Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.3.5 (5'-nucleotidase)
 3,167 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The changes in the biochemical parameters of peritoneal macrophages and their coupling to the secretory and phagocytic functions in CH3A mice during the growth of the reinoculated solid hepatoma 22a were studied. The DNA and RNA synthesis during the active tumour growth was more intense than that in resident macrophages. The activity of uridine kinase increased up to 156.0 +/- 12.0 nmol/hour/10(8) but was absent in resident macrophages. This was accompanied by a 7.2-fold increase of interleukin-1 synthesis as determined by the [3H]thymidine incorporation into thymocyte DNA in response to concanavalin A administration to C3H mice. Similar changes were observed in peptone-stimulated macrophages. A specific feature of macrophages from tumour-bearing mice was the impairment of activity of purine exchange enzymes and the efficiency of phagocytosis that were unobserved in peptone-stimulated macrophages. The activity of adenosine deaminase and purine nucleoside phosphorylase was inhibited as a result of their preincubation with zymosan, a phagocytosis-stimulating agent. This was accompanied by a significant decrease of the first chemiluminescence peak resulting from disturbances in Fc-reception. Macrophages of tumour-bearing animals possessed an increased 2.2-fold activity of membrane-bound AMP 5'-nucleotidase concomitant with the lack or decrease of the amplitude of the second chemiluminescence peak reflecting the disturbances in digestion resulting from phagocytosis.
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PMID:[Change in activity of enzymes for purine metabolism and RNA and DNA biosynthesis in macrophages, reflecting impairment of their functions in neoplastic growth]. 248 7

Adenosine metabolism in hypothyrosis has been shown to decrease in thymocytes (5'-nucleotidase activity decreases by 18% and adenosine deaminase activity increases in thymocyte light fractions). Activation of adenosine synthesis and decay processes (5'-nucleotidase and adenosine deaminase activity increase by 65 and 72%, respectively) was found in the spleen of hypothyroid rats. Adenosine metabolism returns to normal in the spleen and thymocytes as a result of somatotropin action. Adenosine metabolism in the liver of hypothyroid rats remains unchanged.
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PMID:[Dependence of the activity of enzymes of adenosine metabolism in hypothyroid rats on the level of somatotropin in the body]. 254 27

Experiments in vitro were made to study adenosine deaminase (ADA) and 5'-nucleotidase (5-N) activity in NK after their treatment with interferon inductor--Newcastle disease virus (NDV) or with prostaglandin E2 (PGE2). It has been established that treatment of human NK with NDV leads to increasing of their cytotoxic activity (CTA), which is accompanied by rising of ADA activity and reducing of 5-N activity in these cells. Decrease of CTA under the influence of PGE2 occurs together with reduction of ADA activity and increase of 5-N activity in human NK. Changes in NK activity under the influence of various exogenous or endogenous factors may be due to the modification of activity of adenosine metabolism enzymes in these cells.
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PMID:[Enzyme activity of adenosine metabolism in human natural killers (NK cells) during the activation and suppression of their cytotoxic activity]. 254 32

Adenosine deaminase and 5'-nucleotidase activities as well as chemiluminescence emission were measured in peritoneal macrophages of Syrian hamsters in the growth process of tumours with different grade of malignancy. The adenosine deaminase activity was established to decrease, while the 5'nucleotidase activity--to increase in macrophages after the subcutaneous injection of tumour cells with high level of malignancy as compared with these values in normal cells. This is accompanied by a decrease of the macrophage chemiluminescence during the whole experimental period. At the same time adenosine deaminase and 5'-nucleotidase activities as well as chemiluminescence emission in peritoneal macrophages of hamsters treated with low-malignancy cells do not differ from these values in the control group.
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PMID:[Activity of adenosine metabolism enzymes and spontaneous chemiluminescence in macrophages in the tumor growth process]. 254 8

1. Rats (4 weeks old) were made hypothyroid by treatment with propylthiouracil and a low-iodine diet for a further period of 4 weeks. Synaptosomal membranes, myelin and 105,000 g soluble fractions were obtained from six regions of the brain. 2. Hypothyroidism resulted in 2-5-fold increases in membrane-bound 5'-nucleotidase activity in synaptosomal fractions obtained from cerebellum, cortex, striatum and hippocampus. By contrast, myelin 5'-nucleotidase activity was slightly increased only in the medulla oblongata. 3. Hypothyroidism did not change adenosine deaminase activity, but decreased adenosine kinase activity by approx. 40% in soluble fractions obtained from cerebellum, hippocampus, striatum and hypothalamus. 4. It is suggested that these changes in hypothyroidism, in particular the increases in 5'-nucleotidase activity, could enhance the neuromodulatory effect of adenosine to decrease neurotransmitter release.
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PMID:Changes in the activities of adenosine-metabolizing enzymes in six regions of the rat brain on chemical induction of hypothyroidism. 254 78

The purpose of the study was to investigate influence of glucosaminyl muramyl dipeptide (GMDP) and its derivatives on adenosine deaminase (ADA, CE 3.5.4.4.) and 5'-nucleotidase (5-N, CE 3.1.3.5) activity in murine macrophages in vitro. The intensity of superoxide radicals (O2-) formation by these cells has been also studied. GMDP incubated with macrophages was found to inhibit substantially the activity of 5-N, without affecting the activity of ADA in these cells. The maximal effect on 5-N activity was noted following 24 h of co-culture and was accompanied by a higher intensity of O2- formation. GMDP added in doses ranging from 0.01 to 1 microgram/ml induced a gradual decrease in 5-N activity, with an increase in activity of the O2- -generating system. The GMDP analog with double dipeptide link GM(DP)2 has demonstrated the same activating effect as GMDP. The presence of dipeptide alanyl-D-isoglutamine in the GMDP structure is necessary for realization of the drug activating effect, as N-acetylglucosaminyl-N-acetylmuramyl failed to influence macrophage activity. Neither D-D nor L-L isomers of the drug affect the 5-N activity and O2- formation in macrophages. The mechanism of macrophages activation induced by GMDP may include the inhibition of 5-N activity and the stimulation in production of superoxide radicals.
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PMID:Glucosaminylmuramyl dipeptide-induced changes in murine macrophage metabolism. 255 20

AMP-sepharose 4B has been widely used as a general ligand affinity chromatography for purification of AMP deaminase, 5'-nucleotidase, adenosine kinase and other adenine nucleotide metabolizing enzymes. Since these enzymes generally differ in their kinetic properties related to the values of Km for AMP and analogous compounds, it was assumed that there may be a specific elution pattern of some of the enzymes which would enable sequential elution from the column during a single run. Using 0.5 M NaCl, 10 mM ATP and 5 mM adenosine as eluting agents, it was possible to separate on AMP-sepharose column AMP deaminase "high Km" and "low Km" 5'-nucleotidase and adenosine kinase. Adenylate kinase, adenosine deaminase and nonspecific phosphatase did not bind to the column. Using human placental extract, AMP deaminase, "high Km" and "low Km" 5'-nucleotidase and adenosine kinase were purified 2.8, 2.9, 105 and 1240 fold, respectively. AMP deaminase and "high Km" 5'-nucleotidase were further separated using phosphocellulose column chromatography and the final purification was 227 and 143 fold, respectively. The specific activities of purified enzyme preparations were 9.1, 1.0, 0.4 and 0.5 mumols/min/mg protein of AMP deaminase, "high Km" 5'-nucleotidase and adenosine kinase, respectively. This approach provides a rapid method for initial purification of these enzymes from crude soluble extracts.
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PMID:The application of affinity chromatography for the separation of "high Km" and "low Km" 5'-nucleotidase and other AMP metabolizing enzymes. 255 31

The transmural distribution of the adenosine-generating enzyme 5'-nucleotidase (5'N) and of the adenosine-degrading enzymes adenosine deaminase (ADA), AMP deaminase (AMP-D) and adenosine kinase (Ado-K) were determined across the walls of left and right ventricles of control and hypertrophic rat hearts. The enzyme distribution across the left ventricle wall (but not across the right wall) of normal hearts was not uniform: 5'N activity shows its highest levels in the subepicardial and in the subendocardial regions, whereas all the other enzyme activities show their lowest levels. A similar pattern of transmural distribution was also detected in other mammalian species (ox and pig). In the experimental cardiac hypertrophy, caused by two different types of chronic cardiac overload, the levels and the profiles of transmural distribution of 5'N and ADA enzyme activities may significantly change across the rat left ventricle wall.
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PMID:The regional distribution of adenosine-regulating enzymes in the left and right ventricle walls of control and hypertrophic heart. 255 11

The activities of purine-metabolizing enzymes, 5'-nucleotidase, adenosine deaminase, and purine nucleoside phosphorylase in microdissected rat nephron segments were measured. The specific activity of 5'-nucleotidase was highest in the proximal tubules and the cortical collecting duct, but low in the glomerulus. In contrast, the highest activity of adenosine deaminase was found in the glomerulus. The distribution pattern of purine nucleoside phosphorylase was similar to that of adenosine deaminase. These results suggest that various nephron segments can form adenosine and that the glomerulus exhibits highest capacities to metabolize this nucleoside.
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PMID:Intranephron distribution of purine-metabolizing enzymes in rats. 256 Feb 34

Liposomes of different composition and N-acetylglucosaminyl-N-acetylmuramyl-L-alanyl-D-isoglutamine (GMPD) encapsulated in them are studied for their effect on the functional activity of macrophages by means of determining the 5'-nucleotidase and adenosine deaminase activity in the in vivo experiments. It is shown that both liposomes and GMDP encapsulated in them increase the activity of adenoside deaminase and decrease that of 5'-nucleotidase. This evidences for a change in the adenosine metabolism in the alveolar and peritoneal macrophages and an increase in the functional activity of cells which resulted from that rise. The manifestation of the process depends both on the lipid composition of liposomes and their charge. The observed increase in the functional activity of the alveolar macrophages under the effect of liposomes and GMDP encapsulated in them correlates with inhibition of the lung metastases development in mice.
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PMID:[The effect of muramyl dipeptide analog, GMPD, incorporated into liposomes of various composition on the functional activity of macrophages]. 256 Oct 33


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