Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P20020 (adenosine triphosphatase)
 3,299 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Escherichia coli K-12, grown under anaerobic conditions with glucose as the sole source of carbon and energy without any terminal electron acceptor added, contains a fumarate reductase system in which electrons are transferred from formate or reduced nicotinamide adenine dinucleotide via menaquinone and cytochromes to fumarate reductase. This fumarate reductase system plays an important role in the metabolic energy supply of E. coli, grown under so-called "glycolytic conditions," as is indicated by the growth yields and maximal growth rates of mutants impaired in electron transfer or adenosine triphosphatase (uncB). In mutants deficient in menaquinone, cytochromes, or fumarate reductase, these values are considerably lower than in mutants deficient in ubiquinone or a functional adenosine triphosphatase. Electron transfer in this fumarate reductase system leads to the generation of a membrane potential, as is indicated by the uptake of the lipophilic cation triphenylmethylphosphonium by membrane vesicles prepared from cytochrome-sufficient and uncB cells. The generation of a proton-motive force by the fumarate reductase system was also demonstrated by the uptake of amino acids under anaerobic conditions in membrane vesicles of cytochrome containing and uncB cells grown under glycolytic conditions. Membrane vesicles of cytochrome-deficient cells failed to accumulate triphenyl-methylphosphonium and amino acids under these conditions, indicating that cytochromes are essential for the generation of a proton-motive force. Using glutamine uptake as an indication of the generation of ATP and proline uptake as an indication of the generation of a proton-motive force, it was demonstrated in whole cells that the proton-motive force is formed by ATP hydrolysis in cytochrome-deficient cells and by electron transfer in the uncB cells. In cytochrome-containing cells it was not possible to distinguish between these two possibilities, but the growth parameters suggest that, under glycolytic conditions, the proton-motive force is generated via electron transfer in the fumarate reductase system rather than via ATP hydrolysis.
J Bacteriol 1978 Dec
PMID:Energy supply for active transport in anaerobically grown Escherichia coli. 36 96

Phenytoin stimulated renin secretion from rat renal cortical slices. A sigmoid relationship was found between stimulatory effect and log concentration, from 1 to 8 mg/100 ml. The ED5C was 2.8 mg/100 ml. Basal secretion and the stimulation of secretion elicited by phenytoin were blocked by incubating slices in a K-free medium and by adding 1 mM ouabain to the medium (both of which inhibit Na,K-adenosine triphosphatase activity and increase intracellular Na concentration), and by reductions in the Na concentration of the incubation medium. NaCl in the incubation medium was replaced by choline chloride so that osmolality and Cl concentration were held constant. It is suggested that renin secretion rate is directly related to the transmembrane Na gradient, that phenytoin stimulates secretion by increasing the gradient, and that ouabain, K-free medium and reductions in Na concentration of the medium inhibit secretion by reducing the gradient.
J Pharmacol Exp Ther 1979 Dec
PMID:Phenytoin stimulates renin secretion from rat kidney slices. 51 21

Eighteen-month-old identical twins with the muscle histological characteristics of congenital fiber type disproportion are reported. The fiber typing system of pH-dependent adenosine triphosphatase was used to analyze the size and percentage of type 1, 2A, and 2B fibers in muscle tissue obtained by needle biopsy. Both twins had significantly larger type 2 than type 1 fibers, with 2B fibers representing the largest type. One patient also had type 1 predominance at the expense of a reduction in 2B (2B deficiency). The probands as well as other family members had transient delayed motor development, macrocephaly, and normal intelligence. A biopsy obtained from 1 of these family members failed to demonstrate a similar histological abnormality. The disorder is nonprogressive in this family, as evidenced by minimal disability in the older members and gradual improvement in the probands.
Ann Neurol 1977 Dec
PMID:Congenital fiber type disproportion in identical twins. 56 60

Biopsy specimens from the gastrocnemius or rectus femoris muscle of 20 patients with intermittent claudication were studied using fresh frozen cryostat sections and histochemical reactions for adenosine triphosphatase, nicotinamide adenine nucleotide dehydrogenase reductase and phosphorylase and modified Gomori trichrome staining. Neuropathic changes, such as fibertype grouping and small group atrophy, were present to some extent in all of the biopsy specimens. Myogenic muscle changes such as necrosis and phagocytosis were seen in approximately one third and various forms of myofibrillar disorganization in approximately two thirds of the specimens. The amount and size of the type I aerobic fibers increased with the increasing severity of the ischemic disease.
Arch Pathol Lab Med 1977 Dec
PMID:Histochemical changes in striated muscle in patients with intermittent claudication. 57 9

This study demonstrates the changes of concentration and elimination of calcium, phosphate and zinc, as well as alteration of serum alkaline phosphatase and acid phosphatase especially in patients with severe brain injuries in connection with bone fractures. Because the study has not been completed, the presently acquired results should only demonstrate possible development of the examined parameters. To find out the pathogenesis of overgrowing callus in brain-injured patients, further examinations are being carried out to find the histochemical activities of alkaline and acid phosphatase, lactate dehydrogenase, adenosine triphosphatase and acetylcholine esterase.
Helv Chir Acta 1978 Dec
PMID:[Special aspects of fracture healing in cranio-cerebral injuries]. 72 99

The plasmalemma and hyaline ectoplasm together constitute the sensory and motor organ of macrophages. The purpose of this study was to isolate this cell fraction in order to analyze it biochemically and functionally. Brief sonification of warmed rabbit lung macrophages caused release of heterodisperse hyaline blebs and filopodia, which were easily collected by differential centrifugation. Viewed in the electron microscope, these structures consisted of membrane-bounded sacs principally containing actin filaments. Some contained secondary lysosomes. They were enriched threefold over whole cell homogenates in specific adenylate cyclase activity and in trichloroacetic-acid-precipitable (125)I when derived from cells labeled with 125(I) by means of a lactoperoxidase-catalyzed reaction. These markers were found to have identical isopycnic densitites when macrophage homogenates were subjected to sedimentation in a focusing sucrose density gradient system, and these markers had densities distinct from those of other cytoplasmic organelles. These markers were therefore assumed to be associated with macrophage plasma membranes. The specific beta- glucuronidase activity of the bleb fraction was similar to that of homogenates, but the blebs had considerably lower specific succinic dehydrogenase activity and RNA content, and DNA was undetectable. Electrophoresis of blebs solubilized in sodium dodecyl sulfate on polyacrylamide gels revealed polypeptides co-migrating with macrophage actin-binding protein, myosin, and actin; blebs also had EDTA-activated adenosine triphosphatase activity characteristic of myosin. The concentrations of actin-binding protein and myosin were higher in blebs than in cells or cytoplasmic extracts, whereas actin concentrations were similar (relative to extracts) or only slightly greater (than in cells). Blebs and intact cells had high lactate dehydrogenase activities in the presence but not the absence of Triton X-100. Blebs and cells oxidased 1-[(14)C]glucose, and the rate of glucose oxidation was increased substantially in the presence of latex beads. We conclude that intact sacs of plasmalemma encasing contractile proteins and cytoplasmic enzymes can be isolated from macrophages. They are enriched in myosin and actin-binding protein, indicating that the contractile apparatus is regulated in the cell periphery. These structures have the capacity to respond to environmental signals. We suggest the name "podosomes" for them because of their resemblance to macrophage pseudopodia. We propose that podosome formation results from rapid dissolution of the cortical gel when the membrane is in an actively extended configuration.
J Cell Biol 1977 Dec
PMID:Peripheral hyaline blebs (podosomes) of macrophages. 92 88

Macrophage pseudopodia that surround objects during phagocytosis contain a meshwork of actin filaments and exclude organelles. Between these pseudopodia at the base of developing phagosomes, the organelle exclusion ceases, and lysosomes enter the cell periphery to fuse with the phagosomes. Macrophages also extend hyaline pseudopodia on the surface of nylon wool fibers and secrete lysosomal enzymes into the extracellular medium instead of into phagosomes. To analyze biochemically these concurrent alterations in cytoplasmic architecture, we allowed rabbit lung macrophages to spread on nylon wool fibers and then subjected the adherent cells to shear. This procedure caused the selective release of beta-glucoronidase into the extracellular medium and yielded two fractions, cell bodies and isolated pseudopod blebs resembling podosomes, which are plasma-lemma-bounded sacs of cortical cytoplasm. Cytoplasmic extracts of the cell bodies eluted from nylon fibers contained two-thirds less actin-binding protein and myosin, and approximately 20 percent less actin and two-thirds of the other two proteins were accounted for in podosomes. The alterations in protein composition correlated with assays of myosin-associated EDTA-activated adenosine triphosphatase activity, and with a diminution in the capacity of extracts of nylon wool fiber-treated cell bodies to gel, a property dependent on the interaction between actin-binding protein and F-actin. However, the capacity of the remaining actin in cell bodies to polymerize did not change. We propose that actin-binding protein and myosin are concentrated in the cell cortex and particularly in pseudopodia where prominent gelation and syneresis of actin occur. Actin in the regions from which actin-binding protein and myosin are displaced disaggregates without depolymerizing, permitting lysosomes to gain access to the plasmalemma. Translocation of contractile proteins could therefore account for the concomitant differences in organelle exclusion that characterize phagocytosis.
J Cell Biol 1977 Dec
PMID:Evidence for contractile protein translocation in macrophage spreading, phagocytosis, and phagolysosome formation. 92 89

To investigate the physical mechanism by which melittin inhibits Ca-adenosine triphosphatase (ATPase) activity in sarcoplasmic reticulum (SR) membranes, we have used electron paramagnetic resonance spectroscopy to probe the effect of melittin on lipid-protein interactions in SR. Previous studies have shown that melittin substantially restricts the rotational mobility of the Ca-ATPase but only slightly decreases the average lipid hydrocarbon chain fluidity in SR. Therefore, in the present study, we ask whether melittin has a preferential effect on Ca-ATPase boundary lipids, i.e., the annular shell of motionally restricted lipid that surrounds the protein. Paramagnetic derivatives of stearic acid and phosphatidylcholine, spin-labeled at C-14, were incorporated into SR membranes. The electronic paramagnetic resonance spectra of these probes contained two components, corresponding to motionally restricted and motionally fluid lipids, that were analyzed by spectral subtraction. The addition of increasing amounts of melittin, to the level of 10 mol melittin/mol Ca-ATPase, progressively increased the fraction of restricted lipids and increased the hyperfine splitting of both components in the composite spectra, indicating that melittin decreases the hydrocarbon chain rotational mobility for both the fluid and restricted populations of lipids. No further effects were observed above a level of 10 mol melittin/mol Ca-ATPase. In the spectra from control and melittin-containing samples, the fraction of restricted lipids decreased significantly with increasing temperature. The effect of melittin was similar to that of decreased temperature, i.e., each spectrum obtained in the presence of melittin (10:1) was nearly identical to the spectrum obtained without melittin at a temperature approximately 5 degrees C lower. The results suggest that the principal effect of melittin on SR membranes is to induce protein aggregation and this in turn, augmented by direct binding of melittin to the lipid, is responsible for the observed decreases in lipid mobility. Protein aggregation is concluded to be the main cause of inactivation of the Ca-ATPase by melittin, with possible modulation also by the decrease in mobility of the boundary layer lipids.
Biophys J 1992 Dec
PMID:Effects of melittin on lipid-protein interactions in sarcoplasmic reticulum membranes. 133 87

Acquired resistance to cisplatin (cis-diamminedichloroplatinum (II)) has been generated in vitro in the 41M human ovarian carcinoma cell line, established from a previously untreated patient. Three cisplatin-resistant variants were selected at approximately 2, 4 and 6-fold resistance (in terms of 50% inhibitory concentrations), in order to study the underlying mechanisms of acquired cisplatin resistance. Compared to the parent line, platinum accumulation following exposure to equimolar concentrations of cisplatin was on average (across the entire concentration range) 2.9, 3.6 and 4.8-fold lower in the 41McisR2, 41McisR4 and 41McisR6 cell lines, respectively. Thus the difference in uptake corresponded closely with their resistance factor in the three resistant variants. Moreover, a significant reduction in platinum accumulation was observed as early as 5 min after exposure to cisplatin in the 41M vs 41McisR6 cell lines. Platinum accumulation was similar in all cell lines following exposure to equitoxic concentrations (2 h IC50) of cisplatin. Enhanced efflux of drug was not observed between the 41M and 41McisR6 cells. In addition, there was no difference in intracellular glutathione (GSH) levels. Our previous studies have shown no indication of metallothionein involvement and the decrease in cisplatin uptake in the 41McisR6 cells was reflected by a similar reduction in DNA interstrand cross-links (ISC) formation. These results suggest that the mechanism of acquired resistance to cisplatin in the 41McisR6 cell line may be predominantly due to reduced drug uptake. The 41McisR6 cells were not found to be cross-resistant to ouabain, a postulated specific inhibitor of sodium-potassium adenosine triphosphatase (Na+, K(+)-ATPase), suggesting that decreased cisplatin accumulation in these cells is probably not regulated by alterations in their Na+, K(+)-ATPase levels, and Na+ potential across the plasma membrane. Cellular accumulation of a novel class of platinum (IV) ammine/cyclohexylamine dicarboxylates, which exhibit enhanced cytotoxicity over cisplatin and completely circumvent resistance to cisplatin in the 41McisR line, was also examined. The data suggests that increased accumulation of these compounds, as a result of their enhanced lipophilicity, could account for the dramatic increase in their potency over cisplatin.
Br J Cancer 1992 Dec
PMID:Reduced drug accumulation as a major mechanism of acquired resistance to cisplatin in a human ovarian carcinoma cell line: circumvention studies using novel platinum (II) and (IV) ammine/amine complexes. 145 52

The concentration of calcium-binding protein (CaBP) and the activities of calcium adenosine triphosphatase (Ca(2+)-ATPase) and carbonic anhydrase (CA) were determined in the shell gland mucosa of hens in two experiments. In Experiment 1, laying hens on a proprietary layer mash were compared with hens rested from lay by the feeding of whole grain barley. In Experiment 2 comparisons were made of laying hens fed the proprietary layer mash and producing eggs with either strong or weak shells. These latter comparisons were also made when the shell gland was quiescent or active with respect to daily eggshell formation. Feeding whole grain barley reduced egg production to zero after 11 days. This reduction in rate of lay was accompanied by significant reductions in all three markers, the effect on Ca(2+)-ATPase and CaBP being less than for CA. Control values were regained between 10 and 16 days after the barley was replaced with the layer mash. Relative shell strength and the physiological status of the shell gland with respect to time of daily eggshell formation had no significant effect on any marker in Experiment 2.
Poult Sci 1992 Dec
PMID:Calcium and carbonate supply in the shell gland of hens laying eggs with strong and weak shells and during and after a rest from lay. 147 May 88


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