Catabolism of adenine nucleotides in suspension-cultured plant cells

Profiles of the catabolism of adenine nucleotides in cultured plant cells were investigated. Adenine nucleotides, prelabelled by incubation of suspension-cultured Catharantus roseus cells with [8-14C]adenosine, were catabolized rapidly and most of the radioactivity appeared in 14CO2. Allantoin and allantoic acid, intermediates of the oxidative catabolic pathway of purines, were temporarily labelled. When the cells, prelabelled with [8-14C]adenosine, were incubated with high concentrations of adenosine, the rate of catabolism of adenine nucleotides increased. The results suggest that the relative rate of catabolism of adenine nucleotides is strongly dependent on the concentration of adenine nucleotides in the cells. Studies using allopurinol, coformycin and tiazofurin, inhibitors of enzymes involved in purine metabolism, suggest that participation of AMP deaminase and xanthine oxidoreductase in the catabolism of adenine nucleotides in plant cells. AMP deaminase was found in extracts from C. roseus cells and its activity increased significantly in the presence of ATP. In contrast, no adenosine deaminase or adenine deaminase activity was detected. Qualitative differences in the catabolic activity of AMP were observed between suspension-cultured cells from different species of plants.     

Modulation of adenine nucleoside excretion and incorporation in adenosine deaminase deficient human lymphoma cells

The availability of a human lymphoma cell line deficient in adenosine deaminase, adenosine kinase and methylthioadenosine phosphorylase enabled us to compare the effects of nucleoside transport inhibitors on the excretion of endogenously generated adenosine, deoxyadenosine and 5'-methylthioadenosine. The nucleoside transport inhibitors nitrobenzylthioinosine and dipyridamole blocked the efflux of adenosine, but not deoxyadenosine or 5'-methylthioadenosine. The inhibitors also prevented the uptake of exogenous adenosine, but not deoxyadenosine or 5'-methylthioadenosine, by human lymphoblasts. The results show (i) that the transport inhibitors modify adenine nucleoside efflux and influx similarly, and (ii) that the effects of the compounds on the excretion and uptake of these three physiologically important adenine nucleosides are distinctly different.     

Non-covalently bound adenine nucleotides in adenosine triphosphatase of Escherichia coli.

The term, xeroderma pigmentosum variants designates patients who suffer from the clinical manifestations of the disease, but whose cells have normal rates of excision repair of UV-induced lesions in DNA. In contrast to normal human fibroblasts, if cells from such variants are maintained in medium containing caffeine from immediately following exposure to UV until the survivors have undergone three doublings, the cytotoxic and mutagenic effect of UV light is dramatically increased. In the presence of 0.7mM caffeine, the slope of the UV survival curve increases $\text{ca.}$ 3-fold. Similarly, the slope of the curve describing the frequency of mutations to azaguanine resistance induced by UV as a function of dose is $\text{ca.}$ 3-fold steeper.     

Responses of adenine nucleotides in germinating soybean embryonic axes to exogenously applied adenine and adenosine

The ATP content of soybean (Glycine max [L.] Merr. cv. Kent) axes incubated for 3 hours in 1 mm solutions of adenine and adenosine increased over 100% and 75%, respectively, over axes incubated in water. The increase in ATP was primarily due to the conversion of these purines to nucleotides via the nucleotide salvage pathway. The ATP formed was in a metabolically active pool because label from adenine was incorporated into acid-insoluble material. Adenine also increased the levels of GTP, UTP, and CTP, but not to the extent of the ATP level.     

Polymorphism of adenosine deaminase in the pig: allelic variation in erythrocytes

Within the frame of our investigations on genetic variation of pig red cell enzymes, by means of enzymo-electrophoresis and spectrophotometric measurements, four kinds of adenosine deaminase phenotypic patterns were identified in haemolysates from 542 Belgian Landrace and 502 Pietrain pigs. Segregation data are consistent with the hypothesis that these phenotypes are determined by two codominant alleles ADA ^A and ADA ^B and a recessive silent allele ADA ^O, at an autosomal locus. Differences in gene frequencies between the two breeds are highly significant.     

Degradation of adenine nucleotides in the erythrocytes of patients with chronic renal failure

In chronic renal failure AMP-deaminase operates in the erythrocytes at a much higher velocity than in healthy subjects, with a simultaneous shift from the AMP-adenine-inosine-hypoxanthine pathway (55% and 19%, respectively) to the pathway initiated by AMP-deaminase (45% and 81%, respectively).     

Effects of adenine nucleotides on rice-root adenosine triphosphate sulphurylase activity in vitro.

The presence of ATP sulphurylase activity in the 30000g supernatant fraction of rice-root homogenate has been demonstrated. Studies of the effects of adenosine and its nucleotides on the enzymic activity showed that AMP activated but that ADP and adenosine inhibited the enzyme.     

Deoxyadenosine triphosphate acting as an energy-transferring molecule in adenosine deaminase inhibited human erythrocytes

Deoxyadenosine triphosphate (dATP) is present in adenosine deaminase (ADA)-deficient or ADA-inhibited human red cells and in the red cells of the opossum Didelphis virginiana. In order to investigate the functions of dATP in the red cell, red cells were treated with 2'-deoxycoformycin (dCf), a powerful inhibitor of ADA, and incubated with phosphate, deoxyadenosine and glucose. These red cells in which ATP was almost completely replaced by dATP, had the same shape, lactate production, nucleotide consumption, stability of reduced glutathione, osmotic fragility and cell deformability as red cells containing ATP. Cells merely depleted of ATP showed reduced viability. This indicates that dATP compensates well for the absence of ATP and acts as an energy-transferring molecule to maintain cell viability. These results indicate that the accumulation of dATP or the reduction of ATP is not the cause of the hemolysis observed after dCf administration.