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:3.4.15.1 (ACE)
18,300 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The maximal activity of key enzymes of glycolysis, pentose phosphate pathway, TCA cycle and glutaminolysis were measured in the immune tissues of rats fed w-3 PUFA during 6 weeks. Total lipid peroxidation and glutathione peroxidase activity were also measured. The hexokinase activity was enhanced 4-fold in the spleen and thymus, doubled in the liver and was diminished in mesenteric lymph nodes (35%). Citrate synthase activity was decreased in the spleen and lymph nodes and increased in the thymus. G-6-PDH activity was increased 2-fold in the spleen and mesenteric lymph nodes and by 20% in the thymus whereas it was reduced (66%) in the liver. Glutathione peroxidase activity and total lipid peroxides increased in all tissues of rats fed w-3 PUFA. The results presented here suggest that w-3 PUFA, by causing important metabolic changes in the immune tissues and lipid peroxidation may lead to changes of immune function.
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PMID:Metabolic changes induced by w-3 polyunsaturated fatty acid rich-diet (w-3 PUFA) on the thymus, spleen and mesenteric lymph nodes of adult rats. 181 2

Glycerol-3-phosphate dehydrogenase (G-3-PDH) isozymes were investigated in several bee and wasp species to verify if variations detected in G-3-PDH-2 isozymes are closely related to the age and activity of adult workers in the nest or hive of social species. In the solitary, the semisocial, and one social bee species, no phenotypic variations were detected for G-3-PDH-2 isozymes, and this was also the case for all wasp species investigated which were characterized as social. These results allow us to suggest that the variation detected in G-3-PDH-2 isozymes is a phenomenon closely related not only to adult age and activity in the hive, but also to a gradual acquisition of the ability to fly, which is not present in newly emerged worker meliponids in particular.
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PMID:Glycerol-3-phosphate dehydrogenase isozyme variation in adult meliponids (Hymenoptera: Apidae). 182 23

In a previous report we found extreme hyperinsulinemia associated with high testosterone levels in patients with polycystic ovarian syndrome (PCO) and normal insulin levels in a small group of patients with elevated dehydroepiandrosterone (DHEA). From these observations, we hypothesized that DHEA and testosterone may have opposing actions on insulin sensitivity. To test this hypothesis, we studied insulin sensitivity in vivo and in vitro in a) obese PCO women with elevated testosterone, b) obese patients with adult-onset adrenal hyperplasia (AH) and high levels of DHEA, c) weight-matched obese controls, and d) lean controls. Insulin sensitivity was determined by insulin responses to a standard OGTT, hypoglycemic responses to an IV insulin tolerance test (ITT), red blood cell (RBC) insulin binding and receptor kinase activity, and phytohemagglutinin (PHA)-activated T-lymphocyte (T-cell) insulin binding and PDH insulin sensitivity. In PCO patients, we found that basal and glucose-challenged insulin levels were significantly greater than, and hypoglycemic responses to IV insulin, significantly lower than, weight-matched control values. However, AH patients had insulin values significantly below, and hypoglycemic responses significantly above, those of the weight-matched controls. Their values were, in fact, comparable to those observed for the lean control subjects. Similar findings were observed with insulin binding and PDH insulin sensitivity. Insulin sensitivity in all study subjects was found to be negatively correlated to testosterone and positively correlated to DHEA and, more significantly, to the ratio of DHEA/testosterone. These data would suggest that, in females, DHEA and T may have opposing actions on insulin sensitivity. We conclude that in females insulin sensitivity in vivo and in vitro is modulated, at least in part, by the ratios of DHEA to testosterone.
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PMID:Role of adrenal and gonadal androgens in insulin action and metabolism. 183 13

A major issue in the study of the pathogenesis of primary biliary cirrhosis is whether the E2 subunit of the pyruvate dehydrogenase complex (PDH-E2), the major autoantigen in the disease, exists as a tissue-specific isoform. cDNA clones spanning a segment of the 3'-catalytic region of PDH-E2 (nt 1158-1361) have been isolated from human kidney, placenta and bile epithelium cells. Nucleotide sequence analysis of the clones showed differences consistent with the presence of normal variants of PDH-E2 in the human population. However, the existence of tissue-specific isoforms of PDH-E2 cannot yet be discounted.
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PMID:The human pyruvate dehydrogenase complex: a polymorphic region of the lipoate acetyl transferase (E2) subunit gene. 191 85

Cathepsin D, acid phosphatase, beta-galactosidase, N-acetyl hexosaminidase, leucine aminopeptidase (LAP), lactate dehydrogenase, glucose-6-phosphate dehydrogenase (g-6-PDH), and peroxidase activities were measured in the buccal mucosa of rats kept for 60 days on high-sucrose (68% of sucrose) caries-inducing diet. The findings evidence that this diet observed for 30 days results in a significant elevation of beta-galactosidase and LAP activities and in reduction of peroxidase level. After 60-day diet the examined parameters virtually did not differ from the reference characteristics (a control group kept on 68% starch diet), except elevated g-6-PDH and lowered peroxidase activities. Enzymic activity changes are adaptive and evidence changes in the metabolic processes in the buccal mucosa, that may eventuate in the development of periodontal diseases.
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PMID:[The effect of a high-saccharose diet on the enzymatic activity of the oral mucosa in rats]. 192 95

The oxidative pentose phosphate pathway is poorly developed in the rat heart compared with other organs, since the activity of glucose-6-phosphate dehydrogenase (G-6-PDH), the first and rate-limiting enzyme of the oxidative pentose phosphate pathway, is low. As a consequence, the available pool of 5-phosphoribosyl-1-pyrophosphate and the rate of adenine nucleotide biosynthesis are limited. Isoproterenol, 24 hours after subcutaneous administration at 0.1, 1, and 25 mg/kg, stimulated the activity of G-6-PDH in whole hearts dose-dependently from 4.3 +/- 0.16 (control) to 6.6 +/- 0.35, 10.3 +/- 0.82, and 11.5 +/- 0.56 units/g protein, respectively. The activity of 6-phosphogluconate dehydrogenase, another of the enzymes in the oxidative pentose phosphate pathway, remained unchanged. G-6-PDH activity started to increase 12 hours after isoproterenol application, when the glycogenolytic and functional response was over, and reached a peak value between 24 and 48 hours. This stimulating effect was also demonstrated in cardiac myocytes that were isolated 28 hours after isoproterenol application. beta-receptor blockade with atenolol reduced the isoproterenol-induced increase in cardiac G-6-PDH activity by 90%. Cycloheximide, which inhibits translation, and actinomycin D, which interferes with transcription, attenuated it by 83% and 78%, respectively. These results indicate that cardiac beta-adrenergic receptors and enzyme protein synthesis are involved in this effect. Other beta-sympathomimetic agents such as dopamine, dobutamine, fenoterol, salbutamol, and terbutaline also stimulated myocardial G-6-PDH activity in a time- and dose-related manner. The calcium antagonist D 600 (gallopamil) reduced the isoproterenol-elicited stimulation by 65%, and verapamil blunted the fenoterol-induced increase by 50%. This suggests that Ca2+ ions also contribute to the stimulation of the cardiac oxidative pentose phosphate pathway.
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PMID:Beta-adrenergic agonists stimulate the oxidative pentose phosphate pathway in the rat heart. 197 8

The effect of severe insulin-induced hypoglycemia on the activity of the pyruvate dehydrogenase enzyme complex (PDHC) was investigated in homogenates of frozen rat cerebral cortex during burst suppression EEG, after 10, 30, and 60 min of isoelectric EEG, and after 30 and 180 min and 24 h of recovery following 30 min of hypoglycemic coma. Changes in PDHC activity were correlated to levels of labile organic phosphates and glycolytic metabolites. In cortex from control animals, the rate of [1-14C]pyruvate decarboxylation was 7.1 +/- 1.3 U/mg of protein, or 35% of the total PDHC activity. The activity was unchanged during burst suppression EEG whereas the active fraction increased to 81-87% during hypoglycemic coma. Thirty minutes after glucose-induced recovery, the PDHC activity had decreased by 33% compared to control levels, and remained significantly depressed after 3 h of recovery. This decrease in activity was not due to a decrease in the total PDHC activity. At 24 h of recovery, PDHC activity had returned to control levels. We conclude that the activation of PDHC during hypoglycemic coma is probably the result of an increased PDH phosphatase activity following depolarization and calcium influx, and allosteric inhibition of PDH kinase due to increased ADP/ATP ratio. The depression of PDHC activity following hypoglycemic coma is probably due to an increased phosphorylation of the enzyme, as a consequence of an imbalance between PDH phosphatase and kinase activities. Since some reduction of the ATP/ADP ratio persisted and since the lactate/pyruvate ratio had normalized by 3 h of recovery, the depression of PDHC most likely reflects a decrease in PDH phosphatase activity, probably due to a decrease in intramitochondrial Ca2+.
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PMID:Changes in pyruvate dehydrogenase complex activity during and following severe insulin-induced hypoglycemia. 198 96

Primary biliary cirrhosis (PBC) is a chronic autoimmune liver disease that includes the presence of lymphoid infiltrates in portal tracts, high titer autoantibodies against pyruvate dehydrogenase-E2 (PDH-E2) and branched chain ketoacid dehydrogenase-E2 (BCKD-E2), and biliary tract destruction. The mechanism by which the autoimmune response is induced, the specificity of damage to the biliary epithelium, and the role of T cells in PBC are still unknown. To address these issues, we have taken advantage of a mouse mAb, coined C355.1, and studied its reactivity against a panel of liver tissue from normal subjects as well as a panel of liver specimens from patients with PBC, progressive sclerosing cholangitis, and chronic active hepatitis (CAH). C355.1, much like human autoantibodies to PDH-E2, reacts exclusively by immunoblotting with PDH-E2, binds to the inner lipoyl domain of the protein, and inhibits PDH-E2 activity in vitro. In addition, we have also attempted to develop cloned T cell lines that react with PDH-E2 and/or BCKD-E2 using liver biopsies from patients with PBC, compared with CAH. Although monoclonal C355.1 produced typical mitochondrial fluorescence on sections of normal liver, pancreas, lung, heart, thyroid, and kidney, it produced a distinct and intense reactivity when used to stain the bile ducts of patients with PBC. Nine of 13 PBC liver biopsies studied herein contained bile ducts on light microscopy, all of which reacted intensely at a 1:100 culture supernatant dilution of monoclonal C355.1. In contrast, although bile ducts of liver specimens from normals, CAH, and progressive sclerosing cholangitis also reacted with C355.1, such reactivity was exclusively mitochondrial and readily detectable only at a dilution of 1:2. More importantly, we generated CD4+, CD8-, alpha beta TCR+ cloned T cell lines from patients with PBC, but not from CAH, that produced IL-2 specifically in response to PDH-E2 or BCKD-E2.
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PMID:Evidence for the targeting by 2-oxo-dehydrogenase enzymes in the T cell response of primary biliary cirrhosis. 198 55

We have previously shown that normal Wistar rats fed for 3 weeks with an isocaloric sucrose-rich (63%) diet (SRD) develop high levels of plasma free fatty acids and increased triacylglycerol content in the myocardium. We are now reporting that these changes are accompanied by remarkably low levels of the active form of the pyruvate dehydrogenase complex (PDHa; mean +/- SEM, 37.2% +/- 3.7% of the total activity) when compared with levels found in hearts donated by control rats fed the standard chow diet (STD; 71.0% +/- 2.8%; P less than .01). Increased concentrations of both long-chain acyl-CoA (0.21 +/- 0.03 v 0.06 +/- 0.01 mumol.g dry weight-1 found in STD; P less than .01) and acetyl-CoA (0.17 +/- 0.05 v 0.09 +/- 0.01 found in STD; P less than .01), as well as a relative decrease in coenzyme A (CoASH) (0.21 +/- 0.02 v 0.32 +/- 0.05 from STD; P = NS), resulting in an increased acetyl-CoA/CoASH ratio (0.80 +/- 0.13 v 0.29 +/- 0.03 in STD; P less than .01) may have stimulated the PDH kinase, leading in turn to an inactivation of the PDH complex. The above enzymatic and metabolic changes in the in situ heart of SRD-fed rats were still present after perfusing them for 35 minutes with a Krebs-Henseleit buffer containing 11 mmol/L glucose as the only exogenous substrate.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Biochemical abnormalities in the heart of rats fed a sucrose-rich diet: is the low activity of the pyruvate dehydrogenase complex a result of increased fatty acid oxidation? 198 63

Overall 94 patients with different patterns of pulmonary tuberculosis were examined for glutathione peroxidase (GP), glutathione reductase, glucose 6-phosphate dehydrogenase (G 6-PDH) and superoxide dismutase activity in neutrophils and lymphocytes. Chemiluminescence was used to study the capacity of neutrophils to generate free oxygen forms. Neutrophils showed functional deficiency of GP and G 6-PDH. The decrease of the oxygen-producing capacity of neutrophils, unbalance of glutathione-conjugated enzymes in lymphocytes were revealed either. The role of the alterations enumerated in the reduction of function of phagocytizing and immunocompetent cells in patients with pulmonary tuberculosis is discussed.
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PMID:[The oxidative metabolic indices of phagocytizing and immunocompetent cells in patients with pulmonary tuberculosis]. 209 92


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