Relevant bibliographies by topics / 5'-nucleotidase

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Academic literature on the topic '5'-nucleotidase'

Author: Grafiati
Published: 4 June 2021
Last updated: 20 February 2023

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Journal articles on the topic "5'-nucleotidase"

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Olsson, Ray A. "CardiovascularEcto-5′-Nucleotidase." Circulation Research 95, no. 8 (October 15, 2004): 752–53. http://dx.doi.org/10.1161/01.res.0000146278.94064.4b.

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Rees, David C., John A. Duley, and Anthony M. Marinaki. "Pyrimidine 5′ Nucleotidase Deficiency." British Journal of Haematology 120, no. 3 (February 2003): 375–83. http://dx.doi.org/10.1046/j.1365-2141.2003.03980.x.

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Itoh, Roichi. "IMP-GMP 5′-nucleotidase." Comparative Biochemistry and Physiology Part B: Comparative Biochemistry 105, no. 1 (May 1993): 13–19. http://dx.doi.org/10.1016/0305-0491(93)90163-y.

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Piec, G., and M. Le Hir. "The soluble ‘low-Km’ 5′-nucleotidase of rat kidney represents solubilized ecto-5′-nucleotidase." Biochemical Journal 273, no. 2 (January 15, 1991): 409–13. http://dx.doi.org/10.1042/bj2730409.

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A soluble ‘low-Km’ 5′-nucleotidase has been described previously in several organs. It has been presumed to be of cytosolic origin and thus to play a role in the intracellular production of adenosine. Its catalytic properties are similar to those of the ecto-5′-nucleotidase of cell membranes. In the present study we compared molecular properties of the two enzymes in the kidney of the rat. The Mr of the main peak of soluble ‘low-Km‘ 5′-nucleotidase in gel-filtration chromatography was similar to that of the ecto-5′-nucleotidase solubilized by a phosphatidylinositol-specific phospholipase C from renal brush-border membranes. In phase-partition experiments using Triton X-114, the soluble enzyme appeared to be hydrophobic. Its hydrophobicity was decreased on treatment with a phosphatidylinositol-specific phospholipase C, suggesting that the soluble ‘low-Km’ 5′-nucleotidase contains the phosphatidylinositol anchor which is characteristic for the ecto-enzyme. An anti-ecto-5′-nucleotidase antiserum provoked an almost complete inhibition of the soluble enzyme. Immunoblotting using anti-ecto-5′-nucleotidase antiserum revealed in the high-speed supernatants a polypeptide with a similar Mr to the subunit of the ecto-5′-nucleotidase. The soluble ‘low-Km’ 5′-nucleotidase, like the ecto-5′-nucleotidase, bound specifically to concanavalin A. We conclude that the soluble ‘low-Km’ 5′-nucleotidase is not a cytosolic enzyme, but that it most probably originates from the solubilization of the ecto-5′-nucleotidase, and that it therefore cannot participate in the intracellular production of adenosine.
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Darvish, A., R. W. Pomerantz, P. G. Zografides, and P. J. Metting. "Contribution of cytosolic and membrane-bound 5'-nucleotidases to cardiac adenosine production." American Journal of Physiology-Heart and Circulatory Physiology 271, no. 5 (November 1, 1996): H2162—H2167. http://dx.doi.org/10.1152/ajpheart.1996.271.5.h2162.

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The purpose of this study was to evaluate the relative contributions of AMP-specific cytosolic 5'-nucleotidase and ecto-5'-nucleotidase to cardiac adenosine production and its regulation by ADP and Mg2+. 5'-Nucleotidase activity was measured spectrophotometrically in the total homogenate, the 150,000-g supernatant fraction (cytosolic 5'-nucleotidase), and the membrane pellet fraction (ecto-5'-nucleotidase) of dog left ventricles. Increasing [MgCl2] over a range from 0 to 6 mmol/l increased 5'-nucleotidase activity in both the supernatant and pellet; only cytosolic 5'-nucleotidase exhibited an absolute requirement for Mg2+. ADP, (20-480 mumol/l) activated supernatant and inhibited membrane-bound 5'-nucleotidase activity. At 80 mumol/l ADP, 5 mmol/l MgCl2, 100 mumol/l AMP, and pH 7.3, the average 5'-nucleotidase activities of the supernatant vs. pellet were 74% of total and 26% of total, respectively. Total adenosine production in unfractionated samples of ventricular homogenates decreased an average of 73% by specific inhibition of cytosolic 5'-nucleotidase, using antibodies against the cytosolic enzyme, and 46% by specific inhibition of ecto-5'-nucleotidase with alpha, beta-methylene adenosine 5'-diphosphate (AOPCP). These findings support the hypotheses that 1) both cytosolic and ecto-5'-nucleotidase contribute to cardiac adenosine production in dog heart homogenates; 2) AMP-specific cytosolic 5'-nucleotidase activity exceeds ecto-5'-nucleotidase activity at physiological concentrations of ADP, AMP, and Mg2+; and 3) Mg2+ is an important regulator of cardiac adenosine production via activation of both ecto- and AMP-specific cytosolic 5'-nucleotidases.
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Panteghini, M. "Electrophoretic fractionation of 5'-nucleotidase." Clinical Chemistry 40, no. 2 (February 1, 1994): 190–96. http://dx.doi.org/10.1093/clinchem/40.2.190.

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Abstract Human isonucleotidases were separated by electrophoresis on a cellulose acetate membrane. Three 5'-nucleotidase forms, NTP1, NTP2, and NTP3, were resolved with this method and quantified by densitometry. The procedure was not only simple and rapid but also sufficiently precise (between-run CV < 20%) and sensitive (detected nucleotidase fractions of > 0.5 U/L). The effects of various treatments (heat, neuraminidase, glycosidases, proteases, lectins, and detergents) on the electrophoretic pattern of 5'-nucleotidase were studied. NTP1 (mean 12% of total 5'-nucleotidase, SD 5%), NTP2 (mean 30%, SD 8%), and NTP3 (mean 58%, SD 8%) were found in all normal persons studied. The increase in total 5'-nucleotidase in patients with hepatobiliary disease was mainly due to the NTP1 isoform.
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Özsoylu, Şinasi. "About Pyrimidine 5’-Nucleotidase Deficiency." Turkish Journal of Hematology 30, no. 2 (June 5, 2013): 227. http://dx.doi.org/10.4274/tjh.2013.0050.

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Hansen, Thor Willy Ruud, Martin Seip, Carl-Henric Verdier, and ÅKe Ericson. "Erythrocyte Pyrimidine 5‘-Nucleotidase Deficiency." Scandinavian Journal of Haematology 31, no. 2 (April 24, 2009): 122–28. http://dx.doi.org/10.1111/j.1600-0609.1983.tb01518.x.

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Ramaswamy, S. G., and W. B. Jakoby. "(2')3',5'-Bisphosphate nucleotidase." Journal of Biological Chemistry 262, no. 21 (July 1987): 10044–47. http://dx.doi.org/10.1016/s0021-9258(18)61072-5.

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Colaco, Camilo A. L. S. "Potocytosis, 5′-nucleotidase and transport." Trends in Cell Biology 2, no. 8 (August 1992): 223. http://dx.doi.org/10.1016/0962-8924(92)90299-3.

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Dissertations / Theses on the topic "5'-nucleotidase"

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SIEGFRIED, GERALDINE. "Modulation de l'activite 5'-nucleotidase tubulaire renale." Paris 7, 1996. http://www.theses.fr/1996PA077134.

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Dans le rein, la 5'-nucleotidase est principalement localisee au niveau de la bordure en brosse apicale des cellules tubulaires proximales. Elle est ancree dans le feuillet membranaire externe par un glycosyl-phosphatidyl-inositol. Elle est l'enzyme cle d'une cascade faisant intervenir diverses ectoenzymes conduisant a la formation d'adenosine par l'hydrolyse des nucleotides adenyliques (atp, adp, et ampc). La degradation de l'ampc extracellulaire luminal suivie de la capture d'adenosine sont indispensables a l'effet inhibiteur de l'ampc extracellulaire sur la reabsorption proximale de phosphate. L'ampc luminal ajoute au fluide tubulaire sous l'influence de la pth (ampc nephrogenique) participe a son effet phosphaturique et n'est pas seulement un marqueur de l'activite de cette hormone. La 5'-nucleotidase, en hydrolysant l'amp ou en produisant de l'adenosine, est a la base de ces regulations physiologiques. Cette etude presente differents aspects de la modulation de l'activite de l'ecto-5'-nucleotidase tubulaire renale, et les consequences de cette modulation de l'activite du cotransport sodium-phosphate: (1) dans les cellules ok, la pth stimule l'activite 5'-nt en impliquant une synthese proteique et l'activation de la pkc. Cette modulation se traduit de maniere fonctionnelle en termes de modulation de transport de phosphate. La 5'-nt participe ainsi a l'effet phosphaturique de la pth. (2) le monoxyde d'azote produit au cours d'une ischemie renale transitoire inhibe l'activite 5'-nt en se liant a ses groupements sh par un mecanisme de s-nitrosylation. Cette inhibition attenue l'effet inhibiteur de l'ampc extracellulaire sur le cotransport sodium-phosphate. L'expression, par infection stable, de l'ecto-5'-nt humaine dans les cellules mxx depourvues d'activite ecto5'-nt endogene permet d'etablir une lignee de cellules renales. L'enzyme est distribuee majoritairement au niveau de la membrane apicale des cellules. Son activite n'affecte ni l'activite du transport de phosphate ni son adaptation a la depletion phosphatee
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Roever, Lisa. "Inhibitor Studies for 5’-ecto-nucleotidase (CD73)." Ohio University / OhioLINK, 2019. http://rave.ohiolink.edu/etdc/view?acc_num=ohiou1553892946798977.

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Zanin, Rafael Fernandes. "Investigação das ectonucleotidases na diferenciação de macrófagos e na ativação de plaquetas : o papel da homocisteína." reponame:Biblioteca Digital de Teses e Dissertações da UFRGS, 2010. http://hdl.handle.net/10183/61004.

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Os nucleotídeos extracelulares modulam uma variedade de ações biológicas via ativação de receptores purinérgicos. Esses efeitos são controlados pela ação de ectonucleotidases, tais como as E-NTPDases e a ecto-5´-NT/CD73, as quais hidrolisam o ATP até adenosina no meio extracelular. Nas células imunes, o ATP pode atuar como uma molécula sinalizadora de perigo enquanto a adenosina, um produto da degradação do ATP, serve como um mecanismo que controla/limita a inflamação. Já, no sistema vascular, o ADP é um agonista fisiológico envolvido na hemostasia normal e na trombose. Considerando que os macrófagos são elementos chave para processos inflamatórios e quando estímulados exibibem um fenótipo pró-inflamatório/defesa (clássico/M1) ou antiinflamatório/reparatório (alterantivo/M2). O objetivo foi investigar a atividade e expressão das ectonuclotidases em diferentes fenótipos de macrófago e avaliar o efeito da homocisteína sobre essas enzimas em macrófagos e plaquetas.. As análises da diferenciação de macrófagos em fenótipo próinflamatório/ M1 e antiinflamatório/M2 revelaram presença igual de receptores purinérgicos. Entretanto, mudança no perfil das ectonucleotidases como E-NTPDase1, E-NTPDase3 e ecto-5’- nucleotidase foram encontradas, sugerindo que os macrófagos devem alterar a casacata purinérgica durante a ativação fenotípica. No fenótipo pró-inflamatório/M1 houve uma diminuição na hidrólise de ATP, sugerindo um acúmulo do mesmo, enquanto no fenótipo antiinflamatório/M2 as enzimas conduzem para uma progressiva diminuição nas concentrações de nucleotídeos (ATP) e aumento na disponibilidade de adenosina. Já os macrófagos expostos a homocisteína apresentaram uma polarização para o fenótipo pro-inflamatório (M1) e nossos achados sugerem o envolvimento da ENTPDase3 e da ecto-5’-nucleotidase em macrófagos nas complicações inflamatórias associadas a homocisteína. Nas plaquetas, as quais são elementos fundamentais no processo de trombogênese, a homocisteína causou uma diminuição na hifrólise de ADP. Essa elevação no nível de ADP ao redor das plaquetas devido a inativação das ectonucleotidases, causada pela homocisteína, deve estar contribuindo para o aumento do risco trombótico descrito em pacientes com hiperhomocisteinemia. Além disso, os animais que receberam homocisteína tiveram um aumento na agregação plaquetária induzida por ADP. Em conclusão, os resultados do presente estudo reforçam o envolvimento do sistema purinérgico em processos inflamatórios/trombóticos e apontam parar o desenvolvimeto de tratamentos para doenças inflamatórias/trobóticas.
Extracellular nucleotides modulate a variety of biological actions via purinergic receptor activation. These effects are modulated by ectonucleotidases, such as ENTPDases and ecto-5´- NT/CD73, which hydrolyze ATP to adenosine in the extracellular milieu. In the cells of the immune system, the ATP can act as danger signaling whereas adenosine, the ATP breakdown product, serves as a negative feedback mechanism to limit inflammation. Already, in the vasculare system, the ADP is a physiological agonist involved in normal hemostasis and thrombosis. Since, macrophages are key to inflammatory process, that depending on the microenvironmental stimulation exhibit proinflammatory/ defense (classical/M1) and antiinflammatory/reparatory (alternative/M2) phenotype. The objective of this study was investigate the activity and expression of the ectonuclotidases in differential macrophage phenotype and evaluate the homocysteine (Hcy) effects on theses enzymes in macrophages and platelets. . The analysis of differential macrophages in phenotype proinflamatory/ M1 and antiinflamatory/M2 showed the same expression to P1 and P2 purinoreceptors. However, change profile of the ectonucleotidases as E-NTPDase1, E-NTPDase3 and ecto-5’- nucleotidase enzymes in macrophages during phenotypic differentiation were found, suggesting that macrophages must alter the purinergic cascade during macrophages differentiation phenotypic. In the pro-inflamatory/M1 phenotype the ATP hydrolysis decreased, suggesting ATP accumulation. On the other hand, the antiinflamatory/M2 phenotype the enzymes lead to a progressive decrease in nucleotides (ATP) concentrations and an increase the adenosine availability. Already, the macrophages exposed to Hcy present a polarized pro-inflammatory profile (M1) and our findings suggest the involvement of the E-NTPDase3 and ecto-5’-nucleotidase in the inflammatory complications associates to homocysteine. In the Platelets, which are fundamental elements to the thrombogenesis process, the homocysteine decreased ADP hydrolysis. This elevation of ADP around of the platelets due inactivating of ectonucleotidase, probably by the indirect action of Hcy, may be contributing to increase thrombotic risk described in individuals with hyperhomocysteinemia. In addition, the animals that received Hcy treatment potentiate platelet aggregation induced by ADP. In conclusion, in the present study the results reinforce purinergic signaling involvement in inflammatory/thrombosis process and point to development of treatments to inflammatory/thrombotic diseases.
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Bavaresco, Luci. "Estudo do papel da ecto-5'-nucleotidase/CD73 na proliferação de gliomas." reponame:Biblioteca Digital de Teses e Dissertações da UFRGS, 2008. http://hdl.handle.net/10183/12713.

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Os gliomas são os tumores primários mais comuns e devastadores que atingem o sistema nervoso central. O prognóstico para pacientes com estes tumores é ruim, e apesar de intensos esforços para o desenvolvimento de novas terapias, agentes efetivos ainda não estão disponíveis. A ecto-5‟-nucleotidase/CD73 (ecto-5‟-NT/CD73) regula os níveis extracelulares de AMP e adenosina, a qual tem sido amplamente descrita como fator indutor de proliferação celular. A ecto-5‟-NT/CD73 per se tem sido relatada como proteína envolvida no controle dos processos de crescimento, maturação, diferenciação, invasão e migração celular, além do processo de formação de metástases. No presente estudo nós avaliamos a atividade enzimática e as funções da ecto-5‟-NT/CD73 durante o processo proliferativo em linhagens de glioma C6 e U138-MG. Os resultados obtidos demonstram que ocorre um aumento da atividade da ecto-5‟-NT/CD73 com o aumento da confluência celular, quer seja esta obtida por semeadura de crescentes densidades celulares ou por crescentes dias de cultivo, em ambas as linhagens estudadas. As análises por RT-PCR e citometria de fluxo revelaram um aumento dos níveis de mRNA e proteína da ecto-5‟-NT/CD73, respectivamente quando comparadas culturas confluentes com culturas subconfluentes em linhagem de glioma humano U138-MG. Nesta mesma linhagem, o tratamento com 1 M de APCP, inibidor competitivo da ecto-5‟-NT/CD73 causou uma significativa redução de 20% na proliferação celular, enquanto a adenosina aumentou este processo em 25%. Por outro lado, 1 mM e 3 mM de AMP reduziram a proliferação em 29% e 42% respectivamente. Além disso, o silenciamento estável da ecto-5‟-NT/CD73 pela técnica do RNAi reduziu o processo de migração celular na linhagem de glioma humano U138-MG. Em conjunto, Estes resultados sugerem a participação da ecto-5‟-NT/CD73 na proliferação celular, sendo este processo desencadeado pela geração de adenosina (fator proliferativo), pela remoção dos níveis citotóxicos de AMP e pela participação per se da ecto-5‟-NT/CD73 como proteína de adesão.
Malignant gliomas are the most common and devastating primary tumors in the central nervous system. Despite treatment, patients with these tumors have a poor prognosis. Ecto-5‟-nucleotidase/CD73 (ecto-5‟-NT/CD73) may regulate the extracellular AMP and adenosine levels, which have been described as proliferation factor. The participation of ecto-5‟-NT/CD73 per se has been proposed as a proliferative factor, being involved in the control of cell growth, maturation, differentiation, invasion, migration and metastases processes. In the present study, we evaluate the ecto-5‟-NT/CD73 activity and functions in rat C6 and human U138-MG glioma cell lines proliferation process. Crescent confluences and culture times leads to an increase on ecto-5‟-NT/CD73 activity in both C6 and U138-MG glioma cells. RT-PCR analysis and flow cytometry showed a significant increase on ecto-5‟-NT/CD73 mRNA and protein levels respectively, when compared confluent cultures with subconfluent one in human U138-MG glioma cells. Treatment with 1 M APCP, a competitive ecto-5‟-NT inhibitor, caused a significant reduction in glioma cell proliferation of 20% for U138-MG glioma cell line. In addition, 100 M adenosine increases cell proliferation in 25% and AMP 1m M and 3 mM decrease U138-MG glioma cells proliferation in 29% and 42% respectively. The stable silencement of ecto-5‟-NT/CD73 by RNAi technique reduces cell migration in human U138-MG glioma cell line. Taken together these results suggest the participation of ecto-5‟-NT/CD73 in cell proliferation, being this process dependent of enzymatic activity generating adenosine, a proliferative factor and removing toxic levels of AMP, as well as a function as adhesive molecule.
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ZEKRI, MUSTAPHA. "Heterogeneite structurale et fonctionnelle de la 5-nucleotidase." Nantes, 1990. http://www.theses.fr/1990NANT2056.

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La 5-nucleotidase cytosolique de foie de buf a ete purifiee a l'homogeneite par une double chromatographie d'affinite sur concanavaline a sepharose, puis 5-amp sepharose. L'enzyme purifie est un heterodimere de 130000 daltons avec deux sous-unites de 57000 et 65000 daltons, contrairement a l'isoenzyme membranaire qui presente une structure homodimerique (140000 daltons). L'enzyme hydrolyse specifiquement les 5-mononucleotides et le 5-cmp serait son meilleur substrat. Son activite maximale intervient a ph 7,5 et 9,5, et necessite l'apport de cations divalents exogenes. Par contre, la 5-nucleotidase membranaire ne possede qu'un seul ph optimum a 7,5. L'etude des interactions des diverses lectines avec le glycanne de la 5-nucleotidase cytosolique prouve sa nature glycoproteique, et suggere une structure glycannique differente de l'enzyme membranaire. Cependant, les anticorps produits contre la 5-nucleotidase membranaire reconnaissent et inhibent l'enzyme cytosolique. Cette reactivite croisee demontre l'existence d'epitopes communs proches du site catalytique. Par ailleurs, nous avons realise une etude de l'effet de la phospholipase c specifique du phosphatidylinositol (pi-plc) sur l'attachement de la 5-nucleotidase a la membrane plasmique. Nous avons ainsi montre que seule une faible proportion de la molecule est convertie en une forme soluble par ce traitement. De plus, nous avons note une grande variation de sensibilite a l'action de la pi-plc entre la 5-nucleotidase et la phosphatase alcaline, dependante de la nature du tissu et de l'espece etudiee. Les differences de pourcentage de solubilisation des deux enzymes par la pi-plc pourraient etre dues a des raisons d'ordre sterique liees a la topographie des proteines dans la membrane plasmique ou a un polymorphisme d'ancrage de ces proteines dans la membrane
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Knöfel, Thomas. "Röntgenstrukturanalyse der 5'-Nucleotidase aus Escherichia coli mit dinuklearem Metallzentrum." [S.l. : s.n.], 2000. http://www.diss.fu-berlin.de/2000/131/index.html.

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Osborne, Foy Naomi. "Over-Expression of Ecto-5'-Nucleotidase in Pig Endothelial Cells." Thesis, Imperial College London, 2007. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.487200.

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Ecto-5'-nucleotidase (E5'N) is an endothelial surface enzyme that controls conversion of extracellular nucleotides into immunosuppressive adenosine. Species differences and especially lO-fold higher activity of E5'N in human endothelial cells (EC) than in pig EC could be important barrier for xenotransplantation.The major aim ofmy thesis is evaluation whether expression of human E5'N on pig EC is able to attenuate cell death mediated by components ofhuman blood responsible for delayed xenograft rejection (DXR). A pig cell line was transfected with human E5'N and efficiency assessed with flow cytometry and nucleotide breakdown assays using cell monolayers and lysates. Transfected cells were >95% positive for human E5'N/There was a massive increase in E5'N activity in transfected pig EC lysates and intact cells using extracellu~ar AMP as the substrate. Adenosine production from the breakdown of ATP was also significantly higher in transfected cells, proving E5'N to be the rate-limiting enzyme in adenosine production by pig EC. Incubation of transfected cells with AMP showed a time-dependent induction of the antiapoptotic protein Bcl-2 mediated via AI receptors, and subsequent protection of these cells from hydrogen peroxide-mediated apoptosis through AI receptors. Human natural killer (NK) cells were significantly less cytotoxic towards transfected than non-transfected pig EC. This effect was abrogated by an inhibitor of E5'N and mimicked by prior incubation of NK cells with adenosine. Supernatants from transfected cells also significantly inhibited platelet aggregation and expression of E5'N attenuated platelet adhesion to EC compared to nontransfected cells. However, transfection with E5'N did not protect cells from antibody and complement-mediated cytotoxicity. Functional expression of human E5'N in pig EC provided significant protection from apoptosis, NK cell-mediated lysis and platelet adhesion and aggregation, the main mechanisms of xenograft r~jection once hyperacute rejection has been overcome. E5'N is thus a potential candidate for. engineering of transgenic animals for xenotransplantation.
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McMillen, Lyle, and l. mcmillen@sct gu edu au. "Isolation and Characterisation of the 5'-Nucleotidase from Escherichia coli." Griffith University. School of Biomolecular and Biomedical Science, 2001. http://www4.gu.edu.au:8080/adt-root/public/adt-QGU20030226.153545.

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Escherichia coli 5'-nucleotidase is a periplasmically localised enzyme capable of hydrolysing a broad range of substrates, including all 5'-ribo- and 5'-deoxyribonucleotides, uridine diphosphate sugars, and a number of synthetic substrates such as bis (r-nitrophenyl) phosphate. The enzyme has been shown to contain at least one zinc ion following purification, and to have two metal binding sites in the catalytic cleft. 5'-Nucleotidase activity is significantly stimulated by the addition of particular divalent metal ions, most notably cobalt which results in a 30-50 fold increase in activity. Significant sequence homology between the E. coli 5'-nucleotidase and members of the Ser/Thr protein phosphatase family in the catalytic site has lead to 5'-nucleotidase being included in this protein family. This thesis describes the development of a rapid purification methodology for milligram quantities of 5'-nucleotidase, and the investigation of a number of physical and biochemical properties of the enzyme with the aim of comparing these properties to those of certain catalytic site mutants. The molecular weight of the mature protein was estimated as 58219 daltons, with a specific activity for 5'-AMP, in the presence of 4 mM Co2+ and 13 mM Ca2+ at pH 6.0, of 730 mmol/min/mg. The presence of up to two zinc ions associated with the purified enzyme was observed using ICP-ES analysis, suggesting both metal ion binding sites are occupied by zinc in vivo, and some degree of displacement of zinc by cobalt could be observed. Mass spectrometry data, gathered at 60 and 70 mS orifice potential, suggested the presence of a small proportion of material with a mass 118 to 130 daltons greater than the main 5'-nucleotidase mass estimation. This study suggests that this mass difference, only evident at the lower orificepotential, is due to the presence of two zinc ions closely associated with 5'-nucleotidase. To account for the observed high level of activation of 5'-nucleotidase activity by particular divalent metal ions, this thesis describes a proposed model in which these divalent ions may displace the zinc ion at one of the metal ion binding sites. This displacement only occurs at one of the two metal ion binding sites, with the other metal binding site retaining the zinc ion already present. Studies with purified enzyme, each with a single amino acid substitution, lend support to this hypothesis and suggest the identity of the metal ion binding site at which displacement occurs. Seven key catalytic site residues (Asp-41, His-43, Asp-84, His-117, Glu-118, His-217 and His-252) were selected on the basis of sequence conservation within the Ser/Thr protein phosphatases and 5'-nucleotidases. X-ray crystallographic data published by others during this study implicated five of the selected residues (Asp-41, His-43, Asp-84, His-217 and His-252) directly in metal ion binding, including two residues from each metal ion binding site and one directly involved in both sites (Asp-84). The remaining two residues (His-117 and Glu-118) are highly conserved but were not thought to play direct roles in metal ion binding. The seven selected residues were modified by site-directed mutagenesis, and the effect of the amino acid substitutions upon the kinetic properties of 5'-nucleotidase activity was determined. Residues hypothesised to be involved in metal ion displacement, and subsequent activation of 5'-nucleotidase activity, were identified by reductions in metal ion affinity and increased levels of activation by cobalt compared to the wild type 5'-nucleotidase. This study suggests that the metal binding site, M2, that includes residues Asp-84, His-217 and His-252, is involved in metal ion displacement, while the other metal binding site, M1, is not. This, in turn, suggests the metal binding sites are functionally non-equivalent and kinetically distinct. No residues were identified in this study as playing significant roles in substrate binding, as there was no significant reduction observed in affinity for 5'-AMP observed in any of the catalytic site mutants.
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黎錦明 and Kam-ming Lai. "Structure and function of 5'-nucleotidase of the rat brain." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 1991. http://hub.hku.hk/bib/B31232280.

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Eristi, Can M. "Investigation of Transcriptional Regulation of 5'-Nucleotidase in Dictyostelium Discoideum." Diss., Virginia Tech, 2003. http://hdl.handle.net/10919/28822.

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A 5' AMP-degrading activity appears during the course of development in Dictyostelium discoideum between the prestalk and prespore zones. This enzyme is referred as 5'-Nucleotidase (5NT). Given the critical role of cyclic AMP in cell differentiation in this organism, 5NT is thought to be involved in cell positioning during development. Southern blot analysis showed a single form of the gene. The expression of the 5nt gene is known to be developmentally regulated. The message appears first at about 5 hr of the Dictyostelium development and remains constant throughout the rest of the development. Primer extension indicated two potential transcriptional start sites (118 bp and 148 bp upstream of the ATG initiation codon) for the 5nt expression. The 5nt promoter region was cloned and analyzed to investigate the expression of 5nt. Analysis of the cloned 5nt promoter fused to lacZ enabled the localization of the 5nt expression in pstAB cells during development. To identify cis-acting regulatory sequences, a series of 5' and internal promoter deletions were generated and fused to a luciferase reporter gene. The reporter activity driven by the 1,212 bp promoter started at the early aggregation stage, in agreement with temporal expression of the 5nt gene. Also, the expression was induced by exogenous cAMP. The reporter activity was high and relatively equivalent for all deletion constructs that contained 547 bp or more of the promoter region. No luciferase activity was detected using 365 bp or less of the promoter. A gradual decrease in activity was observed when three deletion constructs between -547 and -365 bp were tested suggesting the presence of at least two cis-regulatory elements within this region. Internal deletion analysis indicated another potential regulatory region located between -307 and -226 bp. To identify protein factor(s) that bind specifically to these regulatory sequences, gel shift assays were performed. Two bands, 0.33 Rf and 0.13 Rf, were detected in both cytoplasmic and nuclear extracts using radiolabeled DNA fragments located between -227 and -198 bp and -252 and -203 bp of the promoter region, respectively. Competition experiments confirmed the specificity of binding. The protein factors in these DNA binding activities were purified using various chromatography techniques. Mass spectrometry analysis of the purified 70 kDa protein corresponding to the 0.33 Rf band activity and a subsequent search in the Dictyostelium genomic database revealed that the purified protein was a putative formyltetrahydrofolate synthase.
Ph. D.
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Books on the topic "5'-nucleotidase"

1

Barber, Ian Stuart. 5'-nucleotidase: It's [sic]Membrane/cytoskeletal associations. Birmingham: Universityof Birmingham, 1989.

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Marani, Enrico. Topographic histochemistry of the cerebellum: 5'-nucleotidase, acetylocholinesterase, immunology of FAL. Stuttgart: G. Fischer Verlag, 1986.

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Book chapters on the topic "5'-nucleotidase"

1

Schomburg, Dietmar, and Margit Salzmann. "5’-Nucleotidase." In Enzyme Handbook 3, 309–14. Berlin, Heidelberg: Springer Berlin Heidelberg, 1991. http://dx.doi.org/10.1007/978-3-642-76463-9_66.

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Froehlich, Stephan J., Carlo A. Lackerbauer, Guenter Rudolph, Jan Rémi, Soheyl Noachtar, Werner J. Heppt, Annette Cryer, et al. "5′-Nucleotidase Hyperactivity." In Encyclopedia of Molecular Mechanisms of Disease, 1501–2. Berlin, Heidelberg: Springer Berlin Heidelberg, 2009. http://dx.doi.org/10.1007/978-3-540-29676-8_4.

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Braun-Falco, Markus, Henry J. Mankin, Sharon L. Wenger, Markus Braun-Falco, Stephan DiSean Kendall, Gerard C. Blobe, Christoph K. Weber, et al. "Pyrimidine 5′ Nucleotidase Deficiency." In Encyclopedia of Molecular Mechanisms of Disease, 1798. Berlin, Heidelberg: Springer Berlin Heidelberg, 2009. http://dx.doi.org/10.1007/978-3-540-29676-8_8047.

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Braun-Falco, Markus, Henry J. Mankin, Sharon L. Wenger, Markus Braun-Falco, Stephan DiSean Kendall, Gerard C. Blobe, Christoph K. Weber, et al. "Pyrimidine 5′ Nucleotidase-1 Deficiency." In Encyclopedia of Molecular Mechanisms of Disease, 1798. Berlin, Heidelberg: Springer Berlin Heidelberg, 2009. http://dx.doi.org/10.1007/978-3-540-29676-8_8048.

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Kreutzberg, G. W., D. Heymann, and M. Reddington. "5′-Nucleotidase in the Nervous System." In Proceedings in Life Sciences, 147–64. Berlin, Heidelberg: Springer Berlin Heidelberg, 1986. http://dx.doi.org/10.1007/978-3-642-70664-6_11.

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Marinello, E., A. Tabucchi, F. Carlucci, P. Galieni, and F. Rosi. "Isoenzymes of 5′-Nucleotidase in Human Lymphocytes." In Advances in Experimental Medicine and Biology, 555–58. Boston, MA: Springer US, 1998. http://dx.doi.org/10.1007/978-1-4615-5381-6_107.

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Webster, A. D. B., M. Rowe, S. M. Johnson, G. L. Asherson, and A. Harkness. "Ecto 5′-Nucleotidase Deficiency in Primary Hypogammaglobulinaemia." In Ciba Foundation Symposium 68 - Enzyme Defects and Immune Dysfunction, 135–64. Chichester, UK: John Wiley & Sons, Ltd., 2008. http://dx.doi.org/10.1002/9780470720516.ch9.

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Tozzi, M. G., M. Camici, S. Allegrini, R. Pesi, M. Turriani, A. Del Corso, and P. L. Ipata. "Cytosolic 5′-Nucleotidase/Phosphotransferase of Human Colon Carcinoma." In Advances in Experimental Medicine and Biology, 173–76. New York, NY: Springer US, 1991. http://dx.doi.org/10.1007/978-1-4615-7703-4_39.

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Yamazaki, Y., A. R. Collinson, V. L. Truong, and J. M. Lowenstein. "Regulation of Soluble 5′-Nucleotidase I from Rabbit Heart." In Advances in Experimental Medicine and Biology, 107–11. Boston, MA: Springer US, 1989. http://dx.doi.org/10.1007/978-1-4684-5676-9_17.

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Bontemps, F., G. Van den Berghe, and H. G. Hers. "Identification of a Purine 5′-Nucleotidase in Human Erythrocytes." In Purine and Pyrimidine Metabolism in Man V, 283–90. New York, NY: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4684-1248-2_45.

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Conference papers on the topic "5'-nucleotidase"

1

Nguyen, Anna M., Jianhong Zhou, and Yuchun Du. "Abstract B05: Ecto-5’-nucleotidase (CD73) confers radioresistance in pancreatic cancer." In Abstracts: AACR Special Conference on Pancreatic Cancer: Advances in Science and Clinical Care; May 12-15, 2016; Orlando, FL. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.panca16-b05.

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Jordheim, Lars P., Zsuzsanna Marton, Moez Rhimi, Laurent Chaloin, Emeline Cros-Perrial, Corinne Lionne, Suzanne Peyrottes, Nushin Aghajari, and Charles Dumontet. "Abstract 3835: Identification and characterization of inhibitors of 5′-nucleotidase cN-II issued from virtual screening." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-3835.

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Bowser, Jessica L., Michael R. Blackburn, Gregory L. Shipley, Susu Xie, and Russell R. Broaddus. "Abstract 3384: Down-regulation of 5’-nucleotidase (CD73)-generated adenosine: A novel mechanism for regulating endometrial cancer metastasis." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-3384.

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Matsuyama, Masahiro, Masatoshi Wakui, Makoto Monnai, Tomoko Mizushima, Chiyoko NIshime, Kenji Kawai, Hiroshi Suemizu, et al. "Abstract 2366: Reduced ecto-5′-nucleotidase CD73 expression and altered purine nucleotide metabolism in colorectal cancer cells robustly causing liver metastases." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-2366.

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Zborovsky, AB, BV Zavodovsky, EV Bobicheva, LE Sivordova, and NA Fofanova. "THU0055 Role of antibodies to 5’nucleotidase in rheumatoid arthritis, systemic lupus erythematosus, systemic sclerosis, ankylosing spondylarthritis and reactive arthritis patients." In Annual European Congress of Rheumatology, Annals of the rheumatic diseases ARD July 2001. BMJ Publishing Group Ltd and European League Against Rheumatism, 2001. http://dx.doi.org/10.1136/annrheumdis-2001.899.

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Zborovsky, AB, BV Zavodovsky, TA Pankratova, AV Rvachev, OV Bykova, and TV Serdukova. "SAT0001 Role of determination of succinate dehydrogenase, myeloperoxidase, na ± k ± atph-ase, 5?-nucleotidase in cells of peripheral blood of ankylosing spondylarthritis patients." In Annual European Congress of Rheumatology, Annals of the rheumatic diseases ARD July 2001. BMJ Publishing Group Ltd and European League Against Rheumatism, 2001. http://dx.doi.org/10.1136/annrheumdis-2001.353.

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Goueli, Said A., and Kevin hsiao. "Abstract 414: Biochemical and cellular monitoring of the activity of the ecto-5’-nucleotidase (CD73), a key cancer modulator using HTS-formatted bioluminescent technology." In Proceedings: AACR 107th Annual Meeting 2016; April 16-20, 2016; New Orleans, LA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.am2016-414.

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