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6 results on '"Bugg, B. Y."'

1. Scientific Proceedings Second International Symposium on Cytostatic Drug Resistance

Author

Hill, Bridget T., Hosking, L. K., McClean, S., Shellard, S. A., Dempke, W. C. M., Whelan, R. D. H., Sehested, M., Friche, E., Demant, E. J. F., Jensen, P. B., Kopnin, B. P., Wolf, B., Seidel, A., Nickelsen, M., Brandt, I., Heinemann, G., Dietel, M., Bremer, S., Hoof, T., Tümmler, B., Broxterman, H. J., Versantvoort, C. H. M., Kuiper, C. M., Feller, N., Schuurhuis, G. J., Lankelma, J., Gupta, S., Tsuruo, T., Kim, C., Gollapudi, S., Bittl, A., Nap, M., Jäger, W., Lathan, B., Lang, N., Raikhlin, N. T., Perevozchikov, A. G., Volodina, J. L., Licht T., Fiebig H. H., Bross K. J., Herrmann F., Mertelsmann R., Bashir, I., Sikora, K., Foster, C. S., Castagna, M., Viacava, P., Cianfrigliao, M., Favati, A., Collecchi, P., Caligo, M. A., Cipollini, G., Bevilacqua, G., Schrenk, D., Gant, T. W., Silverman, J. A., Thorgeirsson, S. S., Harstrick, A., Zhang, Z. G., Schmoll, H. J., Rustum, Y., Mitze, M., Beck, T., Weikel, W., Brumm, C., Knapstein, P. G., McDonald, T., Gardner, P., Kang, N., van der Heyden, S. A. M., Elst, H. J., Stein, U., Jandrig, B., Krause, H., Schmidt-Peter, P., Frege, J., Wunderlich, V., Boven, E., van Kalken, C. K., Pinedo, H. M., Gebauer, W., Fallgren-Gebauer, E., Diete, M., Wagner, T., Müller, M. R., Lennartz, K., Nowrousian, H. R., Seeber, S., Shtil, A. A., Kazarov, A. R., Gudkov, A. V., Stavrovskaya, A. A., Djuraeva, F. H., Stromskaya, T. P., Noller, A., Frese, G., Neumann, M., Wilisch, A., Probst, H., Gekeler, V., Handgretinger, R., Schmidt, H., Muller, C. P., Dopfer, R., Klingebiel, T., Niethammer, D., Weger, S., Diddens, H., Daumiller, E., Bunge, A., Lilischkis, R., Salmassi, A., Kopun M., Scherthan H., Granzow C., Leuschner, I., Schmidt, D., Hoffmann, H., Harms, D., Scagliotli, G. V., Leonardo, E., Cappia, S., Esposito, G., Tombesi, M., Cianfriglia, M., Esposito, G. V., Merendino, N., Viora, M., Caserta, M., Tritarelli, E., Rocca, E., Boccoli, G., Samoggia, P., Fossati, C., Testa, U., Peschle, C., Darling, J. L., Ashmore, S. M., Peterson, D. C., Thomas, D. G. T., Kramer, R. A., Stanlunas, R., Summerhayes, T., Lion, T., Shoemaker, R. H., Wu, L., Smythe, A., Boyd, M. R., Beck, W. T., Danks, M. K., Wolverton, J. S., Chen, M., Bugg, B. Y., Suttle, D. P., Catapano, C. V., Fernandes, D. J., Gieseler, F., Boege, F., Erttmann, R., Arps, H., Zwelling, L., Wilms, K., Biersack, H., Kaspers, G. J. L., Pieters, R., Klumper, E., de Waal, F. C., van Wering, E. R., Veerman, A. J. P., Schmidt, C. A., Lorenz, F., Schäfer, A., Kirsch, A., Siegert, W., Huhn, D., Simon, W. E., Siebert, G., Schneider, M., Oettling, M., Reymann, A., Entmann, R., Schmidt, S., Woermann, C., Windmeier, C., Herzig, I., Schaefer, B., Heidebrecht, H. J., Wacker, H. H., Künnemann, H., van Heijningen, Th. H. M., Slovak, M. L., Baak, J. P. A., Steidtmann, K., Fichtinger-Schepman, A. -M. J., Hill, B. I., Scanlon, K. J., Zeller, W. J., Chen, G., Gietema, J. A., de Vries, E. G. E, Sleijfer, D.Th, Willemse, P. H. B., Guchelaar, H. J., Uges, D. R. A., Aulenbacher, P., Voegeli, R., Mulder, N. H., Skrezek, C., Bertermann, H., Eichholtz-Wirth, H., Born, R., Bier, H., Koch, M., Bernhardt, G., Hählen, K., Reile, H., van Zantwijk, C. H., Wering, E. R. van, Görögh, T., Lippert, B., Werner, J. A., Eickbohm, J. E., Mickiseh, G. H., Gottesman, M. M., Pastan, I., Hofmann, J., Wolf, A., Spitaler, M., Bock, G., Grunicke, H., Ponstingl, H., Roth, I., Granzow, C., Dörner, C., Erttmann, R., Looft, G., Ossenkoppele, G. J., Scheffer, G. L., Atassi, G., Pierre, A., Kraus, L., Leonce, S., Regnier, G., Dhainaut, A., Ponstingl H., Stöhr M., Rohlff, C., Glazer, R. I., Cho-Chung, Y. S., Höllt, V., Kouba, M., Vogt, G., Allmeier, H., Nissen, N. I., Cros, S., Guilbaud, N., Dunn, T., Berlion, M., Atassi, G., Bizzari, J. P., Messing, A. M., Matuschek, A., Mutter, I., Kiwit, J. C. W., Bastian, L., Goretzki, P. E., Frilling, A., Simon, D., Röher, H. D., Reichle, A., Altmayr, F., Rastetter, J., Erbil, C., Jaques, G., Maasberg, M., Havemann, K., Häußermann, K., Heidebrecht, H. -J., Van de Vrie, W., Gheuens, E. E. O., Durante, N. M. C., De Bruijn, E. A., Marquet, R. L., Van Oosterom, A. T., Eggermont, A. M. M., Stow, M. W., Vickers, S. E., Warr, J. R., Roller, E., Eichelbaum, M., Klumpp, B., Krause, J., Schumacher, K., Hörner, S., Laßmann, A., Traugott, U., Schlick, E., Bürkle, D., Futscher BW, List AF, Dalton WS, Ladda, E., Bühl, K., Weimer, A., Eser, C., Hamprecht, K., Schalk, K. P., Jackisch, C., Brandt, B., Blum, M., Louwen, F., Schulz, K., Hanker, J. P., Rüther, U., Schmidt, A., Müller, H. A. G., Nunnensiek, C., Bader, H., Eisenberger, F., Jipp, P., Niethammer, B., Muller, C., Ling, V., Joncourt, F., Redmond, S., Stöhr, M., Buser, K., Fey, M., Tobler, A., Brunner, K., Gratwohl, A., Cerrry, T., Nuessler, V., Pelka-Fleischer, R., Nerl, C., Beckert, B., Wilmanns, W., Hegewisch-Becker, S., Fliegner, M., Zander, A., Hossfeld, D. K., Blanz, J., Mewes, K., Ehninger, G., Zeller, K. -P., Schuldes, H., Herrmann, G., Boeckmann, W., Schroeder, R., Jonas, D., Zurborn, K. -H., Bruhn, H. D., Uharek, L., Glass, B., Gassmann, W., Loeffler, H., Mueller-Ruohholtz, W., Gassmann W., Glass B., Uharek L., Loeffler H., Mueller-Ruchholtz W., Jaquet, K., Kreipe, H., Felgner, J., Radzun, H. J., Parwaresch, M. R., Kogan EA, Mazurenko NN, Sekamova SM, Wolf, H., Röhe, K., Wilkens, K., Clausen, M., Henze, E., van der Bosch, J., Rüller, S., Schlaak, M., Köhl, U., Schwabe, D., Rohrbach, E., Montag, E., Bauer, S., Cinatl, J., Cinatl, Jr, I., Mainke, M., Geiss, H., Kornhuber, B., Juhl, H., Stritzel, H., Kalhoff, H., Schniegel, W., Menke, T., Pröbsting, B., Schulze-Westhoff, P., Boos, J., Weidner, J., Wedemeyer, N., Wiedorn, K., Ueda, Y., Blasius, S., Wuisman, P., Böcker, W., Roessner, A., Dockhorn-Dworniczak, B., Ramm, D., Knebel, J., Sass, W., Aufderheide, M., and Seifert, J.

Published
1991
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3. Molecular cloning and nucleotide sequence for the complete coding region of human UMP synthase.

Author

Suttle, D P, Bugg, B Y, Winkler, J K, and Kanalas, J J

Abstract

The last two steps in the de novo biosynthesis of UMP are catalyzed by orotate phosphoribosyltransferase (OPRT; orotidine-5'-phosphate:pyrophosphate phosphoribosyltransferase; EC 2.4.2.10) and orotidine-5'-monophosphate decarboxylase (orotidine-5'-phosphate carboxy-lyase; EC 4.1.1.23). In mammals these two activities are found in a single, bifunctional protein called UMP synthase. A human T-lymphoblastic cell cDNA library constructed in lambda gt10 was screened with a UMP synthase-specific rat cDNA probe. Human UMP synthase cDNAs were isolated and then used to select UMP synthase gene fragments. The complete coding sequence of the mRNA for UMP synthase was determined by analysis of overlapping cDNA and genomic fragments. One of the cDNAs appears to have been synthesized from an incompletely or alternatively processed form of the UMP synthase mRNA. This cDNA lacks a poly(A) tail and has an extended 3'-nontranslated region that hybridizes with larger forms of the UMP synthase mRNA. The UMP synthase protein is composed of 480 amino acids with a molecular weight of 52,199. The two activities of UMP synthase reside in distinct domains encoded by the 3' and 5' halves of the mRNA. The COOH-terminal 258 amino acids of the human UMP synthase protein contain the orotidine-5'-monophosphate decarboxylase catalytic domain. This region is highly homologous to the mouse orotidine-5'-monophosphate decarboxylase sequence. The NH2-terminal 214 amino acids contain the OPRT domain. There is amino acid homology between this protein domain and specific regions of the Escherichia coli OPRT. The human OPRT domain also contains the putative catalytic site common to other human phosphoribosyltransferases.

Published
1988
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4. Single-strand conformational polymorphism analysis of the M(r) 170,000 isozyme of DNA topoisomerase II in human tumor cells.

Author

Danks MK, Warmoth MR, Friche E, Granzen B, Bugg BY, Harker WG, Zwelling LA, Futscher BW, Suttle DP, and Beck WT

Subjects
Adenosine Triphosphate metabolism, Base Sequence, DNA Topoisomerases, Type II chemistry, DNA, Single-Stranded analysis, Humans, Isoenzymes antagonists & inhibitors, Isoenzymes chemistry, Molecular Sequence Data, Molecular Weight, Polymerase Chain Reaction, Protein Conformation, Temperature, Topoisomerase II Inhibitors, Tumor Cells, Cultured, Tyrosine genetics, DNA Topoisomerases, Type II genetics, Isoenzymes genetics, Point Mutation, Polymorphism, Genetic, Precursor Cell Lymphoblastic Leukemia-Lymphoma enzymology
Abstract

Five cell lines selected for resistance to the cytotoxicity of inhibitors of DNA topoisomerase II have point mutations in the gene that codes for the M(r) 170,000 form of this enzyme. In each case, the mutation results in an amino acid change in or near an ATP binding sequence of the M(r) 170,000 isozyme of topoisomerase II. We used single-strand conformational polymorphism analysis to screen for similar mutations in other drug-resistant cell lines or in leukemic cells from patients previously treated with etoposide or teniposide. We also analyzed the region of the gene that codes for amino acids adjacent to the tyrosine at position 804 of topoisomerase II which binds covalently to DNA. CEM/VM-1, CEM/VM-1-5, and HL-60/AMSA human leukemic cell lines were used as controls; 3 of 3 known mutations were detected by migration differences of polymerase chain reaction products from the RNA extracted from these three lines. A previously unknown mutation was found in the tyrosine 804 region of the M(r) 170,000 topoisomerase II expressed by CEM/VM-1 and CEM/VM-1-5 cells. Sequence analysis showed that substitution of a T for a C at nucleotide 2404 resulted in an amino acid change of a serine for a proline at amino acid 802. No mutations in any of the ATP binding sequences or in the tyrosine 804 region were detected in polymerase chain reaction products from RNA extracted from human leukemia HL-60/MX2 or CEM/MX1 cells (both cell lines selected for resistance to mitoxantrone) or in human myeloma 8226/Dox1V cells (selected for resistance by simultaneous exposure to doxorubicin and verapamil). No mutations were detected in polymerase chain reaction products from RNA extracted from blasts of 15 patients with relapsed acute lymphocytic leukemia, previously treated with etoposide or teniposide. We conclude that: (a) single-strand conformational polymorphism analysis is useful for screening for mutations in topoisomerase II; (b) resistance to the cytotoxicity of inhibitors of DNA topoisomerase II is not always associated with mutations in ATP binding sequences or the active site tyrosine region of M(r) 170,000 topoisomerase II; and (c) mutations similar to those detected in drug resistant cells selected in culture have not been identified in blast cells from patients with relapsed acute lymphocytic leukemia, previously treated with etoposide or teniposide.

Published
1993

5. Altered DNA topoisomerase II in multidrug resistance.

Author

Beck WT, Danks MK, Wolverton JS, Granzen B, Chen M, Schmidt CA, Bugg BY, Friche E, and Suttle DP

Subjects
Animals, Drug Resistance genetics, Humans, Topoisomerase II Inhibitors, Tumor Cells, Cultured, Antineoplastic Agents pharmacology, DNA Topoisomerases, Type II metabolism
Abstract

The characteristic feature of multidrug resistance (MDR) associated with drugs that interact with DNA topoisomerase II (topo II) is alterations in topo II activity or amount (at-MDR). We have characterized the at-MDR phenotype in human leukemic CEM cells selected for resistance to the topo II inhibitor, VM-26. Compared to drug-sensitive cells, the key findings are that at-MDR cells exhibit (i) decreased topo II activity; (ii) decreased drug sensitivity, activity and amount of nuclear matrix topo II; (iii) increased ATP requirement of topo II; (iv) a single base mutation in topo II resulting in a change of Arg to Gln at position 449, at the start of the motif B/nucleotide binding site; and (v) decreased topo II phosphorylation, suggesting decreased kinase or increased phosphatase activities. Recent results using single-stranded conformational polymorphism analysis reveals the presence of a mutation in the motif B/nucleotide binding site of the topo II alpha gene in CEM at-MDR cells and in another leukemic cell line selected for resistance to m-AMSA. Finally, we have observed marked changes in the nuclear distribution of topo II in cells treated with anti-topo II drugs and have also found these changes to be attenuated in drug-resistant cells. We postulate that traditional inhibitors of topo II alter the equilibrium of the strand-passing reaction such that the number of enzyme-DNA covalent complexes increases. We further suggest that when the enzyme is bound to DNA it is protected from proteolysis, thus allowing more topo II molecules to be detected.(ABSTRACT TRUNCATED AT 250 WORDS)

Published
1993
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6. Polymerase chain reaction amplification of single-stranded DNA containing a base analog, 2-chloradenine.

Author

Hentosh P, McCastlain JC, Grippo P, and Bugg BY

Subjects
Adenine chemistry, Base Sequence, DNA, Molecular Sequence Data, Adenine analogs & derivatives, DNA, Single-Stranded chemical synthesis, Polymerase Chain Reaction methods
Abstract

By utilization of polymerase chain reaction techniques, single-stranded DNA of defined length and sequence containing a purine analog, 2-chloroadenine, in place of adenine was synthesized. This was accomplished by a combination of standard polymerase chain amplification reactions with Thermus aquaticus DNA polymerase in the presence of four normal deoxynucleoside triphosphates, M13 duplex DNA as template, and two primers to generate double-stranded DNA 118 bases in length. An asymmetric polymerase chain reaction, which produced an excess of single-stranded 98-base DNA, was then conducted with 2-chloro-2'-deoxy-adenosine 5'-triphosphate in place of dATP and with only one primer that annealed internal to the original two primers. Standard polymerase chain reaction techniques alone conducted in the presence of the analog as the fourth nucleotide did not produce duplex DNA that was modified within both strands. This asymmetric technique allows the incorporation of an altered nucleotide at specific sites into large quantities of single-stranded DNA without using chemical phosphoramidite synthesis procedures and circumvents the apparent inability of DNA polymerase to synthesize fully substituted double-stranded DNA during standard amplification reactions. The described method will permit the study of the effects of modified bases in template DNA on a variety of protein-DNA interactions and enzymes.

Published
1992
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