of exogenous CoQ10 and of flavoprotein substitute (PMS)], the distribution and activity of succinate dehydrogenase, NAD(P)H-tetrazolium reductase, glucose-6-phosphate dehydrogenase, lactate dehydrogenase (H and M types), and of L-glutamate dehydrogenase (E.C.1.4.1.2 and E.C.1.4.1.3) have been investigated in the rat cerebellum. It was evident from the study that reliable results could only be obtained if all the aforementioned factors had been considered. The image of actual concentration of SDH in the neuropil of the molecular layer could only be recorded by adding CoQ10, while other structures exhibited greater balance between SDH and endogenous mitochondrial CoQ. Contrary to previous studies, a reversed localization of the activity of G-6-PDH and LDH was noticed. The elements of molecular and Purkinje layers were rich in G-6-PDH, while the granular layer was nearly depleted. The actual level of LDH could only be recorded if NADH-tetrazolium reductase was bypassed with PMS. The H and M types of LDH coexisted in the three cortical layers, the H type being prevalent and the M type attaining its highest level in synaptic glomeruli followed by the structures of the molecular layer and the Purkinje cells. High activity of GDH was noticed in Bergmann glia followed by synaptic glomeruli, while most other structures showed weak to moderate activity. The two GDH types coexisted in all structures showing activity, except for Bergmann cells, which only showed presence of the E.C. 1.4.1.3 type. Furthermore, Bergmann glia was exceptional by showing no activity of SDH and LDH, but strong activity of G-6-PDH and NADPH-tetrazolium reductase. The granular cells were exceptional by showing weak or no activity of all enzymes in question.
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PMID:Methodological aspects of the histochemical localization and activity of some cerebellar dehydrogenases. 66 87

Rats were injected with various amounts of bovine albumin (0.5, 1.0 and 1.75 g/24h), inducing thereby proteinuria ranging from 100 to 400 mg/24h. The glomerular oxygen uptake, dry weight and glucose-6-phosphate dehydrogenase (G-6-PHD) activity were measured on the 4th day of proteinuria and in a group of control animals. Oxygen uptake increased of +60%, expressed per glomerulus and of +25% when expressed per milligram dry weight and this increase was not different between the 3 groups of rats. Glomerular dry weight increased significantly in the 3 series. There was an highly significant relationship between glomerular dry weight and oxygen uptake, combining the 3 series together. G-6-PDH increased as expected from previous experiments and this increase was more marked for the more marked proteinuria. The relationship between G-6-PDH and QO2 was of borderline statistical significance (p=0.05). The glomerular hypertrophy, oxidative hyperactivity and increase in G-6-PDH activity are probably related to transcellular transport of protein.
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PMID:Glomerular metabolism in protein-load proteinuria. 91 75

In fresh human skin homogenates, the activities of four enzymes, lactate dehydrogenase (LDH), glucose-6-phosphate dehydrogenase (G-6-PDH), "acid" phosphatase (AcP), and "leucine aminopeptidase" (LAP) were assayed following an incubation with hydrocortisone, hydrocotisone acetate, or hydrocortisone-17-butyrate, respectively. Concentration of the three compounds measured 2.75 mMol/l. Hydrocortison butyrate inhibited LDH-G-6-PDH-, and AcP-activities. Hydrocortisone and hydrocortisone acetate exerted a significant inhibitory action only in the case of G-6-PDH-activity.--On pure G-6-PDH from yeast, the inhibition exerted by hydrocortisone butyrate was significantly stronger than the inhibition exerted by the two other steroids. Time/action diagrams revealed the fact that hydrocortisone butyrate is superior to the other two compounds from the beginning of the incubation period.--The date sustain the assumption that hydrocortisone butyrate exerts biochemical-pharmacological actions of its own and that it may not be considered just as an esterified transport form of hydrocortisone.
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PMID:Enzyme inhibition in human skin homogenates by hydrocortisone, hydrocortisone acetate and hydrotisone butyrate. 94 55


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