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At least 775 records · Page 43Linked to original sources
PubMed1993

Hormonal regulations of alkaline phosphatase, 5'-nucleotidase and gamma-glutamyltransferase activities in adult rat hepatocytes cultured in serum-free medium on collagen gel.

Primary hepatocytes were cultured on collagen gel in serum-free, alpha-modified Eagle's minimum essential medium containing 0.1 microM insulin, 0.1 microM dexamethasone, 10 mM pyruvate and supplements such as glucagon, epinephrine or growth hormone. The activities of alkaline phosphatase, 5'-nucleotidase and gamma-glutamyltransferase were assayed in cell extracts prepared from the cultures. All three enzyme activities were induced by glucagon, epinephrine or dibutyryl cAMP. The maximally effective concentration of glucagon was 5-10 nM for both alkaline phosphatase and 5'-nucleotidase and 100 nM for gamma-glutamyltransferase. Only alkaline phosphatase activity was suppressed by growth hormone, which caused marked suppression at about 1 microU (0.25 ng)/ml. Taurocholate also induced both alkaline phosphatase and gamma-glutamyltransferase activities at 1 mM.

5'-Nucleotidase↗
PubMed1999

Improvement by 5-amino-4-imidazole carboxamide riboside of the contractile dysfunction that follows brief periods of ischemia through increases in ecto-5-nucleotidase activity and adenosine release in canine hearts.

5-Amino-4-imidazole carboxamide (AICA) riboside increases adenosine release in ischemic myocardium, suggesting that AICA riboside improves contractile dysfunction. In 49 open-chest dogs, contractile function assessed by fractional shortening (FS) was observed 3 h after the onset of reperfusion following 15 min of occlusion of the left anterior descending coronary artery. During reperfusion, the treatment with AICA riboside increased adenosine concentration in the coronary venous blood (536+/-44 vs. 281+/-21 pmol/ml at 3 min of reperfusion, p<0.001) and peak coronary hyperemic flow (367+/-13 vs. 300+/-21 ml/100 g per min, p<0.001) when compared with the untreated group. FS at 3h of reperfusion increased in the AICA riboside group (21.1+/-2.3 vs. 12.8+/-0.6% in the untreated group, p<0.001). AICA riboside increased myocardial ecto-5'-nucleotidase activity. Administration of adenosine also augmented coronary hyperemic flow and increased FS to the levels of the AICA riboside group. Either 8-phenyltheophylline (an antagonist of adenosine receptors) or alpha,beta-methylene-adenosine 5'-diphosphate (an inhibitor of ecto-5'-nucleotidase) completely abolished the increased coronary hyperemic flow and improvements of myocardial contractile function due to AICA riboside. Thus it was concluded that AICA riboside improves the contractile dysfunction that follows a brief period of ischemia via adenosine-dependent mechanisms.

5'-Nucleotidase↗
PubMed2001

Chicken erythrocyte pyrimidine 5'-nucleotidase: purification and characterization of the subclass I enzyme.

Nucleotidase activities resembling subclass I and subclass II of human pyrimidine 5'-nucleotidases (P5N) were detected in chicken red blood cells (RBCs). In chicken RBCs from untreated controls, the activity of the subclass II enzyme was about one third of that of subclass I enzyme, whereas that ratio was approximately 5:1 in rat or human RBCs. The subclass I activity in chicken RBCs was increased 5- to 6-fold upon erythropoietic induction by phenylhydrazine administration, but the subclass II activity did not increase under these conditions. The subclass I enzyme was purified to near homogeneity. Its molecular mass was about 35 kDa as estimated by gel filtration and SDS-polyacrylamide gel electrophoresis. Its N-terminal 12 amino acids, PEFQKKTVHIKD, were also determined. The catalytic properties of the subclass I enzyme were very similar to those of the human enzyme with regard to substrate (preferential hydrolysis of CMP, dCMP, UMP), Km values, optimum pH, and metal ion requirements. Antibodies against chicken P5N subclass I were raised in rats. The chicken P5N-I as well as the rat P5N-I proteins could be detected by antibodies in Western blot analyses, but not the P5N-II proteins. These findings indicate that P5N subclass I may have an important function in chicken erythropoiesis.

5'-Nucleotidase↗
PubMed1975

Simultaneous determination of 5'-nucleotidase and alkaline phosphatase activities in serum.

A simple method is described for the simultaneous determination of alkaline phosphatase (EC 3.1.3.1) and 5'-nucleotidase (EC 3.1.3.5) in serum. The method is based on the determination of inorganic phosphorus released by the action of the two enzymes on adenosine-5'-monophosphate at pH 9.5 (200 mmol/l tris-buffer) in the presence and absence of L-cysteine. This amino acid at a concentration of 2--10 mmol/l was found to be a specific inhibitor for alkaline phosphatase but with no effect on 5'-nucleotidase activity.

Adenosine Monophosphate↗
PubMed1978

Characterization of HeLa 5'-nucleotidase: a stable plasma membrane marker.

5'-Nucleotidase, assayed as 5'-AMPase, has been extensively characterized and established as a stable, quantitative plasma membrane marker in HeLa S3 cells. The membrane 5'-AMPase has a Km of 7.0 microM. Relative affinities of the other 5'-mononucleotides for the enzyme are 5'-GMP > 5'-TMP > 5'-UMP > 5'-CMP. There are activity optima at pH7 and 10; the latter is Mg(2+)-dependent. The membrane preparations have a small amount of acid phosphatase activity that is distinct from 5'-AMPase activity but no alkaline phosphatase. AOPCP, ADP, and ATP are strongly inhibitory. Mg2+, Ca2+, or Co2+ additions do not affect the pH 7.0 activity; Mn2+ activates slightly, whereas Zn2+, Cu2+, and Ni2+ are inhibitory. EDTA slowly inactivates, but removal of the EDTA without the addition of divalent cations restores activity. The inactivation is also substantially reversed by Co2+ or Mn2+, but reactivability by divalent cations decreases with time in EDTA. ConA strongly inhibits, and alpha-methyl-D-mannoside or glucose (the latter much less efficiently) relieves the inhibition, indicating that the 5'-AMPase is a glycoprotein. Histidine is also inhibitory. Ouabain, phloretin, cytochalasin B, cysteine, phenyl-alanine, MalNEt, and IAA are without effect. 5'-AMPase activity codistributes with pulse-bound [3H]ouabain when either of two cell fractionation procedures are used. The 5'-AMPase activity per cell is constant at different cell densities in exponentially growing cells, and activity per unit cell volume remains constant throughout the cell cycle. These properties, together with its absence in other organelles, its stability to storage, its insensitivity to certain experimental manipulations, and its general insensitivity to inhibitors of specific transport systems, make 5'-AMPase a useful quantitative marker in studies on the regulation of HeLa membrane transport systems. Key Words: HeLa, 5'-nucleotidase, plasma membrane marker, non-specific phosphatases, divalent ions, ConA, AOPCP, cell cycle, mitochondria, transport inhibitors.

5'-Nucleotidase↗
PubMed1985

A new 5'-nucleotidase inhibitor, nucleoticidin. I. Taxonomy, fermentation, isolation and biological properties.

A new 5'-nucleotidase inhibitor named nucleoticidin was produced by Pseudomonas sp. YM-3229G. It was isolated from a fermentation broth by trichloroacetic acid extraction, ethanol precipitation and Dowex 1 and DEAE-52 column chromatography. It inhibited 5'-nucleotidase activity of snake venom and rat liver membrane. It also showed antitumor activity against solid type Sarcoma 180.

Animals↗
PubMed1976

[Two forms of alkaline phosphatase and 5'-nucleotidase in the serum of persons with jaundice of different origin].

Distribution of the alkaline phosphatase and 5'-nucleotidase activity was studied in blood serum by means of gel filtration through Sephadex G-200 with jaundices of different origin. Both enzymes have two forms differing in the molecular weight, 5'-nucleotidase presenting mainly a high-molecular form in contrast to alkaline phosphatase. This form activity for both enzymes is higher with obturative jaundices as compared to liver cirrhosis and virus hepatitis. The results of incubating sera with desoxicholate and the subsequent gel filtration in its presence, as well as polyacrylamide gel electrophoresis of butanol extracts of the fractions containing high-molecular fragments, evidence for the fact that these fragments are lipoproteid complexes.

Alkaline Phosphatase↗
PubMed1998

Effects of dietary polyunsaturated fatty acids on adenylate cyclase, 5'nucleotidase and Na+K(+)-ATPase activities in rat brain-plasma membrane.

The incidence of polyunsaturated fatty acids (PUFA) in human nutrition is now generally accepted. As essential membrane components, PUFA may act as enzyme activity modulators. In this study, four different diets, in which PUFA type was the only modifying factor, were evaluated on 5'nucleotidase, adenylate cyclase and Na+/K+ATPase activities in rat brain plasma membranes. Animals fed the total PUFA deficient diet exhibited significant lower body weight and lower brain weight than did the control group. The specific activities of 5'nucleotidase and Na+/K+ATPase in brain plasma membrane were slightly modified by dietary PUFA. The catalytic unit of adenylate cyclase in total PUFA deficient animals presented augmented enzyme activity and animals receiving diets deficient in n-6 PUFA showed reduced activity in relation to the control animals. Our results showed that the epinephrine receptors, in the case of adenylate cyclase are not modified by dietary PUFA, but rather the catalytic unit seems to be altered by dietary PUFA. These results can be partially explained by the fluidity that PUFA confers to membranes facilitating the proximity of enzyme-substrate. The physiological consequences of dietary PUFA incidence on enzyme activity needs further study.

5'-Nucleotidase↗
PubMed2000

Contribution of ecto-5'-nucleotidase to the inhibition of platelet aggregation by human endothelial cells.

We studied the role of adenosine (Ado), which is generated from adenine nucleotides via the activity of ecto-5'-nucleotidase (ecto-5'-NT), in the inhibition of platelet aggregation by endothelial cells (ECs). The enzymatic activity of nucleotidases on human umbilical vein endothelial cells (HUVECs) was examined with regard to (1) the inhibition of adenosine diphosphate (ADP)-induced platelet aggregation and (2) the liberation of inorganic phosphate from adenine nucleotides. Adenosine 5'-monophosphate (AMP) preincubated with HUVECs significantly inhibited ADP-induced platelet aggregation. This was completely blocked by the treatment of HUVECs with a specific inhibitor of ecto-5'-NT, 5'-[alphabeta-methylene] diphosphate (APCP), or by the addition of an A(2a) receptor antagonist. Neither nitric oxide nor prostacyclin was involved in this inhibitory activity, suggesting that Ado generated in the incubation medium by the activity of 5'-NT on HUVECs inhibited platelet aggregation. When ADP was incubated on HUVECs, it lost most of its agonistic activity for platelets. Pretreatment of HUVECs with APCP at a concentration that abolished ecto-5'-NT activity partially restored ADP-induced platelet aggregation. Ecto-5'-NT contributes to EC function by inhibiting platelet aggregation in cooperation with ATP diphosphohydrolase, which degrades ADP to AMP.

5'-Nucleotidase↗
PubMed2001

Histamine increases interstitial adenosine concentration via activation of ecto-5'-nucleotidase in rat hearts in vivo.

We examined whether histamine enhances the production of interstitial adenosine via stimulation of ecto-5'-nucleotidase (a key enzyme responsible for adenosine production) using microdialysis techniques in in situ rat hearts. The microdialysis probe was implanted in the left ventricular myocardium of anesthetized rats and perfused in the presence of adenosine 5'-monophosphate (AMP). Histamine (10-500 microM) administered into the perfusate had a tendency to increase the adenosine concentration. In the presence of prazosin (50 microM), an antagonist of alpha1-adrenoceptors, or of chelerythrine (10 microM), a protein kinase C (PKC) inhibitor, and in reserpinized rats, histamine failed to increase the AMP-primed dialysate adenosine concentration. Accumulation of norepinephrine in the extracellular fluid elicited by pargyline (100 microM), a monoamine oxidase inhibitor, significantly increased histamine-induced adenosine production. Okadaic acid (50 microM), an inhibitor of protein phosphatase, enhanced the histamine-induced increase in adenosine concentration. Norepinephrine is known to activate alpha1-adrenoceptors and PKC. Taken together, the results demonstrate that histamine-released norepinephrine activates both alpha1-adrenoceptors and PKC, which increased ecto-5'-nucleotidase activity and augmented release of adenosine in rat hearts.

5'-Nucleotidase↗
PubMed1975

Function of 5'-nucleotidase in the uptake of adenosine from AMP by human lymphocytes.

The function of 5'-nucleotidase in nucleoside uptake from AMP was investigated in human lymphocytes by comparing the transport in cells containing this enzyme (5'N+) with that in cells deficient in the activity (5'N-). The rate of adenosine and Pi uptake from AMP was 3.9-fold greater in the 5'N+ then in the 5'N- lymphocytes. There was no difference in transport between these cells when incubated with adenosine or Pi. These results indicate that phosphorylytic cleavage of AMP by 5'-nucleotidase is necessary for the uptake of the nucleotide and Pi moieties by the human lymphocyte.

Adenosine↗
PubMed1992

[The effect of dalargin on stress-induced changes in the 5'-nucleotidase activity of the macrophages and in the level of endogenous blood cortisol in mice].

The action of dalargin, synthetic analogue of leuenkephaline, on stress-induced changes in 5'-nucleotidase activity and endogenous hydrocortisone levels was investigated in mice. It was found that there is a direct relation between the activity of 5'-nucleotidase and the level of hydrocortisone in CBA mice. For C57Bl/6 mice the relation was inverse. Dalargin is able to change the dependence from direct to opposite in CBA mice.

5'-Nucleotidase↗
PubMedDate not supplied

[Clinical significance of 5'-nucleotidase].

The paper deals with the current data of molecular organization, localization, activity and clinical significance of 5'-nucleotidase in the diagnosis of different illnesses. The paper also deals with the specificity and sensitivity of 5'-nucleotidase comparing to other laboratory tests.

5'-Nucleotidase↗
PubMed1978

Histochemical studies on the distribution of adenosine triphosphatase and 5'-nucleotidase amongst the constituents of the thoracic ganglia and the associated nerve of Periplaneta americana.

The present study deals with the distribution of adenosine triphosphatase and 5'-nucleotidase in the various constituents of thoracic ganglia and associated nerve of Periplaneta americana. The localization of both the enzymes in the thoracic ganglia is identical. The neural lamella is devoid of any activity for both the enzymes. The ganglion cells are intensely positive at their borders. The neuronal cell surface and/or glial cell processes which envelope the neurons show intense activity for these enzymes. Adenosine triphosphatase and 5'-nucleotidase are present around "giant fibres" and small axons. The activity appears to confine itself in the sheaths. The cytoplasm and the nuclei of the neurons are devoid of enzymatic activity, whereas the nucleoli are slightly active. The nerves are positive for both the enzymes. The role of these enzymes at different sites has also been discussed.

Adenosine Triphosphatases↗
PubMed1976

[Adrenaline-induced release from thrombocytes of beta-lipoprotein, alkaline phosphatase and 5'-nucleotidase].

Platelet aggregation induced by adrenaline is accompanied by release of beta-lipoprotein, alkaline phosphatase, 5'-nucleotidase and factor 3. Electrophoretic mobility of platelet alkaline phosphatase was the same as that of beta-lipoprotein. This suggest that beta-lipoprotein, alkaline phosphatase and 5'-nucleotidase are structural components of platelet compounds which possess factor 3 activity.

Alkaline Phosphatase↗
PubMed1991

Influence of membrane fluidity of 5'-nucleotidase activity in isolated hepatocyte plasma membrane.

The influence of membrane microviscosity on 5'-nucleotidase activity has been investigated on liver plasma membrane preparations from rats during aging and following diet restriction. In addition the microviscosity of membranes from old rats was changed in vitro by the Active Lipids. During aging the membrane microviscosity increased progressively and in parallel the activity of 5'-nucleotidase decreased. Diet restriction was able to slow down the modification of both parameters. The experiment performed with the Active Lipids further supports that membrane microviscosity modulated the enzyme activity.

5'-Nucleotidase↗
PubMed1990

A 3'-deoxyribonucleotidase isolated from rabbit spleen cytosol differs from the rat spleen nucleotidase.

A novel 3'-nucleotidase, which preferably hydrolyzed 3'-dTMP and 3'-dUMP, was isolated and purified from rabbit spleen cytosol. Since the main catalytic properties of the enzyme were similar to the rat liver nucleotidase reported by Fritzson and Smith, we also purified the latter enzyme from rat spleen. These two enzymes were different in several points: the substrate restriction, the molecular mass and the apparent charge. Further analyses with the antiserum raised in rat against the 3'-deoxyribonucleotidase evidenced that these enzymes were immunochemically different as well.

Animals↗
PubMed1990

5'-Nucleotidase from bull seminal plasma. Biochemical and biophysical aspects.

In bull seminal plasma 5'-nucleotidase is present in heterogeneous forms. The heterogeneity is abolished by treatment of bull seminal plasma with the detergent sodium cholate. The purified enzyme, which is a glycoprotein, shows an apparent molecular mass of 160 kDa on gel filtration in the presence of 50 mmol sodium cholate and an apparent molecular mass of 72 kDa upon SDS/polyacrylamide-gel electrophoresis. The 5'-nucleotidase of bull seminal plasma is a metalloprotein containing 2 zinc ions per molecule of dimeric protein. The removal of the two zinc ions from the protein results in a completely inactive apoenzyme. The substitution of the endogenous zinc with Co(II) Cu(II) produces a holoenzyme which is slightly activated in the case of Co(II), whereas, in the case of Cu(II) only 65% of the initial activity is recovered. The enzyme has a covalently attached glycosyl-phosphatidylinositol moiety which can be removed by treatment with phosphatidylinositol-specific phospholipase C. ESR studies have indicated a radius of 35 A for the protein and that Cu(II) binds to the metal-free enzyme to a site in which sulphur donors can be excluded.

5'-Nucleotidase↗