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)

Each of two Desert Sheep was infected with 1500 cercariae of Schistosoma mansoni of Northern Sudan. Signs of infection were anorexia, soft faces, progressive weakness and loss of wool. The sheep were killed 254 and 269 days after infection. The findings were heavy infiltration of the lamina propria with inflammatory cells, numerous ova in the submucosa, hyperplasia of lymphoid tissue, oedema of the mesenteric lymph nodes, and focal pulmonary oedema and congestion. There were egg granulomas, focal necrosis, schistosomal pigment, fatty change, depletion of glycogen and reduction in the activity of adenosine triphosphatase, succinic tetrazolium reductase and glucose-6-phosphatase in the liver. In one sheep 1330 cercariae penetrated and 700 matured to produce males and females in a 5:2 ratio. In the other sheep, about one third of the cercariae penetrated and matured. The ratio of males to females was 3:1.
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PMID:Susceptibility of desert sheep to infection with Schistosoma mansoni of Northern Sudan. 93 26

Na(+)-K(+)-dependent ouabain-sensitive ATPase and Mg(2+)-ATPase activities have been assayed in brain and kidney of healthy and Schistosoma mansoni-infected mice before and after praziquantel (EMBAY 8440, CAS 5526874-1) treatment. Schistosoma mansoni infection caused a moderate decrease of brain Na(+)-K(+)-ATPase activity with a marked inhibition of its Mg-stimulated ATPase. Meanwhile, a marked inhibition in both renal ATPase activities was observed in infected mice. Treatment of the infected mice with praziquantel (2 x 500 mg/kg b.wt.) reversed the inhibitory effect of infection on brain and kidney ATPase, so that the activity of both renal ATPase and that of brain Mg-ATPase were nearly corrected while the activity of brain Na(+)-K(+)-ATPase was increased to an extent greater than normal values. However, treatment of normal mice with praziquantel did not affect any of the measured parameters. Possible explanations of these findings are given.
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PMID:Effect of praziquantel treatment on brain and kidney ATPase activities in healthy and schistosoma mansoni-infected mice. 133 99

The (Ca(2+)-Mg2+)ATPase activity in microsomes of Schistosoma mansoni is fully inhibited by vanadate (I50 = 2.5 microM). 45Ca2+ is accumulated within microsomal vesicles in an ATP-dependent process that is enhanced 5-fold in the presence of 40 mM phosphate. Accumulated 45Ca2+ is rapidly released by 5 microM of the Ca2+ ionophore A23187 (t1/2 less than or equal to 6 s). (Ca(2+)-Mg2+)ATPase activity and Ca2+ uptake share the same subcellular distribution pattern and similar Ca2+ sensitivities (K0.5 = 0.39 microM and 0.15 microM, respectively). The substrate selectivity is high for both ATPase activity and Ca2+ transport. These results indicate the presence of an active transport of Ca2+ coupled to the (Ca(2+)-Mg2+)ATPase activity previously described in this parasite. A plasma membrane localization and physiological role in calcium homeostasis are suggested.
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PMID:A (Ca(2+)-Mg2+)ATPase from Schistosoma mansoni is coupled to an active transport of calcium. 153 90

A Ca-stimulated ATPase activity (pH 9.5) associated with the tegumental membrane enriched (TME) fraction of Schistosoma mansoni adults was partially inhibited by NAP-taurine or by increasing concentrations of chlorpromazine; endogenous calmodulin was found associated with the TME fraction. A similar activity (pH 8.6) was histochemically visualized within the tegument of fixed worms on the cytoplasmic leaflet of both the double surface membrane and the basement membrane; this reaction was inhibited by 1 microM chlorpromazine and it was also observed on the inner side of double membrane vesicles present in the TME fraction. No ATPase activity could be seen at alkaline pH with added Mg or Na/K ions. Without ATP, the addition of external Ca to the fixed worms induced the appearance of lead precipitates on the tegumental discoid bodies; this reaction was inhibited by molybdate and not by chlorpromazine. The intrategumentary regulation of calcium by the systems described and the possible use of phenothiazines against schistosomes are discussed.
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PMID:Tegumental Ca-stimulated adenosine triphosphatase activity in adult Schistosoma mansoni worms. 253 93

Vanadate inhibitory effects on Na+, K+-ATPases from carcass of Schistosoma mansoni and from lamb kidney outer medulla were compared in the presence of various concentrations of Na+, K+ and Mg2+. Depending on the ionic conditions, the schistosomal Na+, K+-ATPase was 2.4- to 175-fold less sensitive to vanadate than the lamb kidney enzyme. In 100 mM Na+, 3 mM K+ and 3 mM Mg2+, schistosomal Na+, K+-ATPase was surprisingly resistant to vanadate (I50 = 944 microM). The difference in vanadate sensitivity between schistosomal and lamb Na+, K+-ATPases may be due to a species difference in the efficacy of Na+, K+ and Mg2+ in promoting conformational changes between E1 and E2 forms of the enzyme.
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PMID:Vanadate sensitivity of Na+, K+-ATPase from Schistosoma mansoni and its modulation by Na+, K+ and Mg2+. 254 77

The distribution of Ca2+-dependent adenosine triphosphatase (EC 3.6.1.3.) and nonspecific (Na-K-Mg) adenosine triphosphatase activity in the tegument and subtegumental tissues of Schistosoma mansoni from both mixed and single sex infections was investigated cytochemically. Differences in the distribution of tegumental Ca-adenosine triphosphatase activity in 60- to 70-day-old female worms were found which could be related to the degree of sexual development in the two types of females, with little or no tegumental activity being found in 70-day-old females from single sex infections. In contrast, 28-day-old females from single sex infections showed low levels of tegumental Ca-adenosine triphosphatase activity, suggesting that the lack of tegumental activity in 70-day-old single sex females may be due to a loss or suppression of activity as a consequence of the failure of females in single sex infections to pair and develop to full sexual maturity. No differences in the distribution of nonspecific (Na-K-Mg) adenosine triphosphatase activity between females from mixed and single sex infections were found. The sexual status or age of male worms appeared to have little or no effect on the distribution of tegumental adenosine triphosphatases.
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PMID:Schistosoma mansoni: fine structural localization of tegumental adenosine triphosphatases. 282 32

A Ca2+-stimulated, Mg2+-dependent ATPase activity was found in subcellular fractions from Schistosoma mansoni. Its specific and relative activities were higher in the heterogeneous cuticle fraction and in the microsomal fraction. The K0.5 for ATPase activation by free Ca2+ was 0.2-0.5 microM. This is the first description of an ATPase activity stimulated by Ca2+ in the micromolar range in S. mansoni.
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PMID:A Ca2+-stimulated, Mg2+-dependent ATPase activity in subcellular fractions from Schistosoma mansoni. 297 94

A tegumental fraction was prepared from Schistosoma mansoni. This fraction exhibited ATPase activity stimulated by Ca2+ in the absence of Mg2+. The Mg2+ independency was assessed by lowering contaminant Mg2+ using CDTA. The peak of activity was 220 mumol Pi mg-1 protein h-1 and the K0.5 for CaATP was 0.32 mM; the same K0.5 was obtained using MgATP as substrate, in the absence of Ca2+. Both activities may be promoted by the same enzyme since the addition of Ca2+ did not increase the ATPase activity measured in the presence of a saturating MgATP concentration.
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PMID:A Mg2+-independent Ca2+-stimulated ATPase activity in the tegument of Schistosoma mansoni. 297 83

In fresh water snails, amebocytes are the principal cells that react to parasitic infection. Ultrastructurally, amebocytes resemble mammalian macrophages. To clarify the relationship between amebocytes and macrophages, we compared the histochemical staining for seven enzymes in Biomphalaria glabrata snail amebocytes, both in the amebocyte-producing organ (APO) and in the encapsulation reaction formed around parasite sporocysts with the staining in macrophages from the lymph nodes of patients with sarcoid or tuberculosis. Snails were infected with Echinostoma paraensei and Schistosoma mansoni miracidia. APOs and ventricular tissue with encapsulated parasites were fixed and embedded in glycol methacrylate monomer. Hardened blocks were sectioned at 2 micron and stained for alkaline phosphatase, acid phosphatase, alpha-naphthyl acetate esterase (ANAE), ATPase, peroxidase, 5'nucleotidase, and chloroacetate esterase. The amebocyte-producing organ contained cells that were positive for acid phosphatase, ANAE, and ATPase. Amebocytes in the capsules formed around echinostome sporocysts showed stronger staining for the same three enzymes. Capsules did not form around schistosome sporocysts, but the connective tissue around them contained numerous amebocytes that were also positive for these three enzymes. The amebocyte enzyme histochemistry resembled that in human granuloma macrophages, but differed from that in neutrophils. The increased expression of enzymes in amebocytes involved in the encapsulation reaction as compared to those in the APO was reminiscent of the alterations observed when human monocytes convert to tissue macrophages. These studies support the hypothesis that the amebocyte is an "invertebrate macrophage."
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PMID:Enzyme histochemical comparison of biomphalaria glabrata amebocytes with human granuloma macrophages. 298 47

The preparation and some biochemical properties of a (Na+ + K+)ATPase from male adult Schistosoma mansoni are described. After incubation in a membrane disruption medium, the tegument and carcass of the worms were separated and treated to obtain fractions enriched in (Na+ + K+)ATPase. The activity of the tegumental ouabain sensitive (Na+ + K+)ATPase at 37 C was 20.3 mumole Pi X mg-1 protein X hr-1 and represented 32% of the total ATPase activity. The (Na+ + K+)ATPase prepared from the carcass had a lower specific activity (3.7 mumole Pi X mg-1 protein X hr-1) but a higher relative activity (55%). Similar concentrations of Na+ and K+ activated the enzymes from both sources, and both enzymes were inhibited by similar concentrations of calcium. However, the enzyme from carcass was ten times more sensitive to ouabain than the enzyme from tegument. Comparison with results obtained on the (Na+ + K+)ATPase of human heart showed that the enzymes from the worms were more resistant to ouabain. The half maximal inhibitory concentration of dihydroouabain compared to that of ouabain was also different in the enzymes from human and worm. We conclude that (1) there exists at least one structural difference between the (Na+ + K+)ATPase of S. mansoni and that of the human host, and (2) it is useful to separately study the enzymes from tegument and carcass because they differ in sensitivity to cardiac glycosides.
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PMID:Schistosoma mansoni: preparation, characterization of (Na+ + K+)ATPase from tegument and carcass. 301 47


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