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)

Sertoli cells and peritubular fibroblasts were collected from sexually mature Wistar rats and incubated by themselves (ASC) or in co-culture (AS/PC) for ten days with or without follicle stimulating hormone (FSH). Freshly collected cells and those of the ASC and AS/PC cultures were processed for histochemical detection of three esterases and four dehydrogenases. The relative staining intensities of azo dye and formazan reaction products were recorded for the cell cultures, co-cultures and appropriate controls. Freshly collected Sertoli cells stained heavily for lactic dehydrogenase (LDH), succinic dehydrogenase (SDH), glucose-6-phosphate dehydrogenase (G-6-PDH), non-specific esterase (Est.) and 3 beta-hydroxysteroid dehydrogenase (3 beta-OLDH). For Sertoli cells alone in culture (ASC) there was a marked decline of enzyme reaction product deposition/cell for LDH and Est. and absence of cellular staining for SDH, G-G-PDH, B-Est. and 3 beta-OLDH. The addition of FSH did not change this histochemical staining pattern for the adult cells in vitro. The presence of peritubular cells in adult Sertoli cell cultures (AS/PC) resulted in the maintenance of metabolic enzyme staining (i.e., LDH, SDH, G-6-PDH and Est.) in Sertoli cells, minimal staining for B-Est., but absence of detectable enzyme reaction product for 3 beta-OLDH. Sertoli cells co-cultured with other fibroblasts or in medium pre-conditioned with peritubular cells but not containing them stained minimally for LDH and Est. and did not generate reaction product for any of the other enzymes. The addition of FSH to the AS/PT co-culture as in the ASC cultures did not affect the enzyme histochemical staining profile of Sertoli cells.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Selected enzyme histochemistry of Sertoli cells. 2. Adult rat Sertoli cells in co-culture with peritubular fibroblasts. 240 3

A study was made of the occurrence of glucose-6-phosphate dehydrogenase (G-6-PDH) deficiency among patients with lung tuberculosis including those suffering from mental diseases (alcoholism or schizophrenia). In Azerbaijani patients, the rate of G-6-PDH demonstration was higher as compared to that among the healthy population. On combined lung tuberculosis and alcoholism the rate of that abnormality demonstration increased whereas on associated lung tuberculosis and schizophrenia, it slightly decreased. Among patients with hereditary G-6-PDH deficiency, the portion of chronic destructive forms of pulmonary tuberculosis is high, the tuberculous process is accompanied more often by isolation of M. tuberculosis. The etiological role of G-6-PDH as a genetic marker is evaluated as 14%; in associated lung tuberculosis and alcoholism, it grows to 18%.
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PMID:[Pulmonary tuberculosis in patients with hereditary glucose-6-phosphate dehydrogenase deficiency]. 253 43

Previous studies in this laboratory have shown that glutamine synthetase (GS) and other key metabolic enzymes are inactivated by metal-catalyzed oxidation reactions in vitro. Oxidative inactivation renders these proteins highly susceptible to proteolysis, especially to a class of newly identified alkaline proteases which exhibit little or no activity against the native enzymes. These studies have suggested that oxidative inactivation may be an important marking step for intracellular protein degradation. Because many of the enzymes which have been shown to accumulate as inactive or less active forms during aging are readily inactivated by metal-catalyzed oxidation reactions in vitro, we have investigated the possible relationship between protein oxidation and proteolysis during aging and oxidative stress in vivo. Oxidized proteins accumulate in hepatocytes of rats exposed to 100% oxygen during the first 48 h of oxygen treatment. In the interval between 48 and 54 h the levels of oxidized proteins decline sharply. The specific activities of at least two liver enzymes, glutamine synthetase and glucose-6-phosphate dehydrogenase (G-6-PDH), decrease during the 54-h experiment. GS and G-6-PDH specific immunological cross-reactivity remains high during the first 48 h of oxygen treatment and then declines in the interval between 48 and 54 h. During this same interval the levels of alkaline proteases which degrade oxidized proteins increase, indicating that these activities are induced or activated in response to oxidative stress and subsequently degrade the proteins which have become oxidized during the initial phase of oxygen treatment. Oxidized proteins accumulate progressively during aging in hepatocytes from rats 3 to 26 months old, with the largest incremental increase between 20 and 26 months. The increase in protein oxidation is correlated with a loss of specific activity of GS and G-6-PDH without a concomitant loss of immunological cross-reactivity. The levels of alkaline proteases which degrade oxidized proteins in hepatocytes from 26-month-old rats is only 20% that of 3-month-old rats, suggesting that oxidized proteins accumulate in hepatocytes from old rats, in part, because the proteases which degrade them are deficient or defective. moreover, when old rats are subjected to treatment with 100% oxygen, the levels of oxidized proteins continue to increase and the alkaline protease activity remains low, indicating that these protease activities are not increased in response to oxidative stress in old rats.
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PMID:Protein oxidation and proteolysis during aging and oxidative stress. 257 64

The effect of manganese exposure (Mn2+ 4 mg Mn/kg intraperitoneally) on certain bioantioxidants in brain, liver, kidney and testes in growing rats maintained on 21% and 8% casein diet were investigated. Manganese administration for 30 days caused significant reduction in the level of GSH (reduced glutathione) in liver and testes and GR (glutathione reductase) and G-6-PDH (glucose-6-phosphate dehydrogenase) in brain, liver and testes. The magnitude of alteration was greater in 8% casein diet fed animals compared to rats maintained on 21% casein diet. These results indicate that protein deficient animals are more susceptible to the manganese induced biochemical changes in various tissues. The mechanism of such changes is discussed.
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PMID:Effect of manganese on some bioantioxidants in various organs of protein-deficient rats. 278 47

The activity of enzymes found in the plasma, malate dehydrogenase (MDH) and lactate dehydrogenase (LDH), and enzymes from erythrocytes, glucose-6-phosphate dehydrogenase (G-6-PDH) and catalase, was studied in rats contaminated by crude oil. Crude oil (tube fed) contamination caused a significant increase in MDH and LDH activity 96 hr after contamination while a decrease in activity was noted in 6-6-PDH and catalase. An additional contamination (1 week after the first contamination), measured 96 hr after contamination, caused a relative decrease in MDH and LDH activity while there was a contrasting relative increase in G-6-PDH and catalase activity. After a recovery period of 3 weeks the only significant change was an increase in catalase activity.
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PMID:Enzymatic activity in crude oil contaminated rats. 287 73

In vivo administration of L-thyroxine (L-T4) in Anabas testudineus, while significantly stimulated the activities of cytochrome c oxidase and alpha-glycerophosphate dehydrogenase (alpha-GPDH), inhibited glucose-6-phosphate dehydrogenase (G-6-PDH), cytosolic and mitochondrial malate dehydrogenase (cyt. MDH; mit. MDH), and Mg2+ DNP-dependent adenosine triphosphatase (Mg2+ ATPase) activities. The activities of lactate dehydrogenase (LDH), succinate dehydrogenase (SDH), and catalase remained unaltered after L-T4 treatment. Administration of protein synthesis inhibitors such as actinomycin D, while significantly inhibited cytochrome oxidase, alpha-GPDH, catalase, SDH, and Mg2+ ATPase activities, did not change LDH, cyt. MDH, and mit. MDH activities. Chloramphenicol injection significantly stimulated cytochrome oxidase, alpha-GPDH, and G-6-PDH activities. Simultaneous injections of actinomycin D or chloramphenicol with 3,5,3'-triiodo-L-thyronine (L-T3) or L-T4 prevented the effects of thyroid hormones on enzyme activities, when compared to the respective controls.
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PMID:Oxidative metabolism in a teleost, Anabas testudineus Bloch: effect of thyroid hormones on hepatic enzyme activities. 292 Sep 3

The aim of the study was to determine a biochemical basis for the augmented oxidative metabolism found in mononuclear leukocytes (MNL) of patients with active psoriasis. Dehydroepiandrosterone (DHEA) is known to inhibit glucose-6-phosphate dehydrogenase (G-6-PDH). We determined the activity of G-6-PDH as well as the penetration and metabolism of DHEA - diminished plasma concentrations of which have been found in psoriatics previously - in 16 patients with active psoriasis and 16 controls. MNL in patients with psoriasis possessed 52% more (p less than 0.05) G-6-PDH activity, based on cell number, and 34% more (p less than 0.05) activity, based on soluble protein. No difference in DHEA penetration and metabolism in MNL was found between psoriatics and controls, in contrast with previous findings of reduced penetration and increased reduction in erythrocytes of psoriatics. We conclude that the enhanced G-6-PDH activity in MNL of patients with active psoriasis is not due to altered DHEA penetration or metabolism.
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PMID:Augmented glucose-6-phosphate dehydrogenase activity and normal penetration and metabolism of dehydroepiandrosterone in mononuclear leukocytes in psoriasis. 294 86

Architectural arrangement, ultrastructure, and selected histochemical properties of the newt (Notophthalmus viridescens) liver were examined. Although hematopoietic tissue (1-4 cells thick) invested the liver, direct vascular communication between this tissue and hepatic parenchyma was not observed. The liver was intensely positive when stained with Oil-red-O and periodic acid-Schiff reagent and connective tissue was limited to large vascular channels and the capsule. A distinctive polarity was observed in the hepatic vascular system when lobes were viewed in cross section. Dorsally, portal venules accompanied arterioles and branches of the biliary system, while tributaries of hepatic veins were observed ventrally. Following perfusion fixation, hepatocytes appeared as sheets of cells 1-5 cells thick; however, lobules as defined in adult mammalian liver were absent. Hepatocytes contained abundant smooth endoplasmic reticulum, mitochondria, electron-dense lysosomes, patches of granular endoplasmic reticulum, and lipid droplets. Continuous endothelial cells lined sinusoids and exhibited fenestrae organized into structures similar to sieve plates observed in mammalian liver. Variable numbers of melanin-containing macrophages and subendothelial macrophages were observed; however, Kupffer cells and lipid containing perisinusoidal fat-storing cells were not seen. Patterns of reaction product for glucose-6-phosphatase (G-6-Pase), glucose-6-phosphate dehydrogenase (G-6-PDH), and succinic dehydrogenase (SDH) were localized in the newt liver. All enzymes exhibited a uniform distribution pattern; however, small punctate regions of intensely positive G-6-PDH cells were noted within hepatic parenchyma. Cells comprising the hematopoietic tissue were intensely positive for G-6-Pase, G-6-PHD, and negative for SDH.
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PMID:Morphologic and histochemical analysis of the newt (Notophthalmus viridescens) liver. 303 62

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

Genital organs and blood were obtained from dairy cows at a local abattoir. 3 recently ovulated follicles and 20 corpora lutea of estrous cycle (CLC) were used for the quantitative enzyme histochemical demonstration of delta 5-3 beta-hydroxysteroid dehydrogenase (3 beta-OHSDH), succinate dehydrogenase (SDH) and glucose-6-phosphate dehydrogenase (G-6-PDH) activity, employing a computerized microscope photometer. Progesterone was determined in blood serum by radioimmunoassay. Luteal tissue was grouped into several stages of development according to micromorphological criteria. Activities per volume unit of 3 beta-OHSDH and SDH in large luteal cells (LLC), as well as in small luteal cells (SLC), and luteal tissue (LT), relative amounts of the 3 beta-OHSDH-positive tissue fraction (PLCC), and progesterone concentrations in blood serum exhibited a significant pattern corresponding to the morphological development of the endocrine gland. G-6-PDH showed an increase in activity per volume unit during tissue development lasting until the beginning of regressive changes, and as significant in LLC and LT. Activities per volume unit of 3 beta-OHSDH (p less than or equal to 0.001) and SDH (p less than or equal to 0.01) were higher in LLC than in SLC, indicating superior steroidogenic capacities, while G-6-PDH activity was distinctly higher in the latter (p less than or equal to 0.001). Almost all parameters tested were correlated positively. 3 beta-OHSDH and SDH exhibited a significantly positive correlation in LLC (p less than or equal to 0.01) and LT (p less than or equal to 0.001) during periods of measureable progesterone secretion. In SLC this correlation was nonsignificant (p greater than 0.05). G-6-PDH showed a relative poor correlation to 3 beta-OHSDH (LLC, p less than or equal to 0.05; LT, p less than or equal to 0.01) and SDH (LT, p less than or equal to 0.05). Enzyme activities in LLC as well as in SLC were generally positively correlated (p less than or equal to 0.001). All enzymes tested exhibited a significantly positive correlation with progesterone concentrations in blood serum. This was significant for SDH only during measurable progesterone secretion, and less marked for G-6-PDH.
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PMID:Delta 5-3 beta-hydroxysteroid dehydrogenase, succinate dehydrogenase and glucose-6-phosphate dehydrogenase in the bovine corpus luteum of estrous cycle: a quantitative histochemical study. 316 57


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