Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.6.1.25 (triphosphatase)
 1,529 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The role of the endothelium was examined in the response to aggregating platelets in cerebral arteries from normal and hypercholesterolemic animals. Male Yorkshire pigs were fed either a normal diet or a 2% high-cholesterol diet for 10 weeks. Endothelium-dependent responses were examined in vitro. In rings of basilar arteries from control animals aggregating platelets caused endothelium-dependent relaxations, which were significantly inhibited by apyrase, an adenosine diphosphatase and triphosphatase, but were augmented by methiothepin, a combined S1- and S2-serotonergic blocker. In quiescent rings platelets induced contractions that were inhibited by the presence of the endothelium; these contractions were significantly inhibited by methiothepin, but not by ketanserin (an S2-serotonergic blocker) or dazoxiben (a thromboxane-synthetase blocker) in the presence or absence of SQ29548 (a thromboxane-receptor blocker). Adenosine diphosphate but not serotonin caused endothelium-dependent relaxations. In cholesterol-fed animals the endothelium-dependent relaxations in response to aggregating platelets and adenosine diphosphate were impaired. These experiments indicate that 1) the endothelium inhibits the vasoconstrictor effect of aggregating platelets in porcine cerebral arteries; 2) platelet-induced relaxations are achieved mainly by a purinergic mechanism, while platelet-induced contractions are mediated by activation of S1-serotonergic receptors with little contribution of thromboxanes; and 3) hypercholesterolemia impairs the endothelium-dependent relaxations in response to aggregating platelets due to the impaired responses to adenosine diphosphate.
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PMID:Endothelium-dependent relaxation to aggregating platelets in isolated basilar arteries of control and hypercholesterolemic pigs. 340 91

The effects of six weeks treatment with multiple i.p. doses of citrinin (15, 25 and 35 mg/kg) on some hormonal activities and on enzymes and substrates of the Embden--Meyerhof pathway in mice were studied. Adenosine triphosphatase, hexokinase, lactate dehydrogenase, lactic acid and pyruvic acid decreased in blood, liver, kidney and brain of citrinin-treated mice. Glucose levels in blood, kidney and brain increased and glycogen content of liver decreased. Cortisol, triiodothyronine and thyroxine levels of serum increased, but insulin levels decreased.
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PMID:Effect of the mycotoxin citrinin on some hormones and on enzymes and substrates of the Embden-Meyerhof pathway in mice. 371 10

After cyclophosphamide priming, subcutaneously (s.c.) transplanted cells from established human leukemia cell lines U937, K562, or HL-60 consistently yielded single, nonmetastatic tumors. Tumorigenesis with KG-1 cells was inconstant. Within each cell line, cytologic, electron-microscopic, cytogenetic, isoenzyme, immunochemical, and enzyme cytochemical studies confirmed identity of cultured and tumor cells. Adenosine triphosphatase reactivity was limited to leukemic cells in vivo. Isoenzyme electrophoretic patterns, distinct for each cell line, provided a reliable criterion to establish clonality and to verify tumor cell origin. Antitumor activity of the active vitamin-D3 metabolite 1,25-(OH)2D3 was assessed in vivo against U937, K562, and HL-60 cells by cell transplantation and concurrent s.c. contralateral implantation of miniosmotic pumps containing the 1,25-(OH)2D3 in a propylene glycol vehicle. Tumors developed in all treated U937 mice, 50% with K562 and 25% bearing HL-60 transplants. All transplants proliferated in mice either with pumps containing only vehicle or no pumps. Coincidence of tumor and vehicle decreased survival time. No differences in cytoreactivities or morphology were apparent between cultured cells and tumor cells in treated or untreated mice. This nude mouse system is useful for in vivo studies of human myelogenous leukemia cells. Implanted miniosmotic pumps provide controlled delivery of antineoplastic agents and their vehicles for in vivo studies. 1,25-(OH)2D3 may be a valuable adjunctive therapeutic for control of human myelogenous leukemias.
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PMID:Action of 1,25-(OH)2D3 in nude mice bearing transplantable human myelogenous leukemic cell lines. 386 96

Adenosine triphosphatase activated by divalent cations is apparently a component of the motile apparatus in flagella of Arbacia sperm, as judged by the activity of this enzyme in intact flagella, glycerol-extracted flagella, and soluble extracts prepared from flagella. However, the variation in the physical properties and in the amount of enzyme obtained after a variety of treatments suggests that additional components are involved in the motile mechanism. These features distinguish the soluble flagellar enzyme from adenosine triphosphatases of other motile cells.
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PMID:Flagellar adenosine triphosphatase from sea urchin sperm: properties and relation to motility. 417 99

1. A rapid method for the isolation of nerve-ending particles from brain is described. This involved the centrifugation of the large-granule fraction over a discontinuous density gradient consisting of 3% (w/v) and 13% (w/v) Ficoll dissolved in 0.32m-sucrose. The results of the biochemical as well as morphological identification of nerve-ending particles are given. 2. Approx. 20% of the (Na(+)+K(+))-stimulated adenosine-triphosphatase activity originally present in the cerebral grey-matter suspension was recovered in the fraction consisting principally of large nerve-ending particles (approx. 1mu in diameter). The activity of the adenosine triphosphatase/mg. of protein in the nerve-ending fraction approximated to that in the small-granule fraction after the treatment with glycol ether diamine-tetra-acetic acid. The conclusion was drawn that the synaptic structure, supposedly the limiting membrane of the nerve-ending particle, is one of the feasible sites of localization of the (Na(+)+K(+))-stimulated adenosine-triphosphatase activity in cerebral tissues. Adenosine triphosphatase in purified cerebral mitochondria was not stimulated by Na(+). 3. No qualitative differences were found between the (Na(+)+K(+))-stimulated adenosine-triphosphatase activities exhibited by the nerve-ending particles and by the cerebral small-granule fraction with respect to pH-dependence, cation requirements and susceptibility to ouabain.
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PMID:Distribution of sodium-plus-potassium-stimulated adenosine-triphosphatase activity in isolated nerve-ending particles. 422 61

Rottem, Shlomo (Hebrew University, Jerusalem, Israel), and Shmuel Razin. Adenosine triphosphatase activity of mycoplasma membranes. J. Bacteriol. 92:714-722. 1966.-Adenosine triphosphatase activity of Mycoplasma laidlawii, M. gallisepticum, and Mycoplasma sp. strain 14 was confined to the cell membrane. The enzymatic activity was dependent on magnesium, but was not activated by sodium and potassium. Ouabain did not inhibit the adenosine triphosphatase activity of the mycoplasmas, and did not interfere with the active accumulation of potassium by M. laidlawii cells. Sulfhydryl-blocking reagents and fluoride inhibited the enzymatic activity, whereas 2,4-dinitrophenol was without any effect. Membranes of M. laidlawii hydrolyzed other nucleotide triphosphates and adenosine diphosphate (ADP), but at a lower rate than adenosine triphosphate (ATP). Nucleoside-2'-(3')-phosphates, ribose-5-phosphate, glucose-6-phosphate, and pyrophosphate were not hydrolyzed by the membrane preparations. It seems that the enzyme(s) involved in ATP hydrolysis by M. laidlawii membranes is strongly bound to the membrane subunits, which would account for the failure to purify the enzyme by protein fractionation techniques. The adenosine triphosphatase activity of mycoplasma membranes resembles in its properties that of similar enzymes studied in bacteria. The mycoplasma enzyme(s) seems to differ from the adenosine triphosphatase associated with ion transport in mammalian cell membranes and from mitochondrial adenosine triphosphatase.
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PMID:Adenosine triphosphatase activity of mycoplasma membranes. 422 19

Mitochondria from brown adipose tissue of cold-acclimated rats (6 degrees C) oxidize alpha-ketoglutarate at a rate twice that of controls (26 degrees C). In both groups, however, the phosphorus: oxygen ratio with alpha-ketoglutarate never exceeded unity, and it is essentially zero with either succinate or alpha-glycerophosphate. Adenosine triphosphatase activity of these mitochondria is very low and it is not stimulated by 2,4-dinitrophenol. In addition, both respiration and phosphorylation are unaffected by adenosine diphosphate, 2,4-dinitrophenol, bovine serum albumin, or glutathione. Endogenous respiration of tissue slices is not stimulated by 2-4-dinitrophenol. It is suggested that brown fat mitochondria are not capable of oxidative phosphorylation, but do phosphorylate at the substrate level. Since these findings provide an unusual example of electron transport by means of an energetically nonconservative pathway, their significance to thermogenesis by brown adipose tissue is particularly emphasized.
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PMID:Nonphosphorylating respiration of mitochondria from brown adipose tissue of rats. 422 65

The activity of adenosine triphosphatase activated by sodium and potassium ions is greatly increased in the gill and pseudobranch of the euryhaline killifish, Fundulus heteroclitus, after its adaptation to seawater. Adenosine triphosphatase activity in gills of fish in salt water is reduced by hypophysectomy. The data suggest that this enzyme is involved in the excretion of sodiumions by the gill and that the adaptive increase which occurs in seawater is influenced by the hypophysis.
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PMID:Sodium- and potassium-activated adenosine triphosphatase of gills: role in adaptation of teleosts to salt water. 422 98

Studies of the relationship between yield coefficient and growth rate, as affected by temperature of growth, in Escherichia coli have shown that, over a wide range of temperature, yield is relatively constant until the specific growth rate falls below about 0.2 hr(-1), at which point the yield begins to fall off precipitously. No intermediates of glucose metabolism in a form utilizable at higher temperatures could be found in the medium, and no toxic product was produced which limited growth. At 10 C, 37% of the carbon from glucose-UL-(14)C was assimilated into cellular material, whereas, at 30 C, 53% was assimilated. Cells grown at 10 C contained more carbohydrate than did cells grown at 37 C, and the glycogen-to-protein ratio of cells grown at 10 C was approximately three times higher than that of cells grown at 37 C. Adenosine triphosphatase activities of cells grown at 10 and 35 C were similar. Growth rates on glucose, glycerol, and succinate were quite similar at 10 C, but at 35 C growth was most rapid on glucose and slowest on succinate. The data suggest that the decrease in yield with decrease in temperature is a result of uncoupling of energy production from energy utilization.
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PMID:Effect of decreasing growth temperature on cell yield of Escherichia coli. 423 77

1. Adenosine triphosphatase activities of dispersions prepared from bovine cerebral cortex that had been frozen, were greater than those of dispersions prepared from fresh tissue. The subcellular distribution of components of the dispersion was not altered by freezing the tissue and a microsomal fraction enriched in Na(+)+K(+)-stimulated adenosine triphosphatase activity was prepared. 2. The bovine cerebral microsomes were further treated with a 2m-sodium iodide reagent to obtain a particulate preparation with minimal Na(+)+K(+)-independent adenosine triphosphatase activity. Na(+)+K(+)-stimulated activity was increased by the sodium iodide treatment and this preparation was shown to be enriched in lipid constituents. 3. Density-gradient centrifugation of the sodium iodide treated preparation gave three main subfractions each containing approximately equal amounts of phospholipid and protein. Further exposure of the sodium iodide-treated preparation to the 2m-sodium iodide reagent altered the distribution of protein and phospholipid among the fractions obtained by density-gradient centrifugation. Dissociation of phospholipids from protein in the sodium iodide-treated preparation was brought about also by high concentrations of arginine. Concentrated solutions of arginine and sodium thiocyanate brought about dissociation of phospholipids from protein of the microsomal preparation. 4. Many amino acids were found to inhibit Na(+)+K(+)-stimulated adenosine triphosphatase activity when present in high concentrations. The inhibition was complex but resulted, in part at least, from diminished affinity for ATP and Na(+) in the presence of the amino acids. 5. A non-ionic detergent, Lubrol W, solubilized up to 40% of the enzyme activity of the sodium iodide-treated preparation together with 30% of the protein and phospholipid in the preparation. Protein was released from the sodium iodide-treated preparation by pancreatic elastase but Na(+)+K(+)-stimulated adenosine triphosphatase activity of the residue was diminished. Ultrasonic treatment of the sodium iodide-treated preparation failed to release a significant proportion of Na(+)+K(+)-stimulated adenosine triphosphatase activity into a form not deposited by ultracentrifugation.
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PMID:The cerebral sodium-plus-potassium ion-stimulated adenosine triphosphatase of bovine brain and its microsomal matrix. 425 Aug 46


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