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 human promyelocytic leukemia cell line HL-60 undergoes terminal myeloid differentiation in vitro in response to a wide variety of chemicals. The tumor promoter phorbol myristate acetate induces these cells to develop macrophage-like morphology, adherence, and enzymatic characteristics. The present study confirms those observations and further documents the induction, by 16 nM phorbol myristate acetate, of 5'-nucleotidase activity, another human macrophage marker enzyme. However, more importantly, functional studies show that phorbol myristate acetate-induced HL-60 cells fail to increase above base line uninduced levels of hexose monophosphate shunt activity, superoxide generation, nitroblue tetrazolium reduction, bacterial ingestion, or complement secretion. These cells therefore possess some macrophage-like properties but do not meet several important functional criteria of macrophage identity.
Cancer Res 1981 May
PMID:Functionally deficient differentiation of HL-60 promyelocytic leukemia cells induced by phorbol myristate acetate. 626 Mar 53

Activities of enzymes of the purine metabolic pathway, adenosine deaminase (ADA), purine nucleoside phosphorylase (PNP), and 5'-nucleotidase (5'-N), were investigated in the lymphoblasts of a patient with B-cell acute lymphoblastic leukemia. These lymphoblasts exhibited increased ADA activity and diminished activities of both PNP and 5'N' as compared to normal lymphocytes as well as non-T, non-B leukemia cells. This enzymatic pattern is identical to that which has been described in T-cell leukemic lymphoblasts and differs from that which has been observed in the malignant cells of undifferentiated B-cell lymphomas. These data suggest that there is biochemical heterogeneity within the spectrum of B-cell malignancies. Furthermore, inhibitors of ADA may be of use in those B-cell lymphoid neoplasms that exhibit increased ADA activity.
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PMID:Lymphoblast purine pathway enzymes in B-cell acute lymphoblastic leukemia. 626 97

A plasma membrane ectoenzyme in mammalian cells, 5'-nucleotidase, was evaluated as a marker for ovarian carcinoma. Activities of this enzyme were determined in homogenates from normal (N = 17) and malignant ovaries (N = 17), as well as in the sera from control women (N = 35), ovarian cancer patients with active disease (N = 24), and those in clinical remission (N = 9). A significant reduction of the activity of 5'-nucleotidase was observed in tumor homogenates compared with homogenates from normal ovaries. Levels of this enzyme in the sera of ovarian cancer patients were higher than in control women, suggesting the possibility of shedding of this enzyme from the tumor cell surface to the systemic circulation of the host. The diagnostic value of serum 5'-necleotidase levels was compared with another enzyme marker for ovarian carcinoma, viz. serum glycoprotein:galactosyltransferase. The upper limit of normal was set at 2 SD higher than the normal mean. Elevation of serum 5'-nucleotidase was observed in 12/24 (50%) patients with active disease, and 1/9 (11%) patients with clinical remission. In contrast, serum glycoprotein:galactosyltransferase was elevated in all the serum samples from patients with active disease and in none of those with clinical remission. There was some correlation between the serum levels of 5'-nucleotidase and those of glycoprotein:galactosyltransferase (0.01 less than P less than 0.05). Elevation of 5'-nucleotidase in the serum of these patients was not due to liver metastasis. Serum 5'-nucleotidase levels seem to correlate with disease status in some ovarian carcinoma patients, but in general it is inferior to serum glycoprotein:galactosyltransferase as a tumor marker.
Cancer 1981 Jun 01
PMID:Evaluation of 5'-nucleotidase as an enzyme marker in ovarian carcinoma. 626 38

The status of three purine pathway enzymes, adenosine deaminase, 5'-nucleotidase, and purine nucleoside phosphorylase, was evaluated in the leukemic cells of patients with acute lymphoblastic leukemia and correlated with routine immunological cell surface markers. A distinct pattern of enzyme activity was noted in T-lymphoblasts which have significantly higher adenosine deaminase activity (p less than 0.02) and lower 5'-nucleotidase (p less than 0.001) and purine nucleoside phosphorylase (p less than 0.01) activities than do non-T, non-B lymphoblasts. This enzyme pattern is similar to that observed in normal human thymocytes but is not shared by the mature, normal T-lymphocytes of peripheral blood, suggesting that it may reflect the differentiation status of malignant T-lymphoblasts. These findings, which confirm the biochemical heterogeneity of acute lymphoblastic leukemia, may provide an avenue for selective chemotherapy of this disease.
Cancer Res 1981 Nov
PMID:Purine pathway enzyme abnormalities in acute lymphoblastic leukemia. 627 95

The activities of three purine pathway enzymes--adenosine deaminase (ADA), 5'-nucleotidase (5'N) and purine nucleoside phosphorylase (PNP)--were examined in the circulating malignant cells (Sezary cells) of eight patients with cutaneous T-cell lymphoma (CTCL). Cell lines derived from two other patients with CTCL were also studied. These were compared with enzyme activities in peripheral blood T-lymphocytes from 11 normal donors and six samples of human thymocytes. ADA activities were similar in the Sezary cells and peripheral blood T-cells (medians 7 U and 15 U, P = 0.14), and both of these groups demonstrated significantly lower activity than did the thymocytes (median 100 U, P = 0.002). 5'N activity in the Sezary cells was also similar to that of the T-lymphocytes (median 0.022 U and 0.030 U, P greater than 0.05) and both of these groups had significantly greater activity than did the thymocytes (median 0.002 U, P = 0.001). Median PNP activity in the Sezary cell population was also comparable to that measured in normal T-cells. These findings suggest there is a characteristic purine pathway enzyme pattern in Sezary cells that is similar to that seen in normal T-lymphocytes. This pattern is clearly distinguishable from that of thymocytes and from that previously described in lymphoblasts from patients with T-cell acute lymphoblastic leukaemia. These results support the concept that Sezary cells are well-differentiated with respect to the T-cell axis. Quantitation of purine pathway enzymes may be useful in defining subsets of T-cell malignancy.
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PMID:Purine pathway enzymes in the circulating malignant cells of patients with cutaneous T-cell lymphoma. 628 63

The kinetic properties of a soluble, magnesium-dependent 5'-nucleotidase from human malignant lymphocytes have been determined. The partially purified enzyme is distinct from plasma membrane-associated 5'-nucleotidase and is free of nonspecific phosphatase activity. Among purine ribonucleotides, it reacted efficiently with inosine 5'-monophosphate and guanosine 5 -monophosphate and to a lesser degree with deoxyguanosine 5'-monophosphate. Adenosine 5'-monophosphate and deoxyadenosine 5'-monophosphate were 30-fold less efficient substrates. Increasing concentrations of adenosine 5'-triphosphate and deoxyadenosine 5'-triphosphate from 0 to 3 mM enhanced 5'-nucleotidase activity up to 7-fold. Guanosine 5'-triphosphate and deoxyguanosine 5'-triphosphate were much less effective enzyme activators, while uridine 5'-triphosphate was without effect. Inorganic phosphate inhibited dephosphorylating activity in both adenosine 5'-triphosphate-supplemented and unsupplemented buffer. The activation of this 5'-nucleotidase by deoxyadenosine 5'-triphosphate, combined with the relative inability of the enzyme to dephosphorylate deoxyadenosine 5'-monophosphate, conceivably may contribute to the adenine nucleotide degradation induced by deoxyadenosine in normal and malignant lymphocytes.
Cancer Res 1982 Nov
PMID:Characterization of an adenosine 5'-triphosphate- and deoxyadenosine 5'-triphosphate-activated nucleotidase from human malignant lymphocytes. 629 30

Female Swiss mice were fed on a control diet (laboratory chow, 6% fat) or high fat diets (laboratory chow with added fat, principally corn oil, to produce a fat content of 16% or 23%). Homogenate of colon mucosa was fractionated by isopycnic banding on a linear sucrose gradient and the distribution of 5'-nucleotidase determined. Two main peaks were detected which we interpret as belonging to basolateral plasma membrane (BLPM) and brush borders. A high fat diet did not affect the relative sizes of the peaks or the median density of the BLPM peak but did significantly reduce the density of the brush border peak from 1.208 g/ml to 1.197 g/ml.
Cancer Lett 1983 Dec
PMID:High fat diets and mouse colon mucosal membranes: a centrifugation study. 631 66

In one experiment Swiss mice were maintained on a 16 or 23% fat diet (laboratory chow with added fat, principally corn oil) or on laboratory chow alone (5.5% fat). In another experiment C57BL/1 mice were given a 23% fat diet (as above) or a low-fat diet (67% laboratory chow, 1.9% corn oil, and 31% starch; 5.5% fat). Colon mucosal samples were analyzed for several enzyme activities. In Swiss mice the analyses revealed the following: 1) Ouabain-insensitive ATPase was unaltered in male mice, but it rose significantly in females fed a high-fat diet (this effect was seen when a resuspended high-speed pellet was analyzed but not seen with the initial homogenate); 2) 5'-nucleotidase activity showed a significant stepwise increase with dietary fat; 3) nonspecific esterase activity tended to rise with a high-fat diet (not significant); 4) beta-glucuronidase levels were not altered by diet fat; and 5) ornithine decarboxylase levels were not altered by diet fat. In C57BL/1 mice analyses were done on ouabain-insensitive ATPase, 5'-nucleotidase, nonspecific esterase, and beta-glucuronidase, but no diet effects were seen. Fecal reductase activity was measured with the use of 2-(p-iodophenyl)-3-(p-nitrophenyl)-5-phenyltetrazolium chloride hydrate). A high-fat diet did not affect the activity in C57BL/1 mice, but it caused a significant rise in Swiss mice.
J Natl Cancer Inst 1984 Mar
PMID:High-fat diets and fecal level of reductase and colon mucosal level of ornithine decarboxylase, beta-glucuronidase, 5'-nucleotidase, ATPase, and esterase in mice. 632 44

5'-nucleotidase activity, arachidonate metabolism and adenosine uptake were measured in P388 murine leukaemia cells and in a subline resistant to doxorubicin. These membranes related activities were found to be increased in the doxorubicin resistant cell line, compared to the drug sensitive cells. It is suggested that these differences do not play a role in the mechanism of resistance to doxorubicin. Rather they reflect alterations in plasma membrane composition and structure between these cell lines. This study also suggests that the use of decreased 5'-nucleotidase activity as a marker of certain leukaemias should be reviewed with caution. An increase in cell enzyme activity in treated patients may not necessarily indicate a shift toward normal behaviour of these cells, but rather a selection of certain cell subpopulations.
Br J Cancer 1984 Apr
PMID:5'-Nucleotidase activity and arachidonate metabolism in doxorubicin sensitive and resistant P388 cells. 632 40

The ribonucleotide content of lymphocytes obtained from normal subjects and patients with chronic lymphocytic leukemia (CLL) was determined by means of high-performance liquid chromatography. The levels of normal B- and T-cells were compared to each other as well as those of their CLL counterparts. Unfractionated CLL lymphocytes, predominantly B-cells, had significantly lower levels of adenosine-5'-triphosphate, cytidine-5'-triphosphate, uridine-5'-triphosphate, cytidine-5'-diphosphate, and guanosine-5'-phosphate, while the concentration of nicotinamide-adenine dinucleotide was significantly higher than in normal unfractionated lymphocytes which consisted mainly of T-cells. For enriched populations: (a) CLL B-cells had much lower adenosine-5'-triphosphate (3439 versus 5689) (pmol/1 X 10(7) cells), cytidine-5'-triphosphate (107 versus 313), guanosine-5'-triphosphate (462 versus 978), and uridine-5'-triphosphate (633 versus 1214) than normal B-cells; (b) CLL T-enriched subpopulations had significantly lower ribonucleoside triphosphates, adenosine-5'-triphosphate (3217 versus 5468), cytidine-5'-triphosphate (119 versus 209), guanosine-5'-triphosphate (422 versus 826), and uridine-5'-triphosphate (504 versus 969) than normal T-cells. The lower ribonucleoside triphosphate levels found in unfractionated CLL lymphocytes, therefore, are the result of differences between the CLL and normal B-cells as well as between CLL and normal T-cells. These findings establish a framework for studying the reasons underlying the decreased ribonucleoside triphosphate levels in unfractionated CLL lymphocytes. T-helper and T-suppressor lymphocytes showed similar ribonucleotide patterns. Nucleoside and base levels were significantly higher in normal monocytes than in normal lymphocytes. The only compound found to be increased in the CLL B-lymphocytes when compared to their normal counterparts was nicotinamide-adenine dinucleotide. The level in CLL lymphocytes was 404 versus 209 pmol/10(7) cells for normal B-lymphocytes. No correlation was found between any ribonucleotide levels and the expression of 5'-nucleotidase activity.
Cancer Res 1983 Nov
PMID:Ribonucleotide content of mononuclear cells from normal subjects and patients with chronic lymphocytic leukemia: increased nicotinamide adenine dinucleotide concentration in chronic lymphocytic leukemia lymphocytes. 660 77


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