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:3.1.3.1 (alkaline phosphatase)
47,916 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Percoll density gradient centrifugation was used for isolating large quantities of bradyzoites of Sarcocystis suicanis, which were used for enzymatic analysis. Crude extracts of bradyzoites contained activities suggestive of several acid hydrolases. Levels of acid and alkaline phosphatase were higher than those of beta-N-acetylhexosaminidase and beta-galactosidase. Acid phosphatase was purified 156-fold with an overall recovery of 54% using DEAE-Sepharose 4B and Sephadex G-200 chromatography. The partially purified enzyme was not a glycoprotein and had a molecular weight of approximately 170,000. The enzyme was markedly inhibited by Cu++, Hg++, and iodoacetamide, suggesting the presence of a sulfhydryl group. Sodium tartrate caused strong inhibition of the enzyme. The acid phosphatase of S. suicanis appears to be a unique enzyme that cannot be classified under high or low molecular weight acid phosphatases of widely diverse origin.
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PMID:Studies on the enzymes of Sarcocystis suicanis: purification and characterization of an acid phosphatase. 311 63

Plasma levels of the lysosomal enzymes, beta-hexosaminidase and beta-glucuronidase, were analyzed in rats with carbon tetrachloride induced liver cirrhosis. Out of 22 animals, 15 showed cirrhotic and 4 pre-cirrhotic livers. 4 cirrhotic animals exhibited cholestatic features with increased bilirubin, alkaline phosphatase (ALP) and aspartate aminotransferase (ASAT) in plasma. The remaining 15 pre-cirrhotic and cirrhotic rats showed clear significant changes only in ASAT levels. These 15 rats showed no consistent increase in plasma, spleen or liver lysosomal enzyme activities, whereas the 4 rats with cholestatic features exhibited considerable increases of lysosomal enzymes. The increased activities might be attributed to decreased biliary excretion and/or increased production of lysosomal enzymes by activated macrophages.
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PMID:Lysosomal enzymes in plasma, liver and spleen from rats with carbon tetrachloride-induced liver cirrhosis. 315 68

In order to establish an animal model for assessing early and sensitive biochemical indicators of pulmonary damage, we studied the effects of inhaled CdCl2 (5 mg/m3.h; mass median aerodynamic diameter (MMAD) = 1.4 microns; SDg = 1.8) on the antioxidant defense and pulmonary surfactant systems of rat lungs. Rats were sacrificed 1, 4, 8, and 16 d after inhalation. Pulmonary edema (wet/dry weight) was observed on d 1. The total activities of the enzymes superoxide dismutase (SOD) and glucose-6-phosphate dehydrogenase (G6PD) in the lung homogenates of the treated animals were significantly throughout the 16-d period. Glutathione reductase (GR) was increased on d 4 and after. The general increases of SOD, GR, and the lysosomal enzymes acid phosphatase and beta-N-acetylglucosaminidase could be attributed to changes in the cellularity of the lung tissue. The significant increase in the specific activity of G6PD on d 4 suggested enzyme stimulation. Concurrently, the response of the surfactant system was measured by assaying the alkaline phosphatase (AKP) and the phospholipid content in the homogenates and in the cell-free bronchoalveolar lavage (BAL) fluids. The AKP activity in the homogenates decreased by 30%, while no activity was detected in the BAL on d 1, suggesting an inhibition of AKP by Cd. The secretion of surfactant seemed altered at this early time: phospholipid in the BAL decreased by 44%, although it increased by 61% in the tissue. The high recovery of phospholipid (312%) in the BAL on d 4 and the important changes in the AKP activity in the BAL from d 4 to 16 may reflect alterations in the processing of the surfactant. The effect of Cd on AKP makes this enzyme a potential marker of the metal redistribution in the pulmonary alveolar region, which could be a useful tool in long-term studies.
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PMID:Toxicity of inhaled cadmium chloride: early responses of the antioxidant and surfactant systems in rat lungs. 334 99

Mouse bone marrow-derived mast cells passively sensitized with monoclonal IgE released paf-acether (platelet-activating factor) and beta-hexosaminidase when challenged with the specific antigen. The formation and the release of paf-acether followed an early increase in the activity of the acetyltransferase, the main enzyme in paf-acether biosynthesis. The antigen-induced activation of the acetyltransferase was dependent on physiologic temperature and on the presence of Ca2+. By using microsomal fractions from unchallenged and challenged mast cells, the Vmax values were 3.5 and 12.0 nmol/min/mg of protein, respectively, whereas in both cases a Km value for acetyl-coenzyme A of 172 microM was measured. The stimulation of acetyltransferase could be mimicked in vitro under experimental conditions which favor phosphorylation, i.e. adding ATP and Mg2+ to lysates from unchallenged mast cells. In contrast, ATP and Mg2+ were uneffective on lysates from challenged cells that exhibited high level of acetyltransferase activity, suggesting that phosphorylation of the enzyme already took place at the time of cell stimulation. Moreover, addition of alkaline phosphatase to microsomal fraction obtained from either antigen-challenged mouse bone marrow-derived mast cells or unchallenged cells, resulted in 52% and 43% loss of acetyltransferase activity, respectively. Phorbol myristate acetate treatment of cells doubled the enzyme activity supporting the phosphorylation hypothesis. Thus, we report on the immunologic activation of a key enzyme for paf-acether synthesis and on the mechanism of this activation in a pure mast cell population. A link between bridging of IgE receptors and the activation of an enzyme critical to the formation of a lipid mediator is thereby evidenced.
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PMID:Biosynthesis of paf-acether. IX. Role for a phosphorylation-dependent activation of acetyltransferase in antigen-stimulated mouse mast cells. 358 83

The efficacy of bronchoalveolar lavage in the removal of cellular and extracellular components of the lining layer from the lungs of silica-treated and control rats was determined. Exponential functions were fitted to curves generated by plotting the quantity of lining layer constituent removed from the lungs by bronchoalveolar lavage versus the lavage number. From these exponential functions we determined the total amount of constituent available in the pulmonary extracellular lining and hence the efficacy of the lavage procedure in removing materials from the lungs. With control rats the removal of extracellular phospholipids, soluble protein, alkaline phosphatase, and beta-N-acetylglucosaminidase by bronchoalveolar lavage occurred at significantly different rates. Removal of 95% of the total available extracellular phospholipid, beta-N-acetylglucosaminidase, soluble protein, and alkaline phosphatase from the lungs required 4, 4, 8, and 11 lavages, respectively. Removal of 95% of the total available alveolar macrophages required 18 lavages. The influence of pulmonary inflammation on the efficacy of the lavage procedure was investigated by injecting silica dust intratracheally into the lungs of rats (50 mg/200- to 250-g rat) and after 3 days performing the analyses. Silica caused an inflammatory condition in the lungs resulting in the accumulation of materials in the alveoli. Highly significant increases in soluble protein (16-fold), alkaline phosphatase (9-fold), and beta-N-acetylglucosaminidase (11-fold), polymorphonuclear leukocytes, eosinophils, and lymphocytes were observed. Alveolar macrophages and extracellular phospholipid were not significantly elevated at 3 days after dosing. Silica did not alter the efficacy of the lavage procedure in removing from the lungs any of the extracellular constituents of the lung lining.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Quantitation of cellular and extracellular constituents of the pulmonary lining in rats by using bronchoalveolar lavage. Effects of silica-induced pulmonary inflammation. 366 42

In order to evaluate the early response of the alveolar epithelium following lung injury, male Long-Evans adult rats (280-350 g) were treated with a single dose (30 mg/kg, ip) of the herbicide paraquat. No animal died during the 72 h that followed the acute administration of the herbicide. When compared to control, total lipid, phosphatidylcholine, and disaturated phosphatidylcholine contents of lung homogenates from the paraquat-treated rats were significantly reduced 48 h postdose (respectively 10, 24, and 37%). Comparatively, the total lung alkaline phosphatase activity was significantly reduced as early as 12 h postdose, and by 48 h the activity had decreased by approximately 50%. Although a significant decrease in total lung acid phosphatase activity was observed 24 and 48 h after the treatment, the effect was much less than with the alkaline phosphatase activity (15% versus 50%, respectively). The lysosomal beta-N-acetylglucosaminidase and the cytoplasmic lactate dehydrogenase activities were not affected by the herbicide treatment. A subcellular fractionation of the treated lungs showed that 48 h postdose, the total alkaline phosphatase activities associated with lamellar body and surfactant fractions were decreased respectively by 60% and 49%. Due to the intrinsic association of a strong alkaline phosphatase activity with the pulmonary surfactant system, these data suggest that the monitoring of the alkaline phosphatase activity in lung fractions could represent an early and sensitive indicator of toxicity to the alveolar epithelium, most probably to type II cells.
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PMID:Lung hydrolases in paraquat poisoning: early response of alkaline phosphatase. 368 20

The present investigation was undertaken to clarify the in vitro effect of zinc on bone metabolism in tissue culture. Calvaria were removed from weanling rats (3-week-old males) and cultured for periods up to 96 hr in Dulbecco's Modified Eagle Medium (high glucose, 4500 mg/dl) supplemented with antibiotics and bovine serum albumin. The experimental cultures contained 10(-7) to 10(-3) M zinc sulfate. All cultures were incubated at 37 degrees in 5% CO2/95% air. Zinc uptake by bone was increased significantly in cultures with concentrations of zinc greater than 10(-6) M. Bone calcium content was increased significantly by the presence of 10(-4) M zinc. This increase was blocked by the presence of 10(-6) M cycloheximide. Bone alkaline phosphatase activity was elevated in the presence of zinc (10(-6) to 10(-3) M), but the effect was inhibited by 10(-7) M cycloheximide or 10(-8) M actinomycin D. Zinc (10(-4) M) also significantly increased ATPase activity in the bone, whereas it did not alter significantly by pyrophosphatase, acid phosphatase and beta-N-acetylglucosaminidase activities. Furthermore, bone collagen content was raised by 10(-6) to 10(-4) M zinc. This elevation was prevented by 10(-7) cycloheximide or 10(-8) M actinomycin D. Bone DNA content and [3H]thymidine incorporation by the bone were not altered significantly by 10(-4) M zinc. These findings indicate that the zinc had a direct stimulatory effect on bone mineralization in vitro, and that bone protein synthesis was a necessary component of this response. Zinc may stimulate bone formation in tissue culture.
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PMID:Stimulatory effect of zinc on bone formation in tissue culture. 368 32

In porcine areolar placental epithelia, 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, nonspecific 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 enzyme activities remained almost unchanged during the period of investigation. Of the dehydrogenases, the diaphorases as well as succinate and lactate dehydrogenase demonstrated generally an intensive activity within the epithelia. The activity of the other dehydrogenases was only low. The activity of unspecific esterase was very intensive within the uterine epithelia but remarkably low within chorionic epithelia. Contrarily, the reaction of adenosine triphosphatase was more intensive within chorionic than uterine epithelia. All investigated glucosidases reacted distinctly positive within chorionic epithelia, but only beta-N-acetyl-hexosaminidase and beta-galactosidase in uterine epithelia. The high activity of acid phosphatase, especially within the chorionic epithelium, seems to be connected with uteroferrin, an iron-binding protein. The histochemical results are discussed in context with the function of the areolae in histiotrophic nutrition and iron transport.
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PMID:[Enzyme-histochemical studies of the pig placenta. II. Histotopics of enzymes in the areolar placenta epithelium]. 392 41

The effects of zinc on the enzymes of femoral tissue were investigated in weanling rats that had been given zinc sulfate (1.0 mg Zn2+/100 g body wt) p.o. for 3 days. Administration of zinc caused a marked elevation of alkaline phosphatase and acid phosphatase activities, whereas it did not cause significant changes in succinate dehydrogenase, 5'-nucleotidase, ATPase, pyrophosphatase and beta-N-acetylglucosaminidase activities. The effect of zinc was greater on alkaline phosphatase of the femoral diaphysis. Zinc content of the femoral diaphysis was raised significantly by administration of zinc. The addition of zinc in concentrations of 10(-2)-10(2) microM did not produce a significant increase in alkaline phosphatase activity in the femoral diaphysis, indicating that zinc could not activate the enzyme. Administration of cycloheximide or actinomycin D completely inhibited the increase in alkaline phosphatase activity produced by administration of zinc. DNA content of the femoral diaphysis, but not epiphysis, was increased markedly by administration of zinc. The increases in both alkaline phosphatase activity and DNA content of the femoral diaphysis were not caused by administration of copper, manganese, cobalt, nickel and chromium(III). The present investigation suggests that zinc may induce the increase in alkaline phosphatase related to DNA synthesis and, as a result, stimulate bone growth.
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PMID:Action of zinc on bone metabolism in rats. Increases in alkaline phosphatase activity and DNA content. 395 86

1. The control of exo-beta-N-acetylglucosaminidase (EC 3.2.1.30) production by Bacillus subtilis B growing on a chemically defined medium was studied. 2. The enzyme was repressed during exponential growth by those carbon sources that enter the glycolytic pathway above the level of phosphoenolpyruvate. When exponential growth ceased as a result of low concentrations of the nitrogen, carbon or metal ion components of the medium, the enzyme was formed and its amount could be increased by the addition of cell-wall fragments as inducer. 3. The enzyme was de-repressed and could be induced during exponential growth on non-glycolytic compounds metabolized directly into pyruvate, acetyl-CoA or tricarboxylic acid cycle intermediates. 4. The major difference in the metabolism of the organism utilizing these two groups of compound was the existence of high activities of phosphoenolpyruvate carboxylase required for gluconeogenesis. 5. It is concluded that the de-repression of glucosaminidase occurs when the only principal change detected in the intermediary metabolism of the organism was the presence of high activities of phosphoenolpyruvate carboxylase. 6. When the organism was grown on media containing repressing compounds, the enzyme was only de-repressed on entry of the cells into the initial stages of sporulation, where phosphoenolpyruvate carboxylase activity, even in the presence of excess of glucose, increased in parallel with glucosaminidase, neutral proteinase and alkaline phosphatase activities. 7. These results suggest a strong link, at the level of the tricarboxylic acid cycle, between the control of phosphoenolpyruvate carboxylase and the control of the de-repression of glucosaminidase and sporulation.
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PMID:Control of the production of exo-beta-N-acetylglucosaminidase by Bacillus subtilis B. 419 60


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