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:3.6.1.25 (triphosphatase)
1,529 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The sodium-potassium activated and magnesium dependent adenosine-5'-triphosphatase (Na(+)-K+/Mg+2 ATPase EC 3.6.1.3.) activity and lipid peroxidation and early ultrastructural findings are determined in rat spinal cord at the early stage of trauma produced by a surgical clip on the thoracal 2-7 segments. The effect of treatment with intravenous methylprednisolone (MP) was evaluated the basis of these biochemical alterations and ultrastructural findings in the same model. The specific activity of the membrane bound enzyme Na(+)-K+/Mg+2 ATPase was promptly reduced in as early as ten minutes following spinal cord injury and remained at a level lower than the levels in the control group and in the sham-operated group. Methylprednisolone treatment immediately after the trauma attenuated the inactivation of Na(+)-K+/Mg+2 ATPase. On the other hand, there was significant difference in lipid peroxide content between the sham-operated and the injured animals. Methylprednisolone treatment reduced thiobarbituric acid reactive substance (TBARS) content in Group IV. We determined a positive relationship among membrane-bound enzyme Na+K+/Mg+2 ATPase activity, malondialdehyde (MDA) content and early ultrastructural changes in the traumatized and treated groups.
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PMID:Correlation of alterations on Na(+)-K+/Mg+2 ATPase activity, lipid peroxidation and ultrastructural findings following experimental spinal cord injury with and without intravenous methylprednisolone treatment. 756 28

Endorphins have been implicated in the pathophysiology of spinal cord injury. The effect of naloxone on the sodium- and potassium-activated and magnesium-dependent adenosine-5'-triphosphatase (Na(+)-K+/Mg+2 ATPase, EC.3.6.1.3.) activity, lipid peroxidation, and early ultrastructural findings were studied in rats at the early stage of spinal cord injury, produced with an aneurysm clip on the T2-T7 segments. The rats were divided into four groups. The 10 rats in Group I, which had no injury and received no medication, were used for determining Na(+)-K+/Mg+2 ATPase activity, the extent of lipid peroxidation (by measuring the level of thiobarbituric acid-reactive substances as malondialdehyde), and normal ultrastructural findings. On the 15 rats in Group II, without spinal cord injury, only laminectomy was performed to determine the effect of surgery on the biochemical indices and findings. In the 15 rats in Group III, physiological saline was administered intraperitoneally in an amount equivalent to that of the naloxone administered immediately after spinal cord injury. In the 15 rats in Group IV, 0.5 mg of naloxone was administered intraperitoneally as a single dose immediately after injury and again 60 minutes after injury. The Na(+)-K+/Mg+2 ATPase activity was promptly reduced after spinal cord injury and remained in a lower level than the levels of Groups I and II during 120 minutes after injury. Naloxone treatment, immediately after trauma, attenuated the inactivation of Na(+)-K+/Mg+2 ATPase. On the other hand, there was a significant difference in the malondialdehyde content between animals in Groups I and III. Naloxone treatment reduced the malondialdehyde content in Group IV.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Effects of naloxone on sodium- and potassium-activated and magnesium-dependent adenosine-5'-triphosphatase activity and lipid peroxidation and early ultrastructural findings after experimental spinal cord injury. 759 12

The SNQ2 gene of Saccharomyces cerevisiae, which encodes an ATP binding cassette protein responsible for resistance to the mutagen 4-nitroquinoline oxide, is regulated by the DNA-binding proteins PDR1 and PDR3. In a plasma membrane-enriched fraction from a pdr1 mutant, the SNQ2 protein is found in the 160-kDa over-expressed band, together with PDR5. The SNQ2 protein was solubilized with n-dodecyl beta-D-maltoside from the plasma membranes of a PDR5-deleted strain and separated from the PMA1 H(+/-)ATPase by sucrose gradient centrifugation. The enzyme shows a nucleoside triphosphatase activity that differs biochemically from that of PDR5 (Decottignies, A., Kolaczkowski, M., Balzi, E., and Goffeau, A. (1994) J. Biol. Chem. 269, 12797-12803) and is sensitive to vanadate, erythrosine B, and Triton X-100 but not to oligomycin, which inhibits the PDR5 activity only. Disruption of both PDR5 and SNQ2 in a pdr1 mutant decreases the cell growth rate and reveals the presence of at least two other ATP binding cassette proteins in the 160-kDa overexpressed band that have been identified by amino-terminal microsequencing.
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PMID:Identification and characterization of SNQ2, a new multidrug ATP binding cassette transporter of the yeast plasma membrane. 762 27

The chicken gizzard smooth muscle extracellular ATPase (ecto-ATPase) is a low abundance, high specific activity, divalent cation-dependent, nonspecific nucleotide triphosphatase (NTPase). The ATPase is a 66-kDa glycoprotein with a protein core of 53 kDa (Stout, J.G. and Kirley, T.L. (1994) J. Biochem. Biophys. Methods 29, 61-75). In this study we evaluated the characteristics of a bank of monoclonal antibodies raised against a partially purified chicken gizzard ecto-ATPase. 18 monoclonal antibodies identified by an ATPase capture assay were tested for effects on ATPase activity as well as for their Western blot and immunoprecipitation potential. The five most promising monoclonal antibodies were used to immunopurify the ecto-ATPase. The one-step immunoaffinity purification of solubilized chicken gizzard membranes with all five of these monoclonal antibodies isolated a 66-kDa protein whose identity was confirmed by N-terminal sequence analysis to be the ecto-ATPase. Several of these monoclonal antibodies stimulated ecto-ATPase activity similar to that observed previously with lectins. Western blot analysis revealed that three of the five monoclonal antibodies recognized a major immunoreactive band at 66 kDa (53-kDa core protein), consistent with previous purification results. The other two antibodies recognized proteins of approximately 90 and 160 kDa on Western blots. The 90-kDa co-immunopurifying (and presumably associated or related) protein was identified by N-terminal analysis as LEP100, a glycoprotein that shuttles between the plasma and lysosomal membranes. The approximately 160-kDa co-immunopurifying protein was identified by N-terminal analysis as integrin, a protein involved in extracellular contacts with adhesion molecules. Extended N-terminal sequence analysis of the immunopurified 66-kDa ecto-ATPase revealed some sequence homology with mouse lysosomal associated membrane protein. Tissue distribution of the ecto-ATPase showed that the highest levels of protein were expressed in muscle tissues (cardiac, skeletal, and smooth) and brain.
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PMID:Properties of and proteins associated with the extracellular ATPase of chicken gizzard smooth muscle. A monoclonal antibody study. 774 34

The effects of melatonin treatment on cardiac sarcolemmal membrane function were investigated in alloxan-injected rats. Ca(2+)-stimulated adenosine-triphosphatase (ATPase, Ca2+ pump) and Mg(2+)-ATPase activities were depressed significantly in sarcolemmal preparations from alloxan-injected rats compared with levels in control rats. These deficits were observed 2 days after alloxan injection, and they were accompanied by an increase in the density of voltage-sensitive calcium channels, as measured by the [3H]nitrendipine-binding assay. In a dose-dependent manner, treatment of rats with melatonin before alloxan injection significantly overcame the suppression of Ca(2+)-stimulated ATPase in cardiac sarcolemma. Melatonin (1, 5, and 10 mg/kg) overcame Ca(2+)-stimulated ATPase suppression by 13, 35, and 70%, respectively. In addition, melatonin at a dose of 10 mg/kg also prevented the suppression of the Mg(2+)-ATPase by 31%. The number of [3H]nitrendipine-binding sites was not influenced by melatonin. The patent Na(+)-K(+)-ATPase and ouabain-sensitive Na(+)-K(+)-ATPase activities were not different between the control and experimental groups. The results indicate that Ca2+ pump activity is suppressed by acute alloxan treatment, whereas the density of voltage-sensitive calcium channels is increased. These changes may be a consequence of alloxan toxicity to the cardiac sarcolemma. Melatonin, likely because of its antioxidant capacity, exerts a protective effect on heart sarcolemmal membrane function in alloxan-injected rats.
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PMID:Melatonin prevents the suppression of cardiac Ca(2+)-stimulated ATPase activity induced by alloxan. 804 13

A Ca(2+)- or Mg(2+)-stimulated ecto-ATPase is thought to regulate the hydrolysis of extracellular ATP in nervous tissues. The hydrolysis of nucleotide triphosphates (NTPs) was analyzed in brain microsomal fractions from crosses of DBA/2J (D2) and C57BL/6J (B6) mice. The nucleotide triphosphatase (NTPase) activity was significantly reduced in D2 mice as compared to B6 mice, and B6D2F1 hybrids had activities intermediate to the parentals. A significant positive correlation was found between the hydrolysis of four NTPs (ATP, CTP, GTP and UTP) in 24 B6 x D2 (BXD) recombinant inbred (RI) strains of mice and in 80 B6D2F1 x D2 backcross mice. The RI strains and backcross mice fell into two distinct groups with respect to the NTPase activity. Linkage of NTPase activity was suggested with the chromosome 2 markers, D2Mit6 and Ass-1, in the RI strains, and was confirmed by analysis of other markers in the backcross population. These data suggest that the Ca(2+)- or Mg(2+)-stimulated hydrolysis of NTPs, designated Ntp, is regulated by a single gene located on proximal chromosome 2. Although an association was observed previously between Ca(2+)-ATPase activity and susceptibility to audiogenic seizures (AGS), no significant association was observed for the expression of Ntp and AGS susceptibility.
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PMID:Genetic analysis of nucleotide triphosphatase activity in the mouse brain. 805 15

The replication of Semliki Forest virus requires four nonstructural proteins (nsP1 to nsP4), all derived from the same polyprotein. One of these, nsP2, is a multifunctional protein needed in RNA replication and in the processing of the nonstructural polyprotein. On the basis of amino acid sequence homologies, nsP2 was predicted to possess nucleoside triphosphatase and RNA helicase activities. Here, we report the engineered expression in Escherichia coli of nsP2 and of an amino-terminal fragment of it by use of the highly efficient T7 expression system. Both polypeptides were produced as fusion proteins with a histidine tag at the amino terminus and purified by immobilized-metal affinity chromatography. The two recombinant proteins exhibited ATPase and GTPase activities, which were further stimulated by the presence of single-stranded RNA. The activities were not found in similarly prepared fractions from uninduced control cells or cells expressing an unrelated polypeptide. Radiolabeled ribonucleoside triphosphates could be cross-linked to both the full-length and the carboxy-terminally truncated nsP2 protein, and both polypeptides had RNA-binding capacity. We also expressed and purified an nsP2 variant which had a single amino acid substitution in the nucleotide-binding motif (Lys-192-->Asn). No nucleoside triphosphatase activity was associated with this mutant protein.
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PMID:ATPase and GTPase activities associated with Semliki Forest virus nonstructural protein nsP2. 805 61

1. Parotid plasma membrane nonpump low-affinity Ca(2+)-ATPase, which possesses high-affinity (Ca2+ + Mg2+)-ATPase activity, was characterized. 2. Purified Ca(2+)-ATPase hydrolyzed the nucleoside triphosphates, GTP, ITP, CTP, UTP, TTP (67-93% of ATP) and nucleoside diphosphates, ADP, GDP, IDP, CDP, TDP (12-40% of ATP) but not AMP and p-NPP. 3. The maximum activities of Ca(2+)- and (Ca2+ + Mg2+)-ATPases were obtained in the presence of 1 mM and 0.13 microM Ca2+, respectively. 4. The Km values for Ca2+ in Ca(2+)- and (Ca2+ + Mg2+)-ATPases were 0.2 mM and 22 nM, respectively. 5. The activities of both Ca(2+)- and (Ca2+ + Mg2+)-ATPases were found in the right-side-out-vesicles obtained from the plasma membrane-rich fraction. 6. These features suggest that Ca(2+)-ATPase is an ecto-Ca(2+)-dependent nucleoside triphosphatase.
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PMID:The possibility that Ca(2+)-ATPase from the plasma membrane-rich fraction of bovine parotid gland is ecto-Ca(2+)-dependent nucleoside triphosphatase. 806 15

Protons generated inside the cells during metabolic activity have to be extruded through active mechanisms from the intracellular to the extracellular space. One of the systems involved in proton transport across membranes are the V-ATPases, which are oligomeric complexes that have been found in several subcellular organelles energizing such organelle through a proton gradient and a membrane potential. In this paper, a V-ATPase activity has been described at the plasma membranes fractions isolated from airway smooth muscle. This activity was measured as a Cl- stimulated Mg2+ ATPase. This Cl- activating effect was also shared by others halogens as I- and Br- but not F-. This Cl- stimulated ATPase is a nucleotide triphosphatase being unable to hydrolyze mono and dinucleotides. The divalent cations showed the following sequence of activation (Mg2+ > Mn2+ > Ca2+) of the Cl- activated Mg2+ ATPase. This Cl- stimulated Mg2+ ATPase was insensitive to ouabain, vanadate, sodium azide and rutamicina. NEM (N-ethylmaleimide) partially inhibited this activity but a complete inhibition was observed with p-CMB (p-chloromercurbenzoate ). Several specific proton transport inhibitors were employed to show the presence of a H+ pump activity. Thus, the strong inhibition induced by DCCD suggest the existence of hydrophobic subunits related to a proton channel. In addition, protonophores as 1799 and FCCP stimulated the Cl- stimulated ATPase indicating the presence of a H+ pump in these plasma membranes vesicles. The chloride requirement could be explained by the existence of a chloride conductor coupled to the proton pump (H+ ATPase-type V) due to the inhibitory effect of duramycin.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:[Role of H+ ATPases in plasma membranes of airway smooth muscle]. 808 4

Zinc, protein, cholesterol, phospholipids, alkaline phosphatase (AlPase), acid phosphatase (AcPase), adenosine-5-triphosphatase(ATPase) and histology were studied in testis of zinc-deficient mice. Zinc and protein decreased in the 3-week experiment whereas they increased in the 6-week experiment. Zinc is involved in several functions of the cell and is regulated by hormones. Inhibition of spermatogenesis indicates for decreased zinc levels in 3-week whereas the increase in 6-week experiment indicates for accumulation of zinc in oedomatous fluid and uncontrolled diffusion of zinc across the blood testis barrier. Glycogen decreased in the 3-week as well as 6-week experiments due to blockage of androgen and spermatogenesis. Cholesterol and phospholipids increased in the 3-week experiment and decreased in 6-week experiment as both the parameters are related to steroidogenesis. Zinc deficiency leads to aspermatogenic condition and comparatively less injury to non-germinal cells. This could have blocked the transport of material across the testis barrier and therefore might have increased AlPase levels. Increased AcPase, probably represents lysosomal enzymes, as the cell debris of disorganised epithelium are to be digested and removed. ATPase increased in 3-week experiment and can be correlated to increased demands of energy of testicular cells to overcome the insults of zinc deficiency whereas the decrease in 6-week experiment could be as a result of inhibition of spermatogenesis.
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PMID:Histological and biochemical changes in testis of zinc deficient BALB/c strain of mice. 808 79


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