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)

Ca2+ -dependent hydroxylamine-sensitive phosphorylated proteins can be demonstrated in a microsomal fraction of porcine antrum (stomach) smooth muscle and in a Ca2+ -transport ATPase ((Ca2+ + Mg2+)-ATPase) purified from this tissue by means of a calmodulin affinity technique. These phosphoproteins represent the phosphorylated intermediates of the (Ca2+ + Mg2+)-ATPases. In the (Ca2+ + Mg2+)-ATPase purified from smooth muscle the phosphorylated intermediate has an Mr of 130000 corresponding to the value found for erythrocyte (Ca2+ + Mg2+)-ATPase. In the smooth muscle microsomal fraction this 130 kDa phosphoprotein can also be seen, although its intensity is usually very low compared to a corresponding phosphorylation at Mr 100000. Including La3+ together with Ca2+ during phosphorylation of the microsomes increased selectively the steady state-level of the 130 kDa phosphoprotein over the value of the 100 kDa one. The 100 kDa Ca2+ -dependent phosphoprotein could either indicate the presence of a (Ca2+ + Mg2+)-ATPase of the same type of sarcoplasmic reticulum of skeletal muscle, or it could represent a proteolytic product of the 130 kDa phosphoprotein.
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PMID:Demonstration of the phosphorylated intermediates of the Ca2+-transport ATPase in a microsomal fraction and in a (Ca2+ + Mg2+)-ATPase purified from smooth muscle by means of calmodulin affinity chromatography. 612 96

Renal basal-lateral and brush border membrane preparations were phosphorylated in the presence of [gamma-32P]ATP. The 32P-labeled membrane proteins were analysed on SDS-polyacrylamide gels. The phosphorylated intermediates formed in different conditions are compared with the intermediates formed in well defined membrane preparations such as erythrocyte plasma membranes and sarcoplasmic reticulum from skeletal muscle, and with the intermediates of purified renal enzymes such as (Na+ + K+)-ATPase and alkaline phosphatase. Two Ca2+-induced, hydroxylamine-sensitive phosphoproteins are formed in the basal-lateral membrane preparations. They migrate with a molecular radius Mr of about 130 000 and 100 000. The phosphorylation of the 130 kDa protein was stimulated by La3+-ions (20 microM) in a similar way as the (Ca2+ + Mg2+)-ATPase from erythrocytes. The 130 kDa phosphoprotein also comigrated with the erythrocyte (Ca2+ + Mg2+)-ATPase. In addition in the same preparation, another hydroxylamine-sensitive 100 kDa phosphoprotein was formed in the presence of Na+. This phosphoprotein comigrates with a preparation of renal (Na+ + K+)-ATPase. In brush border membrane preparations the Ca2+-induced and the Na+-induced phosphorylation bands are absent. This is consistent with the basal-lateral localization of the renal Ca2+-pump and Na+-pump. The predominant phosphoprotein in brush border membrane preparations is a 85 kDa protein that could be identified as the phosphorylated intermediate of renal alkaline phosphatase. This phosphoprotein is also present in basal-lateral membrane preparations, but it can be accounted for by contamination of those membranes with brush border membranes.
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PMID:Phosphorylated intermediates of (Ca2+ + Mg2+)-ATPase and alkaline phosphatase in renal plasma membranes. 613 Jul 91

Plasma membrane vesicles of Ehrlich ascites carcinoma cells have been isolated to a high degree of purity. In the presence of Mg2+, the plasma membrane preparation exhibits a Ca2+-dependent ATPase activity of 2 mumol Pi per h per mg protein. It is suggested that this (Ca2+ + Mg2+)-ATPase activity is related to the measured Ca2+ transport which was characterized by Km values for ATP and Ca2+ of 44 +/- 9 microM and 0.25 +/- 0.10 microM, respectively. Phosphorylation of plasma membranes with [gamma-32P]ATP and analysis of the radioactive species by polyacrylamide gel electrophoresis revealed a Ca2+-dependent hydroxylamine-sensitive phosphoprotein with a molecular mass of 135 kDa. Molecular mass and other data differentiate this phosphoprotein from the catalytic subunit of (Na+ + K+)-ATPase and from the catalytic subunit of (Ca2+ + Mg2+)-ATPase of endoplasmic reticulum. It is suggested that the 135 kDa phosphoprotein represents the phosphorylated catalytic subunit of the (Ca2+ + Mg2+)-ATPase of the plasma membrane of Ehrlich ascites carcinoma cells. This finding is discussed in relation to previous attempts to identify a Ca2+-pump in plasma membranes isolated from nucleated cells.
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PMID:Identification of Ca2+-pump-related phosphoprotein in plasma membrane vesicles of Ehrlich ascites carcinoma cells. 613 90

We have identified and characterized calcium transport and the phosphorylated intermediate of the (Ca2+ + Mg2+)-ATPase in plasma membrane vesicles prepared from rat liver. The calcium transport did not absolutely require the presence of oxalate and was completely inhibited by 1 microM of ionophore A23187. Oxalate, which serves as a trapping agent in calcium uptake of skeletal muscle and liver microsomes, was not absolutely required to maintain the net accumulation of calcium. The Vmax and Km for calcium uptake were 35.2 +/- 10.1 pmol of calcium/mg of protein/min, and 17.6 +/- 2.5 nM of free calcium, respectively. Ten mM magnesium was required for the maximal accumulation of calcium. Substitution of 5 and 10 mM ADP, CTP, GTP, and UTP for ATP could not support calcium uptake. The calcium uptake was not affected by 0.5 mM ouabain, 20 mM azide, or 2 micrograms/ml of oligomycin but was inhibited in a dose-dependent fashion by vanadate, with a Ki of approximately 20 microM for vanadate. The substrate affinities and specificities of this calcium-transport activity suggest that it is closely associated with the (Ca2+ + Mg2+)-ATPase reported in the plasma membranes of liver (Lotersztajn, S., Hanoune, J., and Pecker, F. (1981) J. Biol. Chem. 256, 11209-11215). A calcium-stimulated and magnesium-dependent phosphoprotein was also demonstrated in the same membrane vesicles. The free calcium concentration at which its phosphorylation was half-maximal was 15.5 +/- 5.6 nM. Sodium fluoride, ouabain, sodium azide, oligomycin, adriamycin, and N,N'-dicyclohexylcarbodiimide did not affect its formation while vanadate at 100 microM inhibited the calcium-dependent phosphorylation by approximately 60%. The properties of this phosphoprotein suggest that it may be the phosphorylated intermediate of the (Ca2+ + Mg2+)-ATPase in the plasma membranes of rat liver.
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PMID:Calcium transport and phosphorylated intermediate of (Ca2+ + Mg2+)-ATPase in plasma membranes of rat liver. 613 93

R24571 a derivative of the antimycotic miconazole, appears to be 5 to 8 times more potent than trifluoperazine in its ability to inhibit the calmodulin-dependent phosphorylation of cardiac sarcoplasmic reticulum vesicles. The cAMP-dependent protein kinase mediated phosphorylation of cardiac sarcoplasmic reticulum was not affected by R24571. Sarcoplasmic reticulum Ca-dependent ATPase phosphoprotein intermediate formation was inhibited by R24571 concentrations that were 20 to 30 times greater than those required to inhibit calmodulin-dependent phosphorylation. However, both Ca-dependent and independent ATPase activities, as well as calcium uptake, were inhibited by R24571 concentrations that were similar to, or less than, those concentrations required to inhibit calmodulin-dependent sarcoplasmic reticulum phosphorylation. These results indicate the caution that should be exercised in using this new compound in assessing the possible involvement of calmodulin in other membrane processes.
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PMID:Inhibition of calmodulin-dependent and independent cardiac sarcoplasmic reticulum activities by R24571. 613 10

A phosphorylated intermediate of the CaMg-ATPase is demonstrated in microsomal preparations from uterine smooth muscle. Characterization included the use of activators, inhibitors, and sodium dodecyl sulfate (SDS)-gel electrophoresis. The phosphorylation was a function of the ATP and Ca concentrations. The dissociation constant KATP was 2.7 X 10(-6) M and KCa was 1.7 X 10(-6) M. Mg was obligatory for the reaction. Na azide, ouabain, or the substitution of NaCl for KCl did not affect the reaction. Phosphorylation was inhibited by Salyrgan, ADP, or 20 mM calcium. SDS-polyacrylamide gel electrophoresis at pH 2.4 demonstrated phosphorylation of predominantly one protein with a molecular weight of 100,000. Hydroxylamine and, to a lesser extent, neutral and alkaline pH caused dephosphorylation. This indicates the presence of an acylphosphate bond in the phosphoprotein. The above findings are consistent with the phosphorylated intermediate being a Ca,Mg-ATPase. The inhibition by 20 mM calcium indicates that the Ca,Mg-ATPase of smooth muscle differs from that of striated muscle sarcoplasmic reticulum.
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PMID:Properties of a phosphorylated intermediate of the Ca,Mg-activated ATPase of microsomal vesicles from uterine smooth muscle. 614 19

A high degree of ATP hydrolytic activity present in purified rat pancreatic acinar cells was localized to plasma membranes. This activity was stimulated almost equally by Mg2+ or Ca2+. Kinetic analysis revealed that the enzyme had a higher affinity for Ca2+ (Kd = 1.73 microM) than Mg2+ (Kd = 2.98 microM) but a similar maximal rate of activity. A comparison of substrate requirements revealed very similar profiles for the Mg2+- and Ca2+-stimulated activities. Combinations of saturating concentrations of Mg2+ or Ca2+ produced the same degree of maximal activity. Investigation of the partial reactions of the ATPase activity revealed two phosphoprotein intermediates (Mr = 115,000 and 130,000) in the presence of Ca2+ and Mg2+. A significant stimulation of the Ca2+-ATPase activity by calmodulin was observed (Kd = 0.7 microM). Calmodulin increased the Ca2+-sensitivity of this enzyme system; Mg2+ appeared to be required for this effect. The Ca2+-ATPase activity was also stimulated by acidic phospholipids. Using an 125I-labeled calmodulin gel overlay technique, calmodulin was shown to bind in a Ca2+-dependent fashion to 133,000- and 230,000-dalton proteins present in the plasma membrane-enriched fraction. Under conditions that favor Ca2+-dependent kinase activity, calmodulin enhanced the phosphorylation of a 30,000- and 19,000-dalton protein. The major ATP hydrolytic activity in pancreatic acinar plasma membranes was present as an ectoenzyme.
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PMID:Ca2+-ATPase activity in pancreatic acinar plasma membranes. Regulation by calmodulin and acidic phospholipids. 614 23

Since agents which affect Ca2+ fluxes have been shown to affect the commitment to terminal differentiation of murine erythroleukemia cells treated with an inducer of differentiation (Bridges, K., Levenson, R., Housman, D., and Cantley, L. (1981) J. Cell Biol. 90, 542-544), we investigated the presence of Ca2+-transport systems in plasma membranes isolated from these cells. Plasma membranes from murine erythroleukemia cells exhibited a high affinity (Ca2+-Mg2+)-ATPase activity with a Vmax of 29 +/- 4 nmol/mg/min and an apparent K0.5 for free Ca2+ of 0.13 microM. This activity was strongly inhibited in a dose-dependent fashion by low concentrations of trifluoperazine, compound 48/80, lanthanum, and vanadate with I50 of 29 microM, 1.75 micrograms/ml, 1.5 microM, and 0.4 microM, respectively. The inhibitory effect of compound 48/80 was specifically reversed by exogenously added calmodulin. Phosphorylation of plasma membranes with [gamma-32P] ATP followed by sodium dodecyl sulfate electrophoretic analysis at low pH revealed a Ca2+-dependent phosphoprotein with an apparent molecular mass of 138,000 daltons which co-migrated with the Ca2+-dependent phosphoprotein from human erythrocytes and was separable from sarcoplasmic reticulum (Ca2+-Mg2+)-ATPase. The 32P incorporated into the phosphoprotein could be chased with unlabeled ATP and the protein-phosphate bond was unstable at alkaline pH suggesting an acylphosphate ATPase intermediate like that previously characterized in other (Ca2+-Mg2+)-ATPases.
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PMID:Characterization of a Ca2+-stimulated Mg2+-dependent adenosine triphosphatase in Friend murine erythroleukemia cell plasma membranes. 615 38

Membrane fractions prepared from smooth muscle of the pig stomach (antral part) contain two Ca2+-dependent phosphoprotein intermediates belonging to different Ca2+-transport ATPases. These alkali-labile phosphoproteins can be separated by electrophoresis in acid medium. The 130 kDa phosphoprotein resembles a corresponding protein in the erythrocyte membrane, whereas the 100 kDa protein resembles that of the Ca2+-transport ATPase in sarcoplasmic reticulum from skeletal muscle. These resemblances are expressed in terms of Mr, reaction to La3+ and in a similar proteolytic degradation pattern. The presence of the calmodulin-stimulated ATPase in mixed membranes from smooth muscle is confirmed by its binding of calmodulin and antibodies against erythrocyte Ca2+-transport ATPase, whereas such binding does not occur with proteins present in the presumed endoplasmic reticulum from smooth muscle.
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PMID:Evidence for the presence in smooth muscle of two types of Ca2+-transport ATPase. 615 92

An acid-stable phosphoprotein was formed in a microsomal membrane fraction isolated from bovine aortic smooth muscle in the presence of Mg2+ + ATP and Ca2+. The microsomes also showed Ca2+ uptake activity. The Ca2+ dependence of phosphoprotein formation and of Ca2+ uptake occurred over the same range of Ca2+ concentration (1-10 microM), and resembled similar findings from rabbit skeletal microsomes. The molecular weight of the phosphorylated protein, estimated by SDS-gel electrophoresis, was approximately 105,000. The phosphoprotein was labile at alkaline pH, and its decomposition was accelerated by hydroxylamine. Half-maximum incorporation of 32P in the presence of 10 microM Ca2+ occurred at 60 nM ATP. The calcium-dependent phosphoprotein formation was not affected by 5 mM NaN3, but was inhibited in a dose-dependent fashion by ADP with a 50% inhibition occurring at 180 microM. Fifty mM MgCl2 was required for the maximal phosphorylation. The rate of phosphoprotein decomposition after adding 2 mM EGTA was accelerated by varying the Mg2+ concentration from 10 microM to 3 mM. Alkaline pH (9.0) slowed the rate of phosphoprotein decay. Optimal Ca2+-dependent phosphoprotein occurred at 15 degrees C over a broad pH range (6.4 to 9.0). The activation energy of EGTA-induced phosphoprotein decomposition was 25.6 kcal/mol between 0 and 16 degrees C and 14.6 kcal/mol between 16 and 30 degrees C. The phosphoprotein formed by aortic microsomes was thus quite similar to the acid-stable phosphorylated intermediate of the Ca2+-transport ATPase of sarcoplasmic reticulum from skeletal and cardiac muscle. These data suggest that the Ca2+-dependent phosphoprotein is a reaction intermediate of the Ca2+,Mg2+-ATPase of the aortic microsomes.
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PMID:Ca2+,Mg2+-ATPase of microsomal membranes from bovine aortic smooth muscle. Identification and characterization of an acid-stable phosphorylated intermediate of the Ca2+,Mg2+-ATPase. 615 48


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