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Pesquisa : D08.811.913.400.725.850 [Categoria DeCS]
Referências encontradas : 123 [refinar]
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[PMID]:26677573
[Au] Autor:Bzowska A
[Ti] Título:[Purine and pyrimidine nucleoside phosphorylases - remarkable enzymes still not fully understood].
[Ti] Título:Nukleozydowe fosforylazy purynowe i pirymidynowe - niezwykle enzymy ciagle nie do konca rozszyfrowane..
[So] Source:Postepy Biochem;61(3):260-73, 2015.
[Is] ISSN:0032-5422
[Cp] País de publicação:Poland
[La] Idioma:pol
[Ab] Resumo:Purine and pyrimidine nucleoside phosphorylases catalyze the reversible phosphorolytic cleavage of the glycosidic bond of purine and pyrimidine nucleosides, and are key enzymes of the nucleoside salvage pathway. This metabolic route is the less costly alternative to the de novo synthesis of nucleosides and nucleotides, supplying cells with these important building blocks. Interest in nucleoside phosphorylases is not only due to their important role in metabolism of nucleosides and nucleotides, but also due to the potential medical use of the enzymes (all phosphorylases in activating prodrugs - nucleoside and nucleic base analogs, high-molecular mass purine nucleoside phosphorylases in gene therapy of some solid tumors) and their inhibitors (as selective immunosuppressive, anticancer and antiparasitic agents, and preventing inactivation of other nucleoside drugs). Phosphorylases are also convenient tools for efficient enzymatic synthesis of otherwise inaccessible nucleoside analogues. In this paper the contribution of Professor David Shugar and some of his colleagues and coworkers in studies of these remarkable enzymes carried out over nearly 40 years is discussed on the background of global research in this field.
[Mh] Termos MeSH primário: Bioquímica/história
Purina-Núcleosídeo Fosforilase/história
Pirimidina Fosforilases/história
[Mh] Termos MeSH secundário: Bactérias/enzimologia
Inibidores Enzimáticos/história
Inibidores Enzimáticos/farmacologia
Eucariotos/enzimologia
História do Século XX
História do Século XXI
Cinética
Nucleosídeos/história
Nucleosídeos/metabolismo
Nucleotídeos/história
Nucleotídeos/metabolismo
Polônia
Estrutura Terciária de Proteína
Purina-Núcleosídeo Fosforilase/antagonistas & inibidores
Purina-Núcleosídeo Fosforilase/química
Purina-Núcleosídeo Fosforilase/metabolismo
Pirimidina Fosforilases/antagonistas & inibidores
Pirimidina Fosforilases/química
Pirimidina Fosforilases/metabolismo
Especificidade por Substrato
[Pt] Tipo de publicação:ENGLISH ABSTRACT; HISTORICAL ARTICLE; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Enzyme Inhibitors); 0 (Nucleosides); 0 (Nucleotides); EC 2.4.2.- (Pyrimidine Phosphorylases); EC 2.4.2.1 (Purine-Nucleoside Phosphorylase)
[Em] Mês de entrada:1603
[Cu] Atualização por classe:151218
[Lr] Data última revisão:
151218
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151219
[St] Status:MEDLINE


  2 / 123 MEDLINE  
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[PMID]:24940697
[Au] Autor:Vande Voorde J; Liekens S; Gago F; Balzarini J
[Ad] Endereço:a Rega Institute for Medical Research , KU Leuven , Leuven , Belgium.
[Ti] Título:The pyrimidine nucleoside phosphorylase of Mycoplasma hyorhinis and how it may affect nucleoside-based therapy.
[So] Source:Nucleosides Nucleotides Nucleic Acids;33(4-6):394-402, 2014.
[Is] ISSN:1532-2335
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Mycoplasmas are opportunistic parasites and some species are suggested to preferentially colonize tumor tissue in cancer patients. We could demonstrate that the annotated thymidine phosphorylase (TP) gene in the genome of Mycoplasma hyorhinis encodes a pyrimidine nucleoside phosphorylase (PyNPHyor) that not only efficiently catalyzes thymidine but also uridine phosphorolysis. The kinetic characteristics of PyNPHyor-catalyzed nucleoside and nucleoside analogue (NA) phosphorolysis were determined. We demonstrated that the expression of such an enzyme in mycoplasma-infected cell cultures dramatically alters the activity of various anticancer/antiviral NAs such as 5-halogenated pyrimidine nucleosides, including 5-trifluorothymidine (TFT). Due to their close association with human cancers, the presence of mycoplasmas may markedly influence the therapeutic efficiency of nucleoside-based drugs.
[Mh] Termos MeSH primário: Antivirais/farmacologia
Mycoplasma hyorhinis/enzimologia
Pirimidina Fosforilases/metabolismo
Trifluridina/farmacologia
[Mh] Termos MeSH secundário: Linhagem Celular Tumoral
Seres Humanos
Células MCF-7
Mycoplasma hyorhinis/fisiologia
Pirimidina Fosforilases/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antiviral Agents); EC 2.4.2.- (Pyrimidine Phosphorylases); RMW9V5RW38 (Trifluridine)
[Em] Mês de entrada:1502
[Cu] Atualização por classe:140619
[Lr] Data última revisão:
140619
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140619
[St] Status:MEDLINE
[do] DOI:10.1080/15257770.2013.851394


  3 / 123 MEDLINE  
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[PMID]:24858186
[Au] Autor:Tran NQ; Tabor S; Richardson CC
[Ad] Endereço:Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts, USA.
[Ti] Título:Genetic requirements for sensitivity of bacteriophage t7 to dideoxythymidine.
[So] Source:J Bacteriol;196(15):2842-50, 2014 Aug.
[Is] ISSN:1098-5530
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:We previously reported that the presence of dideoxythymidine (ddT) in the growth medium selectively inhibits the ability of bacteriophage T7 to infect Escherichia coli by inhibiting phage DNA synthese (N. Q. Tran, L. F. Rezende, U. Qimron, C. C. Richardson, and S. Tabor, Proc. Natl. Acad. Sci. U. S. A. 105:9373-9378, 2008, doi:10.1073/pnas.0804164105). In the presence of T7 gene 1.7 protein, ddT is taken up into the E. coli cell and converted to ddTTP. ddTTP is incorporated into DNA as ddTMP by the T7 DNA polymerase, resulting in chain termination. We have identified the pathway by which exogenous ddT is converted to ddTTP. The pathway consists of ddT transport by host nucleoside permeases and phosphorylation to ddTMP by the host thymidine kinase. T7 gene 1.7 protein phosphorylates ddTMP and ddTDP, resulting in ddTTP. A 74-residue peptide of the gene 1.7 protein confers ddT sensitivity to the same extent as the 196-residue wild-type gene 1.7 protein. We also show that cleavage of thymidine to thymine and deoxyribose-1-phosphate by the host thymidine phosphorylase greatly increases the sensitivity of phage T7 to ddT. Finally, a mutation in T7 DNA polymerase that leads to discrimination against the incorporation of ddTMP eliminates ddT sensitivity.
[Mh] Termos MeSH primário: Bacteriófago T7/genética
Didesoxinucleotídeos/farmacologia
Escherichia coli/enzimologia
Inibidores da Síntese de Ácido Nucleico
Inibidores da Síntese de Ácido Nucleico/farmacologia
Nucleotídeos de Timina/farmacologia
[Mh] Termos MeSH secundário: Bacteriófago T7/efeitos dos fármacos
Bacteriófago T7/enzimologia
Bacteriófago T7/crescimento & desenvolvimento
DNA Viral/biossíntese
DNA Polimerase Dirigida por DNA/genética
DNA Polimerase Dirigida por DNA/metabolismo
Didesoxinucleotídeos/metabolismo
Escherichia coli/virologia
Proteínas de Escherichia coli/genética
Proteínas de Escherichia coli/metabolismo
Técnicas de Inativação de Genes
Inibidores da Síntese de Ácido Nucleico/metabolismo
Fosforilação
Pirimidina Fosforilases/genética
Pirimidina Fosforilases/metabolismo
Deleção de Sequência
Timidina/metabolismo
Timidina Quinase/genética
Timidina Quinase/metabolismo
Nucleotídeos de Timina/metabolismo
Proteínas Virais/antagonistas & inibidores
Proteínas Virais/genética
Proteínas Virais/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (DNA, Viral); 0 (Dideoxynucleotides); 0 (Escherichia coli Proteins); 0 (Nucleic Acid Synthesis Inhibitors); 0 (Thymine Nucleotides); 0 (Viral Proteins); EC 2.4.2.- (Pyrimidine Phosphorylases); EC 2.7.1.21 (Thymidine Kinase); EC 2.7.7.7 (DNA-Directed DNA Polymerase); IA883WYU21 (2',3'-dideoxythymidine triphosphate); VC2W18DGKR (Thymidine)
[Em] Mês de entrada:1410
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140527
[St] Status:MEDLINE
[do] DOI:10.1128/JB.01718-14


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[PMID]:24668817
[Au] Autor:Vande Voorde J; Sabuncuoglu S; Noppen S; Hofer A; Ranjbarian F; Fieuws S; Balzarini J; Liekens S
[Ad] Endereço:From the Rega Institute for Medical Research, KU Leuven, Minderbroedersstraat 10, blok x-bus 1030, B-3000 Leuven, Belgium.
[Ti] Título:Nucleoside-catabolizing enzymes in mycoplasma-infected tumor cell cultures compromise the cytostatic activity of the anticancer drug gemcitabine.
[So] Source:J Biol Chem;289(19):13054-65, 2014 May 09.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The intracellular metabolism and cytostatic activity of the anticancer drug gemcitabine (2',2'-difluoro-2'-deoxycytidine; dFdC) was severely compromised in Mycoplasma hyorhinis-infected tumor cell cultures. Pronounced deamination of dFdC to its less cytostatic metabolite 2',2'-difluoro-2'-deoxyuridine was observed, both in cell extracts and spent culture medium (i.e. tumor cell-free but mycoplasma-containing) of mycoplasma-infected tumor cells. This indicates that the decreased antiproliferative activity of dFdC in such cells is attributed to a mycoplasma cytidine deaminase causing rapid drug catabolism. Indeed, the cytostatic activity of gemcitabine could be restored by the co-administration of tetrahydrouridine (a potent cytidine deaminase inhibitor). Additionally, mycoplasma-derived pyrimidine nucleoside phosphorylase (PyNP) activity indirectly potentiated deamination of dFdC: the natural pyrimidine nucleosides uridine, 2'-deoxyuridine and thymidine inhibited mycoplasma-associated dFdC deamination but were efficiently catabolized (removed) by mycoplasma PyNP. The markedly lower anabolism and related cytostatic activity of dFdC in mycoplasma-infected tumor cells was therefore also (partially) restored by a specific TP/PyNP inhibitor (TPI), or by exogenous thymidine. Consequently, no effect on the cytostatic activity of dFdC was observed in tumor cell cultures infected with a PyNP-deficient Mycoplasma pneumoniae strain. Because it has been reported that some commensal mycoplasma species (including M. hyorhinis) preferentially colonize tumor tissue in cancer patients, our findings suggest that the presence of mycoplasmas in the tumor microenvironment could be a limiting factor for the anticancer efficiency of dFdC-based chemotherapy. Accordingly, a significantly decreased antitumor effect of dFdC was observed in mice bearing M. hyorhinis-infected murine mammary FM3A tumors compared with uninfected tumors.
[Mh] Termos MeSH primário: Antimetabólitos Antineoplásicos
Proteínas de Bactérias/metabolismo
Neoplasias da Mama
Desoxicitidina/análogos & derivados
Neoplasias Mamárias Experimentais
Infecções por Mycoplasma/enzimologia
Mycoplasma hyorhinis/enzimologia
Pirimidina Fosforilases/metabolismo
[Mh] Termos MeSH secundário: Animais
Antimetabólitos Antineoplásicos/farmacocinética
Antimetabólitos Antineoplásicos/farmacologia
Neoplasias da Mama/tratamento farmacológico
Neoplasias da Mama/metabolismo
Neoplasias da Mama/microbiologia
Linhagem Celular Tumoral
Desoxicitidina/farmacocinética
Desoxicitidina/farmacologia
Feminino
Seres Humanos
Neoplasias Mamárias Experimentais/tratamento farmacológico
Neoplasias Mamárias Experimentais/metabolismo
Neoplasias Mamárias Experimentais/microbiologia
Camundongos
Tetra-Hidrouridina/farmacocinética
Tetra-Hidrouridina/farmacologia
Timidina/metabolismo
Microambiente Tumoral/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antimetabolites, Antineoplastic); 0 (Bacterial Proteins); 0W860991D6 (Deoxycytidine); 18771-50-1 (Tetrahydrouridine); B76N6SBZ8R (gemcitabine); EC 2.4.2.- (Pyrimidine Phosphorylases); VC2W18DGKR (Thymidine)
[Em] Mês de entrada:1406
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140327
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M114.558924


  5 / 123 MEDLINE  
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[PMID]:22366108
[Au] Autor:Vande Voorde J; Quintiliani M; McGuigan C; Liekens S; Balzarini J
[Ad] Endereço:Rega Institute for Medical Research, KU Leuven, Minderbroedersstraat 10, B-3000 Leuven, Belgium.
[Ti] Título:Inhibition of pyrimidine and purine nucleoside phosphorylases by a 3,5-dichlorobenzoyl-substituted 2-deoxy-D-ribose-1-phosphate derivative.
[So] Source:Biochem Pharmacol;83(10):1358-63, 2012 May 15.
[Is] ISSN:1873-2968
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The 3,5-dichlorobenzoyl-substituted 2-deoxy-D-ribose-1-phosphate derivative, designated Cf2891, was found to inhibit a variety of pyrimidine and purine nucleoside phosphorylases (NPs) with preference for uridine- and inosine-hydrolyzing enzymes [uridine phosphorylase (UP; EC 2.4.2.3), pyrimidine nucleoside phosphorylase (PyNP; EC 2.4.2.2) and purine nucleoside phosphorylase (PNP; EC 2.4.2.1)]. Kinetic analyses revealed that Cf2891 competes with inorganic phosphate (P(i)) for binding to the NPs and, depending on the nature of the enzyme, acts as a competitive or non-competitive inhibitor with regard to the nucleoside binding site. Also, the compound prevents breakdown of pyrimidine analogues used in the treatment of viral infections and cancer. Since NPs are abundantly present in tumor tissue and may be overexpressed due to secondary bacterial infections in immunocompromised patients suffering viral infections, Cf2891 may serve as a lead molecule for the development of inhibitors to be used in nucleoside-based combination therapy.
[Mh] Termos MeSH primário: Inibidores Enzimáticos/farmacologia
Fosfatos/farmacologia
Purina-Núcleosídeo Fosforilase/antagonistas & inibidores
Pirimidina Fosforilases/antagonistas & inibidores
[Mh] Termos MeSH secundário: Bactérias/enzimologia
Sequência de Bases
Primers do DNA
Seres Humanos
Cinética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (DNA Primers); 0 (Enzyme Inhibitors); 0 (Phosphates); EC 2.4.2.- (Pyrimidine Phosphorylases); EC 2.4.2.1 (Purine-Nucleoside Phosphorylase)
[Em] Mês de entrada:1205
[Cu] Atualização por classe:120327
[Lr] Data última revisão:
120327
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120228
[St] Status:MEDLINE
[do] DOI:10.1016/j.bcp.2012.02.005


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[PMID]:21892829
[Au] Autor:McGuigan C; Murziani P; Slusarczyk M; Gonczy B; Vande Voorde J; Liekens S; Balzarini J
[Ad] Endereço:Welsh School of Pharmacy, Cardiff University, King Edward VII Avenue, Cardiff CF10 3NB, UK. mcguigan@cardiff.ac.uk
[Ti] Título:Phosphoramidate ProTides of the anticancer agent FUDR successfully deliver the preformed bioactive monophosphate in cells and confer advantage over the parent nucleoside.
[So] Source:J Med Chem;54(20):7247-58, 2011 Oct 27.
[Is] ISSN:1520-4804
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The fluorinated pyrimidine family of nucleosides continues to represent major current chemotherapeutic agents for treating solid tumors. We herein report their phosphate prodrugs, ProTides, as promising new derivatives, which partially bypass the dependence of the current drugs on active transport and nucleoside kinase-mediated activation. They are also resistant to metabolic deactivation by phosphorolytic enzymes. We report 39 ProTides of the fluorinated pyrimidine FUDR with variation in the aryl, ester, and amino acid regions. Notably, only certain ProTide motifs are successful in delivering the nucleoside monophosphate into intact cells. We also find that the ProTides retain activity in mycoplasma infected cells, unlike FUDR. Data suggest these compounds to be worthy of further progression.
[Mh] Termos MeSH primário: Antineoplásicos/síntese química
Floxuridina/análogos & derivados
Floxuridina/síntese química
Compostos Organofosforados/síntese química
Pró-Fármacos/síntese química
[Mh] Termos MeSH secundário: Antineoplásicos/farmacologia
Técnicas de Cultura de Células
Linhagem Celular Tumoral
Resistência a Medicamentos Antineoplásicos
Ensaios de Seleção de Medicamentos Antitumorais
Transportador Equilibrativo 1 de Nucleosídeo/genética
Floxuridina/farmacologia
Seres Humanos
Mycoplasma hyorhinis/enzimologia
Compostos Organofosforados/farmacologia
Pró-Fármacos/farmacologia
Pirimidina Fosforilases/metabolismo
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antineoplastic Agents); 0 (Equilibrative Nucleoside Transporter 1); 0 (Organophosphorus Compounds); 0 (Prodrugs); 0 (SLC29A1 protein, human); 039LU44I5M (Floxuridine); EC 2.4.2.- (Pyrimidine Phosphorylases)
[Em] Mês de entrada:1201
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:110907
[St] Status:MEDLINE
[do] DOI:10.1021/jm200815w


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[PMID]:21366534
[Au] Autor:Villela AD; Sánchez-Quitian ZA; Ducati RG; Santos DS; Basso LA
[Ad] Endereço:Instituto Nacional de Ciência e Tecnologia em Tuberculose, Centro de Pesquisas em Biologia Molecular e Funcional (CPBMF), Pontifícia Universidade Católica do Rio Grande do Sul, Porto Alegre, RS, Brazil.
[Ti] Título:Pyrimidine salvage pathway in Mycobacterium tuberculosis.
[So] Source:Curr Med Chem;18(9):1286-98, 2011.
[Is] ISSN:1875-533X
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The causative agent of tuberculosis (TB), Mycobacterium tuberculosis, infects one-third of the world population. TB remains the leading cause of mortality due to a single bacterial pathogen. The worldwide increase in incidence of M. tuberculosis has been attributed to the high proliferation rates of multi and extensively drug-resistant strains, and to co-infection with the human immunodeficiency virus. There is thus a continuous requirement for studies on mycobacterial metabolism to identify promising targets for the development of new agents to combat TB. Singular characteristics of this pathogen, such as functional and structural features of enzymes involved in fundamental metabolic pathways, can be evaluated to identify possible targets for drug development. Enzymes involved in the pyrimidine salvage pathway might be attractive targets for rational drug design against TB, since this pathway is vital for all bacterial cells, and is composed of enzymes considerably different from those present in humans. Moreover, the enzymes of the pyrimidine salvage pathway might have an important role in the mycobacterial latent state, since M. tuberculosis has to recycle bases and/or nucleosides to survive in the hostile environment imposed by the host. The present review describes the enzymes of M. tuberculosis pyrimidine salvage pathway as attractive targets for the development of new antimycobacterial agents. Enzyme functional and structural data have been included to provide a broader knowledge on which to base the search for compounds with selective biological activity.
[Mh] Termos MeSH primário: Mycobacterium tuberculosis/enzimologia
Pirimidinas/metabolismo
[Mh] Termos MeSH secundário: Citidina Desaminase/metabolismo
Mycobacterium tuberculosis/metabolismo
Núcleosídeo-Difosfato Quinase/metabolismo
Núcleosídeo-Fosfato Quinase/metabolismo
Nucleotídeo Desaminases/metabolismo
Pentosiltransferases/metabolismo
Pirimidina Fosforilases/metabolismo
Pirofosfatases/metabolismo
Timidilato Sintase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; REVIEW
[Nm] Nome de substância:
0 (Pyrimidines); EC 2.1.1.45 (Thymidylate Synthase); EC 2.4.2.- (Pentosyltransferases); EC 2.4.2.- (Pyrimidine Phosphorylases); EC 2.4.2.9 (uracil phosphoribosyltransferase); EC 2.7.4.4 (Nucleoside-Phosphate Kinase); EC 2.7.4.6 (Nucleoside-Diphosphate Kinase); EC 3.5.4.- (Nucleotide Deaminases); EC 3.5.4.13 (dCTP deaminase); EC 3.5.4.5 (Cytidine Deaminase); EC 3.6.1.- (Pyrophosphatases); EC 3.6.1.23 (dUTP pyrophosphatase); K8CXK5Q32L (pyrimidine)
[Em] Mês de entrada:1106
[Cu] Atualização por classe:121115
[Lr] Data última revisão:
121115
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:110304
[St] Status:MEDLINE


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[PMID]:20871042
[Au] Autor:Honda T; Inagawa H; Nishizawa T; Yoshimura H; Yamamoto I; Soma G
[Ad] Endereço:Department of Medical Technology, School of Life and Environmental Science, Azabu University, Fuchinobe, Chuo-ku, Sagamihara, Kanagawa 252-5201, Japan. hondat@azabu-u.ac.jp
[Ti] Título:The relationship between clinicopathological factors and the reduction of pyrimidine nucleoside phosphorylase activity after preoperative administration of 5'-deoxy-5-fluorouridine.
[So] Source:Anticancer Res;30(8):3207-11, 2010 Aug.
[Is] ISSN:1791-7530
[Cp] País de publicação:Greece
[La] Idioma:eng
[Ab] Resumo:AIM: The response to fluoropyrimidine chemotherapeutic drugs is different in individual tumors. Predictive biomarkers of antitumor effects by these drugs are unknown. 5'-Deoxy-5-fluorouridine (5'-DFUR), a fluoro-pyrimidine chemotherapeutic drug, is converted to 5-fluorouracil (5-FU) by pyrimidine nucleoside phosphorylase (PyNPase). It is suggested that 5'-DFUR will efficiently exert antitumor effects via PyNPase in tumor tissues. The change of PyNPase activity in tumor tissues following 5'-DFUR administration may reflect antitumor effects, and may be useful for detecting predictive factors of antitumor effects. The aim of this study was to search for predictive factors of antitumor effects by analyzing the relationship between clinicopathological factors and the change of PyNPase activity in colorectal tumor tissues after preoperative 5'-DFUR administration. PATIENTS AND METHODS: PyNPase activity in colorectal tissues from 45 patients with colorectal tumors was measured using an ELISA method. RESULTS: The reduction rate of PyNPase activity in colorectal tumor tissues after preoperative 5'-DFUR administration was correlated with significant differences in lymphatic invasion, stage, and histologic classification. It is suggested that lymphatic invasion, stage (distant metastasis), and histologic classification may be predictive factors for evaluating antitumor effects and selecting 5-FU-based chemotherapeutic drugs for patients with colorectal tumors.
[Mh] Termos MeSH primário: Antimetabólitos Antineoplásicos/administração & dosagem
Neoplasias Colorretais/enzimologia
Floxuridina/administração & dosagem
Pentosiltransferases/metabolismo
[Mh] Termos MeSH secundário: Neoplasias Colorretais/patologia
Seres Humanos
Pirimidina Fosforilases
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antimetabolites, Antineoplastic); 039LU44I5M (Floxuridine); EC 2.4.2.- (Pentosyltransferases); EC 2.4.2.- (Pyrimidine Phosphorylases); V1JK16Y2JP (doxifluridine)
[Em] Mês de entrada:1010
[Cu] Atualização por classe:151123
[Lr] Data última revisão:
151123
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:100928
[St] Status:MEDLINE


  9 / 123 MEDLINE  
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[PMID]:18347391
[Au] Autor:Tamesa M; Yamamoto S; Maeda N; Nagashima Y; Oka M
[Ad] Endereço:Dept. of Digestive Surgery and Surgical Oncology, Yamaguchi University Graduate School of Medicine, Japan.
[Ti] Título:[Significance of pyrimidine nucleoside phosphorylase and dihydropyrimidine dehydrogenase levels to predict postoperative recurrence in primary breast cancer].
[So] Source:Gan To Kagaku Ryoho;35(3):431-6, 2008 Mar.
[Is] ISSN:0385-0684
[Cp] País de publicação:Japan
[La] Idioma:jpn
[Ab] Resumo:BACKGROUND: High expression of PyNPase (pyrimidine nucleoside phosphorylase) and DPD (dihydropyrimidine dehydrogenase) in breast cancer has been reported. Breast cancer patients with high expression of PyNPase reportedly have a poor prognosis. METHODS: We evaluated the relationship between postoperative prognosis, and clinicopathological factors including HER2 expression and the levels of PyNPase and DPD in breast cancer. PyNPase and DPD levels in tumors and nontumorous tissues were examined by enzyme-linked immunosorbent assay (ELISA). RESULTS: PyNPase and DPD levels in tumors were significantly higher than in non-tumorous tissues (p<0.001). The DPD levels in tumors associated with> or =2+expression of HER2 were significantly higher than in others (p=0.014). Disease-free survival in patients with<100 U/mg protein of PyNPase levels or<4 of PyNPase/DPD ratio was significantly better compared with others (p=0.022, p=0.014). CONCLUSION: PyNPase/DPD ratio may be a new prognostic marker in breast cancer.
[Mh] Termos MeSH primário: Neoplasias da Mama/diagnóstico
Neoplasias da Mama/enzimologia
Di-Hidrouracila Desidrogenase (NADP)/metabolismo
Pentosiltransferases/metabolismo
[Mh] Termos MeSH secundário: Adulto
Idoso
Idoso de 80 Anos ou mais
Neoplasias da Mama/tratamento farmacológico
Neoplasias da Mama/cirurgia
Feminino
Saúde
Seres Humanos
Meia-Idade
Prognóstico
Pirimidina Fosforilases
Recidiva
[Pt] Tipo de publicação:ENGLISH ABSTRACT; JOURNAL ARTICLE
[Nm] Nome de substância:
EC 1.3.1.2 (Dihydrouracil Dehydrogenase (NADP)); EC 2.4.2.- (Pentosyltransferases); EC 2.4.2.- (Pyrimidine Phosphorylases)
[Em] Mês de entrada:0804
[Cu] Atualização por classe:101118
[Lr] Data última revisão:
101118
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:080319
[St] Status:MEDLINE


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[PMID]:17681069
[Au] Autor:Fujimoto K; Matsumura Y; Tani Y; Ozono S; Hirao Y; Okajima E
[Ad] Endereço:Department of Urology, Nara Medical University, Kashihara, Japan. kiyokun@naramed-u.ac.jp
[Ti] Título:Tissue levels of pyrimidine nucleoside phosphorylase activity in human and rodent bladder cancer and normal bladder tissue.
[So] Source:Int J Urol;14(8):754-9, 2007 Aug.
[Is] ISSN:0919-8172
[Cp] País de publicação:Australia
[La] Idioma:eng
[Ab] Resumo:OBJECTIVES: To assess the relationship between the tissue levels of pyrimidine nucleoside phosphorylase (PyNpase) and clinicopathological parameters in human bladder cancer and to investigate the PyNpase levels in rat and mouse urinary bladder initiated by N-butyl-N-(4-hydroxybutyl) nitrosamine (BBN). METHODS: The PyNpase levels in tumor tissue, normal tissue adjacent to the tumor, and normal tissue apart from the tumor were measured in 102 patients. Additionally, the PyNpase levels were measured in rat and mouse urinary bladders treated with BBN. RESULT: The PyNpase levels of tumor tissue significantly correlated to the tumor grade and growth pattern (papillary/non-papillary), while stage, multiplicity, and tumor shape (peduncle/sessile) were not independent factors. The low-risk tumor of primary, single, G1-Ta showed significantly low levels of PyNpase. The PyNpase levels in the tumor tissue were significantly higher than those in the normal tissue. The PyNpase levels in the adjacent normal tissue were significantly higher than those in the distant normal tissue. The PyNpase levels in rat bladder tissue were significantly higher in the BBN-treatment groups than in those in the control group, only during the early carcinogenic stage. The PyNpase levels in mouse bladder tissue were significantly higher in BBN-treatment groups than in those in the control group during the whole experiment period. CONCLUSION: Our results indicated that not only tumor tissue but also normal tissue adjacent to the tumor had a potential of angiogenesis for tumor development, and transurethral resection of the bladder tumor with a wide normal margin seems to be a reasonable strategy for decreasing the risk of recurrence.
[Mh] Termos MeSH primário: Carcinoma Papilar/metabolismo
Recidiva Local de Neoplasia/metabolismo
Pentosiltransferases/metabolismo
Timidina Fosforilase/metabolismo
Neoplasias da Bexiga Urinária/metabolismo
Bexiga Urinária/enzimologia
[Mh] Termos MeSH secundário: Adulto
Idoso
Idoso de 80 Anos ou mais
Animais
Butilidroxibutilnitrosamina
Carcinógenos
Carcinoma Papilar/epidemiologia
Carcinoma Papilar/patologia
Feminino
Seres Humanos
Masculino
Camundongos
Camundongos Endogâmicos C3H
Meia-Idade
Invasividade Neoplásica
Pirimidina Fosforilases
Ratos
Ratos Endogâmicos F344
Fatores de Risco
Especificidade da Espécie
Bexiga Urinária/patologia
Neoplasias da Bexiga Urinária/epidemiologia
Neoplasias da Bexiga Urinária/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Carcinogens); 3817-11-6 (Butylhydroxybutylnitrosamine); EC 2.4.2.- (Pentosyltransferases); EC 2.4.2.- (Pyrimidine Phosphorylases); EC 2.4.2.4 (Thymidine Phosphorylase)
[Em] Mês de entrada:0802
[Cu] Atualização por classe:101118
[Lr] Data última revisão:
101118
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:070808
[St] Status:MEDLINE



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