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:3.6.3.1 (Mg2+-ATPase)
1,484 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The stimulation by calcium and magnesium of ATPase activity of isolated ghosts, of water-soluble protein (spectrin), and of residual vesicles, derived from normal erythrocytes and from hereditary spherocytes (H.S.), has been measured. The ATPase activity found in normal water-soluble protein (WSP) at low levels of calcium (0.1-2.0 mM) is essentially absent in H.S. water-soluble protein, but the ATPase activity with magnesium and with high levels of calcium (60-100 mM) is the same in H.S. and normal WSP. Compared to normal, H.S. ghosts have increased Mg2+-stimulated activity. This increased activity is retained by the sedimentable vesicles ("residue") after extraction of the ghosts with 0.025 mM EDTA. The Ca2+, Mg2+-ATPase associated with the calcium pump is not significantly different in H.S.
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PMID:Absence of one component of spectrin adenosine triphosphatase in hereditary spherocytosis. 12 93

The effect of the hallucinogenic drug harmaline was tested on rat kidney proximal tubular solute and water transport, using in vivo micropuncture and electrophysiological techniques as well as in vitro biochemical techniques. During peritubular application harmaline (5 mmol/l) was found to block net tubular volume absorption reversibly (by 85%) through inhibition of active Na+ transport and possibly active HCO-3 transport. The inhibition was accompanied by a rapid strong depolarization of the tubular cell membranes. As a biochemical equivalent harmaline inhibited the Na+-K+-ATPase and the Mg2+-ATPase of peritubular cell membrane fractions as well as the HCO-3-stimulated ATPase of a brush border membrane fraction with similar kinetics. By studying glucose tracer efflux and by measuring cell membrane potential and conductance changes in response to glucose perfusions, no evidence for a direct effect of harmaline on Na+-glucose (or amino acid) cotransport mechanisms in the brush border could be obtained. The data suggest that harmaline does not specifically compete with Na+ for transport sites. Neither are the cotransport systems in the brush border membrane specifically inhibited, nor could the inhibition of the Na+ pump in the peritubular cell membrane simply result from a competition between harmaline and Na+.
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PMID:The mechanism of action of harmaline on renal solute transport. 14 Mar 66

The regulation of adrenergic receptors in rat heart was measured in rats made hyperthyroid by injection with thyroxine and made hypothyroid by addition of propylthiouracil to the drinking water. Hyperthyroid rats display cardiac hypertrophy and a decrease in epididymal fat pad weight. The maximal beta-receptor level of ventricular membranes, as determined by (-)-[3H]dihydroalprenolol binding, was increased 60% by thyroxine treatment and decreased about 30% by propylthiouracil treatment. The affinity of the beta receptor was unchanged after thyroxine or propylthiouracil treatment. The maximal activity of the isoproterenol-stimulated adenylate cyclase (EC 4.6.1.1) varied with thyroid state in a manner parallel to the increase in beta-adrenergic binding sites. Thyroxine treatment also increases by 2-fold the beta receptors in isolated rat fat cells. Propylthiouracil treatment lowered the level of alpha receptors in heart by 30% as measured by [3H]dihydroergocryptine binding, but increased the affinity about 2.5-fold. The highest level of alpha receptors was seen in control hearts. These studies indicate that thyroxine may control the turnover of beta-adrenergic receptors in heart and fat cells and regulate physiological responses in these tissues via a hormone-hormone interplay system. Thyroxine treatment reduced the activity of the membrane-bound Mg2+-ATPase (EC 3.6.1.3) and 5'-mononucleotidase (EC 3.1.3.5) but appears to increase the activity of the (Na+ + K+)ATPase (EC 3.6.1.4).
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PMID:Hormone action at the membrane level. VIII. Adrenergic receptors in rat heart and adipocytes and their modulation by thyroxine. 14 63

(1) Photophosphorylation, Ca2+-ATPase and Mg2+-ATPase activities of isolated chloroplasts were inhibited 55--65% when the chemical potential of water was decreased by dehydrating leaves to water potentials (psi w) of --25 bars before isolation of the plastids. The inhibition could be reversed in vivo by rehydrating the leaves. (2) These losses in activity were reflected in coupling factor (CF1) isolated from the leaves, since CF1 from leaves with low psi w had less Ca2+-ATPase activity than control CF1 and did not recouple phosphorylation in CF1-deficient chloroplasts. In contrast, CF1 from leaves having high psi w only partially recoupled phosphorylation by CF1-deficient chloroplasts from leaves havig low psi w. This indicated that low psi w affected chloroplast membranes as well as CF1 itself. (3) Coupling factor from leaves having low psi w had the same number of subunits, and the same electrophoretic mobility, and could be obtained with the same yields as CF1 from control leaves. However, direct measurements of fluorescence polarization, ultraviolet absorption, and circular dichroism showed that CF1 from leaves having low psi w differed from control CF1. The CF1 from leaves having low psi w also had decreased ability to bind fluorescent nucleotides (epsilon-ATP and epsilon-ADP). (4) Exposure of isolated CF1 to low psi w in vitro by preincubation in sucrose-containing media inhibited the Ca2+-ATPase activity of the protein in subsequent assays without sucrose. Inclusion of 5 or 10 mM Mg2+ in the preincubation medium markedly inhibited Ca2+-ATPase activity. (5) These results show that CF1 undergoes changes in cells which alter its phosphorylating ability. Since low cell psi w changed the spectroscopic properties but not other protein properties of CF1, the changes were most likely caused by altered confurn, photophosphorylation. The inhibition of ATPase activity in CF1 in vitro at low psi w and high ion concentration mimicked the change in activity seen in vivo.
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PMID:Conformation and activity of chloroplast coupling factor exposed to low chemical potential of water in cells. 15 20

Electric activity of fragmented sarcoplasmic reticulum (FSR) in the model system organic phase-water was investigated by dynamic capacity method. FSR induced Mg-ATP, Ca2+-dependent change of border volt-potential only when phospholipids were present in the organic phase. It is suggested that FSR electric activity at the interface lipid-water is conditioned by functioning Ca2+, Mg2+-ATPase.
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PMID:[Electric activity of fragmented sarcoplasmic reticulum associated with the organic phase-water interface]. 242 81

Maintenance of Mizuhopecten yessoensis in water with 0.5 mg Cd/l for 60 days increased Cd concentration in the mantle and ovaries about 200 times, in gills 70 times and hepatopancreas 20 times. Alkaline phosphatase activity was inhibited in all organs except the hepatopancreas after a 1-month exposure to Cd and became equal to the control in all the organs after 2 months exposure. Molluscs transferred to flowing water showed a considerable decrease in the activity of alkaline and acid phosphatases. The activity of both acid phosphatase and Mg2+-ATPase decreased in all the organs of experimental molluscs after exposure to Cd. The amount of phospholipids and cholesterol in the organs of control and experimental molluscs did not essentially differ.
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PMID:Cadmium accumulation in organs of the scallop Mizuhopecten yessoensis--I. Activities of phosphatases and composition and amount of lipids. 287

In an effort to determine the effect of chronic ethanol ingestion on myocardial oligomycin sensitive ATPase, guinea pigs were fed 15% ethanol instead of drinking water for 34 weeks. Mg2+-ATPase activity of isolated mitochondria was determined in control and alcohol fed guinea pigs at 16, 20, 24 and 34 weeks. To prove a possible higher fragility of the mitochondria from alcohol fed animals, the ATPase activity was also determined in the supernatant after the isolation of mitochondria "100 000 g fraction". Mg2+-ATPase activity of the isolated mitochondria was time dependent reduced to 56% of the value obtained in the control animals. In the "100 000 g fraction" the ATPase activity, however, started to increase after 8 weeks and after 34 weeks it was about twice as high than in the control group. The findings of this study document a decrease in oligomycin sensitive ATPase activity and an increase in mitochondrial fragility after chronic ethanol ingestion. It supports in the thesis that chronic alcohol intake affects the activity of the intrinsic membrane enzymes by structural derangements of mitochondrial membrane. The changes may play a role in the development of alcoholic cardiomyopathy.
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PMID:The effects of chronic ethanol treatment on oligomycin sensitive ATPase activity in the guinea pig heart. 293 54

The method of dynamic capacity in the model organic phase-water system was used to investigate a possibility of studying the electrical function of Ca2+,Mg2+-ATPase from sarcoplasmic reticulum of the rabbit hind limb skeletal muscles. Decane and decane solution of azolectin were used as an organic phase. It is stated that in the model systems the sarcoplasmic reticulum Ca2+,Mg2+-ATPase did not cause ATP-dependent changes in the boundary Volta potential (delta phi) irrespective of the presence of polyvalent cation chelates in the organic phase. The fragmented sarcoplasmic reticulum is able of realizing Mg-ATP, Ca2+-dependent generation of delta phi only with phospholipids present in the organic phase. It is supposed that generation of delta phi of the fragmented sarcoplasmic reticulum is due to the active transport of calcium ions by the reticulum Ca2+,Mg2+-ATPase.
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PMID:[The use of a model water-lipid system for the study of the electric function of Ca2+, Mg2+-ATPase of the sarcoplasmic reticulum]. 293 82

We have investigated the enzymatic properties of the 120K cross-linked heavy-chain-light-chain derivative formed upon reaction of chymotryptic myosin subfragment 1 (S-1) isoenzymes with the bis(imido esters) dimethyl 3,3'-dithiobis(propionimidate) and dimethyl suberimidate. The formation of the 120K product was accompanied for S-1(A1) but not for S-1(A2) by a loss of the actin-activated ATPase without alteration of the Ca2+-ATPase whereas the Mg2+-ATPase was increased 2-fold. Up to 70%, the inhibition of the acto-S-1(A1) ATPase activity was closely correlated with the extent of cross-linking of the A1 light chain; this activity could be largely restored upon cleavage of the cross-link using the reversible cross-linker dimethyl 3,3'-dithiobis(propionimidate). The covalent link affected the acto-S-1(A1) Mg2+-ATPase activity by reducing 3-fold the Vmax and increasing 2-fold the Kapp. On reacting for the first time the hydrophobic, carboxyl group directed cross-linker N-ethoxycarbonyl-2-ethoxy-1,2-dihydroquinoline (EEDQ) with the acto-S-1(A1 + A2) complex, we found that the N-terminal tail of the A1 light chain was cross-linked to actin to an extent much larger than observed earlier with the water-soluble 1-ethyl-3-[3-(dimethylamino)propyl]carbodiimide; like the latter agent, EEDQ elicited the covalent union of the A1 subunit to the COOH-terminal part of actin. This cross-linker appears to be a valuable chemical probe of the F-actin-A1 light-chain interaction.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Specific interactions of the alkali light chain 1 in skeletal myosin heads probed by chemical cross-linking. 294 76

The sodium pump, (Na+ + K+)-ATPase, which is involved in the transport of cations and water movement by the colonic mucosa, may be decreased in various diarrhoeal states. In this study, we have measured 3H-ouabain binding and (Na+ + K+)-ATPase activity in human colonic biopsy homogenates and the influence of various inflammatory and antiinflammatory compounds on these parameters. 3H-ouabain binds to one site of high affinity (KD 1.9 +/- 0.2 X 10(-9) mol/l) with a maximal binding capacity of 7.5 +/- 0.8 X 10(14) binding sites/g protein. Both arachidonic and linoleic acid inhibited (Na+ + K+)-ATPase activity (IC50 arachidonic acid: 7.5 X 10(-5) mol/l, linoleic acid: 6.5 X 10(-5) mol/l) and Mg2+-ATPase activity (IC50 arachidonic acid: 9 X 10(-5) mol/l, linoleic acid: 4 X 10(-5) mol/l). Arachidonic acid inhibited 3H-ouabain binding, (IC50 3.2 X 10(-5) mol/l). The following antiinflammatory compounds, at concentrations up to 1 X 10(-3) mol/l, did not influence ATPase activity directly nor reverse the arachidonic acid-induced inhibition: indomethacin (cyclooxygenase inhibitor), nordihydroguaiaretic acid (lipoxygenase inhibitor), sulphasalazine and its metabolites: 5-aminosalicylic acid, N-acetylaminosalicylic acid and sulphapyridine. These results indicate that human colonic (Na+ + K+)-ATPase is inhibited by the prostanoid precursors, arachidonic and linoleic acid. From a therapeutic point of view (effect on colonic (Na+ + K+)-ATPase and perhaps diarrhoea), the suppression of the production of these prostanoid precursors by drugs may, therefore, be beneficial in the treatment of inflammatory bowel disease.
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PMID:Inhibition of human colonic (Na+ + K+)-ATPase by arachidonic and linoleic acid. 301 58


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