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Thematische Bibliographien / DNA topoisomerase II beta

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Auswahl der wissenschaftlichen Literatur zum Thema „DNA topoisomerase II beta“

Autor: Grafiati

Veröffentlicht am 28. Juni 2021

Zuletzt aktualisiert am 1. Februar 2022

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Zeitschriftenartikel zum Thema "DNA topoisomerase II beta"

1

Bernard, F. X., S. Sablé, B. Cameron, J. Provost, J. F. Desnottes, J. Crouzet und F. Blanche. „Glycosylated flavones as selective inhibitors of topoisomerase IV.“ Antimicrobial Agents and Chemotherapy 41, Nr. 5 (Mai 1997): 992–98. http://dx.doi.org/10.1128/aac.41.5.992.

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Three flavonoids which promoted Escherichia coli topoisomerase IV-dependent DNA cleavage were isolated from cottonseed flour and identified as quercetin 3-O-beta-D-glucose-[1,6]-O-alpha-L-rhamnose (rutin), quercetin 3-O-beta-D-galactose-[1,6]-O-alpha-L-rhamnose, and quercetin 3-O-beta-D-glucose (isoquercitrin). The most active one (rutin) also inhibited topoisomerase IV-dependent decatenation activity (50% inhibitory concentration, 64 microg/ml) and induced the SOS response of a permeable E. coli strain. Derivatives of quercetin glycosylated at position C-3 were shown to induce two site-specific DNA cleavages of pBR322 DNA, which were mapped by DNA sequence analysis to the gene encoding resistance to tetracycline. Cleavage at these sites was hardly detectable in cleavage reactions with quercetin or fluoroquinolones. None of the three flavonoids isolated from cottonseeds had any stimulatory activity on E. coli DNA gyrase-dependent or calf thymus topoisomerase II-dependent DNA cleavage, and they were therefore specific to topoisomerase IV. These results show that selective inhibitors of topoisomerase IV can be derived from the flavone structure. This is the first report on a DNA topoisomerase inhibitor specific for topoisomerase IV.

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2

Sharma, Kaushal K., Brijendra Singh, Somdutt Mujwar und Prakash S. Bisen. „Molecular Docking Based Analysis to Elucidate the DNA Topoisomerase IIβ as the Potential Target for the Ganoderic Acid; A Natural Therapeutic Agent in Cancer Therapy“. Current Computer-Aided Drug Design 16, Nr. 2 (25.03.2020): 176–89. http://dx.doi.org/10.2174/1573409915666190820144759.

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Introduction: Intermediate covalent complex of DNA-Topoisomerase II enzyme is the most promising target of the anticancer drugs to induce apoptosis in cancer cells. Currently, anticancer drug and chemotherapy are facing major challenges i.e., drug resistance, chemical instability and, dose-limiting side effect. Therefore, in this study, natural therapeutic agents (series of Ganoderic acids) were used for the molecular docking simulation against Human DNATopoisomerase II beta complex (PDB ID:3QX3). Methods: Molecular docking studies were performed on a 50 series of ganoderic acids reported in the NCBI-PubChem database and FDA approved anti-cancer drugs, to find out binding energy, an interacting residue at the active site of Human DNA-Topoisomerase II beta and compare with the molecular arrangements of the interacting residue of etoposide with the Human DNA topoisomerase II beta. The autodock 4.2 was used for the molecular docking and pharmacokinetic and toxicity studies were performed for the analysis of physicochemical properties and to check the toxicity effects. Discovery studio software was used for the visualization and analysis of docked pose. Results and Conclusion: Ganoderic acids (GS-1, A and DM) were found to be a more suitable competitor inhibitor among the ganoderic acid series with appropriate binding energy, pharmacokinetic profile and no toxicity effects. The interacting residue (Met782, DC-8, DC-11 and DA-12) shared a chemical resemblance with the interacting residue of etoposide present at the active site of human topoisomerase II beta receptor.

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3

Vassetzky, Y. S., Q. Dang, P. Benedetti und S. M. Gasser. „Topoisomerase II forms multimers in vitro: effects of metals, beta-glycerophosphate, and phosphorylation of its C-terminal domain.“ Molecular and Cellular Biology 14, Nr. 10 (Oktober 1994): 6962–74. http://dx.doi.org/10.1128/mcb.14.10.6962.

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We present a novel assay for the study of protein-protein interactions involving DNA topoisomerase II. Under various conditions of incubation we observe that topoisomerase II forms complexes at least tetrameric in size, which can be sedimented by centrifugation through glycerol. The multimers are enzymatically active and can be visualized by electron microscopy. Dephosphorylation of topoisomerase II inhibits its multimerization, which can be restored at least partially by rephosphorylation of multiple sites within its 200 C-terminal amino acids by casein kinase II. Truncation of topoisomerase II just upstream of the major phosphoacceptor sites reduces its aggregation, rendering the truncated enzyme insensitive to either kinase treatments or phosphatase treatments. This is consistent with a model in which interactions involving the phosphorylated C-terminal domain of topoisomerase II aid either in chromosome segregation or in chromosome condensation.

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Vassetzky, Y. S., Q. Dang, P. Benedetti und S. M. Gasser. „Topoisomerase II forms multimers in vitro: effects of metals, beta-glycerophosphate, and phosphorylation of its C-terminal domain“. Molecular and Cellular Biology 14, Nr. 10 (Oktober 1994): 6962–74. http://dx.doi.org/10.1128/mcb.14.10.6962-6974.1994.

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We present a novel assay for the study of protein-protein interactions involving DNA topoisomerase II. Under various conditions of incubation we observe that topoisomerase II forms complexes at least tetrameric in size, which can be sedimented by centrifugation through glycerol. The multimers are enzymatically active and can be visualized by electron microscopy. Dephosphorylation of topoisomerase II inhibits its multimerization, which can be restored at least partially by rephosphorylation of multiple sites within its 200 C-terminal amino acids by casein kinase II. Truncation of topoisomerase II just upstream of the major phosphoacceptor sites reduces its aggregation, rendering the truncated enzyme insensitive to either kinase treatments or phosphatase treatments. This is consistent with a model in which interactions involving the phosphorylated C-terminal domain of topoisomerase II aid either in chromosome segregation or in chromosome condensation.

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5

Muller, M. T., und V. B. Mehta. „DNase I hypersensitivity is independent of endogenous topoisomerase II activity during chicken erythrocyte differentiation.“ Molecular and Cellular Biology 8, Nr. 9 (September 1988): 3661–69. http://dx.doi.org/10.1128/mcb.8.9.3661.

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Endogenous topoisomerase II cleavage sites were mapped in the chicken beta A-globin gene of 12- to 14-day embryonic erythrocytes. A major topoisomerase II catalytic site was mapped to the 5' end of the globin gene which contained a nucleosome-free and DNase I-hypersensitive site and additional but minor sites were mapped to the second intron and 3' of the gene to a tissue-specific enhancer. Cleavage sites, mapped in situ by indirect end labeling, were aligned to single-base-pair resolution by comparison to a consensus sequence derived for vertebrate topoisomerase II catalytic sites. In contrast to embryonic erythrocytes, endogenous topoisomerase II cleavages were not detected in erythrocytes from peripheral blood of adult chickens; therefore, as the transcriptional activity of the beta A-globin gene declines during terminal differentiation of erythrocytes, the activity of topoisomerase II in situ declines as well, despite the fact that DNase I hypersensitivity persists. The results showed that DNase I-hypersensitive chromatin can be maintained in the absence of topoisomerase II activity and suggested that topoisomerase II acts at hypersensitive sites because of an inherent attraction to some preexisting combination of DNA sequence or chromatin structure associated with DNase I-hypersensitive regions.

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Muller, M. T., und V. B. Mehta. „DNase I hypersensitivity is independent of endogenous topoisomerase II activity during chicken erythrocyte differentiation“. Molecular and Cellular Biology 8, Nr. 9 (September 1988): 3661–69. http://dx.doi.org/10.1128/mcb.8.9.3661-3669.1988.

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Endogenous topoisomerase II cleavage sites were mapped in the chicken beta A-globin gene of 12- to 14-day embryonic erythrocytes. A major topoisomerase II catalytic site was mapped to the 5' end of the globin gene which contained a nucleosome-free and DNase I-hypersensitive site and additional but minor sites were mapped to the second intron and 3' of the gene to a tissue-specific enhancer. Cleavage sites, mapped in situ by indirect end labeling, were aligned to single-base-pair resolution by comparison to a consensus sequence derived for vertebrate topoisomerase II catalytic sites. In contrast to embryonic erythrocytes, endogenous topoisomerase II cleavages were not detected in erythrocytes from peripheral blood of adult chickens; therefore, as the transcriptional activity of the beta A-globin gene declines during terminal differentiation of erythrocytes, the activity of topoisomerase II in situ declines as well, despite the fact that DNase I hypersensitivity persists. The results showed that DNase I-hypersensitive chromatin can be maintained in the absence of topoisomerase II activity and suggested that topoisomerase II acts at hypersensitive sites because of an inherent attraction to some preexisting combination of DNA sequence or chromatin structure associated with DNase I-hypersensitive regions.

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Jenkins, J. R., M. J. Pocklington und E. Orr. „The F1 ATP synthetase beta-subunit: a major yeast novobiocin binding protein“. Journal of Cell Science 96, Nr. 4 (01.08.1990): 675–82. http://dx.doi.org/10.1242/jcs.96.4.675.

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Novobiocin affects DNA metabolism in both prokaryotes and eukaryotes, resulting in cell death. In prokaryotes, the drug is a specific inhibitor of DNA gyrase, a type II topoisomerase that can be purified on a novobiocin-Sepharose column. The yeast type II topoisomerase is neither the biochemical, nor the genetic target of the antibiotic. We have purified the major yeast novobiocin binding proteins and identified one of them as the beta-subunit of the yeast mitochondrial F1 ATP synthetase, a protein highly conserved throughout evolution. The inactivation of this protein might explain the toxic effects of novobiocin on higher eukaryotic cells.

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Burden, D. A., L. J. Goldsmith und D. M. Sullivan. „Cell-cycle-dependent phosphorylation and activity of Chinese-hamster ovary topoisomerase II“. Biochemical Journal 293, Nr. 1 (01.07.1993): 297–304. http://dx.doi.org/10.1042/bj2930297.

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Cell-cycle-dependent protein levels and phosphorylation of DNA topoisomerase II in relation to its catalytic and cleavage activities were studied in Chinese-hamster ovary cells. Immunoreactive topoisomerase II protein levels were maximal in G2-phase cells, intermediate in S- and M-phase cells, and minimal in a predominantly G1-phase population. When the phosphorylation of topoisomerase II in vivo was corrected for differences in specific radioactivity of intracellular ATP, the apparent phosphorylation of S- and M-phase topoisomerase II was altered significantly. Relative phosphorylation in vivo was found to be greatest in M-phase cells and decreased in the other populations in the order: S > G2 > asynchronous. Phosphoserine was detected in every phase of the cell cycle, with a minor contribution of phosphothreonine demonstrated in M-phase cells. Topoisomerase II activity measured in vivo as 9-(4,6-O-ethylidene-beta-D-glucopyranosyl)-4′-demethylepipodophylloto xin (VP-16)-induced DNA double-strand breaks (determined by neutral filter elution) increased in the order: asynchronous < S < G2 < M. Topoisomerase II cleavage activity, assayed in vitro as the formation of covalent enzyme-DNA complexes, was lowest in S phase, intermediate in asynchronous and G2-phase cells, and maximal in M phase. Topoisomerase II decatenation activity was 1.6-1.8-fold greater in S-, G2- and M-phase populations relative to asynchronous cells. Therefore DNA topoisomerase II activity measured both in vivo and in vitro is maximal in M phase, that phase of the cell cycle with an intermediate level of immunoreactive topoisomerase II but the highest level of enzyme phosphorylation. The discordance between immunoreactive topoisomerase II protein levels, adjusted relative phosphorylation, catalytic activity, cleavage activity and amino acid residue(s) modified, suggests that the site of phosphorylation may be cell-cycle-dependent and critical in determining catalytic and cleavage activity.

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Strehl, Sabine, Karin Nebral, Helmut H. Schmidt und Oskar A. Haas. „Topoisomerase (DNA) II Beta 180 kDa TOP2B) - A New NUP98 Fusion Partner.“ Blood 106, Nr. 11 (16.11.2005): 2849. http://dx.doi.org/10.1182/blood.v106.11.2849.2849.

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Abstract The nucleoporin 98 kDa (NUP98) gene has been reported to be fused to 18 different partner genes in various hematological malignancies with 11p15 aberrations. The most frequently observed fusion partners of NUP98 belong to the homeobox family of transcription factors, whereas the non-HOX NUP98 fusion partners comprise a heterogeneous group of genes that are associated with a wide range of biological functions. Cytogenetic analysis of an adult de novo acute myeloid leukemia (AML-M5a) revealed a t(3;11)(p24;p15) indicating fusion of NUP98 with a novel partner gene. Fluorescence in situ hybridization (FISH) analysis with the NUP98-specific clone 1173K1 showed a split signal, suggesting that NUP98 was indeed disrupted. Selection of possible NUP98 partner genes was performed by computer-aided analysis of the 3p24 region using the University of California Santa Cruz genome browser. Out of the genes located at 3p24, TOP2B was selected as a fusion partner candidate gene. Dual-color fusion gene-specific FISH and RT-PCR analyses verified that NUP98 was indeed fused to TOP2B. In addition to the reciprocal NUP98-TOP2B and TOP2B-NUP98 in-frame fusion transcripts, an alternatively spliced out-of-frame TOP2B-NUP98 transcript that resulted in a premature stop codon was detected. Analysis of the genomic breakpoints revealed typical signs of non-homologous end joining resulting from error-prone DNA repair. TOP2B encodes a type II topoisomerase, which is involved in DNA transcription, replication, recombination, and mitosis. Type II DNA topoisomerases exist as homodimers, with each subunit consisting of three functional domains: an N-terminal ATPase domain, a central DNA breakage-rejoining domain, which contains a nucleotide-binding motif and the catalytic tyrosine, and a relatively poorly conserved C-terminal domain. The C-termini of the two TOP2 isoforms seem to be important for subcellular localization and functional bipartite nuclear localization signal (NLS) sequences as well as nuclear export signals (NES) are located in these domains. The NUP98-TOP2B fusion transcript fuses the N-terminal FG repeat and GLEBs motifs of NUP98 with the C-terminal domain of TOP2B, thereby retaining the functional NLS but eliminating the NES. Consequently, the putative reciprocal TOP2B-NUP98 chimeric protein retains the ATPase, the DNA breakage-rejoining, and the NES domains of TOP2B that are fused to the ribonucleoprotein-binding and the NLS domains of NUP98. The shorter out-of-frame TOP2Bexon24-NUP98exon14 fusion transcript might encode a truncated TOP2B isoform that consists of the ATPase, the DNA breakage-rejoining, and NES domains, which are fused to 18 fusion partner-unrelated amino acids. All proteins encoded by non-HOX NUP98 fusion partners described to date contain regions with a significant probability to adopt a coiled-coil conformation, and protein analysis with the COILS 2.2 and the MULTICOIL programs revealed this remarkable feature also in the C-terminal region of TOP2B. Intriguingly, this is only the second description of a chromosomal rearrangement that involves a topoisomerase and both TOP1 and TOP2B are fused to NUP98. This suggests that the choice of partner genes for NUP98 is not random, and that NUP98-TOP fusions may represent a distinct group, similar to the NUP98-HOX fusions.

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Biersack, H., S. Jensen, I. Gromova, I. S. Nielsen, O. Westergaard und A. H. Andersen. „Active heterodimers are formed from human DNA topoisomerase II alpha and II beta isoforms.“ Proceedings of the National Academy of Sciences 93, Nr. 16 (06.08.1996): 8288–93. http://dx.doi.org/10.1073/pnas.93.16.8288.

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Dissertationen zum Thema "DNA topoisomerase II beta"

1

Errington, Fiona. „An investigation into the cytotoxic mechanisms of DNA topoisomerase II poisons and catalytic inhibitors : the role of DNA topoisomerase II alpha and beta“. Thesis, University of Newcastle Upon Tyne, 2001. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.340718.

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2

Padget, Kay. „Quantitative analysis and drug sensitivity of human DNA topoisomerase II alpha and beta“. Thesis, University of Newcastle Upon Tyne, 1998. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.246093.

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3

McNamara, Suzan. „Topoisomerase II beta negatively modulates retinoic acid receptor alpha function : a novel mechanism of retinoic acid resistance in acute promyelocytic leukemia“. Thesis, McGill University, 2008. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=115693.

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Interactions between the retinoic acid receptor alpha (RARalpha) and coregulators play a key role in coordinating gene transcription and myeloid differentiation. In acute promyelocytic leukemia (APL), RARalpha is fused with the promyelocytic leukemia (PML) gene, resulting in the expression of the fusion protein PML/RARalpha. Here, I report that topoisomerase II beta (topoIIbeta) associates with and negatively modulates PML/RARalpha and RARalpha transcriptional activity, and increased levels and association of topoIIbeta cause resistance to retinoic acid (RA) in APL cell lines. Knock down of topoIIbeta was able to overcome resistance by permitting RA-induced differentiation and increased RA-gene expression. Overexpression of topoIIbeta, in clones from an RA-sensitive cell line, conferred resistance by a reduction in RA-induced expression of target genes and differentiation. Chromatin immunoprecipitation assays indicate that topoIIbeta is bound to an RA-response element, and inhibition of topoIIbeta causes hyper-acetylation of histone 3 at lysine 9 and activation of transcription. These results identify a novel mechanism of resistance in APL and provide further insights to the role of topoIIbeta in gene regulation and differentiation.
Studies to determine the mechanism by which topoIIbeta protein is regulated found that levels of protein kinase C delta (PKCdelta) correlated with topoIIbeta protein expression. Moreover, activation of PKCdelta, by RA or PMA, led to an increase of topoIIbeta protein levels. Most notably, in NB4-MR2 cells, we observed increased phosphorylation levels of threonine 505 on PKCdelta, a marker of activation. Inhibition of PKCdelta was able to overcome the topoIIbeta repressive effects on RA-target genes. In addition, the combination of RA and PKCdelta inhibition led to increased expression of the granulocytic marker, CD11c, in NB4 and NB4-MR2 cells. These results suggest that PKCdelta regulates topoIIbeta expression, and a constitutively active PKCdelta in the NB4-MR2 cell line leads to overexpression of topoIIbeta.
In conclusion, these studies demonstrate that topoIIbeta associates with RARalpha, binds to RAREs and plays a critical role in RA dependent transcriptional regulation and granulocytic differentiation. In addition, I show that topoIIbeta overexpression leads to RA resistance and provide evidence that topoIIbeta protein levels are regulated via a mechanism involving the PKCdelta pathway. This work has contributed to an enhanced understanding of the role of topoIIbeta in gene regulation and brings novel perspectives in the treatment of RA-resistance in APL.

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Wells, Nicholas James. „Phosphorylation of human topoisomerase II“. Thesis, University of Oxford, 1996. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.318833.

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5

Hochhauser, Daniel. „Transcriptional regulation of topoisomerase II“. Thesis, University of Oxford, 1993. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.333178.

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6

Lee, Ka Cheong. „Molecular pharmacology of DNA topoisomerase II drugs“. Thesis, University of Newcastle upon Tyne, 2016. http://hdl.handle.net/10443/3780.

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Topoisomerase II (TOP2) is an important anti-cancer drug target. This study demonstrates that proteasomal inhibition by MG132 or PS341 potentiates the effect of TOP2 poisons on cell growth inhibition. Mitoxantrone was potentiated the most. The presence of the proteasome inhibitor MG132 prolonged the half-life of drug-induced DNA-TOP2 complexes stabilised by mitoxantrone or etoposide. Genotoxicity was measured in K562 cells using in vitro micronucleus assays for combinations of a proteasome inhibitor (MG132 or PS341) and mitoxantrone and for each agent alone. Combinations that potentiated the cytotoxicity reduced the genotoxicity. This suggests that combining a proteasome inhibitor with a TOP2 drug has the potential to reduce late toxicities such as therapy related leukaemia. The genotoxicity of six TOP2 poisons was determined by high throughput in vitro micronucleus assays in three Nalm-6 cell lines with differing TOP2 levels. Lower genotoxicity was observed in TOP2B knock-out and TOP2A knock-down cells, suggesting both TOP2A and TOP2B have a role in genotoxicity triggered by TOP2 poisons.

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Fry, Andrew Mark. „Phosphorylation of the human topoisomerase II protein“. Thesis, University of Oxford, 1992. http://ora.ox.ac.uk/objects/uuid:70d2dbb9-d3fe-43ed-8206-44a95202eeff.

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DNA topoisomerase II is an essential enzyme in eukaryotes and is required for many aspects of DNA metabolism including DNA replication, recombination, chromosome segregation and chromosome condensation. It is also a major component of the nuclear scaffold. Topoisomerase II from lower eukaryotes has been shown to be phosphorylated in vivo and this phosphorylation leads to a modulation of activity. However, unlike these lower eukaryotes, human topoisomerase II exists as two closely related, but genetically distinct, isozymes which have markedly different expression and localization patterns. Topoisomerase IIα is a 170kDa protein and topoisomerase IIβ is 180kDa. This study set out to analyse the phosphorylation of these specific isozymes and understand how this leads to the regulation of their distinct biological functions. In order to undertake this study, two polyclonal anti-topoisomerase II antibodies were generated and a series of other polyclonal and monoclonal antibodies characterized. Furthermore, the α isozyme of human topoisomerase II was purified to near homogeneity from cultured HeLa cells. A kinase activity with the biochemical characteristics of casein kinase II co-purified with and could phosphorylate the purified topoisomerase Hot protein. The α and β isozymes of human topoisomerase II were both shown to be phosphoproteins in vivo. The α isozyme is phosphorylated predominantly on serine residues but with a minor proportion of phosphothreonine. Both the α isozyme and a stable ISOkDa fragment of the β isozyme are phosphorylated in vitro by casein kinase II and the catalytic subunit of PKA (cAMP-dependent protein kinase). The α isozyme can also be phosphorylated in vitro by Ca²⁺-dependent and -independent isozymes of protein kinase C and the cell cycle-regulated p34^cdc2 kinase. Two-dimensional tryptic phosphopeptide mapping suggested that the pattern of phosphorylation of human topoisomerase Ha protein in vivo is complex with phosphorylation occurring on multiple residues. Comparison with in vitro maps suggested that casein kinase II and PKA could account for most of the phosphorylation seen in vivo. Using a one- dimensional phosphopeptide mapping approach, a major site of phosphorylation in vivo appeared to be within the C-terminal 20kDa, and that casein kinase II, PKA and PKC may all phosphorylate this region. Phosphorylation of human topoisomerase Hoc protein by casein kinase II, PKA and PKC all led to a stimulation of activity as measured by plasmid relaxation and decatenation. In contrast, dephosphorylation led to a marked decrease in activity of the enzyme. The dephosphorylated enzyme could be reactivated by casein kinase II but not PKA phosphorylation. These data suggest that phosphorylation plays a crucial role in the control of DNA tertiary structure in human cells via regulation of the activity of topoisomerase II proteins.

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Atwal, Mandeep. „Myeloperoxidase enhances DNA damage induced by drugs targeting DNA topoisomerase II“. Thesis, University of Newcastle upon Tyne, 2017. http://hdl.handle.net/10443/3956.

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Topoisomerase II (TOP2) poisons are effective anti-cancer agents used to treat a wide range of neoplasms. However, TOP2 poisons are subjected to enzymatic conversion which leads to metabolites with altered DNA damaging properties. Myeloperoxidase, present exclusively within developing myeloid progenitors and granulocytes, is capable of the biotransformation of TOP2 poisons to metabolites that are potentially more genotoxic in nature. Whilst TOP2 poisons are valuable chemotherapeutic agents, their use is associated with myelosuppression and with the risk of developing therapy related acute myeloid leukaemia. The reason that myeloid progenitor cells are particularly susceptible to TOP2 poison associated genotoxicity is unclear, however the presence of myeloperoxidase could potentially make myeloid progenitor cells more vulnerable to TOP2 poison mediated damage. This lead to the hypothesis that myeloperoxidase inhibition could protect developing hematopoietic cells from TOP2 poison associated genotoxic and/or cytotoxic damage. Data generated in this thesis supports the proposed hypothesis as expression of myeloperoxidase significantly enhanced the accumulation of TOP2 poison induced TOP2-DNA covalent complexes and the level of DNA breaks within myeloid cell lines. The use of two potential clinically relevant inhibitors of myeloperoxidase showed that reduction in myeloperoxidase activity reduced the abundance of TOP2 poison stabilised TOP2-DNA complexes and DNA breaks. Furthermore, depletion of glutathione to mimic conditions experienced during chemotherapy, resulted in a myeloperoxidase dependent increase in TOP2 poison mediated DNA damage. Taken together these results show inhibition of myeloperoxidase could protect developing hematopoietic cells from TOP2 poison mediated damage without compromising the effectiveness of these drugs as antineoplastic agents.

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Goldstein, Eric D. „Analysis of the repair of topoisomerase II DNA damage“. Honors in the Major Thesis, University of Central Florida, 2011. http://digital.library.ucf.edu/cdm/ref/collection/ETH/id/385.

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A large number of anti-cancer chemotherapeutics target DNA topoisomerases. Etoposide is a specific topoisomerase II poison which causes reversible double strand DNA breaks. The focus of this project is to analyze the repair of DNA damage induced by etoposide.. Double strand DNA break repair is mediated by through either non-homologous end joining (NHEJ) or homologous recombination. NHEJ repairs through direct ligation of a double stranded break while homologous recombination utilizes a homologous template to recover the wild type sequence. A reporter cassette, RYDR-GFP, has been stably integrated into HeLa cells. This reporter contains an ultra-high affinity topoisomerase II cleavage site (RY) placed in the middle of a mutant GFP sequence. Flanking this sequence is a corresponding stretch of wild type GFP that is used as template to repair the break and restore gene function yielding GFP positive cells. Titrations with etoposide have shown that a logarithmic increase in drug concentration yields a corresponding increase in repair through homologous recombination (HR). This result demonstrates that topoisomerase II mediated damage is efficiently repaired by the process of HR. To examine NHEJ repair, a doxycycline inducible, stably integrated NHEJ HeLa cell reporter cassette was also evaluated. The data indicates that repair of topoisomerase II mediated DNA damage occurs more efficiently through the HR pathway. Collectively, the data suggests that tumor cells proficient in HR repair may effectively elude treatment by topoisomerase II targeting drugs.
B.S.
Bachelors
Medicine
Molecular Biology and Microbiology

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10

Fox, Mary Elizabeth. „Mechanisms of action of anticancer DNA topoisomerase II poisons“. Thesis, University of Cambridge, 1991. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.239716.

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Bücher zum Thema "DNA topoisomerase II beta"

1

Pommier, Yves. DNA Topoisomerases and Cancer. New York, NY: Springer Science+Business Media, LLC, 2012.

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2

Milan, Potmesil, Ross Warren E, New York University. Rita and Stanley H. Kaplan Cancer Center., National Cancer Institute (U.S.) und European Organization for Research on Treatment of Cancer., Hrsg. First Conference on DNA Topoisomerases in Cancer Chemotherapy: Alumni Hall, New York University Medical Center, New York, N.Y., November 19-20, 1986. Bethesda, MD: U.S. Dept. of Health and Human Services, Public Health Service, National Institutes of Health, 1987.

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3

Salmena, Leonardo. The cell cycle-dependent regulation of DNA topoisomerase II[alpha] expression is mediated by proteasomal degradation. Ottawa: National Library of Canada, 1999.

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4

International Symposium on DNA Topoisomerases in Chemotherapy (1991 Nagoya-shi, Japan). Molecular biology of DNA topoisomerases and its application to chemotherapy: Proceedings of the International Symposium on DNA Topoisomerases in Chemotherapy, Nagoya, Japan, November 18-20, 1991 (ISTOP 1991). Boca Raton: CRC Press, 1993.

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5

Toso, Robert. Expression and partial purification of a polyhistidine-tagged human DNA Topoisomerase II gas fusion protein, in the baculovirus expression system. Ottawa: National Library of Canada, 1993.

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6

Kay, Lawrence B., und United States. Environmental Protection Agency., Hrsg. Prophage induction by DNA topoisomerase II poisons and reactive-oxygen species: Role of DNA breaks. [Washington, D.C: U.S. Environmental Protection Agency, 1992.

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(Editor), Neil Osheroff, und Mary-Ann Bjornsti (Editor), Hrsg. DNA Topoisomerase Protocols, Part II: Enzymology & Drugs (Methods in Molecular Biology). Humana Press, 2001.

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8

R, Cozzarelli Nicholas, und Wang James C, Hrsg. DNA topology and its biological effects. [Cold Spring Harbor, NY]: Cold Spring Harbor Laboratory Press, 1990.

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9

Pommier, Yves. DNA Topoisomerases and Cancer. Humana, 2013.

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10

McPherson, John Peter. DNA topoisomerase II[alpha]: Role in resistance to antineoplastic agents and induction of apoptosis. 1998.

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Buchteile zum Thema "DNA topoisomerase II beta"

1

Pommier, Yves. „DNA Topoisomerase II Inhibitors“. In Cancer Therapeutics, 153–74. Totowa, NJ: Humana Press, 1997. http://dx.doi.org/10.1007/978-1-59259-717-8_7.

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2

Smith, P. J. „DNA Topoisomerase II Poisons and the Cell Cycle“. In Basic and Clinical Applications of Flow Cytometry, 211–25. Boston, MA: Springer US, 1996. http://dx.doi.org/10.1007/978-1-4613-1253-6_14.

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3

Kaur, Paramjeet, Varinder Kaur und Satwinderjeet Kaur. „DNA Topoisomerase II: Promising Target for Anticancer Drugs“. In Multi-Targeted Approach to Treatment of Cancer, 323–38. Cham: Springer International Publishing, 2014. http://dx.doi.org/10.1007/978-3-319-12253-3_20.

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Bandele, Omari J., und Neil Osheroff. „Cleavage of Plasmid DNA by Eukaryotic Topoisomerase II“. In Methods in Molecular Biology, 39–47. Totowa, NJ: Humana Press, 2009. http://dx.doi.org/10.1007/978-1-60761-340-4_4.

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5

Bromberg, Kenneth D., und Neil Osheroff. „Mechanism of action of topoisomerase II-targeted anticancer drugs“. In DNA Topoisomerases in Cancer Therapy, 53–78. Boston, MA: Springer US, 2003. http://dx.doi.org/10.1007/978-1-4615-0141-1_3.

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Furniss, Katherine, Amit C. J. Vas, Andrew B. Lane und Duncan J. Clarke. „Monitoring the DNA Topoisomerase II Checkpoint in Saccharomyces cerevisiae“. In Methods in Molecular Biology, 217–40. New York, NY: Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4939-7459-7_16.

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Capranico, G., und F. Zunino. „Structural Requirements for DNA Topoisomerase II Inhibition by Anthracyclines“. In The Jerusalem Symposia on Quantum Chemistry and Biochemistry, 167–76. Dordrecht: Springer Netherlands, 1990. http://dx.doi.org/10.1007/978-94-011-3728-7_12.

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Andoh, Toshiwo, Ken Umemura, Kae Yanase und Takao Yamori. „Development of new topoisomerase II-targeting compounds as candidate anticancer drugs“. In DNA Topoisomerases in Cancer Therapy, 167–88. Boston, MA: Springer US, 2003. http://dx.doi.org/10.1007/978-1-4615-0141-1_9.

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Larsen, Annette K., Andrzej Skladanowski und Krzysztof Bojanowski. „The roles of DNA topoisomerase II during the cell cycle“. In Progress in Cell Cycle Research, 229–39. Boston, MA: Springer US, 1996. http://dx.doi.org/10.1007/978-1-4615-5873-6_22.

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10

Beck, W. T., T. Funabiki und M. K. Danks. „The Role of DNA Topoisomerase II in Multidrug Resistance in Human Leukemia“. In Acute Leukemias, 11–15. Berlin, Heidelberg: Springer Berlin Heidelberg, 1992. http://dx.doi.org/10.1007/978-3-642-76591-9_2.

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Konferenzberichte zum Thema "DNA topoisomerase II beta"

1

Sun, Yilun, Sule Bertram und John L. Nitiss. „Abstract 842: DNA opilymerase β participates in the repair of DNA damage from topoisomerase II“. In Proceedings: AACR Annual Meeting 2014; April 5-9, 2014; San Diego, CA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7445.am2014-842.

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Gilbertson, Matthew, Radhika Patel, Karin C. Nitiss und John L. Nitiss. „Abstract 3580: Topoisomerase II mediated DNA damage generates unique classes of genome rearrangements“. 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.am2016-3580.

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Kawatani, Makoto, Hiroshi Takayama, Makoto Muroi, Shinya Kimura, Taira Maekawa und Hiroyuki Osada. „Abstract C157: Identification of a novel DNA topoisomerase II inhibitor by proteomic profiling“. In Abstracts: AACR-NCI-EORTC International Conference: Molecular Targets and Cancer Therapeutics--Nov 15-19, 2009; Boston, MA. American Association for Cancer Research, 2009. http://dx.doi.org/10.1158/1535-7163.targ-09-c157.

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Ramesh, Bhargavi, Yilun Sun, John L. Nitiss, Jay Anand und Karin C. Nitiss. „Abstract 4727: Role of SUMOylating enzymes in repair of Topoisomerase II mediated DNA damage“. In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.sabcs18-4727.

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Ramesh, Bhargavi, Yilun Sun, John L. Nitiss, Jay Anand und Karin C. Nitiss. „Abstract 4727: Role of SUMOylating enzymes in repair of Topoisomerase II mediated DNA damage“. In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.am2019-4727.

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Auzanneau, Céline, Danièle Montaudon, Stéphane Puyo, Rémi Jacquet, Assia Elkaoukabi-Chaibi, Stéphane Quideau, Francesca De Giorgi, François Ichas und Philippe Pourquier. „Abstract 2531: Vescalagin, a polyphenolic ellagitanin specifically inhibiting the alpha isoform of human DNA topoisomerase II“. In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-2531.

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Bau, Jason T., und Ebba U. Kurz. „Abstract C39: Catalytic inhibition of human DNA topoisomerase II α by salicylate and related nonsteroidal anti-inflammatory drugs“. In Abstracts: Second AACR International Conference on Frontiers in Basic Cancer Research--Sep 14-18, 2011; San Francisco, CA. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.fbcr11-c39.

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Nitiss, John L., Margarita Mishina und Jeffrey Berk. „Abstract CN08-02: Repair of topoisomerase II mediated DNA damage: A potential mechanism for targeting specific Top2 isoforms“. In Abstracts: AACR-NCI-EORTC International Conference: Molecular Targets and Cancer Therapeutics--Nov 15-19, 2009; Boston, MA. American Association for Cancer Research, 2009. http://dx.doi.org/10.1158/1535-7163.targ-09-cn08-02.

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Auzanneau, Céline, Danièle Montaudon, Rémi Jacquet, Assia Elkaoukabi-Chaibi, Stéphane Quideau, Francesca De Giorgi, François Ichas und Philippe Pourquier. „Abstract 3519: The polyphenolic ellagitanin vescalagin is a specific inhibitor of the alpha isoform of human DNA topoisomerase II“. 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.am10-3519.

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Frank, Nicole, Richard Olson, Gerald M. Walsh, Todd Talley und Barry Cusack. „Abstract 3428: Effect of a non cardiotoxic Doxorubicin analog, 13-deoxy, 5-imino doxorubicin on decatenation of DNA by Topoisomerase II.“ In Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-3428.

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