Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.6.1.25 (triphosphatase)
 1,529 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A Ca(2+)- or Mg(2+)-stimulated ecto-ATPase is thought to regulate the hydrolysis of extracellular ATP in nervous tissues. The hydrolysis of nucleotide triphosphates (NTPs) was analyzed in brain microsomal fractions from crosses of DBA/2J (D2) and C57BL/6J (B6) mice. The nucleotide triphosphatase (NTPase) activity was significantly reduced in D2 mice as compared to B6 mice, and B6D2F1 hybrids had activities intermediate to the parentals. A significant positive correlation was found between the hydrolysis of four NTPs (ATP, CTP, GTP and UTP) in 24 B6 x D2 (BXD) recombinant inbred (RI) strains of mice and in 80 B6D2F1 x D2 backcross mice. The RI strains and backcross mice fell into two distinct groups with respect to the NTPase activity. Linkage of NTPase activity was suggested with the chromosome 2 markers, D2Mit6 and Ass-1, in the RI strains, and was confirmed by analysis of other markers in the backcross population. These data suggest that the Ca(2+)- or Mg(2+)-stimulated hydrolysis of NTPs, designated Ntp, is regulated by a single gene located on proximal chromosome 2. Although an association was observed previously between Ca(2+)-ATPase activity and susceptibility to audiogenic seizures (AGS), no significant association was observed for the expression of Ntp and AGS susceptibility.
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PMID:Genetic analysis of nucleotide triphosphatase activity in the mouse brain. 805 15

We have observed that in NZBWF1 mice the affinity for L-tryptophan binding to hepatic nuclei in vitro is markedly less than that of Swiss mice. In vitro binding of [3H]tryptophan to hepatic nuclei from both strains was determined without and with unlabeled L-tryptophan (10(-4) mol/L). The relative specific binding of L-tryptophan to hepatic nuclei in vitro was 60.9 +/- 4.4% for Swiss mice and 35.8 +/- 5.4% (P < 0.01) in NZBWF1 mice. The total specific binding (bound radioactivity/mg nuclear protein) of L-tryptophan to hepatic nuclei in vitro was 74.9% (P < 0.05) lower in NZBWF1 mice than in Swiss mice. Other strains (DBA, SJL and BALB/c) had specific binding affinities similar to that of Swiss mice. Serum and hepatic free tryptophan concentrations and hepatic tryptophan dioxygenase activity in mice that were food-deprived overnight or 1 h after tube-feeding L-tryptophan (20 mg/100 g body weight) were similar in the strains of mice. In vitro [14C] leucine incorporation into protein using hepatic microsomes of mice 1 h after tube-feeding L-tryptophan (20 mg/100 g body weight) revealed a significantly greater (P < 0.05) increase relative to food-deprived controls in Swiss mice (76.8 +/- 19.2%) than the increase in NZBWF1 mice (26.5 +/- 2.6%). Nuclear [14C]-labeled RNA release in vitro was increased 77.2 +/- 18.0% by tube-feeding of L-tryptophan in Swiss but only 7.6 +/- 5.8% (P < 0.02) in NZBWF1 mice. Liver nuclear poly(A)-polymerase and nucleoside triphosphatase activities were variably increased by the administration of L-tryptophan in both strains. In summary, compared with Swiss mice, NZBWF1 mice have a lower specific binding affinity for L-tryptophan by hepatic nuclei, and this alteration may account for the other differences in responses to L-tryptophan by the two strains.
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PMID:Differences in tryptophan binding to hepatic nuclei of NZBWF1 and Swiss mice: insight into mechanism of tryptophan's effects. 903 27