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:3.6.1.3 (ATPase)
65,361 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Enzyme histochemistry was assessed in semi-thin glycolmethacrylate sections after 100 mg/kg 2-bromoethanamine (BEA) hydrobromide had been given ip to male Wistar rats to induce renal papillary necrosis. Changes in the proximal tubular marker enzymes alkaline phosphatase (Alk Phos), gamma-glutamytranspeptidase (GGT) and adenosine triphosphatase (ATPase) were not apparent before 8 hr, but there was a progressive loss up to 144 hr. The proteinaceous PAS-positive casts in the loops of Henle and the collecting ducts stained for Alk Phos and GGT (from 12 hr) and for ATPase (from 18 hr). Acid phosphatase (Acid Phos) staining was increased in the proximal tubule lysosomes from 18 hr. There was a marked increase in Alk Phos in all hyperplastic upper urothelial cells from 8 to 24 hr, and a mosaic of staining remained in the pelvis adjacent to the necrosed papilla at 144 hr. At 12 hr, there was an increase in the staining of the pelvic, ureter and bladder vascular endothelial ATPase, the intensity and area of which increased progressively from 18 hr and almost occluded the capillary lumens in the worst affected areas by 144 hr. These data show several distinct series of pathological changes after the administration of BEA. The subtle degenerative changes in the proximal tubule followed the papillary lesion, but exfoliated brush border and proximal tubular cells were important components of the protein casts in the distal nephron. Similarly, the intense Alk Phos staining in the hyperplastic regions of the upper urothelium and the increased pelvic, ureteric and bladder endothelial ATPase staining suggested they develop as a consequence of the papillary lesion.
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PMID:Enzyme histochemical changes in an acutely induced renal papillary necrosis. 197

The localization of some enzyme in adult worms of Clonorchis sinensis was studied by histochemical method in this paper. Acid phosphatase was detected mainly in digestive duct, subtegument and the walls of testis, uterus and ovary; acetylcholinesterase was found in oral sucker, ventral sucker, pharynx; and ATPase was found to exist in oral sucker, ventral sucker, pharynx and muscle layer in the subtegument. The eggs of C. sinensis possessed the above three enzymes.
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PMID:[Histochemical studies on some enzymes in Clonorchis sinensis]. 252 40

Histochemical tests were done on newly excysted metacercariae and worms recovered from an abnormal host (rat) and the definitive host (dog) for some oxidoreductases, phosphatases and glycosidases. The results demonstrate that rat worms have enzymatic distribution and intensities more similar to those of metacercariae than to adult worms from dogs. Ultracytochemical examination of acid and alkaline phosphatase and Mg-ATPase activity was also carried out. Acid phosphatase activity occurred exceptionally in the excretory bladder and caeca of dog worms. No activity was observed in rat worms except for lysosomal granules in the tegument. Alkaline phosphatase activity was exhibited in the excretory bladder in both dog and rat worms. Mg-ATPase activity occurred in the tegument and parenchymal cells in dog worms and in the excretory bladder in rat worms. In metacercariae, little or no reaction for these enzymes was present except for Mg-ATPase activity on the excretory ducts. These observations, together with the histochemical results, indicate that metabolic activity in rat worms is higher than in metacercariae although it is strongly reduced compared with dog worms.
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PMID:Studies on host specificity in Paragonimus westermani: II. Histochemical and cytochemical characterization of metacercariae and worms from rats and dogs. 253 34

To test the possibility that stimulation of secretion leads Na,K-ATPase to be recruited from cytoplasmic pools and inserted into basal-lateral plasma membranes, we surveyed the subcellular distributions of Na,K-ATPase in resting and stimulated fragments of rat exorbital lacrimal gland. After a two-dimensional separation procedure based on differential sedimentation and density gradient centrifugation, we defined six density windows, which differ from one another in their contents of biochemical markers. The membranes equilibrating in window I could be identified as a sample of basal-lateral membranes; in resting preparations these membranes contained Na,K-ATPase enriched 16.6-fold with respect to the initial homogenates. Windows II through VI contained various cytoplasmic membrane populations; these accounted for roughly 80% of the total recovered Na,K-ATPase activity. Thirty-minute stimulation with 10 microM carbachol caused a 1.4-fold increase (P less than 0.05) in the total Na,K-ATPase content of window I; this increase could be largely accounted for by a 1.7-fold decrease in the total Na,K-ATPase content of density window V. Acid phosphatase activity also redistributed following stimulation, but it was recruited from a different source, and it was inserted into membranes equilibrating in windows II and III as well as into the membranes of window I.
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PMID:Stimulation-associated redistribution of Na,K-ATPase in rat lacrimal gland. 284 91

Localized high AMP deaminase activity was found in the rimmed vacuoles of skeletal muscles in acid maltase deficiency, distal myopathy with rimmed vacuole formation, and experimental chloroquine myopathy on histochemical staining. Acid phosphatase activity was also increased in and around these vacuoles, but the vacuoles were negative for other histochemical stainings such as with NADH-tetrazolium reductase, ATPase and phosphorylase. These findings suggest that AMP deaminase is bound to membranous components in addition to myosin in skeletal muscle.
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PMID:High AMP deaminase activity in rimmed vacuoles of skeletal muscle. 294 4

The cytochemical localization of enzymatic activity by means of backscattered electron imaging (BEI) is reviewed and the application of BEI to changes in acid phosphatase and ATPase distribution during physiological (programmed) cell death in Heliothis midgut is explored. Programmed cell death entails the release of nascent free acid phosphatase as extracisternal hydrolase. This shift can readily be detected by means of the atomic number contrast imparted by BEI of the lead phosphatase reaction product, thus enabling the distribution of dying cells to be mapped. BEI is particularly useful in this context as it allows the examination of bulk specimens at low magnification. Death of cells is also accompanied by a collapse in ATPase activity which shows up as cytochemically negative areas in the X-ray microscope and by means of BEI. Acid phosphatase in normal cells is localized in the apical microvilli and lysosomes. Senescent or dying cells, however, clearly show a basally situated free hydrolase which migrates throughout the cell. Parallel TEM results confirm that this enzyme is ribosomal and extracisternal rather than lysosomal in origin. ATPase activity is largely limited to the apical microvilli, although there is some activity associated with the basal plasma membranes. The apical ATPase, however is partially resistant to ouabain. Young and mature cells are positive although in the latter case some microvilli may be lost as the cells acquire a negative cap or dome. Inhibition by bromotetramizole indicates that apical activity is not to any significant extent contributed to by alkaline phosphatase. Degenerate or dead cells are negative and can be seen as a mozaic of "black patches" among normal cells when imaged by means of BEI or X-ray microscopy.
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PMID:The use of backscattered electron imaging, X-ray microanalysis and X-ray microscopy in demonstrating physiological cell death. 297 76

The distribution of several hydrolytic enzymes was investigated in rabbit submandibular glands at both the light and electron microscopical levels. Glands were fixed by either immersion or perfusion fixation with a variety of fixatives containing 1-2% glutaraldehyde and 2-4% formaldehyde in 0.1 M cacodylate buffer at pH 7.2. Light microscopically, the acinar cells showed some staining for ATPase, acid phosphatase and nonspecific esterases but showed weak staining for thiamine pyrophosphatase. Acid phosphatase staining occurred most strongly in granular tubule cells. Staining for esteroproteases was confined to the periluminal rims of intercalary and striated ducts. Alkaline phosphatase was very sensitive to glutaraldehyde and was confined to myoepithelial cells. Electron microscopical observations revealed the presence of acid phosphatase reaction product in lysosomes, immature granules and in GERL-like structures, the last being much more conspicuous in the granular tubule cells. ATPase reaction product was localized to the basal and luminal plasma membranes and lumina of both acinar and granular tubule cells. The Golgi complex of these two types of cells exhibited only moderate amounts of reaction product for thiamine pyrophosphatase. Alkaline phosphatase activity, on the other hand, was exclusively localized to myoepithelial cells in their plasma membranes and sometimes in the nuclear envelope.
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PMID:Histochemistry of hydrolytic enzymes in resting submandibular glands of rabbits. 316 50

Male Sprague-Dawley rats received 4 mg pilocarpine/100 g body wt intraperitoneally or physiological saline as control and were killed at various intervals. Acid phosphatase was reacted on frozen sections from soft palate, parotid and submandibular glands using sodium-alpha-naphthyl acid phosphate as substrate. Various inhibitors were added to the incubation medium. The strongest acid phosphatase activity was in the parotid gland acinar and proximal secretory duct cells; the mucous minor glands of the palate were completely negative. Activity was found in the acinar cells, proximal secretory duct cells, granular and striated duct and excretory duct cells. Pilocarpine injection slightly reduced the activity up to 6 h after injection. Cupric chloride added to the incubation medium lowered the overall activity. Fluoride and molybdate inhibited the acid phosphatase reaction in all structures. Tartrate inhibited the reaction in all structures except the submandibular striated duct cells. The tartrate-resistant activity may be a Na+K+-dependent ATPase involved in re-absorbing water and electrolytes from the primary saliva.
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PMID:A histochemical study of rat salivary gland acid phosphatase. 346 May 42

High yields of mouse macrophage-melanocyte heterokaryons and macrophage-macrophage homokaryons were obtained through the virus-induced fusion of cells spread on a glass surface. After fusion there was a striking reorganization of cellular architecture by means of a colcemid-sensitive process. Heterokaryons were isolated through the use of differential trypsinization and many underwent division to form melanocyte-like hybrids. The selective uptake of dextran sulfate by macrophages served as a useful cytoplasmic marker in identifying hybrids. Many characteristic macrophage properties were altered in the heterokaryons. Within an hour of fusion macrophage nuclei became swollen, nucleoli were more prominent, and increased nuclear RNA synthesis occurred. 3 hr after fusion, a wave of DNA synthesis took place in the previously dormant macrophage nuclei. The fate of typical macrophage markers was examined in both heterokaryons and homokaryons. Macrophage homokaryons continued to exhibit active phagocytosis of sensitized erythrocytes, whereas this capacity was lost irreversibly in heterokaryons. The loss of phagocytic activity of heterokaryons occurred at an exponential rate and was accelerated by high concentrations of calf serum. Another macrophage surface marker, a divalent cation-dependent adenosine triphosphatase (ATPase), could be demonstrated histochemically on heterokaryons. Shortly after fusion, it was present in discrete regions, but it became more diffuse and disappeared within a day. Acid phosphatase-positive secondary lysosomes and retractile lipid droplets disappeared from heterokaryons but continued to accumulate in macrophage homokaryons. These observations indicate that typical macrophage properties cease to be expressed in heterokaryons, and melanocyte functions presumably predominate in heterokaryons and hybrids.
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PMID:Macrophage-melanocyte heterokaryons. I. Preparation and properties. 431 6

The Wachstein and Meisel incubation medium was used to detect ATPase activity in epimastigote, spheromastigote (amastigote), and bloodstream trypomastigote forms of Trypanosoma cruzi. Reaction product, indicative of enzyme activity, was associated with the plasma membrane covering the cell body and the flagellum of the parasite. No reaction product was found in the portion of the plasma membrane lining the flagellar pocket. The plasma membrane-associated ATPase activity was not inhibited by ouabain or oligomycin, was detected in incubation medium without K+, was inhibited by prolonged glutaraldehyde fixation, and its activity was diminished when Mg2+ was omitted from the incubation medium. The Ernst medium was used to detect Na+-K+-ATPase activity in T. cruzi. No reaction product indicative of the presence of this enzyme was detected. Reaction product indicative of 5'-nucleotidase was not detected in T. cruzi. Acid phosphatase activity was detected in lysosomes. Those results indicate that a Mg2+-activated ATPase is present in the plasma membrane of T. cruzi and that it can be used as an enzyme marker, provided that the mitochondrial and flagellar ATPases are inhibited, to assess the purity of plasma membrane fractions isolated from this parasite.
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PMID:Localization of a Mg2+-activated ATPase in the plasma membrane of Trypanosoma cruzi. 614 95


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