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 effect of regucalcin, a calcium-binding protein isolated from rat liver cytosol, on deoxyuridine 5'-triphosphatase (dUTPase) in the cytosol of rat liver was investigated. Addition of Ca2+ up to 5.0 microM to the enzyme reaction mixture caused a significant decrease of dUTPase activity, while Zn2+, Cd2+, Co2+, Al3+, Mn2+ and Ni2+ (10 microM) did not have an appreciable effect. The Ca(2+)-induced decrease of dUTPase activity was reversed by the presence of regucalcin; the effect was complete at 1.0 microM of the protein. Regucalcin had no effect on the basal activity of the enzyme. Meanwhile, the reversible effect of regucalcin on the Ca2+ (10 microM)-induced decrease of dUTPase activity was not altered by the coexistence of Cd2+ or Zn2+ (10 microM). The present data suggest that liver cytosolic dUTPase is uniquely regulated by Ca2+ of various metals, and that the Ca2+ effect is reversed by regucalcin.
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PMID:Reversible effect of calcium-binding protein regucalcin on the Ca(2+)-induced inhibition of deoxyuridine 5'-triphosphatase activity in rat liver cytosol. 131 24

Adenosine 5'-triphosphatase (ATPase) plays a role in the process of energy conversion in the controlled hydrolysis of ATP. The effect of Ca2+ -binding protein on ATPase activity in the brain cytosol of rats of different ages was investigated. ATPase activity in the brain cytosol of 50-week-old rats was significantly decreased as compared with that of 5-week-old rats. The presence of calcium chloride (10(-5) and 10(-4) M) in the enzyme reaction mixture caused a significant increase in ATPase activity in the brain cytosol of rats of different ages. This increase was not altered by trifluoperazine (2x10(-5) M), an antagonist of calmodulin. Calmodulin (5 microg/ml), calbindin (5 microg/ml) or S-100A protein (10 microg/ml), a Ca2+ -binding protein, had no effect on ATPase activity. Meanwhile, regucalcin (10(-9) M), which is present in brain, significantly decreased ATPase activity in young and older rats. However, the effect of regucalcin was weakened by the presence of Ca2+ (10(-5) M). The addition of anti-regucalcin monoclonal antibody in the reaction mixture caused a significant elevation of ATPase activity; this increase was completely abolished by addition of regucalcin (10(-9) M). The present study suggests that regucalcin plays an inhibitory role in the regulation of ATPase activity in the brain cytosol of rats of different ages.
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PMID:Effect of calcium-binding protein on adenosine 5'-triphosphatase activity in the brain cytosol of rats of different ages: the inhibitory role of regucalcin. 1022 Feb 91

The effect of regucalcin, a regulatory protein of Ca2+ signaling, on guanosine triphosphatase (GTPase) activity in the nuclei of rat liver was investigated. GTPase activity was significantly increased by the addition of CaCl2 (50 microm) in the enzyme reaction mixture. This increase was not seen in the presence of trifluoperazine (25 microM), an antagonist of calmodulin, which could decrease nuclear GTPase activity, suggesting that nuclear endogenous calmodulin is involved in an increase in the enzyme activity related to Ca2+ addition. The presence of regucalcin (0.5 microM) in the enzyme reaction mixture caused a significant decrease in nuclear GTPase activity. The enzyme activity was significantly raised in the presence of anti-regucalcin monoclonal antibody (25 and 50 ng/ml) in the reaction mixture. This increase was completely abolished by the addition of regucalcin (0.5 microM). Also, the effect of regucalcin addition in increasing nuclear GTPase activity was seen in the presence of EGTA (0.1 mM), a chelator of Ca2+. The present study demonstrates that endogenous regucalcin has a suppressive effect on GTPase activity in the nuclei of rat liver.
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PMID:Suppressive effect of endogenous regucalcin on guanosine triphosphatase activity in rat liver nucleus. 1151 Apr 94

The effect of regucalcin, a regulatory protein of Ca2+ signaling, on guanosine-5'-triphosphatase (GTPase) activity in isolated rat liver plasma membranes was investigated. GTPase activity was significantly increased by the addition of Ca2+ (25-100 microM) in the enzyme reaction mixture. Such an increase was not seen by other metals (Mg, Co, Zn, Cu, Ni and Mn) with 50 microM. The activatory effect of calcium (50 microM) was significantly decreased by calmodulin (2.5 and 5 microg/ml), indicating that it does not depend on calmodulin. The presence of regucalcin (0.1-0.5 microM) in the enzyme reaction mixture caused a significant increase in GTPase activity. This increase was not significantly enhanced by calcium (50 microM). GTPase activity was significantly increased by dithiothreitol (DTT; 5 mM), a protecting reagent of thiol (SH)-groups, while it was decreased by N-ethylmaleimide (NEM; 5 mM), a modifying reagent of SH-groups. The effect of calcium or regucalcin in increasing GTPase activity was not seen in the presence of NEM. Also, the activatory effect of calcium or regucalcin on GTPase was not seen in the presence of vanadate, an inhibitor of protein phosphorylation, which could inhibit GTPase activity. Moreover, the effect of regucalcin was not seen in the presence of digitonin (0.01%), a solubilizing reagent of membranous lipids, while the effect of calcium was not inhibited by digitonin. The present study demonstrates that regucalcin has an activatory effect on GTPase activity independently of Ca2+ in rat liver plasma membranes.
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PMID:Activatory effect of regucalcin on GTPase activity in rat liver plasma membranes. 1169 88