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)

Activity of a HCO-3 stimulated Mg2+ dependent ATPase is demonstrated in mitochondrial fractions of the avian duodenum. Suppression of eggshell calcification resulted in a slight reduction in Mg2+, Ca2+ and Mg2+HCO-3 ATPase activities. Duodenal carbonic anhydrase activity was lower in birds laying soft-shelled eggs than in birds laying normal eggs. Alkaline phosphatase and calcium binding protein levels both decreased along the length of the small intestine, but the effect was more pronounced for alkaline phosphatase. Suppression of eggshell calcification and treatment of shell-less laying hens with 1,25(OH)2D3 influenced alkaline phosphatase activity only in the duodenal mucosa. Suppression of eggshell calcification reduced CaBP levels in all sections of the intestine. Treatment with 1,25(OH)2D3 restored CaBP levels. Regulation of intestinal CaBP levels by 1,25(OH)2D3 would therefore, seem to be controlled more directly by calcium requirements associated with eggshell calcification than by gonadal hormones.
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PMID:Effects of suppression of eggshell calcification and of 1,25(OH)2D3 on Mg2+, Ca2+ and Mg2+HCO-3 ATPase, alkaline phosphatase, carbonic anhydrase and CaBP levels--II. The laying hen intestine. 614 59

Phosphohydrolase activity of a highly enriched commercial preparation of calf intestinal alkaline phosphatase was stimulated in the presence of HCO3. SO4, Cl, SCN, and acetate did not stimulate hydrolysis, whereas SO3 exhibited a bimodal effect, stimulating at low (25mM) concentration but inhibiting at high (100 mM) concentration. The pH optimum of this stimulation by HCO3 or SO3 was 8.5--9.0 and was maximal at a Mg concentration of 0.5 mM. HCO3 increased the Vmax of the reaction without changing the Km for ATP. ATP, GTP, UTP, and xanthosine triphosphate were equally effective as substrates, whereas AMP and p-nitrophenyl phosphate were much less effective. Alkaline phosphatase activity was inhibited by L-cysteine and L-phenylalanine, compounds that also inhibited the HCO3-ATPase activity of the preparation. Passage of the commercial preparation through an anion-exchange column yielded a fraction with enriched alkaline phosphatase and HCO3-ATPase activities; this fraction proved to be a single protein on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, on isoelectric focusing, and by immunologic techniques. These studies strongly suggest that alkaline phosphatase and anion-stimulated phosphohydrolase activities are properties of the same protein in small intestine. It is possible that alkaline phosphatase may function as a HCO3-ATPase involved in intestinal absorption and secretion.
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PMID:Anion-stimulated phosphohydrolase activity of intestinal alkaline phosphatase. 615 12

Time- and dose-dependent changes in intracellular enzyme activities in kidney and bone from rats injected with calcitonin have been assessed by quantitative cytochemistry. The doses of salmon calcitonin given were similar to those suggested in the Pharmacopoeial rat hypocalcaemia bioassay (1-50 mIU/50 g body weight). The highest doses produced 30% inhibition of alkaline phosphatase activity, maximal within 20 min after injection, in cells of renal proximal tubules and a stimulation of calcium-dependent adenosine triphosphatase activity in kidney cortical and outer medullary cells. Alkaline phosphatase activity in the periosteal bone cells was markedly inhibited at the lowest doses. When doses of human and porcine calcitonins were given which would be equipotent with that of salmon calcitonin in the rat hypocalcaemia bioassay, the effect of the non-mammalian peptide on renal alkaline phosphatase activity was relatively greater than that of the mammalian peptides. Oxidized human calcitonin did not inhibit renal alkaline phosphatase activity even when an amount equivalent to 10 times the highest dose of the unmodified peptide was injected.
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PMID:Quantitative cytochemical responses to exogenously administered calcitonins in rat kidney and bone cells. 622 49

Cysteine-sensitive alkaline phosphatase and/or ouabain-sensitive Na+, K+ -ATPase were studied by ultrastructure cytochemistry in epithelial cells of proximal and distal kidney tubules. Alkaline phosphatase reactivity was confined to the surface of the microvillous luminal cell membrane of proximal tubule cells, whereas distal tubules and collecting ducts were unreactive. The Na+, K+- ATPase reactivity was localized evenly along the cytoplasmic side of the basolateral cell membrane of cells of proximal and distal tubules and in collecting ducts. In the proximal tubules, where the activity was strongest, the Na+, K+- ATPase deposits were also found in the 10--50 nm gap between the cell membrane and the cisternae of tubulo-cisternal endoplasmic reticulum (TER) underlying a major part of the basolateral cell membrane. The restriction of NA+, K+ -ATPase sites, which are involved in extrusion of Na+ from the cell, to a narrow cytoplasmic compartment located between the cell membrane and the cisternae of TER, is consistent with a transport role for the TER.
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PMID:Localization of Na+, K+ -ATPase to the inside of the basolateral cell membranes of epithelial cells of proximal and distal tubules in rabbit kidney. 625 59

A homogeneous population of single cells from the thick ascending limb of Henle's loop (TALH) has been isolated from the rabbit kidney medulla. A total medullary cell suspension was prepared by a series of collagenase, hyaluronidase, and trypsin digestions and separated on a Ficoll gradient (2.6-30.7% wt/wt). Morphologically, the cells isolated from the TALH were homogeneous and showed polarity within their plasma membrane structure, with a few blunt microvilli on their apical surface and deep infoldings of the basal-lateral membrane. Biochemically, the TALH cells were highly enriched in calcitonin-sensitive adenylate cyclase and Na, K-ATPase. Alkaline phosphatase and arginine vasopressin-sensitive adenylate cyclase, highly concentrated in proximal tubule and collecting duct, were present only in low concentrations in the TALH cells. Additionally, furosemide, a diuretic inhibiting sodium chloride transport in the TALH in vivo, inhibited oxygen consumption of the TALH cells in a dose-dependent manner. The TALH cells were viable, as judged by morphological appearance, trypan blue exclusion, the response of oxygen consumption to 2,4-dinitrophenol, succinate and ouabain, and the cellular Na, K and ATP levels.
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PMID:Separation of renal medullary cells: isolation of cells from the thick ascending limb of Henle's loop. 625 27

Although there have been a few reports on Ca2+-ATPase and Na+ + K+-ATPase in human placenta, they are still insufficient for getting more detailed information about human placenta. In this study we investigated some characteristics of the Ca2+-ATPase and measured the activity of Ca2+-ATPase and Na+ + K+-ATPase at various gestational periods. Maximum activity of Ca2+-ATPase was seen at 3 mM and pH 9.0. The enzyme was distinguished from ALP (i.e., Alkaline phosphatase) by such tests as adding L-phenylalanine and heat treatment. Our measurement results of Ca2+-ATPase activity (mumoles Pi/mg protein/30 min) in human placental chorion were 21.9 +/- 2.4 (Mean +/- S.D.) at 10-15 gestational weeks, 19.1 +/- 1.4 at 16-27 gestational weeks, 31.4 +/- 7.2 at 28-35 gestational weeks, and at 36-42 gestational weeks, the AFD group showed 25.8 +/- 4.6, the LFD group, 27.9 +/- 2.1, and the SFD group, 21.2 +/- 1.9. Those of Na+ + K+-ATPase activity (mumoles Pi/mg protein/30 min) were 0.98 +/- 0.05 at 10-15 gestational weeks, 0.82 +/- 0.02 at 16-27 gestational weeks, 1.85 +/- 0.42 at 28-35 gestational weeks and at 36-42 gestational weeks, the AFD group showed 1.58 +/- 0.45, the LFD group, 1.49 +/- 0.37, and the SFD group, 1.68 +/- 0.36. As a result, Ca2+-ATPase activity tended to be higher at 28-35 gestational weeks than for other periods, while it showed lower for the SFD group than for the AFD group. As regards to Na+ + K+-ATPase activity, there were not seen any significant differences between the AFD placenta and the LFD placenta as compared with the AFD placenta.
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PMID:Activities of Ca2+-ATPase and Na+ + K+-ATPase in human placenta. 626 97

1. Incubation of Schistosoma mansoni for 5 min in a phosphate-buffered medium, pH 7.4, released tegumental material containing the following phosphohydrolase activities: alkaline phosphatase, 5'-nucleotidase, glycerol-2-phosphatase, glucose 6-phosphatase, phosphodiesterase and ATPase. 2. Maximum activity of these enzymes was measured at pH 9.5; however, the phosphodiesterase and ATPase activities were also appreciable at pH 7.0. 3. Solubilization of the released tegumental material in 1% Triton X-100 followed by gel filtration distinguished three peaks of enzyme activity: an ATPase (mol.wt. greater than 1000 000), a phosphodiesterase (mol.wt. 1 000 000) and an alkaline phosphomonoesterase with broad specificity (mol.wt. 232 000). 4. The ATPase activity was highly activated by 10 mM-Mg2+ or 1 mM-Ca2+ and was inhibited by chelating agents. Ouabain, Na+ and K+ had little effect on enzyme activity, whereas activity was increased by 50% in the presence of calmodulin. The phosphodiesterase activity was highest in the presence of 100 mM-Na+ or -K+, and 10 mM-Mg2+ or -Ca2+. Alkaline phosphatase activity was also stimulated by 100 mM-Na+ or -K+, and 10 mM-Mg2+; however Ca2+ inhibited at greater than 1 mM. 5. Surface iodination of parasites followed by detergent solubilization and gel filtration of the released tegumental membranes indicated that these enzymes were not accessible. A major surface component, apparent mol.wt. 80 000, was iodinated. 6. Rabbit anti-(mouse liver 5'-nucleotidase) antibodies did not inhibit the phosphohydrolase activities. However, an immunoglobulin G fraction from sera of mice chronically infected with S. mansoni partially inhibited alkaline phosphatase activity, but was without effect on the phosphodiesterase and ATPase activities. 7. The location of the enzymes in the double membrane of the tegument and their significance in host-parasite interactions is discussed.
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PMID:Properties of a series of tegumental membrane-bound phosphohydrolase activities of Schistosoma mansoni. 627 49

Tibias of 6-day-old white Leghorn chick embryos treated with beta-aminopropionitrile (beta-APN; 0.1 mg/egg/day) for 4 days and injected with 3H-proline or 3H-tetracycline on the 11th day were analyzed for incorporation of 3H-proline and 3H-tetracycline. The incorporation of 3H-proline was comparable in the controls and beta-APN-treated embryos. However, the incorporation of 3H-tetracycline was significantly lower in beta-APN-treated embryos. The bone ash contents were also lower in the latter group. Alkaline phosphatase and Ca+2-ATPase were found to be significantly lower in beta-APN-treated embryonic bones. There was, however, no difference in the activity of Na+, K+-ATPase. The histochemical examination showed the alkaline phosphatase to be present on osteoblasts and matrix vesicle plasma membranes at the periosteal surface. The chick embryonic liver tissue showed no significant differences in the activities of any of the above enzymes. The results suggest that beta-APN-induced inhibition of the bone mineralization may be due to the bone-specific inhibition of alkaline phosphatase and Ca+2-ATPase.
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PMID:Investigations of alkaline phosphatase Ca+2-ATPase and Na+, K+-ATPase during beta-APN-induced initial bone mineralization inhibition. 628 59

Hepatocellular neoplasms are known to differ in enzyme activity from the surrounding non-neoplastic liver. We have compared histochemically the enzyme activity of spontaneous hepatocellular tumors in mice with tumors induced by diethylnitrosamine and dieldrin. Some neoplasms had increased activity, others had decreased enzyme activity, yet other had the same activity as the surrounding liver. Alkaline phosphatase, glucose-6-phosphatase, succinic dehydrogenase and adenosine triphosphatase, as well as glycogen levels were studied. Carcinomas differed from adenomas in having elevated enzyme activity significantly more often than adenomas. However, the carcinomas showed elevated glycogen levels less frequently than adenomas. Histochemically, pulmonary metastases resembled the primary hepatocellular carcinomas from which they were derived. Tumors of dieldrin animals were notable in having increased activity of all the enzymes which we studied more frequently than tumors of diethylnitrosamine animals or of controls. Differences in enzyme activity between the three mouse strains were slight.
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PMID:Enzyme histochemical characteristics of spontaneous and induced hepatocellular neoplasms in mice. 629 95

Some ductal cells of pleomorphic adenomas showed evidence of secretory activity, with apical secretory granules, thiamine pyrophosphatase activity in the Golgi apparatus, and acid phosphatase activity in GERL-like structures and in immature secretory granules. Alkaline phosphatase activity was demonstrated rarely at the luminal plasma membrane and in intracellular vesicles, suggesting resorptive activity. ATPase reaction product was associated with contiguous surfaces of tumour cells, particularly of those cells adjacent to the basement membrane, these latter cells apparently differentiating in a different manner to the luminal cells. A comparison of luminal ductal cells of the tumours with normal salivary glands revealed most similarity with intercalary ductal cells.
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PMID:Ultrastructural cytochemistry of phosphatases in the ductal component of pleomorphic adenoma of human parotid and submandibular salivary glands. 629 Apr 30


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