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)

One hour after a single i.v. dose of 250 mg/kg folic acid, the straight portion of distal tubules in the outer medulla of rat kidneys showed a distinct reduction in succinate dehydrogenase, NADH2-diaphorase, glutamate dehydrogenase, cytochrome oxydase, Na+/K+-ATPase, and acid phosphatase activity. In contrast, the proximal tubules exhibited only a reduction in glutamate dehydrogenase and alkaline phosphatase activity. At this time the straight portion of the distal tubules, whose enzyme activity had changed, showed partly regressive epithelial changes. 24 hours after folic acid administration an even greater reduction in enzyme activity had occurred in the straight portion of distal tubules; these structures also became dilated. The adjacent collecting tubules and the corresponding proximal tubules were also severely dilated, the proximal tubules showing a loss in enzyme acitivities similar to those observed in the distal tubules. 48 hours after folic acid administration the changes largely resembled those observed after 24 hours, but were more pronounced. At this time a tubular regeneration was observed. 72 hours after folic administration extensive normalization of the histological and histochemical changes had occured. It is postulated that a disturbance of the hairpin counter-current mechanism occurs as a result of a direct, concentration-dependent effect of folic acid on the enzymes of the energy supplying metabolism. A dilation in the region of the loop of Henle and the collecting tubules occurs subsequently.
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PMID:Enzyme histochemistry of rat folic acid nephropathy. 19 86

The excretory canals of Ascaridia galli (Nematoda) and the protonephridial ducts of Cotylophoron cotylophorum (Trematoda) and Raillietina cesticillus (Cestoda) have been studied with regard to the histochemical localization of lipids, carbohydrates and hydrolytic enzymes. Distinct excretory organs are absent in the acanthocephalan Centrorhynchus corvi. Triglycerides, phospholipids and lipoproteins are seen in association with the wall of excretory canals of A. galli and R. cesticillus, and phospholipids and lipoproteins at the corresponding site in C. cotylophorum. The physiological significance of lipids in association with excretion of substances has been discussed. Low molecular weight glycogen is present in the lumen of excretory canal of A. galli but not in other worms. The common feature of the excretory canals is the presence of enzyme activities of nonspecific alkaline phosphatase and Mg2+-dependent ATPase. Activity of acid phosphatase is seen only in the excretory canals of A. galli. Glucose-6-phosphatase is present in A. galli and C. cotylophorum and absent in R. cesticillus. Weak reaction of 5'-nucleotidase is present in the excretory canals of helminth species studied here. The role of these enzymes in transportation of substances across the wall of excretory canals and also in ionic regulation has been discussed in detail.
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PMID:Comparative histochemical observations on the excretory system of helminth parasites. 19 23

Immature mice were treated for 21 days with daily doses of triamcinolone diacetate. The trigeminal ganglion was studied enzymatically for the activity of alkaline phosphatase, acid phosphatase, ATPase and succinic dehydrogenase. It became apparent that the prolonged treatment with a potent corticosteroid hormone did not affect significantly the in vivo activity of the above enzymes. Some enzymes even appeared to have increased their intracellular activity. The heterogeneous effect of corticosteroid upon their peripheral target organs is discussed.
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PMID:Activity of phosphatases and succinic dehydrogenase in the trigeminal ganglion of the corticosteroid-treated mouse. 20 36

The release of plasma membrane ecto-enzymes by a phosphatidylinositol-specific phospholipase C from Staphylococcus aureus was investigated. There was no effect on L-leucyl-beta-naphthylamidase, alkaline phosphodeisterase I and Ca2+- or MG2+-ATPase, but substantial proportions of the alkaline phosphatase and 5-nucleotidase were released. There was no simultaneous release of phospholipid and the solubilized enzymes were not exluded from Sepharose 6-B. It was therefore concluded that release was not a secondary consequence of membrane vesiculation but occurred as a result of the disruption of specific interactions involving the phosphatidylinositol molecule.
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PMID:Specific release of plasma membrane enzymes by a phosphatidylinositol-specific phospholipase C. 20 48

A study was made of the effect of procedures (freezing-thawing prior to incubation, prefixation with formaldehyde and glutaraldehyde, incubation with DMSO) on the activity of ATPase and beta-glycerophosphatase in leucocytes and erythrocytes of man, and of the effect of these procedures and of homogenization on ATPase activity in the cells of the rat thymus. The homogenization of rat thymocytes decreases ATPase activity by 15%. A repeated freezing-thawing results in a 15% decrease of ATPase activity in the cells of the rat thymus. The homogenization of rat thymocytes decreases ATPase activity in rat thymocytes, in a 2% decrease in human leucocytes, and in a 21% increase in human erythrocytes. Beta-glycerophosphatase activity in leucocytes and in erythrocytes increases thereby by 89 and 38%. Incorporation of 5% DMSO into the medium increases ATPase activity in human leucocytes and erythrocytes by 17 and 16%, while thymocytes this activity drops by 27%. Beta-glycerophosphatase activity increases thereby in leucocytes by 26 and in erythrocytes by 11.5%, resp.
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PMID:[Comparative electron cytochemical and biochemical study of ATPase and beta-glycerophosphatase activity in thymocytes, leukocytes and erythrocytes]. 21 82

To determine the mechanism of the maturation of the brush border membrane in intestinal epithelial cells, purification of the plasma membrane from undifferentiated rat crypt cells and of the basal-lateral membrane from villous cells has been performed. The method is based on density perturbation of the mitochondria to selectively disrupt their association with the membrane. With both cell populations, two membrane subfractions displaying the same respective density on sucrose gradient have been obtained with an overall yield of 15--20% and a 10-fold enrichment of the plasma membrane markers 5'-nucleotidase and (Na+ + K+)-dependent, ouabain-sensitive ATPase chosen to follow their purification. The four fractions were constituted by sheets and apparently closed vesicles of various sizes. Each fraction was characterized by a distinct protein composition and different levels of enzyme activities. The cells, used for the preparation of the membranes, were isolated as a villus to crypt gradient. This separation and that of the membranes, led to the conclusion that the (Na+ + K+)-dependent ATPase is localized principally in the plasma membrane of all cells whatever their state of maturation, while 5'-nucleotidase is predominantly located in the basal-lateral membrane of the villous cells and may serve as a specific marker for the purification of this membrane. Finally it has been shown that aminopeptidase, dissacharidases and alkaline phosphatase do not appear simultaneously in the maturation process of the cells, alkaline phosphatase being absent from the crypt cells and aminopeptidase being the first to be synthesized. This enzyme seems to appear in the crypt cells membrane before being integrated into the mature brush border membrane.
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PMID:Plasma membranes from rat intestinal epithelial cells at different stages of maturation. I. Preparation and characterization of plasma membrane subfractions originating from crypt cells and from villous cells. 21 16

The enzyme Na+,5+-ATPase was cytochemically localized in the rat hepatocyte by a modification of the Ernst potassium-dependent nitrophenyl phosphatase technique. Measurement of nitrophenol release from 50-micrometer liver slices confirmed the presence of ouabain-inhibitable nitrophenyl phosphatase activity that increased over the 30-min incubation period. Electron micrographs demonstrated that sinusoidal and lateral membrane reaction product deposition was K+-dependent, Mg++-dependent, inhibited by ouabain but not by alkaline phosphatase inhibitors, and was localized to the cytoplasmic side of the membrane. In contrast, canalicular reaction product was K+-independent, Mg++-dependent, inhibited by alkaline phosphatase inhibitors but not by ouabain, and was localized to the luminal side of the membrane. These findings indicate that Na+,K+-ATPase is localized to the sinusoidal and lateral portions of the rat hepatocyte plasma membrane and is not detectable on the bile canaliculus where alkaline phosphatase is confined. This basolateral localization of Na+,K+-ATPase is similar to that found in epithelia where secretion is also directed across the apical membrane.
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PMID:Cytochemical localization of Na+, K+-ATPase in the rat hepatocyte. 21 46

The isoform spectra of alkaline and acid phosphatase, pyrophosphataes, and ATPase in periplasm of E. coli were studied using electrophoresis in polyacrylamide gel with subsequent development of zimograms directly in the gel. Wild strains and mutants on 4 regulatory genes of alkaline phosphatase were analyzed. Mutations in regulatory genes were shown to influence the amount of each of the 3 isoforms of alkaline phosphatase and also the spectra of other phosphohydrolases.
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PMID:[Effect of mutations in regulatory genes for alkaline phosphatase on the phosphohydrolase spectrum of E. coli periplasm]. 21 71

Phenylketonuric squirrels have shown marked inhibition of alkaline phosphatase in the olfactory lobes and cerebral hemispheres, whereas the Na+-K+-ATPase remained less altered. In the pathogenesis of phenylketonuria inhibition of alkaline phosphatase at the level of "Blood-Brain Barrier" (BBB), leads transport system to impaired functioning.
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PMID:Imbalance in the activities of alkaline phosphatase and Na+-K+-ATPase in the brain of experimentally induced phenylketonuric squirrels (Funambulus palmarum). 21 45

A correlation was sought between changes in enzymes involved in gastric acid secretion (Mg-, NaK-, K- and HCO3-stimulated ATPases) and histological changes in gastric biopsies. Alkaline phosphatase was also studied. Mg- and NaK-stimulated ATPase activities increased significantly in biopsies from the pylorus and antrum which showed moderate or severe gastritis. NaK ATPase levels increased and HCO3 ATPase decreased in incisural, body and fundic mucosa which had intestinal metaplasia and atrophic gastritis. No K+ ATPase was found in normal mucosa. The total activity of alkaline phosphatase did not vary with histological changes in the gastric mucosa. Results indicate that the ATPase enzyme systems are sensitive indicators of gastric mucosal disease.
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PMID:Mucosal enzyme patterns in gastric epithelial disease. 21 78


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