Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.3.1 (alkaline phosphatase)
 47,916 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Isopycnic sedimentation has been used to separate granulocytes of varying stages of maturity from the bone marrows of normal rabbits and rabbits stimulated to undergo an intense inflammatory response. The separated cell populations were in turn utilized to study the specific activities of six intracellular enzymes. The study revealed an increase with cell maturation in the specific activities of myeloperoxidase, NADPH oxidase, alkaline phosphatase and acid phosphatase in normal animals; in stimulated animals only myeloperoxidase and NADPH oxidase increased significantly with cell maturation. Glucose-6-phosphate dehydrogenase showed no change in specific activity in all animals studied. Malate dehydrogenase tended to show a specific activity decrease in the maturing cells of normal but not in those of stimulated animals.
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PMID:Characterization of marrow granulocyte development: enzyme-specific activity profiles in response to inflammatory reactions. 2 66

Catalase activity in leucocytes was found to be half the normal value in hypocatalasemia and extremely low in acatalasemia. Glucose-6-phosphate dehydrogenase activity in erythrocytes was not significantly different between normal, hypocatalasemia and acatalasemia in three families of acatalasemia, but in one family lower activities than normal were found in hypocatalasemia and actalasemia erythrocytes. Other enzyme activities in blood, such as alkaline phosphatase, lactate dehydrogenase, glutamic oxaloacetic and glutamic pyruvic transaminases were not significantly different between normal subjects, hypocatalasemia and acatalasemia.
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PMID:Activities of catalase in leucocytes and glucose-6-phosphate dehydrogenase in erythrocytes of hypocatalasemia and acatalasemia. 91 59

In continuation of earlier studies on murine neoplastic liver lesions, we characterized by histochemical methods the phenotype of hepatocellular adenomas and carcinomas induced by single injections of diethylnitrosamine (1.25, 2.5, or 5.0 micrograms/g of body weight) in 15-day-old C57BL/6 x male C3H F1 mice. The hepatocellular adenomas were composed predominantly of basophilic cells but stored excessive amounts of fat and glycogen in large portions of the tumors. Irrespective of the carcinogenic dose, the adenomas showed a consistent histochemical pattern. Glycogen synthase and phosphorylase were highly active in the hepatocytes that stored glycogen. In cells poor in, or free of, this polysaccharide, these enzymes were only moderately active or even inactive. In glycogen-storing parts of the adenomas, the activity of adenylate cyclase was reduced compared with normal liver parenchyma, but in fat-storing portions it was elevated. In a few adenomas, uniform increase in adenylate cyclase activity could be encountered. The levels of ATPase, acid phosphatase, and glucose-6-phosphatase were either increased or decreased. Glucose-6-phosphate dehydrogenase and glyceraldehyde-3-phosphate dehydrogenase showed an increased activity in all adenomas compared with preneoplastic foci, which in turn exhibited a higher glucose-6-phosphate dehydrogenase and glyceraldehyde-3-phosphate dehydrogenase activity than the surrounding parenchyma or the liver of untreated controls. The hepatocellular carcinomas showed remarkable histochemical changes compared with adenomas. The levels of fat and glycogen and the activities of glycogen synthase, phosphorylase, and in most cases also that of glucose-6-phosphate dehydrogenase, were reduced significantly. In contrast, adenylate cyclase, glucose-6-phosphatase, glyceraldehyde-3-phosphate dehydrogenase, and also alkaline phosphatase showed a striking elevation in developing carcinomas. Similar, although more pronounced, histochemical changes were seen in the advanced hepatocellular carcinomas. These observations indicated that progression from adenomas to hepatocellular carcinomas was associated with a change in the activity of several enzymes involved in cell membrane function, glycogen metabolism, the oxidative pentose phosphate pathway, and glycolysis.
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PMID:Histochemical profile of mouse hepatocellular adenomas and carcinomas induced by a single dose of diethylnitrosamine. 184 80

Changes in carbohydrate metabolism were studied in midgut gland, muscle, and gill tissues of marine prawn Penaeus indicus exposed to a sublethal concentration (0.3 ppm) of phosphamidon. A significant decrease in glycogen and pyruvate and an increase in lactate content were observed in all phosphamidon-exposed prawn tissues after 96 hr. An increase in phosphorylase a and aldolase activity levels suggested the increased formation of triose sugars during phosphamidon toxicity. LDH activity was considerably decreased and an increment in lactate content was observed which indicates reduced mobilization of pyruvate into the citric acid cycle. Glucose-6-phosphate dehydrogenase activity was considerably increased, suggesting the enhanced oxidation of glucose in the hexose monophosphate shunt pathway. Krebs cycle enzymes such as NAD-isocitrate dehydrogenase, succinate dehydrogenase, and malate dehydrogenase were found to be decreased, suggesting the impairment in mitochondrial oxidative metabolism due to the acute toxic impact of phosphamidon. Cytochrome-c oxidase and Mg2+ ATPase activity levels were also decreased considerably, suggesting impaired energy synthesis and breakdown during phosphamidon toxicity, as a result of reduced oxidation of glucose aerobically. The increase in acid and alkaline phosphatase activities indicates the enhanced breakdown of phosphate to release energy in view of inhibiton or impairment in the ATPase system during phosphamidon-induced stress. These results suggest that phosphamidon has a profound effect on the oxidative metabolism of prawn which results in the triggering of compensatory metabolic pathways for survivability.
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PMID:Modulation of carbohydrate metabolism in the selected tissues of marine prawn, Penaeus indicus (H. Milne Edwards), under phosphamidon-induced stress. 337 38

Kinetics and thermodynamics of the spontaneous formation of glucose-6-arsenate (G6As) and 6-arsenogluconate (6AsG) as well as the ability of these compounds for substituting their phosphorylated homologues in enzymic reactions have been studied. Formation of G6As and glucose-6-phosphate (G6P) shows similar thermodynamic constants. Both reactions are endothermic, endergonic, and occur with a decrease of entropy. However, the kinetic coefficients of the spontaneous formation of the arsenate esters are ca. 10(5) times greater than those of their homologous phosphate esters. The activation energy of the spontaneous formation of G6As (E = +12 kcal mol-1) is even smaller than that of the formation of G6P by alkaline phosphatase (E = +13 kcal mol-1). Similar to the case of monoalkylphosphates, the monoanion species of G6As is much more reactive than the dianion species. This is an important difference with respect to G6P. Arsenate esters are good analogs of the phosphate esters for a variety of enzymes. Glucose-6-phosphate dehydrogenase shows nearly similar values of Km and Vmax for either G6P or G6As, and hexokinase is similarly inhibited by both compounds. 6-phosphogluconate dehydrogenase has the same Vmax with respect to 6PG and 6AsG, although the enzyme shows a much lower affinity for the latter substrate. The calculated half-lives at 25 degrees C and pH 7 of G6As and 6AsG are only ca, 6 and 30 min respectively, they increase at lower temperature and alkaline pH. At 0 degrees C and pH 9 the half-life of G6As is ca. 20 h.
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PMID:[Formation and properties of sugar arsenate esters]. 714 95

Changes in oxidative metabolism were studied in hepatopancreas, muscle, and hemolymph of the edible crab Scylla serrata, exposed to a sublethal concentration (2.5 ppm) of cadmium chloride. A significant decrease in glycogen, total carbohydrates, and pyruvate and an increase in lactate levels in hepatopancreas and muscle were observed. Hemolymph sugar levels were increased in experimental crabs. An increase in phosphorylase suggested increased glycogenolysis during cadmium toxicity. The decrease in lactate dehydrogenase activity and the increase in lactate content indicated reduced mobilization of pyruvate into the citric acid cycle. Krebs cycle enzymes such as succinate dehydrogenase and malate dehydrogenase were found to be decreased, suggesting impairment of mitochondrial oxidative metabolism as a consequence of cadmium toxicity. Glucose-6-phosphate dehydrogenase activity was increased, suggesting enhanced oxidation of glucose by the HMP pathway. Cytochrome-c oxidase and Mg2+ ATPase activity levels decreased, indicating impaired energy synthesis during cadmium stress. Acid and alkaline phosphatase activities increased, suggesting enhanced breakdown of phosphates to release energy in view of impaired ATPase system during cadmium exposure. A significant decrease in protein and free amino acid and an increase in ammonia, urea, and glutamine levels were observed in the tissues during exposure. An increase in protease, alanine aminotransaminase, and aspartate aminotransaminase suggested increased proteolysis and transamination of amino acids. The increase in glutamate dehydrogenase, AMP deaminase, and adenosine deaminase indicated increased ammonia production. The increased arginase and glutamine synthetase suggested the detoxification or mobilization of ammonia toward the production of urea and glutamine. These results suggest that cadmium affects oxidative metabolism and induces hyperammonemia, and crabs switch over their metabolic profiles toward compensatory mechanisms for the survivability in cadmium-polluted habitats.
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PMID:Changes in oxidative metabolism in selected tissues of the crab (Scylla serrata) in response to cadmium toxicity. 753 86

In guided bone regeneration (GBR), a semipermeable membrane is placed over an osseous defect to create a secluded environment in which bone formation can proceed without ingrowth of connective tissue cells from the overlaying soft tissue. Although the cell-occlusive property of GBR membranes appear to be essential to new bone formation, the role of transmembrane tissue fluid diffusion is not known. The objective of this study was to evaluate the degree to which diffusion across commonly used GBR membranes can support functional properties of osteoblast-like cells in vitro. Cells from an established osteoblast-like line (SAOS-2) were cultured on membranes of cross-linked collagen, noncross linked collagen, and ePTFE. The membranes rested on metal grids which allowed the membranes to lightly contact the surface of the culture medium. As a control, cells were directly plated and cultured in control wells. At days 7 and 21, cells were harvested by scraping the membranes or culture wells and analyzed for expression of alkaline phosphatase (ALP), core binding factor 1 (cbfa-1), bone sialoprotein-2 (BSP-2), and osteocalcin (OC). Expression was determined by quantitative real-time PCR. Glucose-6-phosphate dehydrogenase (G6PD) served as a reference gene. The membranes were examined by transmission light microscopy. RT-PCR revealed up-regulation of ALP of up to 60-fold and of cbfa-1 and BSP of up to threefold relative to G6PDH. Expression of OC was less then onefold. The expression profile for each of the four genes tested demonstrated small variations among cells grown on different membranes. Microscopic observations revealed remnants of undisrupted osteoblast-like cells attached to both collagen membranes. Cell morphology and spatial arrangement indicated that vitality was maintained. Diffusion through the three membranes evaluated in this study was sufficient to support osteoblast-like cell differentiation.
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PMID:Cytobiocompatibility of collagen and ePTFE membranes on osteoblast-like cells in vitro. 1806 90

Trichloroethylene (TCE), an industrial solvent, is a major environmental contaminant. Histopathological examinations revealed that TCE caused liver and kidney toxicity and carcinogenicity. However, biochemical mechanism and tissue response to toxic insult are not completely elucidated. We hypothesized that TCE induces oxidative stress to various rat tissues and alters their metabolic functions. Male Wistar rats were given TCE (1000 mg/kg/day) in corn oil orally for 25 d. Blood and tissues were collected and analyzed for various biochemical and enzymatic parameters. TCE administration increased blood urea nitrogen, serum creatinine, cholesterol and alkaline phosphatase but decreased serum glucose, inorganic phosphate and phospholipids indicating kidney and liver toxicity. Activity of hexokinase, lactate dehydrogenase increased in the intestine and liver whereas decreased in renal tissues. Malate dehydrogenase and glucose-6-phosphatase and fructose-1, 6-bisphosphatase decreased in all tissues whereas increased in medulla. Glucose-6-phosphate dehydrogenase increased but NADP-malic enzyme decreased in all tissues except in medulla. The activity of BBM enzymes decreased but renal Na/Pi transport increased. Superoxide dismutase and catalase activities variably declined whereas lipid peroxidation significantly enhanced in all tissues. The present results indicate that TCE caused severe damage to kidney, intestine, liver and brain; altered carbohydrate metabolism and suppressed antioxidant defense system.
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PMID:Effect of trichloroethylene (TCE) toxicity on the enzymes of carbohydrate metabolism, brush border membrane and oxidative stress in kidney and other rat tissues. 1936 49

This study reports the protective effects of selenium on fluoride induced alterations in the activities of pro-oxidative (xanthine oxidase (XOD), lipid peroxidation (LPO) free radical scavenging, [catalase, superoxide dismutase (SOD), glutathione-s-transferase (GST), glutathione peroxidase (GPX), glutathione reductase (GR), glutathione) and metabolic (glucose-6-phosphate dehydrogenase, alanine amino transferase (ALAT), aspartate aminotransferase (AAT), creatine phosphokinase (CPK), acid phosphatase (AP), alkaline phosphatase (ALP)] enzymes along with fluoride and selenium levels in brain of mice. Animals were divided into control, NaF treated group (20 mg kg(-1) body wt.(-1) intraperitonial) and Selenium+NaF treated group (sodium selenite, 5 microg of selenium/0.2 ml distilled water kg(-1) body wt.(-1) day) and were maintained for 14 days on respective treatments. The decreased bodyweight (-11.35%) as well as organosomatic index (-15.1%) of brain in NaF group were recovered in treatment of selenium along with NaF. The increased accumulation of fluoride (32.1%) in brain observed in NaF treated group compared to control was diminished in selenium+NaF treated group. Selenium levels (3.03%) increased in selenium+NaF treated group in compared to decrement in NaF treatment. The SOD (-16.6%), Catalase (-21.5%), GST(-13.72%), GPX (-19.16%), GR (-44.97%) activities and Glutathione (-23%) content in NaF treated group were decreased significantly compared to controls, which were significantly (p < 0.01) recovered in selenium+NaF group. Increased XOD (10.85%) and LPO (8.61%) levels observed in brain of NaF treated mice were reversed with selenium treatment. Glucose-6-phosphate dehydrogenase (-46.98%), ALAT (-10.44%), AAT (-10.21%), CPK (-27.98%) were decreased and alkaline phosphatase (10.6%), acid phosphatase (24.09%) increased in brain of mice after administration of NaF. All metabolic enzymes were significantly (p < 0.01) reversed after administration of selenium to the NaF treated group. Thus, the adverse effects of NaF on oxidative and metabolic enzymes of brain were reversible with ameliorative action of selenium supplementation. As evident in this study the antioxidative nature of selenium coupled with its reversal effect on metabolic enzymes in brain of mice treated with fluoride suggests its use as antidote agent against fluorosis.
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PMID:Protective effects of selenium on fluoride induced alterations in certain enzymes in brain of mice. 2014 19

Activity dynamics of glucose-6-phosphate dehydrogenase, alkaline phosphatase, beta-galactosidase and beta-lactamase in the course of growth and development of Gram-negative bacteria Serratia marcescens was studied. Glucose-6-phosphate dehydrogenase can serve as a marker of cytoplasm and be also used as a marker of plasma membrane continuity. Alkaline phosphatase is a marker ofperiplasm. Glucose-6-phosphate dehydrogenase, beta-lactamase and beta-galactosidase can be additionally used as markers of the outer membrane continuity of microbial cells.
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PMID:[Activity dynamics of potential marker enzymes of Serratia marcescens cytoplasm and periplasm]. 2087 66


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