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 activity of guanine deaminase (GAH, E.C.3.5.4.3) was lower in rat cerebellum soluble and microsomal fractions than in rat brain subfractions. Adenosine deaminase (ADA, E.C.3.5.4.4) activity was released in higher proportion than guanine deaminase, purine nucleoside phosphorylase (PNP, E.C.2.1.2.4), 5'-nucleotidase (5'N, E.C.3.1.3.5), and lactate (LDH, E.C. 1.1.1.27) and malate (MDH, E.C. 1.1.1.37) dehydrogenase in press-juices of rat brain. Furthermore, nerve ending-derived fractions (synaptosomes and synaptic vesicles) showed an enrichment of adenosine deaminase and also of 5'-nucleotidase. The action of deoxycholate over the subfractions did not increase the activity of either enzyme. The contrary occurred with the remaining enzymes studied. Thus, it is possible that one set of enzymes are located on the surface of the particulate vesicles, whereas another set are located inside these vesicles, suggesting a compartmentation of purine catabolic enzymes in different areas of the central nervous system.
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PMID:Heterogeneous localization of some purine enzymes in subcellular fractions of rat brain and cerebellum. 301 Jan 50

The activities of 5'-nucleotidase (5'-ribonucleoside phosphohydrolase, EC 3.1.3.5); adenosine deaminase (adenosine aminohydrolase, EC 3.5.4.4); AMP deaminase (AMP aminohydrolase, EC 3.5.3.6), and ATP-(Mg2+)-ase (ATP phosphohydrolase, EC 3.6.1.3) were assayed in mitochondria of normal and regenerating rat liver 5'-Nucleotidase (5'Nase) and ATP-(Mg2+)-ase activities were compared with similar enzyme activities in the plasma membrane (PM) fraction, obtained from the same biological material. In the regenerating liver, 5'Nase for dTMP diminished its activity by 56% (24 h after partial hepatectomy) and 35 +/- 4% for all substrates in the PM fraction (48 h after operation). In mitochondria, 5'Nase for dTMP manifests sigmoidal substrate activity curve (in contrast with all substrates in the PM fraction and remaining substrates in mitochondria). In vivo 5-azacytidine (a) administered 1 h after partial hepatectomy, prevented changes of 5'Nase activity: (b) administered 24 or 48 h after partial hepatectomy, stabilized low 5'Nase activity (in mitochondria for dTMP, in the PM fraction for all substrates) and decreased ATP-(Mg2+)-ase activity by 51 and 31% in mitochondria and the PM fraction respectively.
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PMID:A distinctive activity of 5'-nucleotidase for dTMP in rat liver mitochondria. 615 75

Adenine nucleotides cause adenosine receptor-mediated increases in cyclic AMP in the VA13 human fibroblast line. Levels of adenosine accumulated in the medium are insufficient to account for the responses to adenine nucleotides. Since rapid conversion of the nucleotides to adenosine by 5'-nucleotidase in the vicinity of the receptor might account for the responses, six experimental methods were developed to distinguish between "local conversion" and direct action of the nucleotides. Results of all six methods favored local conversion. (1)5'-Nucleotidase inhibitors blocked the accumulations of cyclic AMP elicited by AMP, ADP, and ATP, but did not affect the response to adenosine. The most potent inhibitor of both conversion of AMP and response to AMP was alpha, beta-methylene-ADP (APCP). (2) Adenosine deaminase blocked the responses to AMP, ADP, ATP, and adenosine-containing coenzymes. (3) Theophylline, a specific competitive adenosine antagonist, was an insurmountable inhibitor of the increases in cyclic AMP caused by AMP, ADP, and ATP. The insurmountability was presumably due to substrate saturation of the converting enzyme 5'-nucleotidase. (4) Although ADP and ATP had partial agonist-liked dose-response curves, they did not inhibit the response to adenosine. (5) Nine cell lines which responded to adenosine were tested for response to AMP. Cell lines with high levels of 5'-nucleotidase had large responses to AMP, those with intermediate levels of 5'-nucleotidase had large or intermediate responses to AMP, and those with low 5'-nucleotidase levels did not respond to AMP. (6) Inhibition of the uptake of labelled adenosine was used as an indicator of unlabelled adenosine concentrations near the cell membrane. Unlabelled AMP inhibited uptake nearly as effectively as unlabelled adenosine. APCP reversed the inhibition by AMP but not the inhibition by adenosine. The adenosine receptor is concluded to be an entity distinct from adenine nucleotide receptors.
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PMID:Adenosine receptor activation by adenine nucleotides requires conversion of the nucleotides to adenosine. 626 30

5'-Nucleotidase, adenosine phosphorylase, adenosine deaminase and purine nucleoside phosphorylase, four enzymes involved in the utilization of exogenous compounds in Bacillus cereus, were measured in extracts of this organism grown in different conditions. It was found that adenosine deaminase is inducible by addition of adenine derivatives to the growth medium, and purine, nucleoside phosphorylase by metabolizable purine and pyrimidine ribonucleosides. Adenosine deaminase is repressed by inosine, while both enzymes are repressed by glucose. Evidence is presented that during growth of B. cereus in the presence of AMP, the concerted action of 5'-nucleotidase and adenosine phosphorylase, two constitutive enzymes, leads to formation of adenine, and thereby to induction of adenosine deaminase. The ionsine formed would then cause induction of the purine nucleoside phosphorylase and repression of the deaminase. Taken together with our previous findings showing that purine nucleoside phosphorylase of B. cereus acts as a translocase of the ribose moiety of inosine inside the cell (Mura, U., Sgarrella, F. and Ipata, P.L. (1978) J. Biol Chem. 253, 7905-7909), our results provide a clear picture of the molecular events leading to the utilization of the sugar moiety of exogenous AMP, adenosine and inosine as an energy source.
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PMID:Induction and repression of enzymes involved in exogenous purine compound utilization of Bacillus cereus. 627 19

The aim of this study was to determine whether ATP must be hydrolysed to adenosine in order to activate the P1-purinoceptor. Isometric contractions of electrically paced guinea-pig isolated left atria were recorded. Purines evoked negative inotropic responses that were competitively antagonised by theophylline. The order of agonist potency was 2-chloroadenosine greater than adenosine greater than beta, gamma-methylene ATP greater than ATP. Adenosine deaminase alone, or combined with 5'-nucleotidase, attenuated responses to adenosine and 5' AMP, respectively, but did not decrease those to ATP or beta, gamma-methylene ATP. Inhibition of 5'-nucleotidase did not alter responses to ATP. Dipyridamole potentiated responses to ATP both in the absence and in the presence of adenosine deaminase. Alpha, beta-methylene ATP had little agonist activity, however this was not due to its resistance to hydrolysis as the stable beta, gamma-methylene isostere of ATP was a potent agonist. These results indicate that hydrolysis of ATP to adenosine or 5' AMP is not a pre-requisite for activation of the P1-receptor in the guinea-pig atrium.
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PMID:Can ATP stimulate P1-receptors in guinea-pig atrium without conversion to adenosine? 689 58

Serum levels of adenosine deaminase (ADA), 5-nucleotidase (5'-NT) and alkaline phosphatase (ALP) were studied in 25 patients of carcinoma breast and 25 normal subjects. Adenosine deaminase was found to be the better probable parameter for the detection of cancer and to assess the development of various stages of cancer whereas 5'-nucleotidase had only diagnostic significance. Serum alkaline phosphatase levels were important for assessing the spread of cancer at secondary sites. After mastectomy a significant decrease was found in the levels of serum ADA and 5'-NT whereas no variations were found in case of serum ALP.
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PMID:Serum adenosine deaminase, 5'-nucleotidase & alkaline phosphatase in breast cancer patients. 767 35

The activities of some of the enzymes participating in nucleotide metabolism were measured in cancerous and noncancerous gastric tissues from patients with gastric cancer. The enzyme activities measured were found to be higher in the cancerous tissues than in the non-cancerous tissues. Adenosine deaminase (ADA), 5'-nucleotidase (5'-NT), guanase (GUA) and cytidine deaminase (CD) activities in the cancerous tissues were 56.0 +/- 24.0, 45.0 +/- 20.0, 0.34 +/- 0.16 and 4.65 +/- 2.04, respectively. The activities in non-cancerous tissues were 13.2 +/- 6.0, 19.8 +/- 8.3, 0.12 +/- 0.06 and 1.65 +/- 0.8, respectively. Cancerous tissues consisted of 7 gastric tissues with Grade I-II and 8 tissues with Grade III-IV adeno cancer. Non-cancerous adjacent tissues were obtained from the same patients with Grade I-II cancer. There were no meaningful differences between enzyme activities of the gastric tissues with Grade I-II and Grade III-IV cancer. Enzyme activity ratios indicates that ADA activity increased by the highest amount relative to other enzyme activities in the cancerous tissues. In the correlation analysis, we found positive correlations between some of the enzyme activities in the cancerous tissues. Results suggest that increased activities of these enzymes might play a part in the accelerated nucleotide metabolism in the cancerous gastric tissues.
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PMID:Adenosine deaminase, 5'-nucleotidase, guanase and cytidine deaminase activities in gastric tissues from patients with gastric cancer. 807 77

Many enzymes are involved in the biosynthesis, interconversion, and degradation of purine compounds. The exact function of these enzymes is still unknown, but they seem to play important roles other than in purine metabolism. To elucidate their functional roles, it is imperative to clarify their tissue distribution at the cellular or subcellular level. The present review summarizes the currently available information about their histochemical localization and proposed functions. In general, 5'-nucleotidase has been considered as a marker enzyme for the plasma membrane, and is considered to be a key enzyme in the generation of adenosine, a potential vasodilator. However, from its wide range of localization in tissues it is also considered to be related to the membrane movement of cells in the transitional epithelium, cellular motile response, transport process, cellular growth, synthesis of fibrous protein and calcification, lymphocyte activation, neurotransmission, and oxygen sensing mechanism. Adenosine deaminase (ADA) is present in all tissues in mammals. Although the main function of ADA is the development of the immune system in humans, it seems to be associated with the differentiation of epithelial cells and monocytes, neurotransmission, and maintenance of gestation. Purine nucleoside phosphorylase (PNP) is generally considered as a cytosolic enzyme, but recently, mitochondrial PNP, a different protein from cytosolic PNP, was reported. PNP is also widely expressed in human tissues. It is found in most tissues of the body, but the highest activity is in peripheral blood granulocyte and lymphoid tissues. It is also related to the development of T-cell immunity in humans as is ADA. Moreover, its contribution to centriole replication and/or regulation of microtubule assembly has been suggested. Immunohistochemical localization of xanthine oxidase has been reported in various tissues from various animal species. Xanthine oxidase has been suggested to be involved in the pathogenesis of post-ischemic reperfusion tissue injury through the generation of reactive oxygen species, while the extensive tissue localization of xanthine dehydrogenase/oxidase suggests several other roles for this enzyme, including a protective barrier against bacterial infection by producing either superoxide radicals or uric acid. Furthermore, an involvement in cellular proliferation and differentiation has been suggested. Urate oxidase is generally considered a liver-specific enzyme, except for bovines which possess this enzyme in the kidney. Urate oxidase is exclusively located in the peroxisomes of fish, frogs, and rats, but was lost in birds, some reptiles, and primates during evolution. A histochemical demonstration of allantoin-degrading enzymes has not been performed, but these enzymes have been located in peroxisomes by sucrose density gradient centrifugation. AMP deaminase activity is higher in skeletal muscle than in any other tissues. AMP deaminase may be involved in a number of physiological processes, such as the conversion of adenine nucleotide to inosine or guanine nucleotide, stabilizing the adenylate energy charge, and the reaction of the purine nucleotide cycle. There are three distinct isozymes (A, B, C) with different kinetic, physical, and immunological properties. Isozymes A, B, C have been isolated from muscle, liver (kidney), and heart tissue, respectively. In the muscle, AMP deaminase isozymes exist in a different part, suggesting a multiple functional role of this enzyme. High hypoxanthine-guanine phosphoribosyltransferase (HGPRT) activity is found in some regions of a normal adult human brain. However, very little is known regarding the histochemical tissue localization of HGPRT. Immunohistochemical localization of its developmental expression suggests that HGPRT may not be essential for purine nucleotide supplement in the segmentation of brain cells, but may play a significant role in the developing hippocampus.
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PMID:Enzymes involved in purine metabolism--a review of histochemical localization and functional implications. 1050 47

In order to characterize human colorectal cancer, much attention has been paid to enzyme studies. However, little is known about the correlation between the levels of key enzymes of purine nucleotide pathway and some clinical and biological indicators of tumor invasiveness and aggressiveness. Adenosine deaminase (ADA) and 5'-nucleotidase (5'-NT) were measured in cancerous and cancer-free adjacent large bowel tissues from 38 patients with colorectal carcinoma. We have analyzed the relationship between the enzyme levels and some clinical and pathological parameters. The enzymes' activities were markedly higher in primary tumors than in corresponding normal mucosae. The ADA level in tumor tissue was significantly correlated with lymph node metastasis, histologic type, tumor location, and patient's age, whereas the 5'-NT level showed a significant correlation with tumor grade and tumor location. ADA activity in tumor tissues was significantly higher in patients whose clinical course remained stable than in those with recurrent diseases. The purine metabolism and salvage pathway activity of purine nucleotides are accelerated in the cancerous human colorectal tissue. Although our findings suggest that these enzymes' activities are most likely related to the same histomorphological architecture of the tumor, the authors believe that long-term follow-up studies are needed to evaluate the prognostic value of purine enzymes for colorectal cancer.
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PMID:Activities of adenosine deaminase and 5'-nucleotidase in cancerous and noncancerous human colorectal tissues. 1111 12

The mechanism underlying beta,gamma-methylene ATP (beta,gamma-MeATP)-induced cAMP elevation was investigated in rat glioma C6Bu-1 cells. Beta,gamma-MeATP increased forskolin-stimulated cAMP formation in a manner sensitive to both the P1 antagonist xanthine amine congener (XAC) and the P2 antagonist pyridoxalphosphate-6-azophenyl-2',4'-disulfonic acid (PPADS). Adenosine deaminase (ADA; 1 U/mL), which abolished the adenosine-induced response, did not eliminate the beta,gamma-MeATP-induced response. However, combination of ADA with alpha,beta-methylene ADP (alpha,beta-MeADP), an ecto-5'-nucleotidase inhibitor, blocked the beta,gamma-MeATP-induced response. AMP, the substrate for ecto-5'-nucleotidase, also induced cAMP formation in a manner sensitive to XAC and alpha,beta-MeADP inhibition. However, the AMP-induced response was not blocked by PPADS. HPLC analyses revealed that adenosine was generated from beta,gamma-MeATP and AMP. In addition, alpha,beta-MeADP inhibited the conversion of beta,gamma-MeATP and AMP to adenosine, whereas PPADS blocked adenosine formation from beta,gamma-MeATP but not from AMP. [3H]Adenosine generated from [3H]AMP was preserved on the cell surface environment even in the presence of ADA. The mRNAs for ecto-phosphodiesterase/pyrophosphatase 1 (EC 3.1.4.1), ecto-5'-nucleotidase (EC 3.1.3.5) and adenosine A2B receptor were detected by RT-PCR. These results suggest that C6Bu-1 cells possess ecto-enzymes converting beta,gamma-MeATP to adenosine, and the locally accumulated adenosine in this mechanism efficiently stimulates A2B receptors in a manner resistant to exogenous ADA.
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PMID:Beta,gamma-methylene ATP-induced cAMP formation in C6Bu-1 cells: involvement of local metabolism and subsequent stimulation of adenosine A2B receptor. 1115 59


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