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)

The described experiments show the influence of a single dose of cadmium chloride (1.5 mg CdCl2/kg body weight applied intraperitoneally) on development of the male gonads from the 1st d of post-fetal life to 1.5 a of life. In the case of the enzymes triggering transportation processes, adenosine triphosphatase stimulated by Mg++ (Mg++-ATP-ase), alkaline phosphatase (AP), and 5'nucleotidase (5'Nt), a considerable damages begin to appear in the 15th d of life whereas in the case of acid phosphatase (AcP) already in the 1st d of life whereas in the case of acid phosphatase (AcP) already in the 1st d of life. These damages increase with age reaching their maximum in the 45th d of life.
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PMID:Evolution of localization of reactions of adenosine triphosphatase (Mg++-ATP-ase), 5'nucleotidase (5'nt), alkaline phosphatase (AP), and acid phosphatase (AcP) in developing rat testis. II. After CdCl2 treatment. 303 15

Accumulation, distribution of Cd in tissues and its toxic effect depend of the mode of uptake of Cd by the organism. Subcutaneous injections of Cd (0.12-0.24 mg/100 g per day) for 10 days resulted in a significant accumulation of Cd in the liver and kidney. No death cases were observed. Addition of CdCl2 to the aquatic environment (more than 0.002%) caused acute toxic effect on frogs. Within 10 days, significant amounts of Cd were found in the skin, especially in its outside layers, small amounts were found in the kidney and liver. High external concentrations of CdCl2 (0.005%) inhibited the activity of Na,K-ATPase in the skin epithelium. It is suggested that adaptive detoxication of cadmium in the liver and kidney operating in mammals, is ineffective in amphibians provided cadmium uptake occurs via the skin.
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PMID:[Cadmium distribution in tissues and Na,K-ATPase activity of the skin of the frog Rana temporaria in different routes of cadmium uptake by the body]. 303 63

Zinc, lead and cadmium in the form of chloride salts when added to a standard assay system containing 80 X 10(-6) ejaculated washed human spermatozoa caused a dose and duration-dependent inhibition of their motility. The activity of certain key enzymes of carbohydrate and energy metabolism, viz, glycogen phosphorylase, glucose-6-phosphatase, fructose-1, 6-diphosphatase, glucose-6-phosphate isomerase, amylase, Mg2+- dependent ATPase and lactic and succinic acid dehydrogenases were also found to be inhibited. The order of inhibitory effects of the heavy metals were zinc less than lead less than cadmium. The metal chelating agent, ethylene diamine tetra-acetic acid (EDTA, disodium salt) also interfered with the spermatozoal motility and inhibited the enzyme activities.
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PMID:Effect of selected metal ions on the motility and carbohydrate metabolism of ejaculated human spermatozoa. 314 74

The mitogenic response of human peripheral blood lymphocytes to the lectin concanavalin A (conA) is inhibited by micromolar concentrations of CdCl2. This inhibition is partially relieved by an increase in the external Ca2+ concentration (from 0.6 to 2.2 mM). The initial rate of conA-induced 45Ca2+ influx is unaltered by CdCl2, although the level of 45Ca2+ accumulation increases. The basal rate of 45Ca2+ entry is not measurably disturbed by CdCl2 (100 microM). The steady-state efflux of 45Ca2+ and the calmodulin-activated (Ca2+ + Mg2+)-ATPase activity of erythrocyte ghosts are inhibited by CdCl2 (10 microM). Thus, the mechanism behind the Cd2+-induced suppression of the mitogenic response to conA is not due to alteration of mitogen-stimulated Ca2+ influx. We suggest that Cd2+ competes with Ca2+ for intracellular Ca2+-binding molecules, such as calmodulin, essential for the induction of cell proliferation.
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PMID:Effects of Cd2+ upon Ca2+ fluxes and proliferation in concanavalin A-stimulated lymphocytes. 315 5

Treatment of erythrocyte ghosts with micromolar concentrations of Cd2+ results in a noncompetitive inhibition of the calmodulin-dependent (Ca2+ + Mg2+)-ATPase activity. Higher concentrations of Cd2+ are required for inhibition of the (Ca2+ + Mg2+)-ATPase activity of calmodulin-depleted ghosts. The interaction of Cd2+ is time-dependent with an apparent rate constant around 0.12/min. The inhibition is relieved by addition of EGTA with a rate constant around 0.15/min. If Cd2+ is allowed to interact with calmodulin prior to the association of the protein with the ghosts, the inhibition is mainly competitive. The results suggest that the inhibitory effect caused by Cd2+ is due to an interaction with calmodulin. The slow interaction of Cd2+ suggests that calmodulin bound to the (Ca2+ + Mg2+)-ATPase is inaccessible to Cd2+.
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PMID:Interaction of Cd2+ with the calmodulin-activated (Ca2+ + Mg2+)-ATPase activity of human erythrocyte ghosts. 315 38

The heart and gill of a freshwater fish Saccobranchus fossilis have been shown to contain a Ca2+-activated ATPase involved in Ca2+ transport. Enzyme showed optimal activity at 3 mM Ca2+ and 3 mM ATP for gills and at 3 mM Ca2+ and 1 mM ATP for heart. Mg2+ was equally effective in stimulating enzyme activity but was not essential for hydrolysis. Maximum activity was found in heart ventricular muscles as compared to gills. Among all the metals tested Hg2+ was the most toxic (IC50, 0.75 and 0.85 microM for heart and gill, respectively) followed by Pb2+, Mn2+, and Cd2+. The inhibition was concentration dependent and reached almost 100% with each metal at the highest concentration. Stimulation of enzyme activity was observed at lower concentrations of Mn2+ and Cd2+ but not with Pb2+ and Hg2+. Stimulation was more pronounced with Mn2+ than with Cd2+ in both heart and gills. The results indicated that the inhibitory effect of these metals might be through the Ca2+-ATPase which is a manifestation of the calcium pump in various tissues.
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PMID:The effects of some divalent metals on cardiac and branchial Ca2+-ATPase in a freshwater fish Saccobranchus fossilis. 315 61

The mutagenic effect of cadmium chloride on somatic cells of F1 hybrid mice CBA X C57B1/6J in vivo and on an established line of CHO-ATZ-2 Chinese hamster cells in vitro has been studied. The induction of micronuclei has been demonstrated in mouse marrow cells as well as induction of point mutations at loci controlling the synthesis of hypoxanthine-phosphoribosyltransferase, thymidine kinase, adenine phosphoribosyltransferase and the resistance of Na+/K+ ATPase to ouabain in the cell line CHO-AT-2. A peak of mutagenic activity under the action of subtoxic doses of cadmium chloride has been revealed.
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PMID:[Mutagenic action of cadmium chloride in mammals]. 343 31

The physiological relevance of an apparent ionophore activity of cholera toxin towards Ca2+ has been examined in several different systems designed to measure affinity, specificity, rates of ion transfer, and effects on intracellular ion concentrations. Half-maximal transfer rates across porcine jejunal brush-border vesicles were obtained at a concentration of 0.20 microM Ca2+. When examined in the presence of competing ions the transfer process was blocked by very low concentrations of La3+ or Cd2+, Sr2+, Ba2+ and Mg2+ were relatively inefficient competitors for Ca2+ transport mediated by cholera toxin. The relative affinities observed would be compatible with a selectivity for Ca2+ transfer at physiological ion concentrations, as well as an inhibition of this ionophore activity by recognized antagonists of cholera toxin such as lanthanum ions. Entry rates of Ca2+ into brush-border vesicles exposed to cholera toxin were large enough to accelerate the collapse of a Ca2+ gradient generated by endogenous Ca, Mg-ATPase activity. The treatment of isolated jejunal enterocytes with cholera toxin caused a significant elevation in cytosolic Ca2+ concentrations as measured by Quin-2 fluorescence. This effect was specifically prevented by prior exposure of the cholera toxin to excess ganglioside GM1. We conclude that cholera toxin has many of the properties required for promoting transmembranes Ca2+ movement in membrane vesicles and appears to be an effective Ca2+ ionophore in isolated mammalian cells.
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PMID:Calcium transport affinity, ion competition and cholera toxin effects on cytosolic Ca concentration. 361 68

Rat red blood cells were employed to study the uptake of cadmium (109Cd). Suspensions of red blood cells were exposed to Cd concentrations of 0.005-500 microM, which were representative of whole blood concentrations (both bound and free) observed following in vivo Cd administration. Cd uptake was biphasic with an initial rapid phase (less than 1 min) followed by a slower second phase. The rate of Cd uptake at 25 degrees C was one-fourth of that at 37 degrees C. The metabolic inhibitors; sodium fluoride (1 mM), potassium cyanide (1 mM) and carbonyl cyanide-m-chlorophenyl hydrazone (2 microM) and the Na+-K+-ATPase inhibitor, ouabain (1 mM) did not reduce Cd (50 microM) uptake into red blood cells. This suggests that the uptake of Cd into red blood cells was not an active process. Incubation of Cd (10 microM) with an equimolar concentration of Zn did not alter uptake of Cd into red blood cells, but at 5 and 10 times higher concentrations of Zn, Cd uptake was enhanced 5-fold. Mercury at one-tenth and equimolar concentrations of Cd increased Cd uptake by red blood cells 2-fold. N-Ethylmaleimide (0.5-5 mM), which irreversibly inactivates membrane sulfhydryl groups, decreased Cd uptake. The data indicate that Cd uptake into rat red blood cells occurs by passive transport and that alterations of sulfhydryls of red blood cell membrane may modulate the process.
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PMID:Cadmium uptake by rat red blood cells. 379 62

The mechanism of retraction of the longitudinal flagellum of Ceratium tripos was studied by making extracted models of the flagellum. Non-detergent models extracted in low ionic strength medium containing 1 M-glucose, 10 mM-EDTA, and 50 mM-Tris X HCl buffer (pH 8.0), retracted when Ca2+, Mg2+, Ba2+, Sr2+, Mn2+ or Cd2+ was applied locally with a glass capillary. A demembranated model of the flagellum was made with an extraction medium containing 0.8-1.0 M-glucose, 20 mM-Tris-acetate (pH 7.8), 2 mM-EGTA, 5-7 mM-MgSO4, 0.1 M-potassium glutamate and 0.1% Triton X-100. The model required a concentration of Mg2+ of a few mmol/l for successful reactivation of both retraction and undulation, and about 0.1 M-potassium glutamate (or sodium glutamate) for reactivation of undulation. Neither type of motion of the models could be reactivated above 35 degrees C. Ca2+ induced the retraction at pCa 5.5 or less. In addition to Ca2+, Mn2+, Ba2+, Sr2+ and Cd2+ also induced retraction but Mg2+, La3+ or Tb3+ did not. Although ATP was required for undulation, it was not required for retraction. Co-incubation with hexokinase to remove contaminating ATP did not suppress the retraction. The potent ATPase inhibitor, orthovanadate, inhibited undulation at 10 micron but did not inhibit retraction even at 2 mM. SH blockers, N-ethylmaleimide and dithio-bis-nitrobenzoic acid strongly suppressed undulation but had no effect on retraction. Calmodulin inhibitors, trifluoperazine and chlorpromazine, also had no effect on retraction. These data indicate that undulation is generated by a 9 + 2 microtubular axoneme using energy released by hydrolysis of ATP and that retraction can be induced by Ca2+ without a requirement for ATP.
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PMID:Extraction model of the longitudinal flagellum of Ceratium tripos (Dinoflagellida): reactivation of flagellar retraction. 385 92


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